HEADER    MEMBRANE PROTEIN/AGONIST                14-JUL-19   6PT3              
TITLE     CRYSTAL STRUCTURE OF THE ACTIVE DELTA OPIOID RECEPTOR IN COMPLEX WITH 
TITLE    2 THE SMALL MOLECULE AGONIST DPI-287                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DELTA OPIOID RECEPTOR;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, DOP, DOR,         
KEYWDS   2 AGONIST, ACTIVE DOP-DPI-287 STRUCTURE, LCP, MEMBRANE PROTEIN-AGONIST 
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.CLAFF,J.YU,V.BLAIS,N.PATEL,C.MARTIN,L.WU,G.W.HAN,B.J.HOLLERAN,O.VAN 
AUTHOR   2 DER POORTEN,M.A.HANSON,P.SARRET,L.GENDRON,V.CHEREZOV,V.KATRITCH,     
AUTHOR   3 S.BALLET,Z.LIU,C.E.MULLER,R.C.STEVENS                                
REVDAT   2   18-DEC-19 6PT3    1       JRNL                                     
REVDAT   1   11-DEC-19 6PT3    0                                                
JRNL        AUTH   T.CLAFF,J.YU,V.BLAIS,N.PATEL,C.MARTIN,L.WU,G.W.HAN,          
JRNL        AUTH 2 B.J.HOLLERAN,O.VAN DER POORTEN,K.L.WHITE,M.A.HANSON,         
JRNL        AUTH 3 P.SARRET,L.GENDRON,V.CHEREZOV,V.KATRITCH,S.BALLET,Z.J.LIU,   
JRNL        AUTH 4 C.E.MULLER,R.C.STEVENS                                       
JRNL        TITL   ELUCIDATING THE ACTIVE DELTA-OPIOID RECEPTOR CRYSTAL         
JRNL        TITL 2 STRUCTURE WITH PEPTIDE AND SMALL-MOLECULE AGONISTS.          
JRNL        REF    SCI ADV                       V.   5 X9115 2019              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   31807708                                                     
JRNL        DOI    10.1126/SCIADV.AAX9115                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 16341                          
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)  : 0.246                          
REMARK   3   R VALUE            (WORKING SET)  : 0.245                          
REMARK   3   FREE R VALUE                      : 0.269                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.780                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 781                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 8                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.53                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 85.50                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2619                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2390                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2488                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2370                   
REMARK   3   BIN FREE R VALUE                        : 0.2680                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 131                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5646                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 133.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -23.38670                                            
REMARK   3    B22 (A**2) : 23.34800                                             
REMARK   3    B33 (A**2) : 0.03870                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.560               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.526               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
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      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5846   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7996   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2597   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 83     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 859    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5846   ; 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   : 835    ; 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   : 7233   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.20                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.02                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|999 - A|1106 A|41 - A|329 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):    2.9942  -36.3644  -48.5911           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0501 T22:   -0.2649                                    
REMARK   3     T33:   -0.2819 T12:   -0.0079                                    
REMARK   3     T13:    0.0587 T23:   -0.1155                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0786 L22:    0.7152                                    
REMARK   3     L33:    3.5057 L12:   -0.1857                                    
REMARK   3     L13:    0.5653 L23:   -0.5071                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1565 S12:    0.0262 S13:   -0.0698                     
REMARK   3     S21:    0.2453 S22:   -0.0058 S23:    0.0110                     
REMARK   3     S31:   -0.1392 S32:    0.1681 S33:    0.1624                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1003 - B|1100 B|1110 - B|1400 }                    
REMARK   3    ORIGIN FOR THE GROUP (A):    2.2154   -5.7961  -40.2000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1684 T22:   -0.3026                                    
REMARK   3     T33:   -0.3109 T12:   -0.0038                                    
REMARK   3     T13:   -0.0862 T23:   -0.0242                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6052 L22:    2.2251                                    
REMARK   3     L33:    1.8512 L12:   -0.0348                                    
REMARK   3     L13:   -0.8472 L23:   -0.0809                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1712 S12:    0.0875 S13:    0.0244                     
REMARK   3     S21:    0.1273 S22:    0.1212 S23:   -0.2516                     
REMARK   3     S31:    0.1610 S32:    0.1872 S33:    0.0500                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THERE ARE SOME UNKNOWN DENSITIES          
REMARK   3  LOCATED NEAR THE LIGAND BINDING SITE ON BOTH A AND B CHAINS THEY    
REMARK   3  HAVE NOT BEEN MODELLED.                                             
REMARK   4                                                                      
REMARK   4 6PT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243021.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16342                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4N6H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32-35% PEG400, 100-110 MM POTASSIUM      
REMARK 280  CITRATE TRIBASIC MONOHYDRATE AND 100 MM MES PH 6.0, LIPIDIC         
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.54200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.74550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       71.05050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.74550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.54200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       71.05050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN   
REMARK 300 IS UNKNOWN.                                                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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     MET A   951                                                      
REMARK 465     LYS A   952                                                      
REMARK 465     THR A   953                                                      
REMARK 465     ILE A   954                                                      
REMARK 465     ILE A   955                                                      
REMARK 465     ALA A   956                                                      
REMARK 465     LEU A   957                                                      
REMARK 465     SER A   958                                                      
REMARK 465     TYR A   959                                                      
REMARK 465     ILE A   960                                                      
REMARK 465     PHE A   961                                                      
REMARK 465     CYS A   962                                                      
REMARK 465     LEU A   963                                                      
REMARK 465     VAL A   964                                                      
REMARK 465     PHE A   965                                                      
REMARK 465     ALA A   966                                                      
REMARK 465     ASP A   967                                                      
REMARK 465     TYR A   968                                                      
REMARK 465     LYS A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     ASP A   971                                                      
REMARK 465     ASP A   972                                                      
REMARK 465     ASP A   973                                                      
REMARK 465     ALA A   974                                                      
REMARK 465     LYS A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLN A   977                                                      
REMARK 465     THR A   978                                                      
REMARK 465     MET A   979                                                      
REMARK 465     HIS A   980                                                      
REMARK 465     HIS A   981                                                      
REMARK 465     HIS A   982                                                      
REMARK 465     HIS A   983                                                      
REMARK 465     HIS A   984                                                      
REMARK 465     HIS A   985                                                      
REMARK 465     HIS A   986                                                      
REMARK 465     HIS A   987                                                      
REMARK 465     HIS A   988                                                      
REMARK 465     HIS A   989                                                      
REMARK 465     GLU A   990                                                      
REMARK 465     ASN A   991                                                      
REMARK 465     LEU A   992                                                      
REMARK 465     TYR A   993                                                      
REMARK 465     PHE A   994                                                      
REMARK 465     GLN A   995                                                      
REMARK 465     GLY A   996                                                      
REMARK 465     GLY A   997                                                      
REMARK 465     THR A   998                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     CYS A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     LYS A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     CYS A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     MET B   951                                                      
REMARK 465     LYS B   952                                                      
REMARK 465     THR B   953                                                      
REMARK 465     ILE B   954                                                      
REMARK 465     ILE B   955                                                      
REMARK 465     ALA B   956                                                      
REMARK 465     LEU B   957                                                      
REMARK 465     SER B   958                                                      
REMARK 465     TYR B   959                                                      
REMARK 465     ILE B   960                                                      
REMARK 465     PHE B   961                                                      
REMARK 465     CYS B   962                                                      
REMARK 465     LEU B   963                                                      
REMARK 465     VAL B   964                                                      
REMARK 465     PHE B   965                                                      
REMARK 465     ALA B   966                                                      
REMARK 465     ASP B   967                                                      
REMARK 465     TYR B   968                                                      
REMARK 465     LYS B   969                                                      
REMARK 465     ASP B   970                                                      
REMARK 465     ASP B   971                                                      
REMARK 465     ASP B   972                                                      
REMARK 465     ASP B   973                                                      
REMARK 465     ALA B   974                                                      
REMARK 465     LYS B   975                                                      
REMARK 465     LEU B   976                                                      
REMARK 465     GLN B   977                                                      
REMARK 465     THR B   978                                                      
REMARK 465     MET B   979                                                      
REMARK 465     HIS B   980                                                      
REMARK 465     HIS B   981                                                      
REMARK 465     HIS B   982                                                      
REMARK 465     HIS B   983                                                      
REMARK 465     HIS B   984                                                      
REMARK 465     HIS B   985                                                      
REMARK 465     HIS B   986                                                      
REMARK 465     HIS B   987                                                      
REMARK 465     HIS B   988                                                      
REMARK 465     HIS B   989                                                      
REMARK 465     GLU B   990                                                      
REMARK 465     ASN B   991                                                      
REMARK 465     LEU B   992                                                      
REMARK 465     TYR B   993                                                      
REMARK 465     PHE B   994                                                      
REMARK 465     GLN B   995                                                      
REMARK 465     GLY B   996                                                      
REMARK 465     GLY B   997                                                      
REMARK 465     THR B   998                                                      
REMARK 465     THR B   999                                                      
REMARK 465     MET B  1000                                                      
REMARK 465     ALA B  1001                                                      
REMARK 465     ASP B  1002                                                      
REMARK 465     ILE B  1017                                                      
REMARK 465     GLU B  1018                                                      
REMARK 465     LYS B  1019                                                      
REMARK 465     ALA B  1020                                                      
REMARK 465     ASP B  1021                                                      
REMARK 465     ASN B  1022                                                      
REMARK 465     ALA B  1043                                                      
REMARK 465     THR B  1044                                                      
REMARK 465     PRO B  1045                                                      
REMARK 465     PRO B  1046                                                      
REMARK 465     LYS B  1047                                                      
REMARK 465     LEU B  1048                                                      
REMARK 465     GLU B  1049                                                      
REMARK 465     ASP B  1050                                                      
REMARK 465     LYS B  1051                                                      
REMARK 465     SER B  1052                                                      
REMARK 465     PRO B  1053                                                      
REMARK 465     ASP B  1054                                                      
REMARK 465     SER B  1055                                                      
REMARK 465     PRO B  1056                                                      
REMARK 465     GLU B  1057                                                      
REMARK 465     MET B  1058                                                      
REMARK 465     ALA B  1079                                                      
REMARK 465     ASN B  1080                                                      
REMARK 465     GLU B  1081                                                      
REMARK 465     GLY B  1082                                                      
REMARK 465     LYS B  1083                                                      
REMARK 465     VAL B  1084                                                      
REMARK 465     LYS B  1085                                                      
REMARK 465     GLU B  1086                                                      
REMARK 465     ALA B  1087                                                      
REMARK 465     GLN B  1088                                                      
REMARK 465     ALA B  1089                                                      
REMARK 465     TYR B  1101                                                      
REMARK 465     ILE B  1102                                                      
REMARK 465     GLN B  1103                                                      
REMARK 465     LYS B  1104                                                      
REMARK 465     TYR B  1105                                                      
REMARK 465     LEU B  1106                                                      
REMARK 465     ARG B  1107                                                      
REMARK 465     SER B  1108                                                      
REMARK 465     ALA B  1109                                                      
REMARK 465     LYS B   335                                                      
REMARK 465     PRO B   336                                                      
REMARK 465     CYS B   337                                                      
REMARK 465     GLY B   338                                                      
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     GLU A1008    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1019    CG   CD   CE   NZ                                   
REMARK 470     GLU A1049    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1059    CG   CD   CE   NZ                                   
REMARK 470     LYS A1085    CG   CD   CE   NZ                                   
REMARK 470     ARG A  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     LYS A 155    CG   CD   CE   NZ                                   
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     GLU A 251    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     ARG A 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1004    CG   CD   OE1  OE2                                  
REMARK 470     TRP B1007    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B1007    CZ3  CH2                                            
REMARK 470     GLU B1008    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1012    CG   OD1  OD2                                       
REMARK 470     LYS B1015    CG   CD   CE   NZ                                   
REMARK 470     VAL B1016    CG1  CG2                                            
REMARK 470     GLN B1025    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1027    CG   CD   CE   NZ                                   
REMARK 470     LYS B1032    CG   CD   CE   NZ                                   
REMARK 470     ARG B1034    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1038    CG   CD1  CD2                                       
REMARK 470     GLN B1041    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1042    CG   CD   CE   NZ                                   
REMARK 470     LYS B1059    CG   CD   CE   NZ                                   
REMARK 470     ASP B1060    CG   OD1  OD2                                       
REMARK 470     PHE B1061    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B1062    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B1063    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE B1065    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B1068    CG   CD1  CD2                                       
REMARK 470     GLN B1071    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1077    CG   CD   CE   NZ                                   
REMARK 470     LEU B1078    CG   CD1  CD2                                       
REMARK 470     GLU B1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1093    CG   CD   OE1  NE2                                  
REMARK 470     LEU B1094    CG   CD1  CD2                                       
REMARK 470     LYS B1095    CG   CD   CE   NZ                                   
REMARK 470     ARG B1098    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B1099    CG   OD1  ND2                                       
REMARK 470     SER B  44    N    CA                                             
REMARK 470     LEU B  65    CG   CD1  CD2                                       
REMARK 470     MET B 141    CG   SD   CE                                        
REMARK 470     ARG B 244    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 250    CG   CD   CE   NZ                                   
REMARK 470     ARG B 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 261    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 326    CG   CD   CE   NZ                                   
REMARK 470     ARG B 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 334    CG   CD   NE   CZ   NH1  NH2                        
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    TYR A1101      -45.18   -133.19                                   
REMARK 500    SER A  45       50.71    -91.72                                   
REMARK 500    VAL A  75      -61.67   -106.77                                   
REMARK 500    TYR A  77      -79.85   -116.05                                   
REMARK 500    MET A  80       71.52    -67.66                                   
REMARK 500    GLU A 112      -13.06     62.29                                   
REMARK 500    ARG A 160       40.62    -73.63                                   
REMARK 500    PHE A 222      -70.09   -149.22                                   
REMARK 500    LEU A 286      -72.36    -89.77                                   
REMARK 500    ASP A 290       98.80    -62.35                                   
REMARK 500    CYS A 328       41.42    -75.88                                   
REMARK 500    GLU B1092      -32.49   -153.50                                   
REMARK 500    TYR B  77      -72.77   -116.91                                   
REMARK 500    GLU B 112      -14.12     63.29                                   
REMARK 500    ARG B 160       39.26    -74.11                                   
REMARK 500    ASP B 193       40.71     71.11                                   
REMARK 500    PHE B 222      -64.29   -135.98                                   
REMARK 500    LEU B 286      -71.96    -89.96                                   
REMARK 500    LEU B 313       52.05   -106.09                                   
REMARK 500    CYS B 333       75.45    -68.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OWY A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OWY B 1201                
DBREF  6PT3 A  951   338  PDB    6PT3     6PT3           951    338             
DBREF  6PT3 B  951   338  PDB    6PT3     6PT3           951    338             
SEQRES   1 A  454  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  454  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU          
SEQRES   3 A  454  GLN THR MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   4 A  454  GLU ASN LEU TYR PHE GLN GLY GLY THR THR MET ALA ASP          
SEQRES   5 A  454  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES   6 A  454  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES   7 A  454  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES   8 A  454  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES   9 A  454  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  10 A  454  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  11 A  454  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  12 A  454  LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU          
SEQRES  13 A  454  ARG SER ALA SER SER LEU ALA LEU ALA ILE ALA ILE THR          
SEQRES  14 A  454  ALA LEU TYR SER ALA VAL CYS ALA VAL GLY LEU LEU GLY          
SEQRES  15 A  454  ASN VAL LEU VAL MET PHE VAL ILE VAL ARG TYR THR LYS          
SEQRES  16 A  454  MET LYS THR ALA THR ASN ILE TYR ILE PHE SER LEU ALA          
SEQRES  17 A  454  LEU ALA GLY ALA LEU ALA THR SER THR LEU PRO PHE GLN          
SEQRES  18 A  454  SER ALA ASP TYR LEU MET GLU THR TRP PRO PHE GLY GLU          
SEQRES  19 A  454  LEU LEU CYS LYS ALA VAL LEU SER ILE ASP TYR TYR SER          
SEQRES  20 A  454  MET PHE THR SER ILE PHE THR LEU THR MET MET CYS VAL          
SEQRES  21 A  454  ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU          
SEQRES  22 A  454  ASP PHE ARG THR PRO ALA LYS ALA LYS LEU ILE ASN ILE          
SEQRES  23 A  454  CYS ILE TRP VAL LEU ALA SER GLY VAL GLY VAL PRO ILE          
SEQRES  24 A  454  MET VAL MET ALA VAL THR ARG PRO ARG ASP GLY ALA VAL          
SEQRES  25 A  454  VAL CYS MET LEU GLN PHE PRO SER PRO SER TRP TYR TRP          
SEQRES  26 A  454  ASP THR VAL THR LYS ILE CYS VAL PHE LEU PHE ALA PHE          
SEQRES  27 A  454  VAL VAL PRO ILE LEU ILE ILE THR VAL CYS TYR GLY LEU          
SEQRES  28 A  454  MET LEU LEU ARG LEU ARG SER VAL ARG LEU LEU SER GLY          
SEQRES  29 A  454  SER LYS GLU LYS ASP ARG SER LEU ARG ARG ILE THR ARG          
SEQRES  30 A  454  MET VAL LEU VAL VAL VAL VAL ALA PHE VAL VAL CYS TRP          
SEQRES  31 A  454  ALA PRO ILE HIS ILE PHE VAL ILE VAL TRP THR LEU VAL          
SEQRES  32 A  454  ASP ILE ASP ARG ARG ASP PRO LEU VAL VAL ALA ALA LEU          
SEQRES  33 A  454  HIS LEU CYS ILE ALA LEU GLY TYR ILE ASN SER SER LEU          
SEQRES  34 A  454  ASN PRO VAL LEU TYR ALA PHE LEU ASP LYS ASN PHE LYS          
SEQRES  35 A  454  ARG CYS PHE ARG GLN LEU CYS ARG LYS PRO CYS GLY              
SEQRES   1 B  454  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 B  454  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU          
SEQRES   3 B  454  GLN THR MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   4 B  454  GLU ASN LEU TYR PHE GLN GLY GLY THR THR MET ALA ASP          
SEQRES   5 B  454  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES   6 B  454  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES   7 B  454  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES   8 B  454  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES   9 B  454  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  10 B  454  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  11 B  454  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  12 B  454  LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU          
SEQRES  13 B  454  ARG SER ALA SER SER LEU ALA LEU ALA ILE ALA ILE THR          
SEQRES  14 B  454  ALA LEU TYR SER ALA VAL CYS ALA VAL GLY LEU LEU GLY          
SEQRES  15 B  454  ASN VAL LEU VAL MET PHE VAL ILE VAL ARG TYR THR LYS          
SEQRES  16 B  454  MET LYS THR ALA THR ASN ILE TYR ILE PHE SER LEU ALA          
SEQRES  17 B  454  LEU ALA GLY ALA LEU ALA THR SER THR LEU PRO PHE GLN          
SEQRES  18 B  454  SER ALA ASP TYR LEU MET GLU THR TRP PRO PHE GLY GLU          
SEQRES  19 B  454  LEU LEU CYS LYS ALA VAL LEU SER ILE ASP TYR TYR SER          
SEQRES  20 B  454  MET PHE THR SER ILE PHE THR LEU THR MET MET CYS VAL          
SEQRES  21 B  454  ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU          
SEQRES  22 B  454  ASP PHE ARG THR PRO ALA LYS ALA LYS LEU ILE ASN ILE          
SEQRES  23 B  454  CYS ILE TRP VAL LEU ALA SER GLY VAL GLY VAL PRO ILE          
SEQRES  24 B  454  MET VAL MET ALA VAL THR ARG PRO ARG ASP GLY ALA VAL          
SEQRES  25 B  454  VAL CYS MET LEU GLN PHE PRO SER PRO SER TRP TYR TRP          
SEQRES  26 B  454  ASP THR VAL THR LYS ILE CYS VAL PHE LEU PHE ALA PHE          
SEQRES  27 B  454  VAL VAL PRO ILE LEU ILE ILE THR VAL CYS TYR GLY LEU          
SEQRES  28 B  454  MET LEU LEU ARG LEU ARG SER VAL ARG LEU LEU SER GLY          
SEQRES  29 B  454  SER LYS GLU LYS ASP ARG SER LEU ARG ARG ILE THR ARG          
SEQRES  30 B  454  MET VAL LEU VAL VAL VAL VAL ALA PHE VAL VAL CYS TRP          
SEQRES  31 B  454  ALA PRO ILE HIS ILE PHE VAL ILE VAL TRP THR LEU VAL          
SEQRES  32 B  454  ASP ILE ASP ARG ARG ASP PRO LEU VAL VAL ALA ALA LEU          
SEQRES  33 B  454  HIS LEU CYS ILE ALA LEU GLY TYR ILE ASN SER SER LEU          
SEQRES  34 B  454  ASN PRO VAL LEU TYR ALA PHE LEU ASP LYS ASN PHE LYS          
SEQRES  35 B  454  ARG CYS PHE ARG GLN LEU CYS ARG LYS PRO CYS GLY              
HET    OWY  A1201      36                                                       
HET    OWY  B1201      36                                                       
HETNAM     OWY 4-[(R)-[(2S,5R)-4-BENZYL-2,5-DIMETHYLPIPERAZIN-1-YL](3-          
HETNAM   2 OWY  HYDROXYPHENYL)METHYL]-N,N-DIETHYLBENZAMIDE                      
FORMUL   3  OWY    2(C31 H39 N3 O2)                                             
HELIX    1 AA1 THR A  999  VAL A 1016  1                                  18    
HELIX    2 AA2 ASN A 1022  LYS A 1042  1                                  21    
HELIX    3 AA3 SER A 1055  GLY A 1082  1                                  28    
HELIX    4 AA4 LYS A 1083  TYR A 1101  1                                  19    
HELIX    5 AA5 SER A   45  TYR A   77  1                                  33    
HELIX    6 AA6 THR A   82  SER A  100  1                                  19    
HELIX    7 AA7 THR A  101  GLU A  112  1                                  12    
HELIX    8 AA8 PHE A  116  HIS A  152  1                                  37    
HELIX    9 AA9 HIS A  152  ARG A  160  1                                   9    
HELIX   10 AB1 THR A  161  ALA A  176  1                                  16    
HELIX   11 AB2 ALA A  176  MET A  186  1                                  11    
HELIX   12 AB3 PRO A  205  ALA A  221  1                                  17    
HELIX   13 AB4 PHE A  222  SER A  247  1                                  26    
HELIX   14 AB5 SER A  249  VAL A  287  1                                  39    
HELIX   15 AB6 ASP A  293  ASP A  322  1                                  30    
HELIX   16 AB7 ASP A  322  CYS A  328  1                                   7    
HELIX   17 AB8 GLU B 1004  LYS B 1015  1                                  12    
HELIX   18 AB9 ALA B 1024  LYS B 1042  1                                  19    
HELIX   19 AC1 ASP B 1060  LEU B 1078  1                                  19    
HELIX   20 AC2 LEU B 1094  ALA B 1100  1                                   7    
HELIX   21 AC3 SER B   45  TYR B   77  1                                  33    
HELIX   22 AC4 THR B   82  SER B  100  1                                  19    
HELIX   23 AC5 THR B  101  GLU B  112  1                                  12    
HELIX   24 AC6 PHE B  116  HIS B  152  1                                  37    
HELIX   25 AC7 HIS B  152  ARG B  160  1                                   9    
HELIX   26 AC8 THR B  161  ALA B  176  1                                  16    
HELIX   27 AC9 ALA B  176  MET B  186  1                                  11    
HELIX   28 AD1 PRO B  205  ALA B  221  1                                  17    
HELIX   29 AD2 PHE B  222  SER B  247  1                                  26    
HELIX   30 AD3 LYS B  250  VAL B  287  1                                  38    
HELIX   31 AD4 ASP B  293  LEU B  313  1                                  21    
HELIX   32 AD5 ASN B  314  PHE B  325  1                                  12    
HELIX   33 AD6 PHE B  325  PHE B  329  1                                   5    
SHEET    1 AA1 2 SER A  42  SER A  44  0                                        
SHEET    2 AA1 2 ARG B 330  LEU B 332 -1  O  GLN B 331   N  ALA A  43           
SHEET    1 AA2 2 ALA A 187  ARG A 192  0                                        
SHEET    2 AA2 2 ALA A 195  LEU A 200 -1  O  MET A 199   N  VAL A 188           
SHEET    1 AA3 2 ALA B 187  ARG B 192  0                                        
SHEET    2 AA3 2 ALA B 195  LEU B 200 -1  O  MET B 199   N  VAL B 188           
SSBOND   1 CYS A  121    CYS A  198                          1555   1555  2.04  
SSBOND   2 CYS B  121    CYS B  198                          1555   1555  2.03  
CISPEP   1 SER A  204    PRO A  205          0         2.42                     
CISPEP   2 SER B  204    PRO B  205          0         2.80                     
SITE     1 AC1 16 ALA A  98  ASP A 128  SER A 131  MET A 132                    
SITE     2 AC1 16 LYS A 214  VAL A 217  TRP A 274  ILE A 277                    
SITE     3 AC1 16 HIS A 278  VAL A 281  TRP A 284  LEU A 300                    
SITE     4 AC1 16 ILE A 304  GLY A 307  TYR A 308  SER A 311                    
SITE     1 AC2 14 ALA B  98  ASP B 128  SER B 131  MET B 132                    
SITE     2 AC2 14 LYS B 214  VAL B 217  TRP B 274  ILE B 277                    
SITE     3 AC2 14 HIS B 278  TRP B 284  LEU B 300  ILE B 304                    
SITE     4 AC2 14 GLY B 307  SER B 311                                          
CRYST1   49.084  142.101  157.491  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020373  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007037  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006350        0.00000                         
ATOM      1  N   THR A 999      -7.454 -38.807 -71.822  1.00151.33           N  
ANISOU    1  N   THR A 999    20164  19409  17923   -609    515  -1867       N  
ATOM      2  CA  THR A 999      -7.508 -38.171 -70.502  1.00150.46           C  
ANISOU    2  CA  THR A 999    20070  19228  17868   -565    536  -1796       C  
ATOM      3  C   THR A 999      -7.371 -36.637 -70.627  1.00153.85           C  
ANISOU    3  C   THR A 999    20482  19704  18269   -496    498  -1707       C  
ATOM      4  O   THR A 999      -7.064 -36.122 -71.708  1.00153.83           O  
ANISOU    4  O   THR A 999    20456  19783  18208   -490    460  -1692       O  
ATOM      5  CB  THR A 999      -6.439 -38.781 -69.540  1.00157.69           C  
ANISOU    5  CB  THR A 999    21077  20012  18827   -543    580  -1800       C  
ATOM      6  OG1 THR A 999      -6.478 -38.117 -68.271  1.00157.15           O  
ANISOU    6  OG1 THR A 999    21029  19879  18800   -501    595  -1733       O  
ATOM      7  CG2 THR A 999      -5.018 -38.741 -70.100  1.00154.45           C  
ANISOU    7  CG2 THR A 999    20695  19615  18375   -500    577  -1797       C  
ATOM      8  N   MET A1000      -7.628 -35.919 -69.514  1.00149.57           N  
ANISOU    8  N   MET A1000    19966  19105  17761   -445    504  -1649       N  
ATOM      9  CA  MET A1000      -7.494 -34.463 -69.391  1.00148.97           C  
ANISOU    9  CA  MET A1000    19924  19023  17657   -374    462  -1566       C  
ATOM     10  C   MET A1000      -5.998 -34.094 -69.394  1.00149.44           C  
ANISOU   10  C   MET A1000    20053  19026  17702   -381    447  -1523       C  
ATOM     11  O   MET A1000      -5.616 -33.039 -69.904  1.00148.73           O  
ANISOU   11  O   MET A1000    19991  18957  17563   -370    395  -1458       O  
ATOM     12  CB  MET A1000      -8.188 -33.989 -68.097  1.00151.70           C  
ANISOU   12  CB  MET A1000    20297  19312  18032   -308    478  -1534       C  
ATOM     13  CG  MET A1000      -8.132 -32.494 -67.860  1.00156.00           C  
ANISOU   13  CG  MET A1000    20917  19817  18539   -218    426  -1458       C  
ATOM     14  SD  MET A1000      -9.054 -31.515 -69.072  1.00161.74           S  
ANISOU   14  SD  MET A1000    21596  20665  19192   -158    362  -1426       S  
ATOM     15  CE  MET A1000      -8.428 -29.913 -68.672  1.00158.54           C  
ANISOU   15  CE  MET A1000    21358  20133  18746    -81    294  -1335       C  
ATOM     16  N   ALA A1001      -5.165 -34.992 -68.822  1.00143.51           N  
ANISOU   16  N   ALA A1001    19329  18212  16985   -404    491  -1554       N  
ATOM     17  CA  ALA A1001      -3.709 -34.886 -68.737  1.00141.45           C  
ANISOU   17  CA  ALA A1001    19105  17932  16707   -413    487  -1517       C  
ATOM     18  C   ALA A1001      -3.112 -34.741 -70.130  1.00140.69           C  
ANISOU   18  C   ALA A1001    18962  17954  16539   -439    460  -1509       C  
ATOM     19  O   ALA A1001      -2.396 -33.777 -70.369  1.00139.87           O  
ANISOU   19  O   ALA A1001    18875  17880  16391   -458    418  -1427       O  
ATOM     20  CB  ALA A1001      -3.137 -36.114 -68.034  1.00142.08           C  
ANISOU   20  CB  ALA A1001    19206  17950  16828   -411    543  -1567       C  
ATOM     21  N   ASP A1002      -3.464 -35.662 -71.058  1.00134.63           N  
ANISOU   21  N   ASP A1002    18143  17257  15752   -451    480  -1589       N  
ATOM     22  CA  ASP A1002      -3.034 -35.668 -72.460  1.00133.69           C  
ANISOU   22  CA  ASP A1002    17974  17268  15552   -464    462  -1598       C  
ATOM     23  C   ASP A1002      -3.361 -34.324 -73.125  1.00133.05           C  
ANISOU   23  C   ASP A1002    17879  17253  15422   -477    399  -1515       C  
ATOM     24  O   ASP A1002      -2.479 -33.726 -73.743  1.00132.79           O  
ANISOU   24  O   ASP A1002    17835  17297  15322   -499    374  -1449       O  
ATOM     25  CB  ASP A1002      -3.711 -36.827 -73.238  1.00136.72           C  
ANISOU   25  CB  ASP A1002    18332  17693  15924   -476    480  -1711       C  
ATOM     26  CG  ASP A1002      -2.999 -38.176 -73.227  1.00149.93           C  
ANISOU   26  CG  ASP A1002    20040  19335  17591   -452    527  -1796       C  
ATOM     27  OD1 ASP A1002      -2.582 -38.623 -72.131  1.00150.56           O  
ANISOU   27  OD1 ASP A1002    20171  19309  17726   -428    561  -1795       O  
ATOM     28  OD2 ASP A1002      -2.928 -38.824 -74.310  1.00156.13           O1-
ANISOU   28  OD2 ASP A1002    20815  20197  18312   -447    527  -1869       O1-
ATOM     29  N   LEU A1003      -4.620 -33.839 -72.954  1.00125.94           N  
ANISOU   29  N   LEU A1003    16979  16328  14545   -460    375  -1510       N  
ATOM     30  CA  LEU A1003      -5.133 -32.566 -73.490  1.00124.06           C  
ANISOU   30  CA  LEU A1003    16748  16129  14259   -443    311  -1435       C  
ATOM     31  C   LEU A1003      -4.360 -31.390 -72.905  1.00124.06           C  
ANISOU   31  C   LEU A1003    16841  16048  14248   -445    271  -1328       C  
ATOM     32  O   LEU A1003      -4.096 -30.423 -73.618  1.00123.36           O  
ANISOU   32  O   LEU A1003    16780  15998  14092   -465    213  -1248       O  
ATOM     33  CB  LEU A1003      -6.652 -32.424 -73.202  1.00123.84           C  
ANISOU   33  CB  LEU A1003    16695  16101  14258   -392    303  -1458       C  
ATOM     34  CG  LEU A1003      -7.319 -31.037 -73.334  1.00127.79           C  
ANISOU   34  CG  LEU A1003    17234  16604  14717   -323    239  -1377       C  
ATOM     35  CD1 LEU A1003      -7.333 -30.537 -74.775  1.00128.35           C  
ANISOU   35  CD1 LEU A1003    17274  16792  14702   -337    186  -1341       C  
ATOM     36  CD2 LEU A1003      -8.713 -31.078 -72.801  1.00129.34           C  
ANISOU   36  CD2 LEU A1003    17385  16819  14938   -252    249  -1404       C  
ATOM     37  N   GLU A1004      -4.003 -31.483 -71.611  1.00118.32           N  
ANISOU   37  N   GLU A1004    16172  15203  13579   -435    295  -1324       N  
ATOM     38  CA  GLU A1004      -3.240 -30.461 -70.904  1.00117.05           C  
ANISOU   38  CA  GLU A1004    16116  14950  13408   -454    250  -1232       C  
ATOM     39  C   GLU A1004      -1.818 -30.394 -71.473  1.00119.30           C  
ANISOU   39  C   GLU A1004    16379  15314  13637   -541    237  -1175       C  
ATOM     40  O   GLU A1004      -1.341 -29.310 -71.810  1.00118.82           O  
ANISOU   40  O   GLU A1004    16375  15254  13516   -597    170  -1076       O  
ATOM     41  CB  GLU A1004      -3.223 -30.764 -69.397  1.00117.68           C  
ANISOU   41  CB  GLU A1004    16249  14906  13556   -423    285  -1256       C  
ATOM     42  CG  GLU A1004      -3.406 -29.540 -68.522  1.00127.29           C  
ANISOU   42  CG  GLU A1004    17603  15995  14767   -388    229  -1192       C  
ATOM     43  CD  GLU A1004      -2.790 -29.639 -67.143  1.00145.40           C  
ANISOU   43  CD  GLU A1004    19967  18180  17098   -394    243  -1186       C  
ATOM     44  OE1 GLU A1004      -3.124 -30.593 -66.402  1.00140.03           O  
ANISOU   44  OE1 GLU A1004    19247  17483  16477   -357    311  -1252       O  
ATOM     45  OE2 GLU A1004      -1.980 -28.748 -66.799  1.00136.70           O1-
ANISOU   45  OE2 GLU A1004    18969  17010  15960   -447    180  -1111       O1-
ATOM     46  N   ASP A1005      -1.177 -31.569 -71.623  1.00115.14           N  
ANISOU   46  N   ASP A1005    15768  14861  13118   -549    298  -1235       N  
ATOM     47  CA  ASP A1005       0.175 -31.744 -72.146  1.00115.06           C  
ANISOU   47  CA  ASP A1005    15701  14972  13045   -602    305  -1194       C  
ATOM     48  C   ASP A1005       0.274 -31.301 -73.609  1.00118.03           C  
ANISOU   48  C   ASP A1005    16025  15495  13327   -641    274  -1151       C  
ATOM     49  O   ASP A1005       1.231 -30.607 -73.946  1.00117.99           O  
ANISOU   49  O   ASP A1005    16012  15569  13250   -720    237  -1048       O  
ATOM     50  CB  ASP A1005       0.629 -33.211 -71.987  1.00117.15           C  
ANISOU   50  CB  ASP A1005    15904  15276  13332   -552    383  -1288       C  
ATOM     51  CG  ASP A1005       0.724 -33.704 -70.542  1.00129.50           C  
ANISOU   51  CG  ASP A1005    17519  16708  14976   -519    415  -1316       C  
ATOM     52  OD1 ASP A1005       1.129 -32.905 -69.660  1.00130.31           O  
ANISOU   52  OD1 ASP A1005    17681  16741  15091   -555    378  -1239       O  
ATOM     53  OD2 ASP A1005       0.410 -34.892 -70.296  1.00134.96           O1-
ANISOU   53  OD2 ASP A1005    18203  17362  15711   -464    472  -1412       O1-
ATOM     54  N   ASN A1006      -0.710 -31.673 -74.465  1.00113.68           N  
ANISOU   54  N   ASN A1006    15436  14990  12768   -600    283  -1222       N  
ATOM     55  CA  ASN A1006      -0.750 -31.290 -75.889  1.00113.57           C  
ANISOU   55  CA  ASN A1006    15373  15120  12658   -627    253  -1188       C  
ATOM     56  C   ASN A1006      -0.939 -29.770 -76.054  1.00116.37           C  
ANISOU   56  C   ASN A1006    15809  15434  12974   -674    167  -1062       C  
ATOM     57  O   ASN A1006      -0.202 -29.141 -76.816  1.00115.95           O  
ANISOU   57  O   ASN A1006    15742  15482  12830   -749    132   -965       O  
ATOM     58  CB  ASN A1006      -1.856 -32.045 -76.641  1.00113.05           C  
ANISOU   58  CB  ASN A1006    15258  15101  12594   -575    272  -1298       C  
ATOM     59  CG  ASN A1006      -1.594 -33.515 -76.847  1.00132.04           C  
ANISOU   59  CG  ASN A1006    17612  17556  15002   -542    339  -1420       C  
ATOM     60  OD1 ASN A1006      -0.533 -33.931 -77.329  1.00124.61           O  
ANISOU   60  OD1 ASN A1006    16626  16726  13994   -538    369  -1421       O  
ATOM     61  ND2 ASN A1006      -2.592 -34.332 -76.544  1.00124.17           N  
ANISOU   61  ND2 ASN A1006    16624  16488  14069   -514    361  -1524       N  
ATOM     62  N   TRP A1007      -1.900 -29.183 -75.308  1.00112.68           N  
ANISOU   62  N   TRP A1007    15433  14816  12564   -626    134  -1059       N  
ATOM     63  CA  TRP A1007      -2.188 -27.746 -75.316  1.00113.29           C  
ANISOU   63  CA  TRP A1007    15631  14810  12605   -638     47   -951       C  
ATOM     64  C   TRP A1007      -0.923 -26.960 -74.923  1.00116.73           C  
ANISOU   64  C   TRP A1007    16146  15202  13003   -752      0   -832       C  
ATOM     65  O   TRP A1007      -0.687 -25.873 -75.457  1.00116.82           O  
ANISOU   65  O   TRP A1007    16239  15208  12939   -821    -77   -718       O  
ATOM     66  CB  TRP A1007      -3.376 -27.425 -74.375  1.00112.08           C  
ANISOU   66  CB  TRP A1007    15560  14508  12518   -531     35   -986       C  
ATOM     67  CG  TRP A1007      -3.848 -25.995 -74.353  1.00114.09           C  
ANISOU   67  CG  TRP A1007    15965  14656  12728   -493    -56   -894       C  
ATOM     68  CD1 TRP A1007      -3.910 -25.178 -73.264  1.00117.14           C  
ANISOU   68  CD1 TRP A1007    16512  14864  13133   -457    -99   -856       C  
ATOM     69  CD2 TRP A1007      -4.374 -25.235 -75.456  1.00115.07           C  
ANISOU   69  CD2 TRP A1007    16114  14835  12772   -469   -118   -835       C  
ATOM     70  NE1 TRP A1007      -4.411 -23.947 -73.622  1.00117.71           N  
ANISOU   70  NE1 TRP A1007    16723  14861  13139   -407   -187   -778       N  
ATOM     71  CE2 TRP A1007      -4.701 -23.954 -74.963  1.00119.75           C  
ANISOU   71  CE2 TRP A1007    16898  15262  13339   -413   -200   -758       C  
ATOM     72  CE3 TRP A1007      -4.585 -25.507 -76.823  1.00116.91           C  
ANISOU   72  CE3 TRP A1007    16238  15238  12944   -484   -116   -839       C  
ATOM     73  CZ2 TRP A1007      -5.234 -22.947 -75.783  1.00120.37           C  
ANISOU   73  CZ2 TRP A1007    17067  15334  13336   -364   -281   -680       C  
ATOM     74  CZ3 TRP A1007      -5.097 -24.505 -77.636  1.00119.49           C  
ANISOU   74  CZ3 TRP A1007    16636  15574  13190   -448   -194   -758       C  
ATOM     75  CH2 TRP A1007      -5.419 -23.244 -77.116  1.00120.85           C  
ANISOU   75  CH2 TRP A1007    17003  15573  13341   -386   -275   -677       C  
ATOM     76  N   GLU A1008      -0.087 -27.550 -74.032  1.00111.96           N  
ANISOU   76  N   GLU A1008    15516  14579  12442   -783     43   -855       N  
ATOM     77  CA  GLU A1008       1.180 -26.973 -73.589  1.00111.42           C  
ANISOU   77  CA  GLU A1008    15494  14504  12336   -906      2   -749       C  
ATOM     78  C   GLU A1008       2.203 -27.004 -74.739  1.00115.56           C  
ANISOU   78  C   GLU A1008    15906  15246  12757  -1009      3   -674       C  
ATOM     79  O   GLU A1008       2.722 -25.944 -75.078  1.00115.74           O  
ANISOU   79  O   GLU A1008    15995  15279  12703  -1134    -75   -540       O  
ATOM     80  CB  GLU A1008       1.717 -27.697 -72.344  1.00111.70           C  
ANISOU   80  CB  GLU A1008    15512  14489  12442   -891     51   -800       C  
ATOM     81  N   THR A1009       2.452 -28.202 -75.367  1.00111.54           N  
ANISOU   81  N   THR A1009    15238  14908  12234   -955     88   -757       N  
ATOM     82  CA  THR A1009       3.405 -28.389 -76.490  1.00111.71           C  
ANISOU   82  CA  THR A1009    15130  15172  12142  -1017    108   -703       C  
ATOM     83  C   THR A1009       3.103 -27.496 -77.659  1.00117.36           C  
ANISOU   83  C   THR A1009    15870  15954  12768  -1077     48   -615       C  
ATOM     84  O   THR A1009       4.023 -26.999 -78.314  1.00118.63           O  
ANISOU   84  O   THR A1009    15982  16273  12821  -1195     22   -494       O  
ATOM     85  CB  THR A1009       3.446 -29.812 -77.031  1.00111.70           C  
ANISOU   85  CB  THR A1009    14998  15311  12134   -905    203   -834       C  
ATOM     86  OG1 THR A1009       2.730 -30.701 -76.186  1.00110.17           O  
ANISOU   86  OG1 THR A1009    14836  14970  12052   -798    249   -966       O  
ATOM     87  CG2 THR A1009       4.860 -30.287 -77.264  1.00109.11           C  
ANISOU   87  CG2 THR A1009    14539  15197  11719   -930    247   -794       C  
ATOM     88  N   LEU A1010       1.809 -27.321 -77.939  1.00113.18           N  
ANISOU   88  N   LEU A1010    15405  15323  12273   -996     28   -670       N  
ATOM     89  CA  LEU A1010       1.334 -26.460 -78.997  1.00113.52           C  
ANISOU   89  CA  LEU A1010    15490  15405  12236  -1027    -35   -592       C  
ATOM     90  C   LEU A1010       1.847 -25.033 -78.731  1.00119.47           C  
ANISOU   90  C   LEU A1010    16389  16062  12943  -1165   -136   -422       C  
ATOM     91  O   LEU A1010       2.665 -24.539 -79.509  1.00119.91           O  
ANISOU   91  O   LEU A1010    16413  16260  12888  -1294   -167   -298       O  
ATOM     92  CB  LEU A1010      -0.201 -26.526 -79.049  1.00112.60           C  
ANISOU   92  CB  LEU A1010    15420  15184  12179   -897    -43   -684       C  
ATOM     93  CG  LEU A1010      -0.850 -25.926 -80.269  1.00117.21           C  
ANISOU   93  CG  LEU A1010    16015  15842  12678   -886    -95   -635       C  
ATOM     94  CD1 LEU A1010      -1.296 -26.989 -81.192  1.00116.85           C  
ANISOU   94  CD1 LEU A1010    15830  15960  12608   -819    -35   -751       C  
ATOM     95  CD2 LEU A1010      -2.017 -25.058 -79.881  1.00119.73           C  
ANISOU   95  CD2 LEU A1010    16473  15985  13033   -804   -162   -617       C  
ATOM     96  N   ASN A1011       1.470 -24.440 -77.570  1.00116.73           N  
ANISOU   96  N   ASN A1011    16202  15481  12670  -1148   -185   -416       N  
ATOM     97  CA  ASN A1011       1.833 -23.073 -77.165  1.00117.80           C  
ANISOU   97  CA  ASN A1011    16529  15464  12765  -1271   -296   -272       C  
ATOM     98  C   ASN A1011       3.341 -22.921 -76.874  1.00121.83           C  
ANISOU   98  C   ASN A1011    17001  16064  13223  -1462   -313   -165       C  
ATOM     99  O   ASN A1011       3.863 -21.811 -77.000  1.00122.73           O  
ANISOU   99  O   ASN A1011    17242  16130  13259  -1626   -412    -14       O  
ATOM    100  CB  ASN A1011       0.993 -22.625 -75.965  1.00119.10           C  
ANISOU  100  CB  ASN A1011    16874  15363  13015  -1168   -334   -321       C  
ATOM    101  CG  ASN A1011      -0.508 -22.663 -76.217  1.00141.74           C  
ANISOU  101  CG  ASN A1011    19766  18170  15917   -979   -325   -407       C  
ATOM    102  OD1 ASN A1011      -1.015 -22.256 -77.279  1.00132.06           O  
ANISOU  102  OD1 ASN A1011    18546  17005  14626   -955   -359   -366       O  
ATOM    103  ND2 ASN A1011      -1.255 -23.145 -75.233  1.00134.33           N  
ANISOU  103  ND2 ASN A1011    18836  17130  15075   -844   -280   -520       N  
ATOM    104  N   ASP A1012       4.039 -24.032 -76.545  1.00117.23           N  
ANISOU  104  N   ASP A1012    16246  15625  12671  -1445   -221   -236       N  
ATOM    105  CA  ASP A1012       5.484 -24.045 -76.300  1.00117.52           C  
ANISOU  105  CA  ASP A1012    16197  15808  12649  -1604   -224   -140       C  
ATOM    106  C   ASP A1012       6.223 -23.930 -77.615  1.00121.27           C  
ANISOU  106  C   ASP A1012    16537  16553  12987  -1714   -220    -33       C  
ATOM    107  O   ASP A1012       7.122 -23.100 -77.731  1.00121.76           O  
ANISOU  107  O   ASP A1012    16623  16684  12958  -1919   -291    130       O  
ATOM    108  CB  ASP A1012       5.928 -25.311 -75.543  1.00118.71           C  
ANISOU  108  CB  ASP A1012    16207  16030  12867  -1509   -126   -254       C  
ATOM    109  CG  ASP A1012       5.720 -25.274 -74.037  1.00133.65           C  
ANISOU  109  CG  ASP A1012    18221  17697  14863  -1475   -144   -305       C  
ATOM    110  OD1 ASP A1012       5.738 -24.156 -73.453  1.00135.20           O  
ANISOU  110  OD1 ASP A1012    18600  17719  15051  -1583   -246   -217       O  
ATOM    111  OD2 ASP A1012       5.592 -26.361 -73.431  1.00140.94           O1-
ANISOU  111  OD2 ASP A1012    19069  18616  15864  -1345    -61   -428       O1-
ATOM    112  N   ASN A1013       5.810 -24.731 -78.621  1.00117.46           N  
ANISOU  112  N   ASN A1013    15921  16226  12482  -1589   -141   -121       N  
ATOM    113  CA  ASN A1013       6.397 -24.737 -79.963  1.00118.63           C  
ANISOU  113  CA  ASN A1013    15932  16654  12490  -1657   -122    -39       C  
ATOM    114  C   ASN A1013       5.999 -23.489 -80.763  1.00125.25           C  
ANISOU  114  C   ASN A1013    16903  17437  13250  -1767   -221     96       C  
ATOM    115  O   ASN A1013       6.517 -23.289 -81.860  1.00125.74           O  
ANISOU  115  O   ASN A1013    16870  17725  13180  -1857   -220    197       O  
ATOM    116  CB  ASN A1013       5.999 -26.003 -80.728  1.00115.54           C  
ANISOU  116  CB  ASN A1013    15391  16414  12096  -1473    -15   -195       C  
ATOM    117  CG  ASN A1013       6.816 -27.226 -80.388  1.00121.53           C  
ANISOU  117  CG  ASN A1013    15987  17330  12857  -1390     85   -282       C  
ATOM    118  OD1 ASN A1013       7.955 -27.394 -80.846  1.00119.91           O  
ANISOU  118  OD1 ASN A1013    15631  17393  12536  -1449    118   -206       O  
ATOM    119  ND2 ASN A1013       6.237 -28.126 -79.612  1.00101.32           N  
ANISOU  119  ND2 ASN A1013    13453  14622  10421  -1241    135   -441       N  
ATOM    120  N   LEU A1014       5.094 -22.654 -80.207  1.00123.39           N  
ANISOU  120  N   LEU A1014    16890  16908  13084  -1749   -306    102       N  
ATOM    121  CA  LEU A1014       4.586 -21.420 -80.813  1.00125.03           C  
ANISOU  121  CA  LEU A1014    17276  17003  13226  -1820   -413    223       C  
ATOM    122  C   LEU A1014       5.558 -20.262 -80.583  1.00133.94           C  
ANISOU  122  C   LEU A1014    18531  18089  14272  -2077   -521    424       C  
ATOM    123  O   LEU A1014       5.671 -19.385 -81.437  1.00134.93           O  
ANISOU  123  O   LEU A1014    18734  18247  14286  -2205   -596    572       O  
ATOM    124  CB  LEU A1014       3.181 -21.101 -80.249  1.00123.82           C  
ANISOU  124  CB  LEU A1014    17308  16562  13175  -1650   -451    130       C  
ATOM    125  CG  LEU A1014       2.243 -20.159 -81.019  1.00128.67           C  
ANISOU  125  CG  LEU A1014    18079  17076  13735  -1606   -535    195       C  
ATOM    126  CD1 LEU A1014       2.311 -20.359 -82.532  1.00129.53           C  
ANISOU  126  CD1 LEU A1014    18046  17438  13731  -1627   -508    238       C  
ATOM    127  CD2 LEU A1014       0.825 -20.333 -80.547  1.00129.02           C  
ANISOU  127  CD2 LEU A1014    18195  16948  13879  -1377   -524     57       C  
ATOM    128  N   LYS A1015       6.277 -20.278 -79.452  1.00133.30           N  
ANISOU  128  N   LYS A1015    18470  17944  14235  -2166   -534    435       N  
ATOM    129  CA  LYS A1015       7.270 -19.256 -79.138  1.00136.24           C  
ANISOU  129  CA  LYS A1015    18954  18285  14525  -2439   -644    622       C  
ATOM    130  C   LYS A1015       8.652 -19.690 -79.663  1.00143.75           C  
ANISOU  130  C   LYS A1015    19644  19608  15365  -2605   -592    722       C  
ATOM    131  O   LYS A1015       9.535 -18.850 -79.816  1.00145.41           O  
ANISOU  131  O   LYS A1015    19894  19890  15466  -2871   -679    912       O  
ATOM    132  CB  LYS A1015       7.297 -18.960 -77.623  1.00138.64           C  
ANISOU  132  CB  LYS A1015    19430  18326  14920  -2458   -701    585       C  
ATOM    133  CG  LYS A1015       7.697 -17.521 -77.264  1.00156.67           C  
ANISOU  133  CG  LYS A1015    21989  20405  17133  -2703   -868    758       C  
ATOM    134  CD  LYS A1015       6.672 -16.458 -77.709  1.00167.17           C  
ANISOU  134  CD  LYS A1015    23605  21474  18438  -2653   -969    801       C  
ATOM    135  CE  LYS A1015       7.278 -15.074 -77.764  1.00177.33           C  
ANISOU  135  CE  LYS A1015    25144  22623  19609  -2944  -1136   1009       C  
ATOM    136  NZ  LYS A1015       6.486 -14.146 -78.616  1.00183.78           N  
ANISOU  136  NZ  LYS A1015    26183  23283  20362  -2910  -1221   1087       N  
ATOM    137  N   VAL A1016       8.823 -20.995 -79.971  1.00141.14           N  
ANISOU  137  N   VAL A1016    19053  19523  15050  -2444   -453    599       N  
ATOM    138  CA  VAL A1016      10.061 -21.576 -80.519  1.00142.86           C  
ANISOU  138  CA  VAL A1016    18997  20131  15153  -2528   -380    667       C  
ATOM    139  C   VAL A1016      10.241 -21.056 -81.965  1.00150.23           C  
ANISOU  139  C   VAL A1016    19877  21274  15929  -2643   -399    809       C  
ATOM    140  O   VAL A1016      11.373 -20.935 -82.430  1.00151.43           O  
ANISOU  140  O   VAL A1016    19865  21729  15942  -2819   -393    956       O  
ATOM    141  CB  VAL A1016      10.056 -23.138 -80.406  1.00145.44           C  
ANISOU  141  CB  VAL A1016    19113  20608  15541  -2278   -231    473       C  
ATOM    142  CG1 VAL A1016      11.024 -23.818 -81.381  1.00146.47           C  
ANISOU  142  CG1 VAL A1016    18966  21161  15527  -2274   -139    512       C  
ATOM    143  CG2 VAL A1016      10.330 -23.589 -78.973  1.00144.10           C  
ANISOU  143  CG2 VAL A1016    18955  20315  15482  -2234   -218    394       C  
ATOM    144  N   ILE A1017       9.121 -20.682 -82.625  1.00147.94           N  
ANISOU  144  N   ILE A1017    19730  20827  15654  -2551   -430    777       N  
ATOM    145  CA  ILE A1017       9.092 -20.103 -83.973  1.00149.98           C  
ANISOU  145  CA  ILE A1017    19982  21233  15771  -2643   -461    908       C  
ATOM    146  C   ILE A1017       9.671 -18.663 -83.894  1.00159.10           C  
ANISOU  146  C   ILE A1017    21318  22298  16834  -2958   -608   1151       C  
ATOM    147  O   ILE A1017      10.388 -18.236 -84.805  1.00160.68           O  
ANISOU  147  O   ILE A1017    21433  22744  16875  -3149   -627   1327       O  
ATOM    148  CB  ILE A1017       7.652 -20.164 -84.576  1.00151.60           C  
ANISOU  148  CB  ILE A1017    20294  21281  16028  -2432   -457    791       C  
ATOM    149  CG1 ILE A1017       7.175 -21.629 -84.714  1.00149.56           C  
ANISOU  149  CG1 ILE A1017    19853  21133  15839  -2166   -321    562       C  
ATOM    150  CG2 ILE A1017       7.562 -19.425 -85.930  1.00154.02           C  
ANISOU  150  CG2 ILE A1017    20631  21708  16183  -2532   -508    942       C  
ATOM    151  CD1 ILE A1017       5.673 -21.831 -84.706  1.00151.94           C  
ANISOU  151  CD1 ILE A1017    20269  21212  16249  -1952   -323    407       C  
ATOM    152  N   GLU A1018       9.396 -17.946 -82.785  1.00157.56           N  
ANISOU  152  N   GLU A1018    21377  21757  16730  -3018   -712   1160       N  
ATOM    153  CA  GLU A1018       9.917 -16.591 -82.545  1.00160.39           C  
ANISOU  153  CA  GLU A1018    21961  21971  17011  -3323   -869   1373       C  
ATOM    154  C   GLU A1018      11.431 -16.679 -82.296  1.00166.19           C  
ANISOU  154  C   GLU A1018    22501  22992  17651  -3582   -864   1509       C  
ATOM    155  O   GLU A1018      12.211 -15.951 -82.918  1.00167.47           O  
ANISOU  155  O   GLU A1018    22651  23320  17661  -3865   -933   1727       O  
ATOM    156  CB  GLU A1018       9.192 -15.915 -81.355  1.00161.50           C  
ANISOU  156  CB  GLU A1018    22433  21661  17270  -3277   -974   1315       C  
ATOM    157  CG  GLU A1018       7.677 -16.092 -81.335  1.00174.16           C  
ANISOU  157  CG  GLU A1018    24166  23021  18985  -2962   -950   1141       C  
ATOM    158  CD  GLU A1018       6.898 -15.236 -82.315  1.00204.27           C  
ANISOU  158  CD  GLU A1018    28165  26723  22726  -2942  -1028   1226       C  
ATOM    159  OE1 GLU A1018       6.731 -15.662 -83.482  1.00202.14           O1-
ANISOU  159  OE1 GLU A1018    27721  26691  22392  -2875   -958   1226       O1-
ATOM    160  OE2 GLU A1018       6.437 -14.145 -81.907  1.00201.68           O  
ANISOU  160  OE2 GLU A1018    28168  26063  22398  -2977  -1161   1289       O  
ATOM    161  N   LYS A1019      11.828 -17.648 -81.439  1.00162.57           N  
ANISOU  161  N   LYS A1019    21867  22625  17276  -3472   -775   1379       N  
ATOM    162  CA  LYS A1019      13.200 -17.982 -81.039  1.00163.58           C  
ANISOU  162  CA  LYS A1019    21767  23051  17336  -3643   -749   1464       C  
ATOM    163  C   LYS A1019      13.990 -18.670 -82.173  1.00168.43           C  
ANISOU  163  C   LYS A1019    22034  24156  17805  -3641   -633   1522       C  
ATOM    164  O   LYS A1019      15.209 -18.828 -82.062  1.00169.37           O  
ANISOU  164  O   LYS A1019    21937  24594  17823  -3803   -615   1635       O  
ATOM    165  CB  LYS A1019      13.173 -18.888 -79.793  1.00164.25           C  
ANISOU  165  CB  LYS A1019    21794  23050  17564  -3457   -682   1281       C  
ATOM    166  N   ALA A1020      13.299 -19.080 -83.251  1.00164.36           N  
ANISOU  166  N   ALA A1020    21463  23717  17268  -3450   -556   1445       N  
ATOM    167  CA  ALA A1020      13.923 -19.711 -84.409  1.00165.09           C  
ANISOU  167  CA  ALA A1020    21257  24259  17211  -3415   -446   1485       C  
ATOM    168  C   ALA A1020      14.687 -18.677 -85.213  1.00172.11           C  
ANISOU  168  C   ALA A1020    22129  25357  17908  -3749   -528   1761       C  
ATOM    169  O   ALA A1020      14.253 -17.524 -85.308  1.00172.58           O  
ANISOU  169  O   ALA A1020    22461  25153  17960  -3926   -662   1882       O  
ATOM    170  CB  ALA A1020      12.873 -20.378 -85.273  1.00164.47           C  
ANISOU  170  CB  ALA A1020    21167  24159  17166  -3128   -360   1315       C  
ATOM    171  N   ASP A1021      15.836 -19.090 -85.776  1.00170.40           N  
ANISOU  171  N   ASP A1021    21597  25620  17528  -3831   -449   1865       N  
ATOM    172  CA  ASP A1021      16.725 -18.230 -86.564  1.00173.01           C  
ANISOU  172  CA  ASP A1021    21847  26241  17650  -4167   -509   2146       C  
ATOM    173  C   ASP A1021      16.957 -18.805 -87.987  1.00176.32           C  
ANISOU  173  C   ASP A1021    22002  27091  17900  -4051   -384   2162       C  
ATOM    174  O   ASP A1021      17.437 -18.092 -88.869  1.00177.89           O  
ANISOU  174  O   ASP A1021    22155  27517  17919  -4294   -425   2386       O  
ATOM    175  CB  ASP A1021      18.065 -18.034 -85.815  1.00176.70           C  
ANISOU  175  CB  ASP A1021    22157  26940  18042  -4436   -548   2303       C  
ATOM    176  CG  ASP A1021      17.928 -17.567 -84.366  1.00185.77           C  
ANISOU  176  CG  ASP A1021    23547  27694  19342  -4541   -666   2273       C  
ATOM    177  OD1 ASP A1021      17.480 -16.417 -84.149  1.00186.70           O1-
ANISOU  177  OD1 ASP A1021    23996  27454  19489  -4747   -820   2372       O1-
ATOM    178  OD2 ASP A1021      18.294 -18.342 -83.453  1.00190.33           O  
ANISOU  178  OD2 ASP A1021    23994  28324  19999  -4411   -606   2154       O  
ATOM    179  N   ASN A1022      16.590 -20.083 -88.198  1.00170.52           N  
ANISOU  179  N   ASN A1022    21117  26454  17217  -3684   -238   1926       N  
ATOM    180  CA  ASN A1022      16.708 -20.818 -89.461  1.00170.65           C  
ANISOU  180  CA  ASN A1022    20905  26848  17086  -3503   -110   1883       C  
ATOM    181  C   ASN A1022      15.528 -21.790 -89.623  1.00171.90           C  
ANISOU  181  C   ASN A1022    21139  26797  17379  -3124    -29   1592       C  
ATOM    182  O   ASN A1022      14.980 -22.255 -88.623  1.00169.44           O  
ANISOU  182  O   ASN A1022    20939  26181  17258  -2968    -28   1414       O  
ATOM    183  CB  ASN A1022      18.048 -21.563 -89.538  1.00172.23           C  
ANISOU  183  CB  ASN A1022    20739  27566  17134  -3478      4   1929       C  
ATOM    184  CG  ASN A1022      18.411 -22.360 -88.304  1.00190.35           C  
ANISOU  184  CG  ASN A1022    22959  29813  19553  -3334     48   1790       C  
ATOM    185  OD1 ASN A1022      17.795 -23.383 -87.985  1.00179.96           O  
ANISOU  185  OD1 ASN A1022    21670  28338  18368  -3009    127   1538       O  
ATOM    186  ND2 ASN A1022      19.448 -21.922 -87.599  1.00183.20           N  
ANISOU  186  ND2 ASN A1022    21951  29061  18597  -3584     -6   1960       N  
ATOM    187  N   ALA A1023      15.171 -22.120 -90.883  1.00168.94           N  
ANISOU  187  N   ALA A1023    20692  26604  16891  -2987     36   1551       N  
ATOM    188  CA  ALA A1023      14.055 -22.991 -91.286  1.00166.95           C  
ANISOU  188  CA  ALA A1023    20503  26204  16725  -2665    102   1297       C  
ATOM    189  C   ALA A1023      14.061 -24.367 -90.589  1.00169.12           C  
ANISOU  189  C   ALA A1023    20685  26463  17111  -2374    209   1049       C  
ATOM    190  O   ALA A1023      12.990 -24.955 -90.419  1.00166.96           O  
ANISOU  190  O   ALA A1023    20541  25916  16979  -2161    224    836       O  
ATOM    191  CB  ALA A1023      14.059 -23.179 -92.795  1.00169.03           C  
ANISOU  191  CB  ALA A1023    20641  26789  16793  -2598    164   1323       C  
ATOM    192  N   ALA A1024      15.254 -24.863 -90.179  1.00165.86           N  
ANISOU  192  N   ALA A1024    20051  26344  16625  -2371    277   1086       N  
ATOM    193  CA  ALA A1024      15.438 -26.142 -89.481  1.00163.87           C  
ANISOU  193  CA  ALA A1024    19708  26100  16454  -2103    375    878       C  
ATOM    194  C   ALA A1024      14.671 -26.156 -88.157  1.00163.94           C  
ANISOU  194  C   ALA A1024    19936  25641  16713  -2072    314    757       C  
ATOM    195  O   ALA A1024      14.023 -27.154 -87.830  1.00161.80           O  
ANISOU  195  O   ALA A1024    19721  25194  16561  -1817    370    528       O  
ATOM    196  CB  ALA A1024      16.921 -26.392 -89.233  1.00166.30           C  
ANISOU  196  CB  ALA A1024    19745  26819  16622  -2151    434    995       C  
ATOM    197  N   GLN A1025      14.727 -25.031 -87.421  1.00159.47           N  
ANISOU  197  N   GLN A1025    19506  24870  16214  -2339    194    913       N  
ATOM    198  CA  GLN A1025      14.037 -24.836 -86.148  1.00156.74           C  
ANISOU  198  CA  GLN A1025    19380  24088  16085  -2340    123    829       C  
ATOM    199  C   GLN A1025      12.546 -24.566 -86.385  1.00156.01           C  
ANISOU  199  C   GLN A1025    19529  23638  16111  -2257     73    723       C  
ATOM    200  O   GLN A1025      11.715 -25.086 -85.635  1.00154.08           O  
ANISOU  200  O   GLN A1025    19403  23104  16037  -2090     83    543       O  
ATOM    201  CB  GLN A1025      14.655 -23.660 -85.360  1.00159.28           C  
ANISOU  201  CB  GLN A1025    19783  24330  16408  -2661      1   1040       C  
ATOM    202  CG  GLN A1025      16.142 -23.749 -85.021  1.00177.49           C  
ANISOU  202  CG  GLN A1025    21848  26995  18593  -2799     25   1178       C  
ATOM    203  CD  GLN A1025      16.653 -22.447 -84.432  1.00197.48           C  
ANISOU  203  CD  GLN A1025    24492  29437  21105  -3168   -120   1404       C  
ATOM    204  OE1 GLN A1025      17.514 -21.759 -85.003  1.00192.16           O  
ANISOU  204  OE1 GLN A1025    24037  28396  20578  -3232   -210   1374       O  
ATOM    205  NE2 GLN A1025      16.125 -22.073 -83.277  1.00190.26           N  
ANISOU  205  NE2 GLN A1025    23434  28860  19996  -3426   -150   1638       N  
ATOM    206  N   VAL A1026      12.217 -23.748 -87.426  1.00150.30           N  
ANISOU  206  N   VAL A1026    18868  22953  15286  -2374     18    844       N  
ATOM    207  CA  VAL A1026      10.849 -23.340 -87.785  1.00147.96           C  
ANISOU  207  CA  VAL A1026    18786  22364  15068  -2310    -41    780       C  
ATOM    208  C   VAL A1026       9.993 -24.552 -88.208  1.00150.03           C  
ANISOU  208  C   VAL A1026    19005  22618  15384  -2010     54    534       C  
ATOM    209  O   VAL A1026       8.849 -24.657 -87.762  1.00147.99           O  
ANISOU  209  O   VAL A1026    18905  22050  15276  -1894     26    400       O  
ATOM    210  CB  VAL A1026      10.798 -22.230 -88.869  1.00152.88           C  
ANISOU  210  CB  VAL A1026    19474  23066  15547  -2497   -119    980       C  
ATOM    211  CG1 VAL A1026       9.427 -21.562 -88.907  1.00151.62           C  
ANISOU  211  CG1 VAL A1026    19577  22545  15486  -2454   -212    946       C  
ATOM    212  CG2 VAL A1026      11.880 -21.180 -88.655  1.00154.53           C  
ANISOU  212  CG2 VAL A1026    19683  23377  15654  -2824   -202   1241       C  
ATOM    213  N   LYS A1027      10.539 -25.453 -89.063  1.00146.90           N  
ANISOU  213  N   LYS A1027    18400  22564  14853  -1888    161    476       N  
ATOM    214  CA  LYS A1027       9.837 -26.649 -89.557  1.00145.02           C  
ANISOU  214  CA  LYS A1027    18129  22337  14635  -1620    245    244       C  
ATOM    215  C   LYS A1027       9.572 -27.655 -88.427  1.00145.20           C  
ANISOU  215  C   LYS A1027    18185  22157  14829  -1449    292     46       C  
ATOM    216  O   LYS A1027       8.482 -28.225 -88.367  1.00143.01           O  
ANISOU  216  O   LYS A1027    18007  21671  14658  -1299    298   -131       O  
ATOM    217  CB  LYS A1027      10.624 -27.325 -90.689  1.00148.64           C  
ANISOU  217  CB  LYS A1027    18374  23215  14886  -1530    344    238       C  
ATOM    218  CG  LYS A1027       9.724 -27.961 -91.744  1.00158.32           C  
ANISOU  218  CG  LYS A1027    19625  24464  16066  -1350    377     78       C  
ATOM    219  CD  LYS A1027      10.441 -28.985 -92.621  1.00167.75           C  
ANISOU  219  CD  LYS A1027    20634  26026  17078  -1177    492     -6       C  
ATOM    220  CE  LYS A1027      11.324 -28.366 -93.681  1.00180.59           C  
ANISOU  220  CE  LYS A1027    22104  28044  18468  -1304    507    196       C  
ATOM    221  NZ  LYS A1027      11.560 -29.300 -94.813  1.00189.65           N1+
ANISOU  221  NZ  LYS A1027    23126  29505  19430  -1098    606     80       N1+
ATOM    222  N   ASP A1028      10.562 -27.847 -87.534  1.00141.08           N  
ANISOU  222  N   ASP A1028    17577  21704  14324  -1483    319     87       N  
ATOM    223  CA  ASP A1028      10.523 -28.747 -86.380  1.00139.49           C  
ANISOU  223  CA  ASP A1028    17397  21336  14266  -1340    362    -67       C  
ATOM    224  C   ASP A1028       9.380 -28.372 -85.403  1.00139.57           C  
ANISOU  224  C   ASP A1028    17626  20923  14482  -1359    287   -129       C  
ATOM    225  O   ASP A1028       8.664 -29.264 -84.932  1.00137.75           O  
ANISOU  225  O   ASP A1028    17456  20512  14371  -1189    325   -316       O  
ATOM    226  CB  ASP A1028      11.891 -28.713 -85.666  1.00142.89           C  
ANISOU  226  CB  ASP A1028    17687  21956  14648  -1423    382     47       C  
ATOM    227  CG  ASP A1028      11.950 -29.431 -84.328  1.00157.21           C  
ANISOU  227  CG  ASP A1028    19536  23587  16609  -1313    407    -70       C  
ATOM    228  OD1 ASP A1028      12.075 -30.679 -84.326  1.00157.96           O  
ANISOU  228  OD1 ASP A1028    19564  23752  16700  -1084    499   -231       O  
ATOM    229  OD2 ASP A1028      11.906 -28.740 -83.281  1.00164.51           O1-
ANISOU  229  OD2 ASP A1028    20567  24298  17642  -1454    332      2       O1-
ATOM    230  N   ALA A1029       9.215 -27.061 -85.114  1.00134.34           N  
ANISOU  230  N   ALA A1029    17087  20109  13845  -1561    181     29       N  
ATOM    231  CA  ALA A1029       8.190 -26.534 -84.206  1.00131.62           C  
ANISOU  231  CA  ALA A1029    16955  19387  13668  -1575    104     -7       C  
ATOM    232  C   ALA A1029       6.786 -26.707 -84.782  1.00131.42           C  
ANISOU  232  C   ALA A1029    17023  19217  13693  -1446     97   -129       C  
ATOM    233  O   ALA A1029       5.875 -27.100 -84.057  1.00129.46           O  
ANISOU  233  O   ALA A1029    16870  18731  13588  -1335     99   -264       O  
ATOM    234  CB  ALA A1029       8.457 -25.065 -83.912  1.00133.24           C  
ANISOU  234  CB  ALA A1029    17286  19489  13851  -1815    -13    199       C  
ATOM    235  N   LEU A1030       6.622 -26.427 -86.085  1.00126.65           N  
ANISOU  235  N   LEU A1030    16383  18778  12962  -1466     87    -77       N  
ATOM    236  CA  LEU A1030       5.349 -26.547 -86.794  1.00124.58           C  
ANISOU  236  CA  LEU A1030    16186  18432  12717  -1357     72   -175       C  
ATOM    237  C   LEU A1030       4.902 -28.008 -86.903  1.00125.09           C  
ANISOU  237  C   LEU A1030    16180  18526  12825  -1156    162   -401       C  
ATOM    238  O   LEU A1030       3.710 -28.277 -86.775  1.00123.44           O  
ANISOU  238  O   LEU A1030    16052  18139  12711  -1064    145   -522       O  
ATOM    239  CB  LEU A1030       5.444 -25.913 -88.187  1.00125.72           C  
ANISOU  239  CB  LEU A1030    16296  18780  12692  -1436     42    -50       C  
ATOM    240  CG  LEU A1030       5.551 -24.393 -88.233  1.00130.33           C  
ANISOU  240  CG  LEU A1030    17009  19279  13233  -1633    -70    171       C  
ATOM    241  CD1 LEU A1030       6.090 -23.935 -89.566  1.00132.13           C  
ANISOU  241  CD1 LEU A1030    17154  19787  13262  -1738    -78    319       C  
ATOM    242  CD2 LEU A1030       4.224 -23.727 -87.926  1.00130.69           C  
ANISOU  242  CD2 LEU A1030    17255  19018  13382  -1586   -158    149       C  
ATOM    243  N   THR A1031       5.853 -28.948 -87.106  1.00120.46           N  
ANISOU  243  N   THR A1031    15449  18160  12161  -1088    251   -457       N  
ATOM    244  CA  THR A1031       5.575 -30.386 -87.202  1.00119.03           C  
ANISOU  244  CA  THR A1031    15229  17995  12002   -897    331   -671       C  
ATOM    245  C   THR A1031       5.016 -30.887 -85.862  1.00119.73           C  
ANISOU  245  C   THR A1031    15412  17799  12281   -836    334   -786       C  
ATOM    246  O   THR A1031       4.019 -31.616 -85.859  1.00118.25           O  
ANISOU  246  O   THR A1031    15283  17481  12166   -735    344   -944       O  
ATOM    247  CB  THR A1031       6.837 -31.163 -87.647  1.00127.18           C  
ANISOU  247  CB  THR A1031    16103  19329  12892   -820    422   -685       C  
ATOM    248  OG1 THR A1031       7.319 -30.619 -88.877  1.00126.67           O  
ANISOU  248  OG1 THR A1031    15943  19545  12642   -889    419   -562       O  
ATOM    249  CG2 THR A1031       6.581 -32.659 -87.823  1.00126.21           C  
ANISOU  249  CG2 THR A1031    15977  19205  12771   -611    496   -911       C  
ATOM    250  N   LYS A1032       5.646 -30.472 -84.734  1.00115.31           N  
ANISOU  250  N   LYS A1032    14868  17152  11792   -913    321   -699       N  
ATOM    251  CA  LYS A1032       5.232 -30.831 -83.371  1.00113.48           C  
ANISOU  251  CA  LYS A1032    14725  16662  11729   -869    322   -783       C  
ATOM    252  C   LYS A1032       3.866 -30.217 -83.054  1.00115.76           C  
ANISOU  252  C   LYS A1032    15154  16700  12129   -890    253   -798       C  
ATOM    253  O   LYS A1032       3.006 -30.905 -82.508  1.00114.20           O  
ANISOU  253  O   LYS A1032    15010  16339  12042   -799    271   -934       O  
ATOM    254  CB  LYS A1032       6.275 -30.380 -82.331  1.00116.00           C  
ANISOU  254  CB  LYS A1032    15028  16975  12073   -964    311   -666       C  
ATOM    255  CG  LYS A1032       7.558 -31.190 -82.305  1.00129.63           C  
ANISOU  255  CG  LYS A1032    16607  18932  13716   -900    390   -675       C  
ATOM    256  CD  LYS A1032       8.442 -30.722 -81.159  1.00138.59           C  
ANISOU  256  CD  LYS A1032    17730  20042  14887  -1004    365   -563       C  
ATOM    257  CE  LYS A1032       9.894 -30.623 -81.542  1.00148.13           C  
ANISOU  257  CE  LYS A1032    18760  21584  15940  -1065    393   -436       C  
ATOM    258  NZ  LYS A1032      10.539 -29.427 -80.936  1.00154.34           N1+
ANISOU  258  NZ  LYS A1032    19560  22367  16716  -1293    310   -243       N1+
ATOM    259  N   MET A1033       3.665 -28.934 -83.427  1.00112.63           N  
ANISOU  259  N   MET A1033    14818  16287  11691  -1006    172   -653       N  
ATOM    260  CA  MET A1033       2.415 -28.189 -83.252  1.00112.02           C  
ANISOU  260  CA  MET A1033    14873  16003  11686  -1005     98   -645       C  
ATOM    261  C   MET A1033       1.251 -28.861 -83.972  1.00115.19           C  
ANISOU  261  C   MET A1033    15255  16417  12093   -892    115   -784       C  
ATOM    262  O   MET A1033       0.164 -28.947 -83.405  1.00114.26           O  
ANISOU  262  O   MET A1033    15205  16127  12081   -830     97   -860       O  
ATOM    263  CB  MET A1033       2.558 -26.766 -83.781  1.00115.75           C  
ANISOU  263  CB  MET A1033    15418  16491  12073  -1135      9   -459       C  
ATOM    264  CG  MET A1033       3.131 -25.818 -82.790  1.00120.45           C  
ANISOU  264  CG  MET A1033    16119  16944  12704  -1259    -52   -329       C  
ATOM    265  SD  MET A1033       2.766 -24.043 -82.996  1.00126.90           S  
ANISOU  265  SD  MET A1033    17137  17608  13471  -1382   -190   -141       S  
ATOM    266  CE  MET A1033       2.105 -23.947 -84.635  1.00124.74           C  
ANISOU  266  CE  MET A1033    16816  17499  13081  -1337   -201   -129       C  
ATOM    267  N   ARG A1034       1.486 -29.337 -85.228  1.00111.40           N  
ANISOU  267  N   ARG A1034    14679  16159  11488   -868    146   -814       N  
ATOM    268  CA  ARG A1034       0.502 -29.998 -86.086  1.00110.08           C  
ANISOU  268  CA  ARG A1034    14489  16042  11295   -782    153   -942       C  
ATOM    269  C   ARG A1034      -0.020 -31.260 -85.420  1.00111.74           C  
ANISOU  269  C   ARG A1034    14704  16138  11613   -687    204  -1127       C  
ATOM    270  O   ARG A1034      -1.231 -31.402 -85.239  1.00111.53           O  
ANISOU  270  O   ARG A1034    14719  15997  11661   -654    176  -1202       O  
ATOM    271  CB  ARG A1034       1.103 -30.327 -87.461  1.00109.71           C  
ANISOU  271  CB  ARG A1034    14343  16266  11077   -773    184   -941       C  
ATOM    272  CG  ARG A1034       0.103 -30.144 -88.595  1.00120.55           C  
ANISOU  272  CG  ARG A1034    15720  17707  12377   -753    137   -965       C  
ATOM    273  CD  ARG A1034       0.444 -30.958 -89.824  1.00128.62           C  
ANISOU  273  CD  ARG A1034    16654  18966  13248   -697    184  -1049       C  
ATOM    274  NE  ARG A1034      -0.320 -32.205 -89.870  1.00134.14           N  
ANISOU  274  NE  ARG A1034    17367  19611  13990   -602    208  -1257       N  
ATOM    275  CZ  ARG A1034      -1.321 -32.446 -90.710  1.00148.33           C  
ANISOU  275  CZ  ARG A1034    19169  21450  15739   -577    169  -1338       C  
ATOM    276  NH1 ARG A1034      -1.680 -31.532 -91.601  1.00136.25           N  
ANISOU  276  NH1 ARG A1034    17627  20026  14117   -619    109  -1230       N  
ATOM    277  NH2 ARG A1034      -1.955 -33.610 -90.685  1.00135.62           N1+
ANISOU  277  NH2 ARG A1034    17583  19781  14166   -520    184  -1523       N1+
ATOM    278  N   ALA A1035       0.902 -32.142 -84.999  1.00105.89           N  
ANISOU  278  N   ALA A1035    13924  15434  10877   -647    275  -1187       N  
ATOM    279  CA  ALA A1035       0.587 -33.395 -84.336  1.00104.00           C  
ANISOU  279  CA  ALA A1035    13710  15076  10728   -564    324  -1351       C  
ATOM    280  C   ALA A1035      -0.189 -33.145 -83.058  1.00106.53           C  
ANISOU  280  C   ALA A1035    14109  15161  11207   -581    299  -1353       C  
ATOM    281  O   ALA A1035      -1.205 -33.802 -82.838  1.00105.76           O  
ANISOU  281  O   ALA A1035    14043  14961  11179   -547    300  -1468       O  
ATOM    282  CB  ALA A1035       1.869 -34.149 -84.040  1.00104.79           C  
ANISOU  282  CB  ALA A1035    13765  15258  10792   -508    396  -1377       C  
ATOM    283  N   ALA A1036       0.262 -32.152 -82.252  1.00103.02           N  
ANISOU  283  N   ALA A1036    13698  14639  10806   -644    271  -1221       N  
ATOM    284  CA  ALA A1036      -0.328 -31.752 -80.973  1.00101.69           C  
ANISOU  284  CA  ALA A1036    13613  14255  10769   -651    247  -1206       C  
ATOM    285  C   ALA A1036      -1.755 -31.244 -81.139  1.00105.04           C  
ANISOU  285  C   ALA A1036    14080  14604  11227   -636    192  -1215       C  
ATOM    286  O   ALA A1036      -2.601 -31.599 -80.322  1.00104.68           O  
ANISOU  286  O   ALA A1036    14066  14426  11281   -597    201  -1285       O  
ATOM    287  CB  ALA A1036       0.526 -30.683 -80.311  1.00102.37           C  
ANISOU  287  CB  ALA A1036    13741  14298  10856   -732    212  -1055       C  
ATOM    288  N   ALA A1037      -2.028 -30.432 -82.191  1.00100.94           N  
ANISOU  288  N   ALA A1037    13553  14183  10615   -661    137  -1138       N  
ATOM    289  CA  ALA A1037      -3.359 -29.884 -82.482  1.00100.30           C  
ANISOU  289  CA  ALA A1037    13501  14066  10542   -627     79  -1134       C  
ATOM    290  C   ALA A1037      -4.320 -30.993 -82.883  1.00103.80           C  
ANISOU  290  C   ALA A1037    13881  14561  11000   -580    104  -1285       C  
ATOM    291  O   ALA A1037      -5.468 -31.009 -82.436  1.00102.28           O  
ANISOU  291  O   ALA A1037    13695  14296  10872   -543     85  -1325       O  
ATOM    292  CB  ALA A1037      -3.271 -28.842 -83.589  1.00101.94           C  
ANISOU  292  CB  ALA A1037    13719  14382  10630   -663     15  -1011       C  
ATOM    293  N   LEU A1038      -3.831 -31.936 -83.707  1.00102.03           N  
ANISOU  293  N   LEU A1038    13596  14467  10703   -584    144  -1368       N  
ATOM    294  CA  LEU A1038      -4.590 -33.078 -84.210  1.00103.07           C  
ANISOU  294  CA  LEU A1038    13690  14646  10825   -563    157  -1519       C  
ATOM    295  C   LEU A1038      -5.009 -34.024 -83.078  1.00108.37           C  
ANISOU  295  C   LEU A1038    14390  15166  11619   -552    197  -1624       C  
ATOM    296  O   LEU A1038      -6.063 -34.661 -83.166  1.00108.74           O  
ANISOU  296  O   LEU A1038    14421  15205  11690   -562    183  -1718       O  
ATOM    297  CB  LEU A1038      -3.758 -33.845 -85.254  1.00103.79           C  
ANISOU  297  CB  LEU A1038    13745  14892  10798   -552    193  -1584       C  
ATOM    298  CG  LEU A1038      -3.488 -33.150 -86.590  1.00108.54           C  
ANISOU  298  CG  LEU A1038    14304  15685  11252   -566    159  -1503       C  
ATOM    299  CD1 LEU A1038      -2.319 -33.809 -87.305  1.00109.07           C  
ANISOU  299  CD1 LEU A1038    14334  15906  11202   -538    215  -1542       C  
ATOM    300  CD2 LEU A1038      -4.730 -33.118 -87.467  1.00110.92           C  
ANISOU  300  CD2 LEU A1038    14582  16059  11505   -567    100  -1547       C  
ATOM    301  N   ASP A1039      -4.172 -34.116 -82.032  1.00105.24           N  
ANISOU  301  N   ASP A1039    14033  14662  11293   -545    241  -1600       N  
ATOM    302  CA  ASP A1039      -4.411 -34.957 -80.863  1.00105.08           C  
ANISOU  302  CA  ASP A1039    14050  14491  11384   -536    281  -1679       C  
ATOM    303  C   ASP A1039      -5.308 -34.245 -79.863  1.00106.16           C  
ANISOU  303  C   ASP A1039    14209  14514  11615   -536    255  -1623       C  
ATOM    304  O   ASP A1039      -6.041 -34.910 -79.130  1.00105.89           O  
ANISOU  304  O   ASP A1039    14181  14393  11658   -540    274  -1693       O  
ATOM    305  CB  ASP A1039      -3.077 -35.360 -80.205  1.00107.97           C  
ANISOU  305  CB  ASP A1039    14444  14812  11768   -513    337  -1672       C  
ATOM    306  CG  ASP A1039      -2.484 -36.674 -80.722  1.00131.79           C  
ANISOU  306  CG  ASP A1039    17466  17880  14728   -470    385  -1792       C  
ATOM    307  OD1 ASP A1039      -2.451 -36.877 -81.974  1.00135.17           O1-
ANISOU  307  OD1 ASP A1039    17862  18450  15044   -460    374  -1833       O1-
ATOM    308  OD2 ASP A1039      -2.021 -37.486 -79.885  1.00140.38           O  
ANISOU  308  OD2 ASP A1039    18599  18866  15871   -435    431  -1845       O  
ATOM    309  N   ALA A1040      -5.251 -32.899 -79.832  1.00100.92           N  
ANISOU  309  N   ALA A1040    13564  13848  10933   -529    210  -1496       N  
ATOM    310  CA  ALA A1040      -6.051 -32.079 -78.921  1.00 99.81           C  
ANISOU  310  CA  ALA A1040    13464  13602  10859   -496    181  -1439       C  
ATOM    311  C   ALA A1040      -7.502 -32.006 -79.380  1.00104.21           C  
ANISOU  311  C   ALA A1040    13965  14230  11401   -467    144  -1469       C  
ATOM    312  O   ALA A1040      -8.386 -31.921 -78.526  1.00104.28           O  
ANISOU  312  O   ALA A1040    13971  14176  11472   -428    146  -1476       O  
ATOM    313  CB  ALA A1040      -5.466 -30.684 -78.804  1.00100.33           C  
ANISOU  313  CB  ALA A1040    13603  13624  10893   -495    133  -1299       C  
ATOM    314  N   GLN A1041      -7.760 -32.054 -80.716  1.00100.41           N  
ANISOU  314  N   GLN A1041    13426  13898  10826   -482    111  -1484       N  
ATOM    315  CA  GLN A1041      -9.128 -32.028 -81.244  1.00100.64           C  
ANISOU  315  CA  GLN A1041    13383  14029  10826   -461     68  -1511       C  
ATOM    316  C   GLN A1041      -9.830 -33.358 -80.970  1.00106.79           C  
ANISOU  316  C   GLN A1041    14105  14817  11653   -511    101  -1640       C  
ATOM    317  O   GLN A1041     -11.054 -33.377 -80.829  1.00107.89           O  
ANISOU  317  O   GLN A1041    14177  15014  11804   -502     77  -1654       O  
ATOM    318  CB  GLN A1041      -9.197 -31.650 -82.731  1.00102.21           C  
ANISOU  318  CB  GLN A1041    13543  14388  10902   -466     15  -1484       C  
ATOM    319  CG  GLN A1041      -8.421 -32.509 -83.713  1.00106.23           C  
ANISOU  319  CG  GLN A1041    14033  14990  11338   -523     39  -1557       C  
ATOM    320  CD  GLN A1041      -8.785 -32.244 -85.167  1.00117.44           C  
ANISOU  320  CD  GLN A1041    15401  16589  12631   -525    -16  -1546       C  
ATOM    321  OE1 GLN A1041      -9.483 -31.280 -85.522  1.00105.56           O  
ANISOU  321  OE1 GLN A1041    13881  15142  11086   -482    -77  -1461       O  
ATOM    322  NE2 GLN A1041      -8.316 -33.111 -86.052  1.00112.10           N  
ANISOU  322  NE2 GLN A1041    14705  16008  11878   -562      2  -1634       N  
ATOM    323  N   LYS A1042      -9.048 -34.452 -80.826  1.00103.54           N  
ANISOU  323  N   LYS A1042    13728  14347  11265   -562    152  -1726       N  
ATOM    324  CA  LYS A1042      -9.531 -35.799 -80.495  1.00103.61           C  
ANISOU  324  CA  LYS A1042    13729  14319  11318   -627    180  -1846       C  
ATOM    325  C   LYS A1042     -10.059 -35.859 -79.042  1.00108.88           C  
ANISOU  325  C   LYS A1042    14404  14871  12094   -623    211  -1830       C  
ATOM    326  O   LYS A1042     -10.898 -36.708 -78.727  1.00108.72           O  
ANISOU  326  O   LYS A1042    14352  14851  12106   -690    217  -1896       O  
ATOM    327  CB  LYS A1042      -8.404 -36.833 -80.682  1.00105.08           C  
ANISOU  327  CB  LYS A1042    13986  14450  11490   -646    225  -1930       C  
ATOM    328  CG  LYS A1042      -8.105 -37.186 -82.127  1.00112.30           C  
ANISOU  328  CG  LYS A1042    14890  15494  12284   -656    201  -1989       C  
ATOM    329  CD  LYS A1042      -7.546 -38.594 -82.251  1.00119.76           C  
ANISOU  329  CD  LYS A1042    15914  16378  13211   -671    237  -2120       C  
ATOM    330  CE  LYS A1042      -6.077 -38.606 -82.569  1.00128.51           C  
ANISOU  330  CE  LYS A1042    17057  17511  14260   -595    280  -2108       C  
ATOM    331  NZ  LYS A1042      -5.612 -39.976 -82.893  1.00137.25           N1+
ANISOU  331  NZ  LYS A1042    18252  18578  15320   -575    306  -2249       N1+
ATOM    332  N   ALA A1043      -9.557 -34.946 -78.170  1.00106.35           N  
ANISOU  332  N   ALA A1043    14131  14459  11820   -554    227  -1737       N  
ATOM    333  CA  ALA A1043      -9.869 -34.827 -76.738  1.00106.08           C  
ANISOU  333  CA  ALA A1043    14119  14313  11875   -526    260  -1710       C  
ATOM    334  C   ALA A1043     -11.190 -34.104 -76.480  1.00112.13           C  
ANISOU  334  C   ALA A1043    14814  15152  12637   -471    229  -1662       C  
ATOM    335  O   ALA A1043     -11.891 -33.737 -77.431  1.00113.00           O  
ANISOU  335  O   ALA A1043    14852  15403  12677   -458    178  -1651       O  
ATOM    336  CB  ALA A1043      -8.736 -34.099 -76.022  1.00105.80           C  
ANISOU  336  CB  ALA A1043    14175  14158  11868   -476    276  -1635       C  
ATOM    337  N   THR A1044     -11.527 -33.927 -75.180  1.00109.26           N  
ANISOU  337  N   THR A1044    14468  14709  12338   -427    262  -1635       N  
ATOM    338  CA  THR A1044     -12.725 -33.245 -74.681  1.00110.29           C  
ANISOU  338  CA  THR A1044    14534  14910  12461   -339    247  -1588       C  
ATOM    339  C   THR A1044     -12.315 -32.202 -73.636  1.00115.90           C  
ANISOU  339  C   THR A1044    15351  15488  13197   -224    255  -1513       C  
ATOM    340  O   THR A1044     -11.631 -32.559 -72.668  1.00115.24           O  
ANISOU  340  O   THR A1044    15340  15270  13176   -248    300  -1524       O  
ATOM    341  CB  THR A1044     -13.738 -34.256 -74.122  1.00117.11           C  
ANISOU  341  CB  THR A1044    15297  15842  13358   -413    283  -1641       C  
ATOM    342  OG1 THR A1044     -14.204 -35.077 -75.198  1.00121.79           O  
ANISOU  342  OG1 THR A1044    15806  16560  13907   -527    254  -1706       O  
ATOM    343  CG2 THR A1044     -14.921 -33.589 -73.419  1.00111.70           C  
ANISOU  343  CG2 THR A1044    14529  15255  12658   -304    285  -1586       C  
ATOM    344  N   PRO A1045     -12.742 -30.921 -73.801  1.00114.15           N  
ANISOU  344  N   PRO A1045    15155  15296  12921    -94    204  -1438       N  
ATOM    345  CA  PRO A1045     -12.376 -29.883 -72.823  1.00114.33           C  
ANISOU  345  CA  PRO A1045    15315  15171  12953     18    196  -1373       C  
ATOM    346  C   PRO A1045     -12.970 -30.144 -71.441  1.00121.43           C  
ANISOU  346  C   PRO A1045    16197  16043  13900     73    252  -1391       C  
ATOM    347  O   PRO A1045     -13.925 -30.923 -71.347  1.00122.24           O  
ANISOU  347  O   PRO A1045    16158  16278  14010     42    287  -1432       O  
ATOM    348  CB  PRO A1045     -12.971 -28.602 -73.428  1.00116.76           C  
ANISOU  348  CB  PRO A1045    15654  15535  13177    156    123  -1302       C  
ATOM    349  CG  PRO A1045     -13.213 -28.910 -74.834  1.00121.42           C  
ANISOU  349  CG  PRO A1045    16141  16278  13716     92     90  -1317       C  
ATOM    350  CD  PRO A1045     -13.561 -30.347 -74.883  1.00116.73           C  
ANISOU  350  CD  PRO A1045    15408  15781  13164    -34    143  -1409       C  
ATOM    351  N   PRO A1046     -12.445 -29.515 -70.357  1.00119.08           N  
ANISOU  351  N   PRO A1046    16038  15584  13623    145    259  -1357       N  
ATOM    352  CA  PRO A1046     -13.059 -29.729 -69.034  1.00119.16           C  
ANISOU  352  CA  PRO A1046    16028  15584  13661    212    316  -1371       C  
ATOM    353  C   PRO A1046     -14.502 -29.182 -69.025  1.00123.67           C  
ANISOU  353  C   PRO A1046    16505  16318  14165    371    306  -1349       C  
ATOM    354  O   PRO A1046     -15.419 -29.865 -68.567  1.00123.27           O  
ANISOU  354  O   PRO A1046    16311  16404  14122    365    359  -1373       O  
ATOM    355  CB  PRO A1046     -12.116 -28.969 -68.093  1.00120.64           C  
ANISOU  355  CB  PRO A1046    16409  15567  13861    264    302  -1335       C  
ATOM    356  CG  PRO A1046     -11.498 -27.881 -68.950  1.00125.13           C  
ANISOU  356  CG  PRO A1046    17100  16067  14377    283    217  -1277       C  
ATOM    357  CD  PRO A1046     -11.336 -28.532 -70.291  1.00120.57           C  
ANISOU  357  CD  PRO A1046    16408  15606  13796    161    209  -1298       C  
ATOM    358  N   LYS A1047     -14.688 -27.978 -69.629  1.00120.80           N  
ANISOU  358  N   LYS A1047    16215  15955  13727    507    234  -1295       N  
ATOM    359  CA  LYS A1047     -15.927 -27.221 -69.841  1.00121.90           C  
ANISOU  359  CA  LYS A1047    16291  16246  13779    701    204  -1262       C  
ATOM    360  C   LYS A1047     -17.019 -28.089 -70.505  1.00126.42           C  
ANISOU  360  C   LYS A1047    16611  17089  14334    639    226  -1291       C  
ATOM    361  O   LYS A1047     -18.192 -27.998 -70.128  1.00127.70           O  
ANISOU  361  O   LYS A1047    16644  17430  14445    764    248  -1279       O  
ATOM    362  CB  LYS A1047     -15.604 -25.997 -70.740  1.00124.48           C  
ANISOU  362  CB  LYS A1047    16763  16496  14036    791    109  -1200       C  
ATOM    363  CG  LYS A1047     -16.748 -25.013 -70.950  1.00136.61           C  
ANISOU  363  CG  LYS A1047    18287  18150  15468   1037     63  -1155       C  
ATOM    364  CD  LYS A1047     -16.382 -23.917 -71.943  1.00146.47           C  
ANISOU  364  CD  LYS A1047    19692  19311  16648   1097    -37  -1088       C  
ATOM    365  CE  LYS A1047     -17.446 -22.841 -72.012  1.00156.80           C  
ANISOU  365  CE  LYS A1047    21037  20696  17843   1383    -88  -1040       C  
ATOM    366  NZ  LYS A1047     -17.304 -21.992 -73.225  1.00162.35           N1+
ANISOU  366  NZ  LYS A1047    21840  21373  18471   1422   -186   -971       N1+
ATOM    367  N   LEU A1048     -16.619 -28.920 -71.490  1.00121.02           N  
ANISOU  367  N   LEU A1048    15859  16443  13680    446    216  -1327       N  
ATOM    368  CA  LEU A1048     -17.526 -29.763 -72.255  1.00120.79           C  
ANISOU  368  CA  LEU A1048    15619  16648  13628    348    217  -1360       C  
ATOM    369  C   LEU A1048     -17.423 -31.248 -71.860  1.00125.36           C  
ANISOU  369  C   LEU A1048    16119  17231  14282    138    280  -1428       C  
ATOM    370  O   LEU A1048     -17.863 -32.103 -72.631  1.00125.57           O  
ANISOU  370  O   LEU A1048    16018  17396  14296     -4    268  -1469       O  
ATOM    371  CB  LEU A1048     -17.266 -29.594 -73.771  1.00120.54           C  
ANISOU  371  CB  LEU A1048    15583  16667  13549    295    147  -1357       C  
ATOM    372  CG  LEU A1048     -17.023 -28.184 -74.347  1.00124.82           C  
ANISOU  372  CG  LEU A1048    16256  17149  14021    455     73  -1282       C  
ATOM    373  CD1 LEU A1048     -16.794 -28.250 -75.844  1.00124.74           C  
ANISOU  373  CD1 LEU A1048    16215  17219  13963    368     15  -1281       C  
ATOM    374  CD2 LEU A1048     -18.179 -27.237 -74.052  1.00128.30           C  
ANISOU  374  CD2 LEU A1048    16657  17710  14381    696     48  -1227       C  
ATOM    375  N   GLU A1049     -16.918 -31.560 -70.639  1.00122.39           N  
ANISOU  375  N   GLU A1049    15825  16704  13973    120    341  -1439       N  
ATOM    376  CA  GLU A1049     -16.795 -32.949 -70.140  1.00122.28           C  
ANISOU  376  CA  GLU A1049    15769  16664  14028    -66    399  -1494       C  
ATOM    377  C   GLU A1049     -18.181 -33.577 -69.824  1.00128.07           C  
ANISOU  377  C   GLU A1049    16303  17626  14732   -115    429  -1492       C  
ATOM    378  O   GLU A1049     -18.253 -34.696 -69.305  1.00127.53           O  
ANISOU  378  O   GLU A1049    16202  17544  14711   -274    474  -1523       O  
ATOM    379  CB  GLU A1049     -15.890 -33.001 -68.891  1.00122.46           C  
ANISOU  379  CB  GLU A1049    15938  16474  14118    -51    451  -1493       C  
ATOM    380  N   ASP A1050     -19.264 -32.852 -70.191  1.00126.18           N  
ANISOU  380  N   ASP A1050    15931  17605  14408     17    398  -1448       N  
ATOM    381  CA  ASP A1050     -20.690 -33.139 -69.967  1.00127.20           C  
ANISOU  381  CA  ASP A1050    15835  18019  14478     13    416  -1421       C  
ATOM    382  C   ASP A1050     -21.533 -33.072 -71.266  1.00129.08           C  
ANISOU  382  C   ASP A1050    15909  18501  14634    -10    347  -1416       C  
ATOM    383  O   ASP A1050     -22.691 -33.503 -71.268  1.00128.92           O  
ANISOU  383  O   ASP A1050    15675  18749  14561    -71    351  -1396       O  
ATOM    384  CB  ASP A1050     -21.250 -32.126 -68.938  1.00130.06           C  
ANISOU  384  CB  ASP A1050    16184  18445  14787    272    452  -1360       C  
ATOM    385  CG  ASP A1050     -20.696 -30.717 -69.101  1.00141.88           C  
ANISOU  385  CG  ASP A1050    17861  19792  16253    509    406  -1333       C  
ATOM    386  OD1 ASP A1050     -19.597 -30.443 -68.560  1.00141.24           O1-
ANISOU  386  OD1 ASP A1050    17989  19446  16232    525    416  -1343       O1-
ATOM    387  OD2 ASP A1050     -21.332 -29.906 -69.815  1.00149.45           O1-
ANISOU  387  OD2 ASP A1050    18760  20898  17125    664    352  -1297       O1-
ATOM    388  N   LYS A1051     -20.952 -32.515 -72.349  1.00124.14           N  
ANISOU  388  N   LYS A1051    15377  17800  13991     33    281  -1425       N  
ATOM    389  CA  LYS A1051     -21.598 -32.345 -73.653  1.00124.44           C  
ANISOU  389  CA  LYS A1051    15290  18046  13947     27    207  -1418       C  
ATOM    390  C   LYS A1051     -21.271 -33.513 -74.593  1.00127.92           C  
ANISOU  390  C   LYS A1051    15718  18475  14411   -238    177  -1494       C  
ATOM    391  O   LYS A1051     -20.174 -34.090 -74.533  1.00125.40           O  
ANISOU  391  O   LYS A1051    15554  17927  14167   -351    199  -1549       O  
ATOM    392  CB  LYS A1051     -21.192 -31.012 -74.310  1.00126.19           C  
ANISOU  392  CB  LYS A1051    15632  18197  14118    234    148  -1373       C  
ATOM    393  CG  LYS A1051     -21.047 -29.814 -73.364  1.00138.93           C  
ANISOU  393  CG  LYS A1051    17377  19689  15721    491    167  -1315       C  
ATOM    394  CD  LYS A1051     -22.362 -29.122 -73.014  1.00153.02           C  
ANISOU  394  CD  LYS A1051    19014  21719  17407    720    167  -1256       C  
ATOM    395  CE  LYS A1051     -22.167 -27.673 -72.608  1.00166.25           C  
ANISOU  395  CE  LYS A1051    20875  23258  19036   1015    143  -1201       C  
ATOM    396  NZ  LYS A1051     -21.473 -27.520 -71.296  1.00173.27           N1+
ANISOU  396  NZ  LYS A1051    21937  23908  19989   1058    201  -1212       N1+
ATOM    397  N   SER A1052     -22.243 -33.842 -75.470  1.00126.75           N  
ANISOU  397  N   SER A1052    15387  18588  14186   -322    123  -1499       N  
ATOM    398  CA  SER A1052     -22.203 -34.925 -76.464  1.00127.23           C  
ANISOU  398  CA  SER A1052    15420  18686  14237   -569     77  -1575       C  
ATOM    399  C   SER A1052     -20.974 -34.829 -77.375  1.00130.67           C  
ANISOU  399  C   SER A1052    16038  18922  14687   -578     47  -1624       C  
ATOM    400  O   SER A1052     -20.606 -33.711 -77.741  1.00130.57           O  
ANISOU  400  O   SER A1052    16093  18874  14645   -396     23  -1574       O  
ATOM    401  CB  SER A1052     -23.474 -34.902 -77.316  1.00132.21           C  
ANISOU  401  CB  SER A1052    15823  19655  14757   -601      7  -1552       C  
ATOM    402  OG  SER A1052     -23.558 -35.986 -78.228  1.00139.44           O  
ANISOU  402  OG  SER A1052    16712  20618  15649   -855    -47  -1631       O  
ATOM    403  N   PRO A1053     -20.346 -35.964 -77.799  1.00126.06           N  
ANISOU  403  N   PRO A1053    15542  18220  14137   -782     43  -1716       N  
ATOM    404  CA  PRO A1053     -19.200 -35.866 -78.720  1.00124.39           C  
ANISOU  404  CA  PRO A1053    15480  17865  13917   -774     20  -1759       C  
ATOM    405  C   PRO A1053     -19.611 -35.265 -80.062  1.00128.31           C  
ANISOU  405  C   PRO A1053    15898  18548  14305   -722    -61  -1740       C  
ATOM    406  O   PRO A1053     -18.756 -34.805 -80.806  1.00126.55           O  
ANISOU  406  O   PRO A1053    15779  18247  14057   -663    -81  -1738       O  
ATOM    407  CB  PRO A1053     -18.739 -37.318 -78.871  1.00126.06           C  
ANISOU  407  CB  PRO A1053    15775  17960  14161   -988     28  -1869       C  
ATOM    408  CG  PRO A1053     -19.312 -38.031 -77.683  1.00130.93           C  
ANISOU  408  CG  PRO A1053    16348  18563  14838  -1090     75  -1866       C  
ATOM    409  CD  PRO A1053     -20.637 -37.377 -77.483  1.00127.96           C  
ANISOU  409  CD  PRO A1053    15762  18447  14408  -1022     57  -1784       C  
ATOM    410  N   ASP A1054     -20.929 -35.228 -80.338  1.00126.99           N  
ANISOU  410  N   ASP A1054    15536  18646  14067   -740   -108  -1713       N  
ATOM    411  CA  ASP A1054     -21.497 -34.649 -81.549  1.00128.17           C  
ANISOU  411  CA  ASP A1054    15585  19010  14102   -682   -190  -1685       C  
ATOM    412  C   ASP A1054     -22.402 -33.425 -81.232  1.00130.85           C  
ANISOU  412  C   ASP A1054    15799  19526  14390   -452   -204  -1571       C  
ATOM    413  O   ASP A1054     -23.282 -33.087 -82.026  1.00132.12           O  
ANISOU  413  O   ASP A1054    15812  19939  14448   -409   -272  -1538       O  
ATOM    414  CB  ASP A1054     -22.253 -35.721 -82.353  1.00132.18           C  
ANISOU  414  CB  ASP A1054    15972  19705  14544   -908   -253  -1759       C  
ATOM    415  CG  ASP A1054     -21.365 -36.840 -82.866  1.00145.01           C  
ANISOU  415  CG  ASP A1054    17752  21153  16190  -1095   -256  -1880       C  
ATOM    416  OD1 ASP A1054     -20.281 -36.537 -83.423  1.00144.86           O  
ANISOU  416  OD1 ASP A1054    17880  20991  16168  -1023   -250  -1898       O  
ATOM    417  OD2 ASP A1054     -21.761 -38.015 -82.733  1.00153.02           O1-
ANISOU  417  OD2 ASP A1054    18746  22180  17213  -1312   -268  -1952       O1-
ATOM    418  N   SER A1055     -22.147 -32.736 -80.101  1.00124.62           N  
ANISOU  418  N   SER A1055    15085  18603  13662   -288   -142  -1514       N  
ATOM    419  CA  SER A1055     -22.882 -31.522 -79.729  1.00124.34           C  
ANISOU  419  CA  SER A1055    14981  18692  13571    -29   -152  -1414       C  
ATOM    420  C   SER A1055     -22.287 -30.318 -80.493  1.00126.04           C  
ANISOU  420  C   SER A1055    15339  18815  13735    149   -204  -1357       C  
ATOM    421  O   SER A1055     -21.169 -30.447 -80.996  1.00124.52           O  
ANISOU  421  O   SER A1055    15302  18437  13574     64   -207  -1390       O  
ATOM    422  CB  SER A1055     -22.849 -31.303 -78.216  1.00126.89           C  
ANISOU  422  CB  SER A1055    15348  18900  13964     74    -71  -1386       C  
ATOM    423  OG  SER A1055     -21.532 -31.142 -77.718  1.00132.30           O  
ANISOU  423  OG  SER A1055    16266  19264  14739     80    -29  -1402       O  
ATOM    424  N   PRO A1056     -22.989 -29.163 -80.626  1.00122.79           N  
ANISOU  424  N   PRO A1056    14884  18534  13235    395   -246  -1268       N  
ATOM    425  CA  PRO A1056     -22.422 -28.040 -81.403  1.00122.23           C  
ANISOU  425  CA  PRO A1056    14974  18360  13108    542   -306  -1204       C  
ATOM    426  C   PRO A1056     -21.151 -27.435 -80.806  1.00123.65           C  
ANISOU  426  C   PRO A1056    15418  18203  13362    591   -275  -1181       C  
ATOM    427  O   PRO A1056     -20.271 -27.015 -81.557  1.00122.19           O  
ANISOU  427  O   PRO A1056    15377  17892  13159    568   -312  -1157       O  
ATOM    428  CB  PRO A1056     -23.554 -27.009 -81.416  1.00125.96           C  
ANISOU  428  CB  PRO A1056    15353  19034  13472    816   -352  -1115       C  
ATOM    429  CG  PRO A1056     -24.787 -27.780 -81.102  1.00131.92           C  
ANISOU  429  CG  PRO A1056    15831  20091  14202    758   -332  -1140       C  
ATOM    430  CD  PRO A1056     -24.343 -28.832 -80.143  1.00126.19           C  
ANISOU  430  CD  PRO A1056    15119  19229  13598    555   -247  -1215       C  
ATOM    431  N   GLU A1057     -21.058 -27.395 -79.468  1.00120.15           N  
ANISOU  431  N   GLU A1057    15030  17631  12992    650   -209  -1185       N  
ATOM    432  CA  GLU A1057     -19.908 -26.872 -78.717  1.00119.16           C  
ANISOU  432  CA  GLU A1057    15144  17195  12936    684   -180  -1166       C  
ATOM    433  C   GLU A1057     -18.683 -27.759 -78.951  1.00121.92           C  
ANISOU  433  C   GLU A1057    15567  17392  13367    444   -148  -1231       C  
ATOM    434  O   GLU A1057     -17.556 -27.272 -79.026  1.00120.74           O  
ANISOU  434  O   GLU A1057    15600  17040  13236    430   -158  -1202       O  
ATOM    435  CB  GLU A1057     -20.209 -26.783 -77.200  1.00120.53           C  
ANISOU  435  CB  GLU A1057    15334  17304  13160    791   -114  -1167       C  
ATOM    436  CG  GLU A1057     -21.609 -26.323 -76.810  1.00135.80           C  
ANISOU  436  CG  GLU A1057    17120  19466  15013   1011   -117  -1128       C  
ATOM    437  CD  GLU A1057     -22.692 -27.389 -76.768  1.00166.74           C  
ANISOU  437  CD  GLU A1057    20751  23681  18921    899    -84  -1168       C  
ATOM    438  OE1 GLU A1057     -22.407 -28.521 -76.315  1.00164.67           O  
ANISOU  438  OE1 GLU A1057    20442  23379  18745    679    -25  -1233       O  
ATOM    439  OE2 GLU A1057     -23.838 -27.082 -77.170  1.00168.73           O1-
ANISOU  439  OE2 GLU A1057    20827  24211  19070   1030   -120  -1128       O1-
ATOM    440  N   MET A1058     -18.923 -29.068 -79.055  1.00118.67           N  
ANISOU  440  N   MET A1058    15013  17085  12991    257   -113  -1317       N  
ATOM    441  CA  MET A1058     -17.914 -30.088 -79.294  1.00117.52           C  
ANISOU  441  CA  MET A1058    14921  16824  12907     49    -81  -1395       C  
ATOM    442  C   MET A1058     -17.417 -30.010 -80.739  1.00120.95           C  
ANISOU  442  C   MET A1058    15380  17304  13270    -10   -138  -1397       C  
ATOM    443  O   MET A1058     -16.216 -30.146 -80.987  1.00119.43           O  
ANISOU  443  O   MET A1058    15308  16967  13101    -85   -123  -1411       O  
ATOM    444  CB  MET A1058     -18.520 -31.462 -78.994  1.00120.31           C  
ANISOU  444  CB  MET A1058    15133  17281  13300   -117    -43  -1482       C  
ATOM    445  CG  MET A1058     -17.578 -32.420 -78.309  1.00122.95           C  
ANISOU  445  CG  MET A1058    15563  17418  13733   -256     24  -1550       C  
ATOM    446  SD  MET A1058     -16.522 -31.739 -77.008  1.00125.53           S  
ANISOU  446  SD  MET A1058    16076  17478  14143   -150     79  -1502       S  
ATOM    447  CE  MET A1058     -14.947 -32.246 -77.657  1.00121.28           C  
ANISOU  447  CE  MET A1058    15668  16785  13627   -273     86  -1549       C  
ATOM    448  N   LYS A1059     -18.346 -29.755 -81.681  1.00118.44           N  
ANISOU  448  N   LYS A1059    14940  17206  12854     34   -203  -1375       N  
ATOM    449  CA  LYS A1059     -18.068 -29.618 -83.107  1.00118.33           C  
ANISOU  449  CA  LYS A1059    14932  17276  12750     -5   -264  -1369       C  
ATOM    450  C   LYS A1059     -17.297 -28.317 -83.407  1.00121.80           C  
ANISOU  450  C   LYS A1059    15540  17588  13151    118   -299  -1263       C  
ATOM    451  O   LYS A1059     -16.476 -28.327 -84.330  1.00121.64           O  
ANISOU  451  O   LYS A1059    15582  17549  13087     43   -319  -1259       O  
ATOM    452  CB  LYS A1059     -19.365 -29.689 -83.927  1.00122.11           C  
ANISOU  452  CB  LYS A1059    15225  18041  13130     13   -330  -1368       C  
ATOM    453  N   ASP A1060     -17.532 -27.212 -82.643  1.00117.42           N  
ANISOU  453  N   ASP A1060    15070  16942  12600    302   -310  -1175       N  
ATOM    454  CA  ASP A1060     -16.793 -25.955 -82.850  1.00116.87           C  
ANISOU  454  CA  ASP A1060    15197  16717  12491    398   -355  -1068       C  
ATOM    455  C   ASP A1060     -15.387 -26.088 -82.285  1.00116.29           C  
ANISOU  455  C   ASP A1060    15274  16413  12498    287   -307  -1074       C  
ATOM    456  O   ASP A1060     -14.437 -25.525 -82.842  1.00115.67           O  
ANISOU  456  O   ASP A1060    15321  16247  12381    246   -337  -1009       O  
ATOM    457  CB  ASP A1060     -17.505 -24.730 -82.223  1.00120.55           C  
ANISOU  457  CB  ASP A1060    15742  17140  12922    642   -393   -980       C  
ATOM    458  CG  ASP A1060     -16.736 -23.403 -82.346  1.00136.73           C  
ANISOU  458  CG  ASP A1060    18040  18984  14927    726   -453   -865       C  
ATOM    459  OD1 ASP A1060     -16.108 -23.165 -83.414  1.00139.04           O  
ANISOU  459  OD1 ASP A1060    18387  19283  15159    642   -497   -817       O  
ATOM    460  OD2 ASP A1060     -16.769 -22.600 -81.381  1.00141.65           O1-
ANISOU  460  OD2 ASP A1060    18813  19442  15567    870   -459   -821       O1-
ATOM    461  N   PHE A1061     -15.262 -26.817 -81.166  1.00109.93           N  
ANISOU  461  N   PHE A1061    14449  15524  11796    236   -233  -1144       N  
ATOM    462  CA  PHE A1061     -13.974 -27.036 -80.519  1.00107.64           C  
ANISOU  462  CA  PHE A1061    14279  15035  11583    138   -185  -1155       C  
ATOM    463  C   PHE A1061     -13.026 -27.651 -81.525  1.00109.36           C  
ANISOU  463  C   PHE A1061    14485  15293  11774    -16   -178  -1187       C  
ATOM    464  O   PHE A1061     -11.953 -27.094 -81.769  1.00108.31           O  
ANISOU  464  O   PHE A1061    14470  15066  11619    -53   -194  -1119       O  
ATOM    465  CB  PHE A1061     -14.130 -27.926 -79.256  1.00108.51           C  
ANISOU  465  CB  PHE A1061    14343  15087  11799    102   -106  -1236       C  
ATOM    466  CG  PHE A1061     -12.842 -28.484 -78.686  1.00108.70           C  
ANISOU  466  CG  PHE A1061    14451  14949  11899    -16    -50  -1269       C  
ATOM    467  CD1 PHE A1061     -11.951 -27.665 -77.997  1.00110.86           C  
ANISOU  467  CD1 PHE A1061    14888  15037  12196     14    -56  -1199       C  
ATOM    468  CD2 PHE A1061     -12.515 -29.827 -78.846  1.00110.38           C  
ANISOU  468  CD2 PHE A1061    14588  15198  12152   -154      1  -1368       C  
ATOM    469  CE1 PHE A1061     -10.758 -28.178 -77.481  1.00110.44           C  
ANISOU  469  CE1 PHE A1061    14892  14866  12204    -91     -9  -1223       C  
ATOM    470  CE2 PHE A1061     -11.319 -30.339 -78.330  1.00111.99           C  
ANISOU  470  CE2 PHE A1061    14866  15269  12416   -235     52  -1394       C  
ATOM    471  CZ  PHE A1061     -10.451 -29.510 -77.650  1.00109.31           C  
ANISOU  471  CZ  PHE A1061    14660  14775  12098   -202     48  -1319       C  
ATOM    472  N   ARG A1062     -13.467 -28.761 -82.153  1.00105.14           N  
ANISOU  472  N   ARG A1062    13808  14913  11227   -103   -162  -1284       N  
ATOM    473  CA  ARG A1062     -12.727 -29.500 -83.166  1.00104.47           C  
ANISOU  473  CA  ARG A1062    13701  14893  11099   -227   -153  -1338       C  
ATOM    474  C   ARG A1062     -12.567 -28.692 -84.452  1.00112.15           C  
ANISOU  474  C   ARG A1062    14694  15966  11951   -202   -220  -1257       C  
ATOM    475  O   ARG A1062     -11.581 -28.909 -85.154  1.00112.75           O  
ANISOU  475  O   ARG A1062    14799  16059  11981   -281   -209  -1259       O  
ATOM    476  CB  ARG A1062     -13.394 -30.836 -83.470  1.00100.49           C  
ANISOU  476  CB  ARG A1062    13070  14511  10599   -319   -135  -1467       C  
ATOM    477  CG  ARG A1062     -13.351 -31.806 -82.316  1.00101.09           C  
ANISOU  477  CG  ARG A1062    13145  14478  10785   -379    -67  -1548       C  
ATOM    478  CD  ARG A1062     -13.910 -33.154 -82.705  1.00113.51           C  
ANISOU  478  CD  ARG A1062    14631  16148  12351   -501    -62  -1671       C  
ATOM    479  NE  ARG A1062     -15.316 -33.068 -83.108  1.00127.65           N  
ANISOU  479  NE  ARG A1062    16285  18129  14088   -492   -117  -1668       N  
ATOM    480  CZ  ARG A1062     -16.344 -33.407 -82.338  1.00142.27           C  
ANISOU  480  CZ  ARG A1062    18042  20033  15983   -508   -107  -1683       C  
ATOM    481  NH1 ARG A1062     -16.140 -33.888 -81.118  1.00132.73           N1+
ANISOU  481  NH1 ARG A1062    16873  18683  14874   -537    -42  -1705       N1+
ATOM    482  NH2 ARG A1062     -17.586 -33.283 -82.787  1.00126.13           N  
ANISOU  482  NH2 ARG A1062    15850  18201  13872   -498   -161  -1669       N  
ATOM    483  N   HIS A1063     -13.507 -27.760 -84.760  1.00110.40           N  
ANISOU  483  N   HIS A1063    14458  15821  11668    -83   -288  -1180       N  
ATOM    484  CA  HIS A1063     -13.419 -26.906 -85.951  1.00111.44           C  
ANISOU  484  CA  HIS A1063    14624  16039  11677    -48   -359  -1086       C  
ATOM    485  C   HIS A1063     -12.242 -25.931 -85.857  1.00114.44           C  
ANISOU  485  C   HIS A1063    15179  16259  12044    -58   -372   -968       C  
ATOM    486  O   HIS A1063     -11.592 -25.671 -86.872  1.00114.72           O  
ANISOU  486  O   HIS A1063    15240  16358  11988   -118   -399   -912       O  
ATOM    487  CB  HIS A1063     -14.720 -26.129 -86.210  1.00113.88           C  
ANISOU  487  CB  HIS A1063    14888  16460  11921    106   -431  -1026       C  
ATOM    488  CG  HIS A1063     -14.620 -25.179 -87.374  1.00118.77           C  
ANISOU  488  CG  HIS A1063    15568  17147  12413    154   -510   -915       C  
ATOM    489  ND1 HIS A1063     -14.088 -25.579 -88.598  1.00120.87           N  
ANISOU  489  ND1 HIS A1063    15796  17536  12594     42   -520   -930       N  
ATOM    490  CD2 HIS A1063     -14.955 -23.869 -87.454  1.00121.68           C  
ANISOU  490  CD2 HIS A1063    16049  17465  12718    305   -582   -786       C  
ATOM    491  CE1 HIS A1063     -14.127 -24.507 -89.373  1.00121.41           C  
ANISOU  491  CE1 HIS A1063    15941  17634  12554    114   -595   -803       C  
ATOM    492  NE2 HIS A1063     -14.650 -23.457 -88.735  1.00122.26           N  
ANISOU  492  NE2 HIS A1063    16150  17633  12672    273   -639   -713       N  
ATOM    493  N   GLY A1064     -11.990 -25.410 -84.654  1.00109.88           N  
ANISOU  493  N   GLY A1064    14716  15488  11546    -11   -358   -928       N  
ATOM    494  CA  GLY A1064     -10.891 -24.488 -84.387  1.00109.49           C  
ANISOU  494  CA  GLY A1064    14845  15268  11490    -45   -379   -815       C  
ATOM    495  C   GLY A1064      -9.525 -25.069 -84.709  1.00112.27           C  
ANISOU  495  C   GLY A1064    15185  15634  11839   -209   -331   -828       C  
ATOM    496  O   GLY A1064      -8.660 -24.371 -85.256  1.00112.49           O  
ANISOU  496  O   GLY A1064    15300  15648  11794   -276   -366   -717       O  
ATOM    497  N   PHE A1065      -9.341 -26.374 -84.385  1.00106.90           N  
ANISOU  497  N   PHE A1065    14398  14992  11229   -270   -251   -960       N  
ATOM    498  CA  PHE A1065      -8.112 -27.115 -84.653  1.00105.90           C  
ANISOU  498  CA  PHE A1065    14241  14902  11094   -389   -195   -995       C  
ATOM    499  C   PHE A1065      -7.943 -27.399 -86.146  1.00111.43           C  
ANISOU  499  C   PHE A1065    14864  15802  11671   -433   -208  -1003       C  
ATOM    500  O   PHE A1065      -6.812 -27.484 -86.608  1.00111.06           O  
ANISOU  500  O   PHE A1065    14820  15810  11568   -510   -183   -969       O  
ATOM    501  CB  PHE A1065      -8.062 -28.409 -83.851  1.00106.21           C  
ANISOU  501  CB  PHE A1065    14217  14903  11236   -413   -114  -1135       C  
ATOM    502  CG  PHE A1065      -7.738 -28.140 -82.410  1.00106.45           C  
ANISOU  502  CG  PHE A1065    14334  14743  11370   -399    -90  -1110       C  
ATOM    503  CD1 PHE A1065      -6.450 -27.782 -82.026  1.00109.22           C  
ANISOU  503  CD1 PHE A1065    14763  15013  11725   -464    -78  -1038       C  
ATOM    504  CD2 PHE A1065      -8.726 -28.197 -81.440  1.00108.10           C  
ANISOU  504  CD2 PHE A1065    14541  14872  11660   -322    -83  -1151       C  
ATOM    505  CE1 PHE A1065      -6.155 -27.494 -80.692  1.00109.57           C  
ANISOU  505  CE1 PHE A1065    14894  14881  11855   -455    -66  -1015       C  
ATOM    506  CE2 PHE A1065      -8.428 -27.925 -80.103  1.00110.39           C  
ANISOU  506  CE2 PHE A1065    14919  14990  12033   -300    -62  -1130       C  
ATOM    507  CZ  PHE A1065      -7.145 -27.573 -79.738  1.00108.24           C  
ANISOU  507  CZ  PHE A1065    14738  14623  11767   -368    -57  -1066       C  
ATOM    508  N   ASP A1066      -9.063 -27.516 -86.898  1.00108.92           N  
ANISOU  508  N   ASP A1066    14471  15612  11300   -380   -248  -1042       N  
ATOM    509  CA  ASP A1066      -9.061 -27.704 -88.350  1.00109.39           C  
ANISOU  509  CA  ASP A1066    14465  15869  11228   -410   -273  -1049       C  
ATOM    510  C   ASP A1066      -8.539 -26.429 -89.020  1.00113.69           C  
ANISOU  510  C   ASP A1066    15097  16430  11669   -417   -332   -877       C  
ATOM    511  O   ASP A1066      -7.797 -26.511 -90.002  1.00114.74           O  
ANISOU  511  O   ASP A1066    15206  16695  11695   -482   -325   -847       O  
ATOM    512  CB  ASP A1066     -10.463 -28.066 -88.879  1.00111.96           C  
ANISOU  512  CB  ASP A1066    14690  16327  11523   -357   -315  -1124       C  
ATOM    513  CG  ASP A1066     -10.961 -29.464 -88.553  1.00122.05           C  
ANISOU  513  CG  ASP A1066    15877  17631  12866   -398   -269  -1295       C  
ATOM    514  OD1 ASP A1066     -10.118 -30.399 -88.457  1.00121.11           O  
ANISOU  514  OD1 ASP A1066    15764  17483  12768   -466   -205  -1382       O  
ATOM    515  OD2 ASP A1066     -12.199 -29.643 -88.462  1.00129.78           O1-
ANISOU  515  OD2 ASP A1066    16778  18673  13858   -363   -302  -1338       O1-
ATOM    516  N   ILE A1067      -8.903 -25.250 -88.466  1.00109.29           N  
ANISOU  516  N   ILE A1067    14656  15735  11136   -349   -391   -761       N  
ATOM    517  CA  ILE A1067      -8.437 -23.948 -88.953  1.00109.73           C  
ANISOU  517  CA  ILE A1067    14841  15754  11099   -365   -461   -583       C  
ATOM    518  C   ILE A1067      -6.937 -23.839 -88.635  1.00112.33           C  
ANISOU  518  C   ILE A1067    15230  16017  11434   -501   -423   -516       C  
ATOM    519  O   ILE A1067      -6.145 -23.475 -89.515  1.00112.62           O  
ANISOU  519  O   ILE A1067    15277  16157  11358   -592   -439   -415       O  
ATOM    520  CB  ILE A1067      -9.259 -22.765 -88.360  1.00113.17           C  
ANISOU  520  CB  ILE A1067    15417  16029  11555   -236   -539   -491       C  
ATOM    521  CG1 ILE A1067     -10.777 -22.962 -88.564  1.00113.80           C  
ANISOU  521  CG1 ILE A1067    15398  16213  11627    -87   -567   -561       C  
ATOM    522  CG2 ILE A1067      -8.804 -21.434 -88.976  1.00115.75           C  
ANISOU  522  CG2 ILE A1067    15909  16302  11769   -263   -626   -302       C  
ATOM    523  CD1 ILE A1067     -11.652 -22.334 -87.493  1.00122.36           C  
ANISOU  523  CD1 ILE A1067    16564  17148  12777     73   -596   -546       C  
ATOM    524  N   LEU A1068      -6.565 -24.219 -87.386  1.00106.80           N  
ANISOU  524  N   LEU A1068    14550  15171  10857   -516   -371   -573       N  
ATOM    525  CA  LEU A1068      -5.205 -24.210 -86.858  1.00106.05           C  
ANISOU  525  CA  LEU A1068    14494  15017  10784   -635   -333   -524       C  
ATOM    526  C   LEU A1068      -4.256 -25.091 -87.692  1.00113.28           C  
ANISOU  526  C   LEU A1068    15276  16141  11623   -721   -266   -565       C  
ATOM    527  O   LEU A1068      -3.253 -24.572 -88.185  1.00114.39           O  
ANISOU  527  O   LEU A1068    15435  16356  11670   -827   -279   -440       O  
ATOM    528  CB  LEU A1068      -5.211 -24.666 -85.407  1.00104.22           C  
ANISOU  528  CB  LEU A1068    14283  14620  10697   -607   -286   -608       C  
ATOM    529  CG  LEU A1068      -4.219 -23.954 -84.539  1.00108.22           C  
ANISOU  529  CG  LEU A1068    14915  14972  11232   -695   -304   -503       C  
ATOM    530  CD1 LEU A1068      -4.917 -23.130 -83.507  1.00108.08           C  
ANISOU  530  CD1 LEU A1068    15053  14729  11283   -608   -359   -474       C  
ATOM    531  CD2 LEU A1068      -3.308 -24.926 -83.873  1.00110.14           C  
ANISOU  531  CD2 LEU A1068    15076  15231  11540   -753   -218   -580       C  
ATOM    532  N   VAL A1069      -4.595 -26.399 -87.902  1.00110.37           N  
ANISOU  532  N   VAL A1069    14781  15876  11279   -674   -201   -734       N  
ATOM    533  CA  VAL A1069      -3.796 -27.359 -88.699  1.00110.06           C  
ANISOU  533  CA  VAL A1069    14630  16030  11157   -712   -135   -803       C  
ATOM    534  C   VAL A1069      -3.618 -26.801 -90.111  1.00116.60           C  
ANISOU  534  C   VAL A1069    15436  17048  11818   -748   -176   -704       C  
ATOM    535  O   VAL A1069      -2.507 -26.845 -90.634  1.00117.17           O  
ANISOU  535  O   VAL A1069    15463  17265  11792   -817   -141   -645       O  
ATOM    536  CB  VAL A1069      -4.372 -28.812 -88.714  1.00112.47           C  
ANISOU  536  CB  VAL A1069    14851  16375  11507   -650    -80  -1009       C  
ATOM    537  CG1 VAL A1069      -3.649 -29.711 -89.704  1.00112.60           C  
ANISOU  537  CG1 VAL A1069    14784  16591  11406   -658    -27  -1084       C  
ATOM    538  CG2 VAL A1069      -4.357 -29.440 -87.330  1.00110.97           C  
ANISOU  538  CG2 VAL A1069    14683  16011  11468   -631    -31  -1095       C  
ATOM    539  N   GLY A1070      -4.690 -26.234 -90.668  1.00114.88           N  
ANISOU  539  N   GLY A1070    15247  16839  11562   -696   -249   -672       N  
ATOM    540  CA  GLY A1070      -4.700 -25.620 -91.990  1.00116.93           C  
ANISOU  540  CA  GLY A1070    15501  17266  11663   -719   -300   -568       C  
ATOM    541  C   GLY A1070      -3.653 -24.537 -92.131  1.00122.48           C  
ANISOU  541  C   GLY A1070    16283  17966  12288   -831   -329   -366       C  
ATOM    542  O   GLY A1070      -2.904 -24.521 -93.114  1.00123.25           O  
ANISOU  542  O   GLY A1070    16322  18264  12244   -900   -313   -299       O  
ATOM    543  N   GLN A1071      -3.564 -23.659 -91.118  1.00118.87           N  
ANISOU  543  N   GLN A1071    15962  17287  11918   -859   -373   -267       N  
ATOM    544  CA  GLN A1071      -2.593 -22.569 -91.076  1.00120.00           C  
ANISOU  544  CA  GLN A1071    16213  17384  11998   -997   -418    -67       C  
ATOM    545  C   GLN A1071      -1.183 -23.103 -90.846  1.00123.74           C  
ANISOU  545  C   GLN A1071    16593  17966  12456  -1114   -339    -59       C  
ATOM    546  O   GLN A1071      -0.238 -22.547 -91.411  1.00124.87           O  
ANISOU  546  O   GLN A1071    16733  18235  12479  -1250   -353     96       O  
ATOM    547  CB  GLN A1071      -2.971 -21.540 -90.000  1.00121.54           C  
ANISOU  547  CB  GLN A1071    16605  17287  12286   -982   -495     13       C  
ATOM    548  CG  GLN A1071      -4.118 -20.633 -90.446  1.00145.44           C  
ANISOU  548  CG  GLN A1071    19755  20236  15271   -876   -594     78       C  
ATOM    549  CD  GLN A1071      -4.782 -19.887 -89.319  1.00166.39           C  
ANISOU  549  CD  GLN A1071    22589  22607  18023   -782   -656     94       C  
ATOM    550  OE1 GLN A1071      -4.620 -20.209 -88.140  1.00164.04           O  
ANISOU  550  OE1 GLN A1071    22306  22173  17848   -775   -617     20       O  
ATOM    551  NE2 GLN A1071      -5.584 -18.896 -89.668  1.00157.26           N  
ANISOU  551  NE2 GLN A1071    21577  21367  16809   -688   -753    186       N  
ATOM    552  N   ILE A1072      -1.045 -24.188 -90.039  1.00118.75           N  
ANISOU  552  N   ILE A1072    15879  17304  11936  -1059   -256   -219       N  
ATOM    553  CA  ILE A1072       0.243 -24.841 -89.763  1.00118.38           C  
ANISOU  553  CA  ILE A1072    15729  17374  11876  -1127   -174   -233       C  
ATOM    554  C   ILE A1072       0.781 -25.405 -91.092  1.00126.18           C  
ANISOU  554  C   ILE A1072    16571  18672  12699  -1131   -121   -245       C  
ATOM    555  O   ILE A1072       1.955 -25.209 -91.408  1.00126.84           O  
ANISOU  555  O   ILE A1072    16588  18928  12676  -1237    -95   -130       O  
ATOM    556  CB  ILE A1072       0.158 -25.927 -88.645  1.00119.13           C  
ANISOU  556  CB  ILE A1072    15786  17357  12120  -1041   -103   -408       C  
ATOM    557  CG1 ILE A1072      -0.262 -25.330 -87.293  1.00118.46           C  
ANISOU  557  CG1 ILE A1072    15840  16987  12180  -1040   -150   -386       C  
ATOM    558  CG2 ILE A1072       1.491 -26.654 -88.488  1.00119.21           C  
ANISOU  558  CG2 ILE A1072    15680  17521  12094  -1080    -18   -424       C  
ATOM    559  CD1 ILE A1072      -0.922 -26.313 -86.309  1.00123.68           C  
ANISOU  559  CD1 ILE A1072    16487  17516  12992   -926    -98   -566       C  
ATOM    560  N   ASP A1073      -0.099 -26.039 -91.885  1.00124.97           N  
ANISOU  560  N   ASP A1073    16372  18600  12512  -1020   -112   -374       N  
ATOM    561  CA  ASP A1073       0.214 -26.603 -93.194  1.00127.34           C  
ANISOU  561  CA  ASP A1073    16556  19181  12647   -997    -69   -410       C  
ATOM    562  C   ASP A1073       0.717 -25.526 -94.163  1.00134.59           C  
ANISOU  562  C   ASP A1073    17480  20258  13398  -1112   -118   -198       C  
ATOM    563  O   ASP A1073       1.631 -25.792 -94.948  1.00135.89           O  
ANISOU  563  O   ASP A1073    17534  20685  13411  -1147    -63   -159       O  
ATOM    564  CB  ASP A1073      -1.021 -27.304 -93.775  1.00129.95           C  
ANISOU  564  CB  ASP A1073    16871  19523  12979   -877    -82   -577       C  
ATOM    565  CG  ASP A1073      -1.352 -28.639 -93.129  1.00145.21           C  
ANISOU  565  CG  ASP A1073    18775  21372  15025   -782    -21   -798       C  
ATOM    566  OD1 ASP A1073      -0.401 -29.399 -92.802  1.00146.42           O  
ANISOU  566  OD1 ASP A1073    18874  21580  15178   -767     59   -858       O  
ATOM    567  OD2 ASP A1073      -2.561 -28.956 -93.006  1.00152.09           O1-
ANISOU  567  OD2 ASP A1073    19673  22141  15972   -721    -56   -907       O1-
ATOM    568  N   ASP A1074       0.140 -24.312 -94.089  1.00132.00           N  
ANISOU  568  N   ASP A1074    17291  19774  13088  -1166   -219    -57       N  
ATOM    569  CA  ASP A1074       0.538 -23.172 -94.911  1.00133.94           C  
ANISOU  569  CA  ASP A1074    17588  20120  13185  -1293   -283    166       C  
ATOM    570  C   ASP A1074       1.872 -22.606 -94.429  1.00138.83           C  
ANISOU  570  C   ASP A1074    18212  20761  13774  -1473   -277    335       C  
ATOM    571  O   ASP A1074       2.682 -22.177 -95.245  1.00139.80           O  
ANISOU  571  O   ASP A1074    18282  21102  13734  -1598   -276    491       O  
ATOM    572  CB  ASP A1074      -0.549 -22.086 -94.887  1.00136.56           C  
ANISOU  572  CB  ASP A1074    18097  20240  13549  -1268   -402    253       C  
ATOM    573  CG  ASP A1074      -1.875 -22.519 -95.479  1.00150.29           C  
ANISOU  573  CG  ASP A1074    19811  22006  15289  -1107   -422    118       C  
ATOM    574  OD1 ASP A1074      -1.863 -23.197 -96.538  1.00151.98           O  
ANISOU  574  OD1 ASP A1074    19899  22463  15382  -1071   -381     47       O  
ATOM    575  OD2 ASP A1074      -2.925 -22.140 -94.915  1.00157.04           O1-
ANISOU  575  OD2 ASP A1074    20769  22652  16247  -1016   -484     91       O1-
ATOM    576  N   ALA A1075       2.098 -22.615 -93.103  1.00135.14           N  
ANISOU  576  N   ALA A1075    17802  20087  13458  -1494   -273    307       N  
ATOM    577  CA  ALA A1075       3.333 -22.137 -92.488  1.00135.88           C  
ANISOU  577  CA  ALA A1075    17899  20191  13539  -1673   -275    454       C  
ATOM    578  C   ALA A1075       4.496 -23.112 -92.745  1.00141.91           C  
ANISOU  578  C   ALA A1075    18439  21261  14217  -1680   -158    409       C  
ATOM    579  O   ALA A1075       5.650 -22.680 -92.829  1.00143.42           O  
ANISOU  579  O   ALA A1075    18568  21619  14307  -1850   -154    575       O  
ATOM    580  CB  ALA A1075       3.124 -21.945 -90.995  1.00135.08           C  
ANISOU  580  CB  ALA A1075    17925  19780  13621  -1667   -306    413       C  
ATOM    581  N   LEU A1076       4.187 -24.419 -92.871  1.00137.88           N  
ANISOU  581  N   LEU A1076    17817  20831  13739  -1495    -68    189       N  
ATOM    582  CA  LEU A1076       5.156 -25.484 -93.132  1.00138.29           C  
ANISOU  582  CA  LEU A1076    17678  21159  13707  -1437     46    110       C  
ATOM    583  C   LEU A1076       5.732 -25.399 -94.546  1.00145.07           C  
ANISOU  583  C   LEU A1076    18413  22371  14335  -1475     76    206       C  
ATOM    584  O   LEU A1076       6.923 -25.660 -94.715  1.00146.25           O  
ANISOU  584  O   LEU A1076    18411  22789  14370  -1517    146    268       O  
ATOM    585  CB  LEU A1076       4.514 -26.866 -92.939  1.00137.06           C  
ANISOU  585  CB  LEU A1076    17492  20945  13642  -1224    115   -157       C  
ATOM    586  CG  LEU A1076       4.555 -27.466 -91.547  1.00140.14           C  
ANISOU  586  CG  LEU A1076    17911  21126  14211  -1167    146   -271       C  
ATOM    587  CD1 LEU A1076       3.443 -28.482 -91.380  1.00139.26           C  
ANISOU  587  CD1 LEU A1076    17841  20863  14207   -999    167   -502       C  
ATOM    588  CD2 LEU A1076       5.916 -28.105 -91.252  1.00142.60           C  
ANISOU  588  CD2 LEU A1076    18079  21638  14464  -1156    236   -269       C  
ATOM    589  N   LYS A1077       4.891 -25.055 -95.559  1.00142.19           N  
ANISOU  589  N   LYS A1077    18103  22029  13894  -1450     27    218       N  
ATOM    590  CA  LYS A1077       5.307 -24.953 -96.961  1.00143.75           C  
ANISOU  590  CA  LYS A1077    18196  22559  13863  -1478     50    306       C  
ATOM    591  C   LYS A1077       6.345 -23.839 -97.152  1.00149.25           C  
ANISOU  591  C   LYS A1077    18869  23405  14435  -1715     16    589       C  
ATOM    592  O   LYS A1077       7.288 -24.024 -97.918  1.00149.87           O  
ANISOU  592  O   LYS A1077    18784  23836  14325  -1753     83    666       O  
ATOM    593  CB  LYS A1077       4.104 -24.790 -97.911  1.00146.33           C  
ANISOU  593  CB  LYS A1077    18599  22854  14145  -1402     -8    260       C  
ATOM    594  CG  LYS A1077       3.373 -23.458 -97.944  1.00159.73           C  
ANISOU  594  CG  LYS A1077    20473  24347  15872  -1507   -136    426       C  
ATOM    595  CD  LYS A1077       2.143 -23.580 -98.826  1.00169.42           C  
ANISOU  595  CD  LYS A1077    21739  25572  17059  -1382   -180    335       C  
ATOM    596  CE  LYS A1077       1.226 -22.391 -98.742  1.00179.66           C  
ANISOU  596  CE  LYS A1077    23223  26635  18406  -1422   -307    460       C  
ATOM    597  NZ  LYS A1077      -0.069 -22.662 -99.421  1.00188.34           N1+
ANISOU  597  NZ  LYS A1077    24338  27731  19490  -1273   -346    341       N1+
ATOM    598  N   LEU A1078       6.208 -22.731 -96.401  1.00146.20           N  
ANISOU  598  N   LEU A1078    18648  22755  14147  -1874    -86    739       N  
ATOM    599  CA  LEU A1078       7.134 -21.600 -96.422  1.00147.93           C  
ANISOU  599  CA  LEU A1078    18890  23051  14266  -2139   -143   1015       C  
ATOM    600  C   LEU A1078       8.460 -21.983 -95.754  1.00152.37           C  
ANISOU  600  C   LEU A1078    19290  23789  14813  -2225    -71   1052       C  
ATOM    601  O   LEU A1078       9.505 -21.516 -96.197  1.00152.95           O  
ANISOU  601  O   LEU A1078    19255  24136  14722  -2413    -64   1254       O  
ATOM    602  CB  LEU A1078       6.511 -20.369 -95.748  1.00147.83           C  
ANISOU  602  CB  LEU A1078    19144  22656  14367  -2259   -284   1135       C  
ATOM    603  CG  LEU A1078       5.071 -20.024 -96.173  1.00152.24           C  
ANISOU  603  CG  LEU A1078    19872  23003  14970  -2128   -360   1076       C  
ATOM    604  CD1 LEU A1078       4.457 -18.991 -95.252  1.00152.02           C  
ANISOU  604  CD1 LEU A1078    20110  22574  15076  -2181   -484   1148       C  
ATOM    605  CD2 LEU A1078       4.984 -19.607 -97.644  1.00156.38           C  
ANISOU  605  CD2 LEU A1078    20372  23756  15290  -2168   -383   1202       C  
ATOM    606  N   ALA A1079       8.419 -22.868 -94.732  1.00148.84           N  
ANISOU  606  N   ALA A1079    18814  23212  14526  -2083    -15    863       N  
ATOM    607  CA  ALA A1079       9.604 -23.403 -94.047  1.00149.60           C  
ANISOU  607  CA  ALA A1079    18746  23478  14617  -2112     61    865       C  
ATOM    608  C   ALA A1079      10.324 -24.416 -94.966  1.00156.74           C  
ANISOU  608  C   ALA A1079    19402  24810  15341  -1975    191    796       C  
ATOM    609  O   ALA A1079      11.558 -24.505 -94.950  1.00157.30           O  
ANISOU  609  O   ALA A1079    19288  25185  15292  -2056    247    905       O  
ATOM    610  CB  ALA A1079       9.206 -24.058 -92.727  1.00148.01           C  
ANISOU  610  CB  ALA A1079    18614  22987  14637  -1978     76    677       C  
ATOM    611  N   ASN A1080       9.536 -25.161 -95.781  1.00154.91           N  
ANISOU  611  N   ASN A1080    19170  24610  15078  -1764    234    617       N  
ATOM    612  CA  ASN A1080      10.018 -26.133 -96.771  1.00156.65           C  
ANISOU  612  CA  ASN A1080    19203  25202  15116  -1597    349    522       C  
ATOM    613  C   ASN A1080      10.720 -25.389 -97.920  1.00164.59           C  
ANISOU  613  C   ASN A1080    20093  26568  15874  -1758    348    753       C  
ATOM    614  O   ASN A1080      11.724 -25.875 -98.446  1.00166.09           O  
ANISOU  614  O   ASN A1080    20071  27154  15879  -1710    446    781       O  
ATOM    615  CB  ASN A1080       8.860 -27.005 -97.316  1.00156.07           C  
ANISOU  615  CB  ASN A1080    19204  25016  15078  -1364    366    274       C  
ATOM    616  CG  ASN A1080       8.254 -28.006 -96.347  1.00174.76           C  
ANISOU  616  CG  ASN A1080    21650  27102  17648  -1186    389     28       C  
ATOM    617  OD1 ASN A1080       8.935 -28.837 -95.732  1.00166.30           O  
ANISOU  617  OD1 ASN A1080    20495  26089  16604  -1083    467    -65       O  
ATOM    618  ND2 ASN A1080       6.933 -28.009 -96.260  1.00165.72           N  
ANISOU  618  ND2 ASN A1080    20663  25669  16635  -1135    324    -87       N  
ATOM    619  N   GLU A1081      10.191 -24.197 -98.289  1.00162.21           N  
ANISOU  619  N   GLU A1081    19936  26134  15561  -1944    237    926       N  
ATOM    620  CA  GLU A1081      10.731 -23.316 -99.333  1.00164.64           C  
ANISOU  620  CA  GLU A1081    20180  26729  15646  -2139    212   1177       C  
ATOM    621  C   GLU A1081      12.059 -22.675 -98.885  1.00171.29           C  
ANISOU  621  C   GLU A1081    20907  27765  16411  -2399    208   1421       C  
ATOM    622  O   GLU A1081      12.869 -22.282 -99.731  1.00173.48           O  
ANISOU  622  O   GLU A1081    21038  28414  16463  -2543    233   1618       O  
ATOM    623  CB  GLU A1081       9.714 -22.215 -99.690  1.00165.87           C  
ANISOU  623  CB  GLU A1081    20568  26619  15837  -2254     78   1287       C  
ATOM    624  CG  GLU A1081       8.575 -22.663-100.592  1.00173.79           C  
ANISOU  624  CG  GLU A1081    21627  27590  16816  -2049     79   1123       C  
ATOM    625  CD  GLU A1081       7.233 -22.000-100.332  1.00187.97           C  
ANISOU  625  CD  GLU A1081    23672  28981  18765  -2041    -45   1103       C  
ATOM    626  OE1 GLU A1081       7.200 -20.772-100.087  1.00172.76           O1-
ANISOU  626  OE1 GLU A1081    21903  26878  16858  -2241   -154   1313       O1-
ATOM    627  OE2 GLU A1081       6.205 -22.712-100.388  1.00182.61           O  
ANISOU  627  OE2 GLU A1081    23036  28168  18177  -1831    -37    879       O  
ATOM    628  N   GLY A1082      12.251 -22.570 -97.567  1.00167.13           N  
ANISOU  628  N   GLY A1082    20444  26996  16062  -2466    173   1411       N  
ATOM    629  CA  GLY A1082      13.444 -21.991 -96.956  1.00168.42           C  
ANISOU  629  CA  GLY A1082    20514  27301  16179  -2723    153   1625       C  
ATOM    630  C   GLY A1082      13.312 -20.527 -96.577  1.00173.28           C  
ANISOU  630  C   GLY A1082    21353  27647  16840  -3042     -5   1858       C  
ATOM    631  O   GLY A1082      14.323 -19.880 -96.284  1.00174.70           O  
ANISOU  631  O   GLY A1082    21465  27976  16938  -3319    -42   2080       O  
ATOM    632  N   LYS A1083      12.065 -19.991 -96.579  1.00168.47           N  
ANISOU  632  N   LYS A1083    21016  26643  16352  -3006   -104   1812       N  
ATOM    633  CA  LYS A1083      11.766 -18.594 -96.236  1.00168.65           C  
ANISOU  633  CA  LYS A1083    21312  26346  16421  -3259   -265   2009       C  
ATOM    634  C   LYS A1083      11.239 -18.500 -94.799  1.00169.98           C  
ANISOU  634  C   LYS A1083    21680  26069  16836  -3217   -330   1892       C  
ATOM    635  O   LYS A1083      10.088 -18.850 -94.524  1.00167.78           O  
ANISOU  635  O   LYS A1083    21531  25505  16711  -2988   -336   1693       O  
ATOM    636  CB  LYS A1083      10.790 -17.922 -97.236  1.00171.60           C  
ANISOU  636  CB  LYS A1083    21865  26601  16732  -3244   -341   2069       C  
ATOM    637  CG  LYS A1083      10.011 -18.863 -98.156  1.00178.77           C  
ANISOU  637  CG  LYS A1083    22677  27639  17607  -2945   -252   1861       C  
ATOM    638  CD  LYS A1083       8.757 -18.209 -98.714  1.00184.38           C  
ANISOU  638  CD  LYS A1083    23620  28098  18337  -2887   -352   1871       C  
ATOM    639  CE  LYS A1083       8.871 -17.852-100.173  1.00191.05           C  
ANISOU  639  CE  LYS A1083    24405  29238  18947  -2954   -352   2023       C  
ATOM    640  NZ  LYS A1083       7.595 -17.298-100.696  1.00196.89           N1+
ANISOU  640  NZ  LYS A1083    25362  29739  19708  -2862   -449   2016       N1+
ATOM    641  N   VAL A1084      12.108 -18.033 -93.888  1.00166.67           N  
ANISOU  641  N   VAL A1084    21272  25616  16439  -3445   -379   2022       N  
ATOM    642  CA  VAL A1084      11.840 -17.886 -92.452  1.00164.79           C  
ANISOU  642  CA  VAL A1084    21210  24997  16407  -3443   -442   1939       C  
ATOM    643  C   VAL A1084      11.095 -16.577 -92.131  1.00169.10           C  
ANISOU  643  C   VAL A1084    22124  25109  17019  -3579   -611   2050       C  
ATOM    644  O   VAL A1084      10.632 -16.410 -91.006  1.00167.07           O  
ANISOU  644  O   VAL A1084    22054  24495  16932  -3532   -669   1960       O  
ATOM    645  CB  VAL A1084      13.136 -18.003 -91.602  1.00169.36           C  
ANISOU  645  CB  VAL A1084    21632  25750  16968  -3623   -423   2024       C  
ATOM    646  CG1 VAL A1084      13.767 -19.376 -91.756  1.00168.62           C  
ANISOU  646  CG1 VAL A1084    21202  26037  16830  -3419   -255   1880       C  
ATOM    647  CG2 VAL A1084      14.143 -16.900 -91.933  1.00172.15           C  
ANISOU  647  CG2 VAL A1084    21984  26282  17142  -4022   -515   2344       C  
ATOM    648  N   LYS A1085      11.007 -15.649 -93.094  1.00168.17           N  
ANISOU  648  N   LYS A1085    22119  25022  16756  -3741   -692   2248       N  
ATOM    649  CA  LYS A1085      10.321 -14.374 -92.896  1.00168.86           C  
ANISOU  649  CA  LYS A1085    22580  24700  16879  -3854   -860   2366       C  
ATOM    650  C   LYS A1085       8.806 -14.578 -92.911  1.00170.91           C  
ANISOU  650  C   LYS A1085    22997  24667  17272  -3531   -866   2164       C  
ATOM    651  O   LYS A1085       8.135 -14.136 -91.978  1.00169.30           O  
ANISOU  651  O   LYS A1085    23047  24068  17213  -3469   -950   2101       O  
ATOM    652  CB  LYS A1085      10.744 -13.354 -93.966  1.00174.59           C  
ANISOU  652  CB  LYS A1085    23377  25567  17392  -4130   -944   2654       C  
ATOM    653  N   GLU A1086       8.283 -15.278 -93.953  1.00167.40           N  
ANISOU  653  N   GLU A1086    22394  24439  16771  -3322   -775   2058       N  
ATOM    654  CA  GLU A1086       6.858 -15.576 -94.168  1.00165.86           C  
ANISOU  654  CA  GLU A1086    22292  24056  16673  -3023   -772   1872       C  
ATOM    655  C   GLU A1086       6.330 -16.660 -93.222  1.00167.49           C  
ANISOU  655  C   GLU A1086    22419  24145  17076  -2771   -687   1593       C  
ATOM    656  O   GLU A1086       5.166 -16.590 -92.819  1.00165.86           O  
ANISOU  656  O   GLU A1086    22372  23653  16996  -2585   -728   1469       O  
ATOM    657  CB  GLU A1086       6.600 -16.004 -95.618  1.00167.89           C  
ANISOU  657  CB  GLU A1086    22389  24621  16783  -2920   -708   1859       C  
ATOM    658  CG  GLU A1086       6.729 -14.877 -96.625  1.00181.36           C  
ANISOU  658  CG  GLU A1086    24224  26380  18305  -3115   -806   2120       C  
ATOM    659  CD  GLU A1086       8.011 -14.888 -97.434  1.00202.17           C  
ANISOU  659  CD  GLU A1086    26644  29443  20730  -3344   -751   2305       C  
ATOM    660  OE1 GLU A1086       9.108 -14.845 -96.830  1.00194.49           O1-
ANISOU  660  OE1 GLU A1086    25583  28571  19745  -3548   -737   2397       O1-
ATOM    661  OE2 GLU A1086       7.913 -14.917 -98.682  1.00197.49           O  
ANISOU  661  OE2 GLU A1086    25964  29099  19974  -3322   -725   2365       O  
ATOM    662  N   ALA A1087       7.168 -17.672 -92.901  1.00163.17           N  
ANISOU  662  N   ALA A1087    21622  23833  16541  -2757   -568   1500       N  
ATOM    663  CA  ALA A1087       6.827 -18.772 -91.995  1.00160.35           C  
ANISOU  663  CA  ALA A1087    21183  23387  16357  -2542   -483   1251       C  
ATOM    664  C   ALA A1087       6.705 -18.272 -90.540  1.00163.21           C  
ANISOU  664  C   ALA A1087    21745  23390  16880  -2591   -559   1244       C  
ATOM    665  O   ALA A1087       5.825 -18.729 -89.812  1.00160.94           O  
ANISOU  665  O   ALA A1087    21520  22879  16751  -2393   -543   1059       O  
ATOM    666  CB  ALA A1087       7.867 -19.878 -92.098  1.00160.91           C  
ANISOU  666  CB  ALA A1087    20960  23811  16369  -2520   -348   1185       C  
ATOM    667  N   GLN A1088       7.567 -17.316 -90.136  1.00161.38           N  
ANISOU  667  N   GLN A1088    21617  23106  16594  -2864   -647   1450       N  
ATOM    668  CA  GLN A1088       7.557 -16.691 -88.808  1.00160.95           C  
ANISOU  668  CA  GLN A1088    21782  22712  16659  -2947   -739   1469       C  
ATOM    669  C   GLN A1088       6.338 -15.766 -88.662  1.00164.34           C  
ANISOU  669  C   GLN A1088    22535  22756  17148  -2860   -858   1473       C  
ATOM    670  O   GLN A1088       5.772 -15.661 -87.570  1.00162.10           O  
ANISOU  670  O   GLN A1088    22415  22169  17008  -2756   -894   1370       O  
ATOM    671  CB  GLN A1088       8.856 -15.894 -88.597  1.00164.55           C  
ANISOU  671  CB  GLN A1088    22261  23253  17006  -3298   -813   1706       C  
ATOM    672  CG  GLN A1088       9.558 -16.143 -87.264  1.00182.37           C  
ANISOU  672  CG  GLN A1088    24488  25445  19358  -3375   -808   1667       C  
ATOM    673  CD  GLN A1088      11.005 -15.683 -87.256  1.00202.89           C  
ANISOU  673  CD  GLN A1088    26989  28279  21819  -3719   -847   1890       C  
ATOM    674  OE1 GLN A1088      11.920 -16.455 -86.948  1.00198.55           O  
ANISOU  674  OE1 GLN A1088    26180  28006  21256  -3740   -757   1862       O  
ATOM    675  NE2 GLN A1088      11.253 -14.413 -87.567  1.00195.02           N  
ANISOU  675  NE2 GLN A1088    26203  27181  20712  -4001   -988   2124       N  
ATOM    676  N   ALA A1089       5.948 -15.099 -89.775  1.00162.85           N  
ANISOU  676  N   ALA A1089    22439  22598  16840  -2889   -918   1595       N  
ATOM    677  CA  ALA A1089       4.811 -14.176 -89.874  1.00163.52           C  
ANISOU  677  CA  ALA A1089    22822  22366  16942  -2788  -1034   1623       C  
ATOM    678  C   ALA A1089       3.466 -14.918 -89.937  1.00166.36           C  
ANISOU  678  C   ALA A1089    23128  22672  17408  -2445   -970   1395       C  
ATOM    679  O   ALA A1089       2.458 -14.378 -89.477  1.00166.10           O  
ANISOU  679  O   ALA A1089    23321  22339  17449  -2296  -1046   1353       O  
ATOM    680  CB  ALA A1089       4.965 -13.286 -91.096  1.00166.62           C  
ANISOU  680  CB  ALA A1089    23306  22852  17151  -2945  -1114   1845       C  
ATOM    681  N   ALA A1090       3.446 -16.145 -90.509  1.00161.54           N  
ANISOU  681  N   ALA A1090    22224  22357  16796  -2319   -836   1251       N  
ATOM    682  CA  ALA A1090       2.242 -16.981 -90.586  1.00159.44           C  
ANISOU  682  CA  ALA A1090    21880  22076  16624  -2031   -774   1032       C  
ATOM    683  C   ALA A1090       1.840 -17.469 -89.190  1.00160.53           C  
ANISOU  683  C   ALA A1090    22050  21996  16950  -1901   -743    861       C  
ATOM    684  O   ALA A1090       0.658 -17.723 -88.955  1.00158.86           O  
ANISOU  684  O   ALA A1090    21874  21658  16828  -1685   -739    722       O  
ATOM    685  CB  ALA A1090       2.476 -18.164 -91.510  1.00159.84           C  
ANISOU  685  CB  ALA A1090    21639  22483  16610  -1966   -649    928       C  
ATOM    686  N   ALA A1091       2.834 -17.569 -88.264  1.00156.46           N  
ANISOU  686  N   ALA A1091    21513  21453  16480  -2041   -725    884       N  
ATOM    687  CA  ALA A1091       2.683 -17.960 -86.857  1.00154.51           C  
ANISOU  687  CA  ALA A1091    21304  21008  16395  -1959   -700    751       C  
ATOM    688  C   ALA A1091       1.864 -16.921 -86.074  1.00158.75           C  
ANISOU  688  C   ALA A1091    22147  21176  16996  -1899   -816    779       C  
ATOM    689  O   ALA A1091       1.268 -17.268 -85.048  1.00156.70           O  
ANISOU  689  O   ALA A1091    21926  20745  16869  -1748   -793    637       O  
ATOM    690  CB  ALA A1091       4.048 -18.140 -86.212  1.00155.23           C  
ANISOU  690  CB  ALA A1091    21311  21189  16482  -2152   -673    811       C  
ATOM    691  N   GLU A1092       1.845 -15.648 -86.557  1.00157.32           N  
ANISOU  691  N   GLU A1092    22193  20873  16709  -2009   -943    964       N  
ATOM    692  CA  GLU A1092       1.043 -14.564 -85.974  1.00157.62           C  
ANISOU  692  CA  GLU A1092    22557  20555  16775  -1925  -1066   1001       C  
ATOM    693  C   GLU A1092      -0.442 -14.877 -86.187  1.00158.89           C  
ANISOU  693  C   GLU A1092    22701  20680  16991  -1617  -1040    856       C  
ATOM    694  O   GLU A1092      -1.244 -14.670 -85.277  1.00157.84           O  
ANISOU  694  O   GLU A1092    22710  20313  16947  -1445  -1067    769       O  
ATOM    695  CB  GLU A1092       1.431 -13.213 -86.613  1.00161.75           C  
ANISOU  695  CB  GLU A1092    23326  20981  17151  -2123  -1207   1242       C  
ATOM    696  CG  GLU A1092       0.610 -12.005 -86.174  1.00176.52           C  
ANISOU  696  CG  GLU A1092    25577  22473  19018  -2020  -1349   1294       C  
ATOM    697  CD  GLU A1092       0.795 -10.738 -86.995  1.00203.58           C  
ANISOU  697  CD  GLU A1092    29262  25799  22289  -2176  -1490   1526       C  
ATOM    698  OE1 GLU A1092       0.971 -10.841 -88.232  1.00202.26           O  
ANISOU  698  OE1 GLU A1092    28957  25881  22013  -2247  -1468   1616       O  
ATOM    699  OE2 GLU A1092       0.724  -9.635 -86.404  1.00197.65           O1-
ANISOU  699  OE2 GLU A1092    28872  24709  21517  -2219  -1628   1616       O1-
ATOM    700  N   GLN A1093      -0.800 -15.390 -87.384  1.00154.13           N  
ANISOU  700  N   GLN A1093    21912  20326  16323  -1549   -988    832       N  
ATOM    701  CA  GLN A1093      -2.168 -15.787 -87.731  1.00152.44           C  
ANISOU  701  CA  GLN A1093    21635  20143  16143  -1284   -963    701       C  
ATOM    702  C   GLN A1093      -2.602 -17.013 -86.881  1.00151.75           C  
ANISOU  702  C   GLN A1093    21366  20086  16207  -1139   -850    478       C  
ATOM    703  O   GLN A1093      -3.796 -17.184 -86.632  1.00150.26           O  
ANISOU  703  O   GLN A1093    21179  19834  16078   -923   -846    368       O  
ATOM    704  CB  GLN A1093      -2.264 -16.089 -89.237  1.00154.40           C  
ANISOU  704  CB  GLN A1093    21721  20674  16270  -1291   -938    734       C  
ATOM    705  CG  GLN A1093      -3.675 -15.970 -89.813  1.00173.52           C  
ANISOU  705  CG  GLN A1093    24160  23100  18671  -1058   -972    681       C  
ATOM    706  CD  GLN A1093      -3.811 -16.552 -91.210  1.00200.21           C  
ANISOU  706  CD  GLN A1093    27338  26788  21946  -1050   -929    666       C  
ATOM    707  OE1 GLN A1093      -3.180 -17.554 -91.569  1.00197.26           O  
ANISOU  707  OE1 GLN A1093    26742  26646  21563  -1128   -829    591       O  
ATOM    708  NE2 GLN A1093      -4.689 -15.968 -92.021  1.00194.18           N  
ANISOU  708  NE2 GLN A1093    26649  26036  21092   -933  -1003    726       N  
ATOM    709  N   LEU A1094      -1.624 -17.831 -86.413  1.00145.91           N  
ANISOU  709  N   LEU A1094    20475  19445  15519  -1259   -763    423       N  
ATOM    710  CA  LEU A1094      -1.841 -19.022 -85.584  1.00143.26           C  
ANISOU  710  CA  LEU A1094    19983  19131  15317  -1154   -658    230       C  
ATOM    711  C   LEU A1094      -2.114 -18.668 -84.120  1.00145.85           C  
ANISOU  711  C   LEU A1094    20476  19183  15759  -1092   -687    191       C  
ATOM    712  O   LEU A1094      -2.912 -19.347 -83.470  1.00143.86           O  
ANISOU  712  O   LEU A1094    20158  18891  15611   -931   -631     39       O  
ATOM    713  CB  LEU A1094      -0.642 -19.967 -85.667  1.00142.55           C  
ANISOU  713  CB  LEU A1094    19691  19250  15220  -1287   -562    200       C  
ATOM    714  CG  LEU A1094      -0.673 -20.968 -86.806  1.00146.84           C  
ANISOU  714  CG  LEU A1094    20009  20081  15701  -1247   -480    119       C  
ATOM    715  CD1 LEU A1094       0.710 -21.468 -87.124  1.00147.14           C  
ANISOU  715  CD1 LEU A1094    19896  20340  15669  -1395   -415    162       C  
ATOM    716  CD2 LEU A1094      -1.588 -22.124 -86.484  1.00147.88           C  
ANISOU  716  CD2 LEU A1094    20024  20222  15940  -1070   -404    -91       C  
ATOM    717  N   LYS A1095      -1.448 -17.615 -83.601  1.00143.29           N  
ANISOU  717  N   LYS A1095    20369  18671  15403  -1229   -778    329       N  
ATOM    718  CA  LYS A1095      -1.617 -17.115 -82.229  1.00142.42           C  
ANISOU  718  CA  LYS A1095    20459  18280  15374  -1183   -825    307       C  
ATOM    719  C   LYS A1095      -3.014 -16.496 -82.034  1.00145.90           C  
ANISOU  719  C   LYS A1095    21068  18539  15827   -942   -884    272       C  
ATOM    720  O   LYS A1095      -3.552 -16.535 -80.928  1.00145.06           O  
ANISOU  720  O   LYS A1095    21036  18272  15806   -805   -874    179       O  
ATOM    721  CB  LYS A1095      -0.540 -16.073 -81.885  1.00145.79           C  
ANISOU  721  CB  LYS A1095    21100  18557  15738  -1416   -928    477       C  
ATOM    722  CG  LYS A1095       0.826 -16.643 -81.535  1.00153.58           C  
ANISOU  722  CG  LYS A1095    21936  19682  16736  -1630   -873    498       C  
ATOM    723  CD  LYS A1095       1.800 -15.527 -81.151  1.00161.82           C  
ANISOU  723  CD  LYS A1095    23205  20572  17708  -1880   -995    675       C  
ATOM    724  CE  LYS A1095       3.181 -16.034 -80.814  1.00164.97           C  
ANISOU  724  CE  LYS A1095    23436  21143  18101  -2099   -949    713       C  
ATOM    725  NZ  LYS A1095       4.117 -14.922 -80.515  1.00169.59           N1+
ANISOU  725  NZ  LYS A1095    24233  21602  18603  -2379  -1080    900       N1+
ATOM    726  N   THR A1096      -3.588 -15.927 -83.108  1.00142.83           N  
ANISOU  726  N   THR A1096    20734  18194  15342   -881   -943    349       N  
ATOM    727  CA  THR A1096      -4.911 -15.304 -83.101  1.00143.40           C  
ANISOU  727  CA  THR A1096    20949  18138  15398   -633  -1003    332       C  
ATOM    728  C   THR A1096      -6.021 -16.361 -83.193  1.00145.95           C  
ANISOU  728  C   THR A1096    21026  18639  15789   -427   -906    163       C  
ATOM    729  O   THR A1096      -7.070 -16.186 -82.571  1.00145.64           O  
ANISOU  729  O   THR A1096    21048  18500  15788   -207   -916     94       O  
ATOM    730  CB  THR A1096      -5.039 -14.284 -84.246  1.00155.97           C  
ANISOU  730  CB  THR A1096    22696  19717  16848   -654  -1111    494       C  
ATOM    731  OG1 THR A1096      -4.784 -14.921 -85.501  1.00154.94           O  
ANISOU  731  OG1 THR A1096    22332  19882  16659   -744  -1057    509       O  
ATOM    732  CG2 THR A1096      -4.121 -13.075 -84.067  1.00157.85           C  
ANISOU  732  CG2 THR A1096    23240  19728  17009   -853  -1234    675       C  
ATOM    733  N   THR A1097      -5.790 -17.445 -83.974  1.00141.29           N  
ANISOU  733  N   THR A1097    20164  18317  15201   -501   -816     99       N  
ATOM    734  CA  THR A1097      -6.734 -18.549 -84.224  1.00139.41           C  
ANISOU  734  CA  THR A1097    19685  18270  15013   -362   -732    -56       C  
ATOM    735  C   THR A1097      -7.005 -19.353 -82.946  1.00140.78           C  
ANISOU  735  C   THR A1097    19784  18383  15323   -291   -652   -202       C  
ATOM    736  O   THR A1097      -8.158 -19.706 -82.705  1.00139.41           O  
ANISOU  736  O   THR A1097    19531  18249  15190   -118   -627   -298       O  
ATOM    737  CB  THR A1097      -6.207 -19.432 -85.370  1.00143.55           C  
ANISOU  737  CB  THR A1097    19992  19063  15487   -485   -671    -79       C  
ATOM    738  OG1 THR A1097      -6.104 -18.621 -86.542  1.00143.63           O  
ANISOU  738  OG1 THR A1097    20078  19136  15361   -531   -748     64       O  
ATOM    739  CG2 THR A1097      -7.096 -20.640 -85.667  1.00140.38           C  
ANISOU  739  CG2 THR A1097    19361  18850  15128   -380   -594   -243       C  
ATOM    740  N   ARG A1098      -5.964 -19.631 -82.131  1.00136.96           N  
ANISOU  740  N   ARG A1098    19318  17819  14902   -427   -613   -210       N  
ATOM    741  CA  ARG A1098      -6.119 -20.388 -80.886  1.00135.92           C  
ANISOU  741  CA  ARG A1098    19127  17623  14893   -374   -538   -337       C  
ATOM    742  C   ARG A1098      -6.966 -19.605 -79.880  1.00142.57           C  
ANISOU  742  C   ARG A1098    20150  18257  15763   -199   -588   -340       C  
ATOM    743  O   ARG A1098      -7.655 -20.215 -79.063  1.00141.94           O  
ANISOU  743  O   ARG A1098    19991  18176  15765    -82   -527   -453       O  
ATOM    744  CB  ARG A1098      -4.766 -20.811 -80.280  1.00134.50           C  
ANISOU  744  CB  ARG A1098    18928  17417  14758   -551   -495   -333       C  
ATOM    745  CG  ARG A1098      -3.831 -19.701 -79.838  1.00143.67           C  
ANISOU  745  CG  ARG A1098    20311  18400  15879   -683   -581   -194       C  
ATOM    746  CD  ARG A1098      -3.004 -20.151 -78.652  1.00152.18           C  
ANISOU  746  CD  ARG A1098    21381  19402  17037   -767   -536   -236       C  
ATOM    747  NE  ARG A1098      -1.794 -19.342 -78.499  1.00162.54           N  
ANISOU  747  NE  ARG A1098    22834  20631  18292   -970   -610    -96       N  
ATOM    748  CZ  ARG A1098      -1.702 -18.262 -77.730  1.00175.06           C  
ANISOU  748  CZ  ARG A1098    24681  21971  19862   -994   -709    -22       C  
ATOM    749  NH1 ARG A1098      -2.741 -17.855 -77.012  1.00161.11           N1+
ANISOU  749  NH1 ARG A1098    23062  20020  18131   -797   -736    -81       N1+
ATOM    750  NH2 ARG A1098      -0.563 -17.582 -77.669  1.00160.80           N  
ANISOU  750  NH2 ARG A1098    22992  20112  17995  -1217   -783    112       N  
ATOM    751  N   ASN A1099      -6.938 -18.264 -79.974  1.00141.75           N  
ANISOU  751  N   ASN A1099    20296  17984  15580   -176   -700   -213       N  
ATOM    752  CA  ASN A1099      -7.716 -17.356 -79.137  1.00143.17           C  
ANISOU  752  CA  ASN A1099    20693  17952  15752     17   -764   -206       C  
ATOM    753  C   ASN A1099      -9.173 -17.270 -79.614  1.00149.92           C  
ANISOU  753  C   ASN A1099    21481  18912  16569    263   -771   -242       C  
ATOM    754  O   ASN A1099     -10.103 -17.376 -78.805  1.00149.26           O  
ANISOU  754  O   ASN A1099    21381  18805  16524    461   -742   -323       O  
ATOM    755  CB  ASN A1099      -7.092 -15.946 -79.150  1.00145.11           C  
ANISOU  755  CB  ASN A1099    21265  17961  15910    -59   -895    -52       C  
ATOM    756  CG  ASN A1099      -5.689 -15.814 -78.590  1.00165.51           C  
ANISOU  756  CG  ASN A1099    23946  20429  18513   -309   -913      6       C  
ATOM    757  OD1 ASN A1099      -5.001 -16.794 -78.282  1.00159.10           O  
ANISOU  757  OD1 ASN A1099    22943  19733  17774   -437   -824    -58       O  
ATOM    758  ND2 ASN A1099      -5.228 -14.580 -78.458  1.00157.77           N  
ANISOU  758  ND2 ASN A1099    23272  19218  17455   -386  -1039    134       N  
ATOM    759  N   ALA A1100      -9.360 -16.998 -80.923  1.00149.18           N  
ANISOU  759  N   ALA A1100    21354  18943  16384    254   -817   -168       N  
ATOM    760  CA  ALA A1100     -10.642 -16.769 -81.591  1.00150.87           C  
ANISOU  760  CA  ALA A1100    21514  19278  16532    471   -847   -171       C  
ATOM    761  C   ALA A1100     -11.579 -17.996 -81.663  1.00155.57           C  
ANISOU  761  C   ALA A1100    21797  20126  17185    553   -749   -312       C  
ATOM    762  O   ALA A1100     -12.770 -17.808 -81.940  1.00156.60           O  
ANISOU  762  O   ALA A1100    21870  20363  17266    758   -772   -323       O  
ATOM    763  CB  ALA A1100     -10.391 -16.254 -83.002  1.00152.84           C  
ANISOU  763  CB  ALA A1100    21801  19606  16666    393   -918    -49       C  
ATOM    764  N   TYR A1101     -11.071 -19.233 -81.452  1.00150.97           N  
ANISOU  764  N   TYR A1101    21021  19648  16694    397   -650   -411       N  
ATOM    765  CA  TYR A1101     -11.922 -20.419 -81.584  1.00150.17           C  
ANISOU  765  CA  TYR A1101    20649  19772  16638    438   -571   -538       C  
ATOM    766  C   TYR A1101     -11.805 -21.436 -80.437  1.00151.65           C  
ANISOU  766  C   TYR A1101    20734  19936  16948    392   -472   -656       C  
ATOM    767  O   TYR A1101     -12.836 -21.949 -80.004  1.00151.84           O  
ANISOU  767  O   TYR A1101    20626  20060  17006    504   -431   -736       O  
ATOM    768  CB  TYR A1101     -11.626 -21.155 -82.908  1.00151.76           C  
ANISOU  768  CB  TYR A1101    20680  20186  16796    295   -553   -555       C  
ATOM    769  CG  TYR A1101     -11.703 -20.301 -84.158  1.00156.02           C  
ANISOU  769  CG  TYR A1101    21290  20785  17206    317   -642   -438       C  
ATOM    770  CD1 TYR A1101     -12.917 -20.084 -84.805  1.00159.52           C  
ANISOU  770  CD1 TYR A1101    21658  21377  17576    481   -686   -433       C  
ATOM    771  CD2 TYR A1101     -10.555 -19.756 -84.725  1.00157.25           C  
ANISOU  771  CD2 TYR A1101    21572  20872  17302    165   -682   -326       C  
ATOM    772  CE1 TYR A1101     -12.991 -19.314 -85.966  1.00162.08           C  
ANISOU  772  CE1 TYR A1101    22051  21758  17773    507   -771   -321       C  
ATOM    773  CE2 TYR A1101     -10.616 -18.983 -85.883  1.00159.77           C  
ANISOU  773  CE2 TYR A1101    21962  21249  17495    174   -764   -208       C  
ATOM    774  CZ  TYR A1101     -11.836 -18.768 -86.504  1.00169.41           C  
ANISOU  774  CZ  TYR A1101    23122  22598  18647    351   -808   -208       C  
ATOM    775  OH  TYR A1101     -11.901 -18.003 -87.644  1.00173.22           O  
ANISOU  775  OH  TYR A1101    23682  23136  18998    368   -892    -86       O  
ATOM    776  N   ILE A1102     -10.572 -21.772 -79.993  1.00145.44           N  
ANISOU  776  N   ILE A1102    19994  19046  16220    222   -435   -661       N  
ATOM    777  CA  ILE A1102     -10.310 -22.827 -78.999  1.00142.73           C  
ANISOU  777  CA  ILE A1102    19557  18685  15989    160   -342   -767       C  
ATOM    778  C   ILE A1102     -10.202 -22.304 -77.548  1.00144.27           C  
ANISOU  778  C   ILE A1102    19913  18668  16237    232   -343   -760       C  
ATOM    779  O   ILE A1102     -10.614 -23.020 -76.630  1.00143.26           O  
ANISOU  779  O   ILE A1102    19700  18548  16185    273   -273   -848       O  
ATOM    780  CB  ILE A1102      -9.033 -23.617 -79.400  1.00144.70           C  
ANISOU  780  CB  ILE A1102    19739  18981  16259    -45   -295   -785       C  
ATOM    781  CG1 ILE A1102      -9.188 -24.263 -80.786  1.00145.04           C  
ANISOU  781  CG1 ILE A1102    19623  19243  16244   -101   -286   -816       C  
ATOM    782  CG2 ILE A1102      -8.676 -24.678 -78.368  1.00144.55           C  
ANISOU  782  CG2 ILE A1102    19649  18925  16348    -99   -206   -885       C  
ATOM    783  CD1 ILE A1102      -7.914 -24.329 -81.559  1.00151.52           C  
ANISOU  783  CD1 ILE A1102    20448  20112  17013   -256   -285   -764       C  
ATOM    784  N   GLN A1103      -9.652 -21.089 -77.341  1.00139.66           N  
ANISOU  784  N   GLN A1103    19567  17893  15604    237   -424   -655       N  
ATOM    785  CA  GLN A1103      -9.455 -20.470 -76.022  1.00138.64           C  
ANISOU  785  CA  GLN A1103    19632  17540  15504    296   -444   -644       C  
ATOM    786  C   GLN A1103     -10.714 -20.498 -75.148  1.00140.17           C  
ANISOU  786  C   GLN A1103    19801  17739  15718    524   -413   -714       C  
ATOM    787  O   GLN A1103     -10.605 -20.666 -73.931  1.00138.90           O  
ANISOU  787  O   GLN A1103    19688  17475  15614    550   -374   -761       O  
ATOM    788  CB  GLN A1103      -8.975 -19.023 -76.175  1.00141.48           C  
ANISOU  788  CB  GLN A1103    20280  17700  15777    291   -565   -515       C  
ATOM    789  CG  GLN A1103      -8.056 -18.541 -75.055  1.00163.30           C  
ANISOU  789  CG  GLN A1103    23251  20231  18565    206   -596   -487       C  
ATOM    790  CD  GLN A1103      -6.963 -19.520 -74.694  1.00185.78           C  
ANISOU  790  CD  GLN A1103    25964  23131  21491      0   -522   -527       C  
ATOM    791  OE1 GLN A1103      -7.025 -20.195 -73.663  1.00178.77           O  
ANISOU  791  OE1 GLN A1103    25012  22228  20684     30   -450   -615       O  
ATOM    792  NE2 GLN A1103      -5.948 -19.627 -75.540  1.00181.93           N  
ANISOU  792  NE2 GLN A1103    25427  22723  20973   -201   -535   -458       N  
ATOM    793  N   LYS A1104     -11.898 -20.367 -75.782  1.00135.84           N  
ANISOU  793  N   LYS A1104    19161  17340  15114    687   -427   -718       N  
ATOM    794  CA  LYS A1104     -13.234 -20.403 -75.170  1.00135.31           C  
ANISOU  794  CA  LYS A1104    19016  17356  15039    917   -396   -772       C  
ATOM    795  C   LYS A1104     -13.459 -21.673 -74.341  1.00136.91           C  
ANISOU  795  C   LYS A1104    19020  17660  15341    863   -283   -880       C  
ATOM    796  O   LYS A1104     -14.185 -21.629 -73.347  1.00137.35           O  
ANISOU  796  O   LYS A1104    19069  17715  15403   1020   -249   -916       O  
ATOM    797  CB  LYS A1104     -14.336 -20.340 -76.258  1.00138.29           C  
ANISOU  797  CB  LYS A1104    19249  17956  15339   1039   -423   -757       C  
ATOM    798  CG  LYS A1104     -14.153 -19.280 -77.346  1.00148.62           C  
ANISOU  798  CG  LYS A1104    20714  19211  16543   1069   -532   -646       C  
ATOM    799  CD  LYS A1104     -15.116 -19.504 -78.510  1.00154.53           C  
ANISOU  799  CD  LYS A1104    21267  20221  17225   1141   -547   -643       C  
ATOM    800  CE  LYS A1104     -15.062 -18.378 -79.514  1.00160.52           C  
ANISOU  800  CE  LYS A1104    22197  20925  17868   1208   -658   -524       C  
ATOM    801  NZ  LYS A1104     -15.930 -18.647 -80.687  1.00167.72           N1+
ANISOU  801  NZ  LYS A1104    22909  22107  18710   1263   -675   -520       N1+
ATOM    802  N   TYR A1105     -12.847 -22.803 -74.772  1.00130.89           N  
ANISOU  802  N   TYR A1105    18102  16987  14643    650   -228   -928       N  
ATOM    803  CA  TYR A1105     -12.991 -24.148 -74.199  1.00128.64           C  
ANISOU  803  CA  TYR A1105    17634  16797  14448    563   -128  -1026       C  
ATOM    804  C   TYR A1105     -11.803 -24.575 -73.334  1.00130.53           C  
ANISOU  804  C   TYR A1105    17951  16877  14766    426    -86  -1048       C  
ATOM    805  O   TYR A1105     -11.938 -25.533 -72.564  1.00128.99           O  
ANISOU  805  O   TYR A1105    17657  16710  14643    388     -8  -1120       O  
ATOM    806  CB  TYR A1105     -13.191 -25.181 -75.336  1.00128.74           C  
ANISOU  806  CB  TYR A1105    17438  17016  14462    437   -104  -1074       C  
ATOM    807  CG  TYR A1105     -14.272 -24.787 -76.322  1.00130.63           C  
ANISOU  807  CG  TYR A1105    17587  17436  14612    549   -155  -1047       C  
ATOM    808  CD1 TYR A1105     -15.619 -24.851 -75.972  1.00133.56           C  
ANISOU  808  CD1 TYR A1105    17831  17957  14960    698   -139  -1069       C  
ATOM    809  CD2 TYR A1105     -13.948 -24.292 -77.582  1.00131.24           C  
ANISOU  809  CD2 TYR A1105    17701  17547  14615    515   -223   -987       C  
ATOM    810  CE1 TYR A1105     -16.617 -24.444 -76.855  1.00135.59           C  
ANISOU  810  CE1 TYR A1105    17994  18399  15124    817   -192  -1036       C  
ATOM    811  CE2 TYR A1105     -14.939 -23.876 -78.472  1.00133.12           C  
ANISOU  811  CE2 TYR A1105    17865  17952  14764    631   -277   -955       C  
ATOM    812  CZ  TYR A1105     -16.272 -23.953 -78.103  1.00140.16           C  
ANISOU  812  CZ  TYR A1105    18625  18994  15634    786   -263   -980       C  
ATOM    813  OH  TYR A1105     -17.260 -23.553 -78.965  1.00139.79           O  
ANISOU  813  OH  TYR A1105    18486  19137  15490    911   -320   -944       O  
ATOM    814  N   LEU A1106     -10.650 -23.884 -73.458  1.00126.80           N  
ANISOU  814  N   LEU A1106    17652  16251  14277    342   -140   -980       N  
ATOM    815  CA  LEU A1106      -9.450 -24.262 -72.715  1.00125.38           C  
ANISOU  815  CA  LEU A1106    17530  15950  14159    205   -109   -990       C  
ATOM    816  C   LEU A1106      -8.831 -23.095 -71.921  1.00129.03           C  
ANISOU  816  C   LEU A1106    18244  16188  14595    230   -177   -919       C  
ATOM    817  O   LEU A1106      -7.750 -22.612 -72.271  1.00127.91           O  
ANISOU  817  O   LEU A1106    18208  15967  14425     97   -232   -846       O  
ATOM    818  CB  LEU A1106      -8.398 -24.892 -73.664  1.00124.82           C  
ANISOU  818  CB  LEU A1106    17376  15958  14091     17    -97   -984       C  
ATOM    819  CG  LEU A1106      -8.764 -26.223 -74.350  1.00128.75           C  
ANISOU  819  CG  LEU A1106    17658  16643  14617    -37    -29  -1073       C  
ATOM    820  CD1 LEU A1106      -7.732 -26.605 -75.364  1.00128.59           C  
ANISOU  820  CD1 LEU A1106    17592  16699  14568   -179    -29  -1058       C  
ATOM    821  CD2 LEU A1106      -8.893 -27.353 -73.353  1.00130.07           C  
ANISOU  821  CD2 LEU A1106    17744  16802  14873    -54     57  -1164       C  
ATOM    822  N   ARG A  41      -9.490 -22.695 -70.808  1.00126.78           N  
ANISOU  822  N   ARG A  41    18051  15807  14312    389   -173   -942       N  
ATOM    823  CA  ARG A  41      -8.995 -21.632 -69.917  1.00127.71           C  
ANISOU  823  CA  ARG A  41    18432  15694  14398    427   -241   -894       C  
ATOM    824  C   ARG A  41      -8.225 -22.243 -68.763  1.00131.29           C  
ANISOU  824  C   ARG A  41    18889  16071  14923    331   -188   -936       C  
ATOM    825  O   ARG A  41      -8.667 -23.240 -68.191  1.00129.64           O  
ANISOU  825  O   ARG A  41    18525  15955  14778    360    -95  -1014       O  
ATOM    826  CB  ARG A  41     -10.124 -20.715 -69.384  1.00129.53           C  
ANISOU  826  CB  ARG A  41    18798  15855  14563    689   -277   -895       C  
ATOM    827  CG  ARG A  41     -10.823 -19.852 -70.445  1.00141.62           C  
ANISOU  827  CG  ARG A  41    20384  17423  16001    817   -354   -835       C  
ATOM    828  CD  ARG A  41     -10.042 -18.612 -70.856  1.00152.45           C  
ANISOU  828  CD  ARG A  41    22037  18589  17298    754   -480   -730       C  
ATOM    829  NE  ARG A  41     -10.519 -18.089 -72.142  1.00164.31           N  
ANISOU  829  NE  ARG A  41    23538  20170  18724    812   -541   -664       N  
ATOM    830  CZ  ARG A  41     -10.095 -16.958 -72.701  1.00178.14           C  
ANISOU  830  CZ  ARG A  41    25531  21765  20391    784   -658   -558       C  
ATOM    831  NH1 ARG A  41      -9.176 -16.210 -72.105  1.00164.25           N1+
ANISOU  831  NH1 ARG A  41    24038  19758  18610    681   -735   -505       N1+
ATOM    832  NH2 ARG A  41     -10.585 -16.573 -73.876  1.00162.69           N  
ANISOU  832  NH2 ARG A  41    23553  19898  18362    845   -706   -499       N  
ATOM    833  N   SER A  42      -7.073 -21.641 -68.425  1.00129.61           N  
ANISOU  833  N   SER A  42    18856  15696  14694    206   -254   -877       N  
ATOM    834  CA  SER A  42      -6.180 -22.090 -67.352  1.00129.38           C  
ANISOU  834  CA  SER A  42    18849  15591  14718    103   -223   -901       C  
ATOM    835  C   SER A  42      -6.014 -21.028 -66.244  1.00135.28           C  
ANISOU  835  C   SER A  42    19872  16109  15418    166   -300   -878       C  
ATOM    836  O   SER A  42      -6.076 -19.824 -66.516  1.00136.64           O  
ANISOU  836  O   SER A  42    20263  16144  15509    207   -406   -813       O  
ATOM    837  CB  SER A  42      -4.810 -22.446 -67.922  1.00132.77           C  
ANISOU  837  CB  SER A  42    19216  16070  15160   -131   -233   -850       C  
ATOM    838  OG  SER A  42      -4.898 -23.393 -68.974  1.00142.10           O  
ANISOU  838  OG  SER A  42    20172  17451  16369   -179   -169   -878       O  
ATOM    839  N   ALA A  43      -5.782 -21.491 -65.003  1.00131.37           N  
ANISOU  839  N   ALA A  43    19381  15565  14967    170   -252   -930       N  
ATOM    840  CA  ALA A  43      -5.566 -20.651 -63.822  1.00132.10           C  
ANISOU  840  CA  ALA A  43    19729  15449  15016    222   -317   -926       C  
ATOM    841  C   ALA A  43      -4.188 -20.930 -63.211  1.00135.72           C  
ANISOU  841  C   ALA A  43    20211  15854  15502     12   -333   -903       C  
ATOM    842  O   ALA A  43      -3.726 -22.071 -63.258  1.00134.79           O  
ANISOU  842  O   ALA A  43    19880  15878  15457    -86   -249   -928       O  
ATOM    843  CB  ALA A  43      -6.661 -20.900 -62.796  1.00132.87           C  
ANISOU  843  CB  ALA A  43    19809  15558  15119    447   -244  -1010       C  
ATOM    844  N   SER A  44      -3.537 -19.898 -62.639  1.00132.79           N  
ANISOU  844  N   SER A  44    20107  15282  15065    -53   -447   -854       N  
ATOM    845  CA  SER A  44      -2.205 -20.020 -62.035  1.00132.20           C  
ANISOU  845  CA  SER A  44    20067  15166  14999   -262   -483   -819       C  
ATOM    846  C   SER A  44      -2.270 -20.568 -60.597  1.00134.06           C  
ANISOU  846  C   SER A  44    20299  15369  15269   -185   -422   -897       C  
ATOM    847  O   SER A  44      -2.835 -19.924 -59.699  1.00135.53           O  
ANISOU  847  O   SER A  44    20687  15403  15404    -33   -455   -936       O  
ATOM    848  CB  SER A  44      -1.480 -18.678 -62.059  1.00138.34           C  
ANISOU  848  CB  SER A  44    21138  15745  15680   -399   -645   -727       C  
ATOM    849  OG  SER A  44      -0.139 -18.801 -61.611  1.00148.45           O  
ANISOU  849  OG  SER A  44    22417  17028  16958   -634   -688   -677       O  
ATOM    850  N   SER A  45      -1.651 -21.747 -60.386  1.00126.48           N  
ANISOU  850  N   SER A  45    19121  14552  14383   -283   -336   -917       N  
ATOM    851  CA  SER A  45      -1.596 -22.450 -59.106  1.00124.27           C  
ANISOU  851  CA  SER A  45    18805  14271  14141   -234   -269   -978       C  
ATOM    852  C   SER A  45      -0.343 -22.061 -58.298  1.00125.97           C  
ANISOU  852  C   SER A  45    19155  14390  14317   -399   -356   -933       C  
ATOM    853  O   SER A  45       0.404 -22.927 -57.832  1.00125.20           O  
ANISOU  853  O   SER A  45    18924  14384  14263   -484   -307   -937       O  
ATOM    854  CB  SER A  45      -1.651 -23.954 -59.337  1.00126.51           C  
ANISOU  854  CB  SER A  45    18802  14748  14518   -238   -135  -1022       C  
ATOM    855  OG  SER A  45      -2.857 -24.284 -60.004  1.00137.37           O  
ANISOU  855  OG  SER A  45    20064  16212  15920   -103    -67  -1064       O  
ATOM    856  N   LEU A  46      -0.123 -20.742 -58.147  1.00121.10           N  
ANISOU  856  N   LEU A  46    18815  13586  13610   -444   -493   -887       N  
ATOM    857  CA  LEU A  46       0.959 -20.133 -57.377  1.00120.16           C  
ANISOU  857  CA  LEU A  46    18879  13348  13431   -613   -607   -840       C  
ATOM    858  C   LEU A  46       0.474 -19.957 -55.966  1.00122.69           C  
ANISOU  858  C   LEU A  46    19365  13531  13721   -458   -605   -918       C  
ATOM    859  O   LEU A  46       1.250 -20.131 -55.027  1.00122.59           O  
ANISOU  859  O   LEU A  46    19383  13499  13695   -553   -630   -918       O  
ATOM    860  CB  LEU A  46       1.384 -18.781 -58.000  1.00121.61           C  
ANISOU  860  CB  LEU A  46    19305  13380  13520   -759   -769   -746       C  
ATOM    861  CG  LEU A  46       2.427 -17.918 -57.249  1.00127.26           C  
ANISOU  861  CG  LEU A  46    20267  13937  14148   -962   -923   -688       C  
ATOM    862  CD1 LEU A  46       3.771 -18.608 -57.148  1.00126.83           C  
ANISOU  862  CD1 LEU A  46    20007  14063  14117  -1201   -915   -628       C  
ATOM    863  CD2 LEU A  46       2.602 -16.576 -57.908  1.00130.66           C  
ANISOU  863  CD2 LEU A  46    20970  14191  14483  -1086  -1082   -599       C  
ATOM    864  N   ALA A  47      -0.827 -19.636 -55.818  1.00118.69           N  
ANISOU  864  N   ALA A  47    18951  12952  13195   -205   -570   -985       N  
ATOM    865  CA  ALA A  47      -1.500 -19.438 -54.532  1.00118.77           C  
ANISOU  865  CA  ALA A  47    19114  12855  13159     -5   -552  -1067       C  
ATOM    866  C   ALA A  47      -1.430 -20.700 -53.678  1.00119.47           C  
ANISOU  866  C   ALA A  47    18989  13085  13318     18   -425  -1115       C  
ATOM    867  O   ALA A  47      -1.234 -20.610 -52.467  1.00118.93           O  
ANISOU  867  O   ALA A  47    19044  12936  13207     49   -442  -1150       O  
ATOM    868  CB  ALA A  47      -2.948 -19.046 -54.761  1.00120.24           C  
ANISOU  868  CB  ALA A  47    19354  13019  13312    275   -512  -1118       C  
ATOM    869  N   LEU A  48      -1.559 -21.870 -54.327  1.00113.75           N  
ANISOU  869  N   LEU A  48    17961  12564  12695     -4   -306  -1116       N  
ATOM    870  CA  LEU A  48      -1.514 -23.171 -53.682  1.00111.75           C  
ANISOU  870  CA  LEU A  48    17503  12444  12515      9   -184  -1153       C  
ATOM    871  C   LEU A  48      -0.087 -23.523 -53.264  1.00112.76           C  
ANISOU  871  C   LEU A  48    17602  12590  12651   -194   -225  -1108       C  
ATOM    872  O   LEU A  48       0.112 -23.935 -52.120  1.00113.04           O  
ANISOU  872  O   LEU A  48    17652  12616  12682   -168   -197  -1136       O  
ATOM    873  CB  LEU A  48      -2.098 -24.253 -54.603  1.00110.85           C  
ANISOU  873  CB  LEU A  48    17112  12514  12491     38    -64  -1167       C  
ATOM    874  CG  LEU A  48      -2.542 -25.538 -53.895  1.00114.93           C  
ANISOU  874  CG  LEU A  48    17457  13141  13071    110     70  -1217       C  
ATOM    875  CD1 LEU A  48      -3.840 -25.327 -53.105  1.00115.80           C  
ANISOU  875  CD1 LEU A  48    17626  13234  13139    328    124  -1272       C  
ATOM    876  CD2 LEU A  48      -2.689 -26.674 -54.876  1.00115.76           C  
ANISOU  876  CD2 LEU A  48    17315  13406  13264     60    158  -1219       C  
ATOM    877  N   ALA A  49       0.902 -23.340 -54.171  1.00106.13           N  
ANISOU  877  N   ALA A  49    16717  11794  11814   -391   -294  -1033       N  
ATOM    878  CA  ALA A  49       2.313 -23.612 -53.894  1.00104.36           C  
ANISOU  878  CA  ALA A  49    16440  11628  11583   -589   -340   -976       C  
ATOM    879  C   ALA A  49       2.794 -22.828 -52.672  1.00107.13           C  
ANISOU  879  C   ALA A  49    17029  11826  11848   -636   -448   -972       C  
ATOM    880  O   ALA A  49       3.563 -23.373 -51.887  1.00106.54           O  
ANISOU  880  O   ALA A  49    16894  11810  11777   -704   -441   -964       O  
ATOM    881  CB  ALA A  49       3.162 -23.275 -55.104  1.00105.22           C  
ANISOU  881  CB  ALA A  49    16488  11813  11677   -783   -409   -885       C  
ATOM    882  N   ILE A  50       2.297 -21.577 -52.480  1.00103.44           N  
ANISOU  882  N   ILE A  50    16844  11158  11299   -583   -548   -985       N  
ATOM    883  CA  ILE A  50       2.631 -20.723 -51.325  1.00103.79           C  
ANISOU  883  CA  ILE A  50    17169  11022  11245   -611   -664   -997       C  
ATOM    884  C   ILE A  50       2.013 -21.327 -50.041  1.00108.29           C  
ANISOU  884  C   ILE A  50    17733  11592  11821   -415   -568  -1086       C  
ATOM    885  O   ILE A  50       2.709 -21.436 -49.028  1.00108.86           O  
ANISOU  885  O   ILE A  50    17859  11648  11856   -487   -607  -1086       O  
ATOM    886  CB  ILE A  50       2.203 -19.235 -51.533  1.00107.25           C  
ANISOU  886  CB  ILE A  50    17944  11224  11583   -580   -799   -994       C  
ATOM    887  CG1 ILE A  50       2.979 -18.598 -52.699  1.00108.19           C  
ANISOU  887  CG1 ILE A  50    18089  11337  11680   -821   -911   -885       C  
ATOM    888  CG2 ILE A  50       2.382 -18.412 -50.250  1.00107.37           C  
ANISOU  888  CG2 ILE A  50    18279  11031  11485   -568   -913  -1032       C  
ATOM    889  CD1 ILE A  50       2.310 -17.367 -53.334  1.00115.37           C  
ANISOU  889  CD1 ILE A  50    19269  12048  12519   -753  -1008   -874       C  
ATOM    890  N   ALA A  51       0.723 -21.731 -50.101  1.00103.24           N  
ANISOU  890  N   ALA A  51    17016  10991  11220   -180   -446  -1152       N  
ATOM    891  CA  ALA A  51      -0.018 -22.308 -48.983  1.00101.95           C  
ANISOU  891  CA  ALA A  51    16828  10854  11055     13   -342  -1226       C  
ATOM    892  C   ALA A  51       0.644 -23.581 -48.477  1.00105.15           C  
ANISOU  892  C   ALA A  51    17017  11407  11529    -70   -259  -1212       C  
ATOM    893  O   ALA A  51       0.719 -23.787 -47.266  1.00105.69           O  
ANISOU  893  O   ALA A  51    17146  11452  11558    -18   -245  -1243       O  
ATOM    894  CB  ALA A  51      -1.448 -22.585 -49.397  1.00102.07           C  
ANISOU  894  CB  ALA A  51    16739  10941  11103    233   -226  -1273       C  
ATOM    895  N   ILE A  52       1.158 -24.408 -49.397  1.00100.91           N  
ANISOU  895  N   ILE A  52    16244  11016  11082   -190   -212  -1166       N  
ATOM    896  CA  ILE A  52       1.844 -25.657 -49.078  1.00100.06           C  
ANISOU  896  CA  ILE A  52    15935  11047  11037   -256   -138  -1148       C  
ATOM    897  C   ILE A  52       3.196 -25.333 -48.424  1.00106.57           C  
ANISOU  897  C   ILE A  52    16844  11848  11801   -424   -250  -1099       C  
ATOM    898  O   ILE A  52       3.475 -25.868 -47.346  1.00107.39           O  
ANISOU  898  O   ILE A  52    16939  11973  11892   -397   -222  -1112       O  
ATOM    899  CB  ILE A  52       1.952 -26.545 -50.341  1.00101.80           C  
ANISOU  899  CB  ILE A  52    15910  11419  11352   -309    -63  -1123       C  
ATOM    900  CG1 ILE A  52       0.611 -27.267 -50.532  1.00101.68           C  
ANISOU  900  CG1 ILE A  52    15783  11454  11397   -143     69  -1180       C  
ATOM    901  CG2 ILE A  52       3.124 -27.539 -50.251  1.00101.93           C  
ANISOU  901  CG2 ILE A  52    15761  11564  11404   -420    -41  -1081       C  
ATOM    902  CD1 ILE A  52       0.272 -27.720 -51.928  1.00111.76           C  
ANISOU  902  CD1 ILE A  52    16893  12830  12741   -160    120  -1176       C  
ATOM    903  N   THR A  53       3.989 -24.409 -49.038  1.00103.13           N  
ANISOU  903  N   THR A  53    16498  11370  11316   -601   -383  -1037       N  
ATOM    904  CA  THR A  53       5.299 -23.937 -48.550  1.00102.53           C  
ANISOU  904  CA  THR A  53    16504  11287  11166   -803   -514   -974       C  
ATOM    905  C   THR A  53       5.130 -23.360 -47.153  1.00104.73           C  
ANISOU  905  C   THR A  53    17027  11410  11355   -742   -577  -1024       C  
ATOM    906  O   THR A  53       5.985 -23.565 -46.303  1.00104.53           O  
ANISOU  906  O   THR A  53    17001  11425  11290   -833   -622  -1001       O  
ATOM    907  CB  THR A  53       5.917 -22.918 -49.536  1.00106.52           C  
ANISOU  907  CB  THR A  53    17091  11758  11623  -1006   -648   -895       C  
ATOM    908  OG1 THR A  53       6.052 -23.547 -50.816  1.00110.69           O  
ANISOU  908  OG1 THR A  53    17375  12454  12226  -1042   -574   -854       O  
ATOM    909  CG2 THR A  53       7.280 -22.414 -49.092  1.00100.08           C  
ANISOU  909  CG2 THR A  53    16344  10961  10722  -1252   -793   -816       C  
ATOM    910  N   ALA A  54       4.002 -22.696 -46.914  1.00101.01           N  
ANISOU  910  N   ALA A  54    16752  10779  10847   -569   -574  -1094       N  
ATOM    911  CA  ALA A  54       3.667 -22.116 -45.626  1.00102.14           C  
ANISOU  911  CA  ALA A  54    17146  10771  10892   -463   -622  -1157       C  
ATOM    912  C   ALA A  54       3.386 -23.202 -44.593  1.00104.54           C  
ANISOU  912  C   ALA A  54    17320  11175  11224   -327   -495  -1199       C  
ATOM    913  O   ALA A  54       3.889 -23.113 -43.470  1.00104.19           O  
ANISOU  913  O   ALA A  54    17386  11095  11107   -357   -548  -1210       O  
ATOM    914  CB  ALA A  54       2.464 -21.199 -45.766  1.00103.83           C  
ANISOU  914  CB  ALA A  54    17577  10820  11053   -270   -634  -1220       C  
ATOM    915  N   LEU A  55       2.600 -24.228 -44.970  1.00100.19           N  
ANISOU  915  N   LEU A  55    16545  10751  10773   -194   -333  -1219       N  
ATOM    916  CA  LEU A  55       2.259 -25.318 -44.065  1.00100.08           C  
ANISOU  916  CA  LEU A  55    16408  10831  10788    -76   -207  -1247       C  
ATOM    917  C   LEU A  55       3.510 -26.067 -43.648  1.00107.07           C  
ANISOU  917  C   LEU A  55    17175  11817  11690   -223   -224  -1192       C  
ATOM    918  O   LEU A  55       3.760 -26.173 -42.446  1.00107.42           O  
ANISOU  918  O   LEU A  55    17299  11845  11673   -196   -238  -1205       O  
ATOM    919  CB  LEU A  55       1.225 -26.271 -44.685  1.00 98.69           C  
ANISOU  919  CB  LEU A  55    16019  10768  10713     49    -47  -1265       C  
ATOM    920  CG  LEU A  55       0.667 -27.407 -43.797  1.00102.54           C  
ANISOU  920  CG  LEU A  55    16390  11345  11227    168     91  -1286       C  
ATOM    921  CD1 LEU A  55       0.246 -26.931 -42.409  1.00103.72           C  
ANISOU  921  CD1 LEU A  55    16725  11420  11264    299     82  -1332       C  
ATOM    922  CD2 LEU A  55      -0.513 -28.065 -44.451  1.00104.21           C  
ANISOU  922  CD2 LEU A  55    16438  11645  11513    274    221  -1306       C  
ATOM    923  N   TYR A  56       4.327 -26.500 -44.633  1.00105.43           N  
ANISOU  923  N   TYR A  56    16789  11720  11549   -369   -233  -1129       N  
ATOM    924  CA  TYR A  56       5.568 -27.242 -44.419  1.00106.52           C  
ANISOU  924  CA  TYR A  56    16782  11991  11700   -491   -248  -1068       C  
ATOM    925  C   TYR A  56       6.635 -26.450 -43.675  1.00112.84           C  
ANISOU  925  C   TYR A  56    17730  12752  12392   -644   -403  -1031       C  
ATOM    926  O   TYR A  56       7.372 -27.042 -42.892  1.00113.43           O  
ANISOU  926  O   TYR A  56    17739  12914  12444   -673   -406  -1003       O  
ATOM    927  CB  TYR A  56       6.138 -27.772 -45.726  1.00108.26           C  
ANISOU  927  CB  TYR A  56    16788  12352  11996   -587   -223  -1013       C  
ATOM    928  CG  TYR A  56       5.386 -28.958 -46.295  1.00110.97           C  
ANISOU  928  CG  TYR A  56    16948  12770  12445   -459    -67  -1043       C  
ATOM    929  CD1 TYR A  56       4.822 -29.925 -45.455  1.00112.64           C  
ANISOU  929  CD1 TYR A  56    17122  12990  12687   -324     42  -1078       C  
ATOM    930  CD2 TYR A  56       5.289 -29.151 -47.667  1.00112.14           C  
ANISOU  930  CD2 TYR A  56    16967  12986  12656   -490    -35  -1030       C  
ATOM    931  CE1 TYR A  56       4.158 -31.034 -45.973  1.00112.59           C  
ANISOU  931  CE1 TYR A  56    16966  13041  12770   -238    172  -1100       C  
ATOM    932  CE2 TYR A  56       4.633 -30.260 -48.197  1.00112.53           C  
ANISOU  932  CE2 TYR A  56    16865  13098  12794   -391     95  -1061       C  
ATOM    933  CZ  TYR A  56       4.059 -31.193 -47.345  1.00118.55           C  
ANISOU  933  CZ  TYR A  56    17605  13852  13585   -272    194  -1096       C  
ATOM    934  OH  TYR A  56       3.407 -32.276 -47.869  1.00117.72           O  
ANISOU  934  OH  TYR A  56    17374  13794  13561   -203    309  -1122       O  
ATOM    935  N   SER A  57       6.719 -25.138 -43.888  1.00110.15           N  
ANISOU  935  N   SER A  57    17598  12278  11977   -745   -538  -1027       N  
ATOM    936  CA  SER A  57       7.705 -24.332 -43.177  1.00110.91           C  
ANISOU  936  CA  SER A  57    17860  12322  11958   -920   -704   -992       C  
ATOM    937  C   SER A  57       7.303 -24.160 -41.704  1.00112.80           C  
ANISOU  937  C   SER A  57    18295  12450  12114   -796   -714  -1063       C  
ATOM    938  O   SER A  57       8.165 -24.272 -40.832  1.00112.63           O  
ANISOU  938  O   SER A  57    18288  12480  12028   -889   -782  -1036       O  
ATOM    939  CB  SER A  57       7.892 -22.982 -43.857  1.00116.23           C  
ANISOU  939  CB  SER A  57    18731  12862  12568  -1080   -855   -964       C  
ATOM    940  OG  SER A  57       6.663 -22.291 -44.006  1.00126.27           O  
ANISOU  940  OG  SER A  57    20204  13944  13828   -915   -839  -1039       O  
ATOM    941  N   ALA A  58       5.996 -23.923 -41.435  1.00107.92           N  
ANISOU  941  N   ALA A  58    17811  11704  11490   -578   -642  -1149       N  
ATOM    942  CA  ALA A  58       5.457 -23.769 -40.083  1.00107.97           C  
ANISOU  942  CA  ALA A  58    17997  11620  11407   -423   -631  -1223       C  
ATOM    943  C   ALA A  58       5.522 -25.090 -39.338  1.00109.85           C  
ANISOU  943  C   ALA A  58    18037  12012  11690   -340   -504  -1214       C  
ATOM    944  O   ALA A  58       5.834 -25.094 -38.143  1.00109.86           O  
ANISOU  944  O   ALA A  58    18138  12000  11603   -327   -542  -1229       O  
ATOM    945  CB  ALA A  58       4.029 -23.263 -40.133  1.00108.85           C  
ANISOU  945  CB  ALA A  58    18251  11608  11498   -193   -569  -1306       C  
ATOM    946  N   VAL A  59       5.271 -26.212 -40.048  1.00103.89           N  
ANISOU  946  N   VAL A  59    17015  11396  11063   -294   -364  -1186       N  
ATOM    947  CA  VAL A  59       5.349 -27.525 -39.421  1.00103.02           C  
ANISOU  947  CA  VAL A  59    16732  11414  10997   -223   -248  -1168       C  
ATOM    948  C   VAL A  59       6.814 -27.857 -39.135  1.00107.43           C  
ANISOU  948  C   VAL A  59    17207  12080  11532   -386   -331  -1095       C  
ATOM    949  O   VAL A  59       7.111 -28.414 -38.072  1.00108.45           O  
ANISOU  949  O   VAL A  59    17329  12257  11619   -345   -313  -1087       O  
ATOM    950  CB  VAL A  59       4.606 -28.670 -40.145  1.00105.60           C  
ANISOU  950  CB  VAL A  59    16838  11834  11453   -123    -82  -1166       C  
ATOM    951  CG1 VAL A  59       3.104 -28.466 -40.086  1.00105.80           C  
ANISOU  951  CG1 VAL A  59    16927  11796  11477     56     10  -1232       C  
ATOM    952  CG2 VAL A  59       5.074 -28.917 -41.554  1.00104.73           C  
ANISOU  952  CG2 VAL A  59    16561  11800  11434   -232    -84  -1121       C  
ATOM    953  N   CYS A  60       7.734 -27.414 -40.020  1.00102.48           N  
ANISOU  953  N   CYS A  60    16528  11497  10911   -573   -433  -1038       N  
ATOM    954  CA  CYS A  60       9.165 -27.635 -39.827  1.00101.75           C  
ANISOU  954  CA  CYS A  60    16335  11547  10781   -738   -522   -958       C  
ATOM    955  C   CYS A  60       9.696 -26.821 -38.643  1.00104.95           C  
ANISOU  955  C   CYS A  60    16951  11881  11045   -826   -667   -964       C  
ATOM    956  O   CYS A  60      10.210 -27.406 -37.699  1.00104.06           O  
ANISOU  956  O   CYS A  60    16792  11855  10891   -807   -665   -943       O  
ATOM    957  CB  CYS A  60       9.949 -27.333 -41.098  1.00101.84           C  
ANISOU  957  CB  CYS A  60    16224  11652  10819   -919   -589   -887       C  
ATOM    958  SG  CYS A  60      11.696 -27.792 -41.009  1.00106.42           S  
ANISOU  958  SG  CYS A  60    16599  12483  11351  -1096   -671   -774       S  
ATOM    959  N   ALA A  61       9.543 -25.494 -38.671  1.00101.89           N  
ANISOU  959  N   ALA A  61    16811  11324  10576   -915   -796   -995       N  
ATOM    960  CA  ALA A  61      10.051 -24.629 -37.622  1.00103.21           C  
ANISOU  960  CA  ALA A  61    17217  11400  10598  -1020   -954  -1008       C  
ATOM    961  C   ALA A  61       9.435 -24.934 -36.255  1.00108.98           C  
ANISOU  961  C   ALA A  61    18064  12073  11269   -826   -893  -1081       C  
ATOM    962  O   ALA A  61      10.165 -24.890 -35.269  1.00110.49           O  
ANISOU  962  O   ALA A  61    18315  12304  11363   -902   -982  -1065       O  
ATOM    963  CB  ALA A  61       9.840 -23.179 -37.984  1.00104.92           C  
ANISOU  963  CB  ALA A  61    17717  11408  10742  -1125  -1096  -1037       C  
ATOM    964  N   VAL A  62       8.132 -25.271 -36.179  1.00104.70           N  
ANISOU  964  N   VAL A  62    17538  11466  10777   -586   -744  -1152       N  
ATOM    965  CA  VAL A  62       7.522 -25.574 -34.877  1.00104.80           C  
ANISOU  965  CA  VAL A  62    17647  11451  10721   -401   -676  -1211       C  
ATOM    966  C   VAL A  62       8.074 -26.929 -34.401  1.00107.80           C  
ANISOU  966  C   VAL A  62    17791  12021  11148   -385   -589  -1148       C  
ATOM    967  O   VAL A  62       8.594 -27.010 -33.285  1.00107.74           O  
ANISOU  967  O   VAL A  62    17849  12044  11042   -399   -644  -1142       O  
ATOM    968  CB  VAL A  62       5.962 -25.506 -34.898  1.00108.33           C  
ANISOU  968  CB  VAL A  62    18167  11808  11187   -154   -544  -1294       C  
ATOM    969  CG1 VAL A  62       5.343 -26.187 -33.678  1.00107.95           C  
ANISOU  969  CG1 VAL A  62    18118  11807  11089     36   -429  -1327       C  
ATOM    970  CG2 VAL A  62       5.487 -24.061 -34.982  1.00109.59           C  
ANISOU  970  CG2 VAL A  62    18632  11760  11247   -129   -655  -1367       C  
ATOM    971  N   GLY A  63       8.022 -27.932 -35.285  1.00103.15           N  
ANISOU  971  N   GLY A  63    16947  11550  10698   -361   -470  -1101       N  
ATOM    972  CA  GLY A  63       8.499 -29.282 -35.016  1.00102.03           C  
ANISOU  972  CA  GLY A  63    16589  11568  10610   -325   -381  -1040       C  
ATOM    973  C   GLY A  63       9.961 -29.345 -34.642  1.00107.01           C  
ANISOU  973  C   GLY A  63    17159  12324  11176   -481   -503   -966       C  
ATOM    974  O   GLY A  63      10.288 -29.516 -33.463  1.00108.02           O  
ANISOU  974  O   GLY A  63    17350  12481  11214   -455   -535   -960       O  
ATOM    975  N   LEU A  64      10.848 -29.211 -35.651  1.00102.83           N  
ANISOU  975  N   LEU A  64    16495  11893  10684   -642   -572   -904       N  
ATOM    976  CA  LEU A  64      12.311 -29.264 -35.525  1.00102.74           C  
ANISOU  976  CA  LEU A  64    16371  12055  10611   -808   -689   -816       C  
ATOM    977  C   LEU A  64      12.836 -28.402 -34.363  1.00107.72           C  
ANISOU  977  C   LEU A  64    17201  12642  11084   -921   -850   -823       C  
ATOM    978  O   LEU A  64      13.454 -28.970 -33.451  1.00107.46           O  
ANISOU  978  O   LEU A  64    17111  12727  10991   -900   -866   -785       O  
ATOM    979  CB  LEU A  64      12.981 -28.867 -36.861  1.00102.29           C  
ANISOU  979  CB  LEU A  64    16186  12087  10591   -984   -753   -757       C  
ATOM    980  CG  LEU A  64      14.511 -28.790 -36.953  1.00107.22           C  
ANISOU  980  CG  LEU A  64    16660  12934  11143  -1185   -881   -651       C  
ATOM    981  CD1 LEU A  64      15.176 -30.130 -36.680  1.00106.87           C  
ANISOU  981  CD1 LEU A  64    16378  13108  11120  -1071   -801   -590       C  
ATOM    982  CD2 LEU A  64      14.922 -28.319 -38.317  1.00109.09           C  
ANISOU  982  CD2 LEU A  64    16791  13244  11413  -1346   -926   -599       C  
ATOM    983  N   LEU A  65      12.541 -27.074 -34.348  1.00104.73           N  
ANISOU  983  N   LEU A  65    17077  12084  10633  -1023   -969   -877       N  
ATOM    984  CA  LEU A  65      13.043 -26.220 -33.266  1.00106.37           C  
ANISOU  984  CA  LEU A  65    17507  12229  10679  -1143  -1137   -893       C  
ATOM    985  C   LEU A  65      12.454 -26.591 -31.892  1.00109.13           C  
ANISOU  985  C   LEU A  65    17980  12523  10962   -949  -1074   -957       C  
ATOM    986  O   LEU A  65      13.207 -26.632 -30.921  1.00109.41           O  
ANISOU  986  O   LEU A  65    18043  12639  10889  -1015  -1165   -930       O  
ATOM    987  CB  LEU A  65      12.840 -24.736 -33.559  1.00107.72           C  
ANISOU  987  CB  LEU A  65    17961  12190  10776  -1286  -1284   -941       C  
ATOM    988  CG  LEU A  65      13.712 -24.179 -34.695  1.00112.83           C  
ANISOU  988  CG  LEU A  65    18522  12910  11438  -1555  -1401   -854       C  
ATOM    989  CD1 LEU A  65      13.322 -22.749 -35.043  1.00113.58           C  
ANISOU  989  CD1 LEU A  65    18932  12752  11470  -1669  -1533   -903       C  
ATOM    990  CD2 LEU A  65      15.199 -24.274 -34.353  1.00117.23           C  
ANISOU  990  CD2 LEU A  65    18940  13692  11909  -1789  -1537   -748       C  
ATOM    991  N   GLY A  66      11.159 -26.913 -31.846  1.00104.01           N  
ANISOU  991  N   GLY A  66    17377  11767  10374   -718   -917  -1030       N  
ATOM    992  CA  GLY A  66      10.460 -27.320 -30.632  1.00103.59           C  
ANISOU  992  CA  GLY A  66    17419  11680  10261   -519   -831  -1083       C  
ATOM    993  C   GLY A  66      11.039 -28.560 -29.995  1.00107.57           C  
ANISOU  993  C   GLY A  66    17728  12368  10776   -470   -766  -1010       C  
ATOM    994  O   GLY A  66      11.256 -28.573 -28.781  1.00108.36           O  
ANISOU  994  O   GLY A  66    17931  12484  10756   -440   -811  -1019       O  
ATOM    995  N   ASN A  67      11.305 -29.607 -30.814  1.00103.40           N  
ANISOU  995  N   ASN A  67    16932  11975  10381   -454   -666   -939       N  
ATOM    996  CA  ASN A  67      11.876 -30.882 -30.365  1.00103.38           C  
ANISOU  996  CA  ASN A  67    16740  12140  10398   -386   -600   -862       C  
ATOM    997  C   ASN A  67      13.336 -30.744 -29.923  1.00109.23           C  
ANISOU  997  C   ASN A  67    17424  13040  11038   -545   -757   -787       C  
ATOM    998  O   ASN A  67      13.717 -31.385 -28.937  1.00109.79           O  
ANISOU  998  O   ASN A  67    17468  13204  11044   -477   -752   -749       O  
ATOM    999  CB  ASN A  67      11.773 -31.943 -31.440  1.00102.32           C  
ANISOU  999  CB  ASN A  67    16373  12084  10420   -321   -467   -817       C  
ATOM   1000  CG  ASN A  67      10.369 -32.414 -31.736  1.00123.99           C  
ANISOU 1000  CG  ASN A  67    19131  14718  13262   -158   -297   -870       C  
ATOM   1001  OD1 ASN A  67       9.932 -32.413 -32.881  1.00123.76           O  
ANISOU 1001  OD1 ASN A  67    19028  14657  13339   -165   -242   -886       O  
ATOM   1002  ND2 ASN A  67       9.630 -32.824 -30.712  1.00109.98           N  
ANISOU 1002  ND2 ASN A  67    17442  12900  11445    -18   -212   -893       N  
ATOM   1003  N   VAL A  68      14.146 -29.915 -30.630  1.00105.66           N  
ANISOU 1003  N   VAL A  68    16951  12632  10564   -762   -900   -757       N  
ATOM   1004  CA  VAL A  68      15.557 -29.661 -30.278  1.00106.61           C  
ANISOU 1004  CA  VAL A  68    17001  12932  10573   -953  -1067   -677       C  
ATOM   1005  C   VAL A  68      15.605 -28.993 -28.882  1.00113.03           C  
ANISOU 1005  C   VAL A  68    18059  13665  11220   -990  -1187   -723       C  
ATOM   1006  O   VAL A  68      16.389 -29.408 -28.019  1.00114.17           O  
ANISOU 1006  O   VAL A  68    18140  13964  11274  -1002  -1243   -668       O  
ATOM   1007  CB  VAL A  68      16.298 -28.839 -31.372  1.00109.94           C  
ANISOU 1007  CB  VAL A  68    17359  13416  10998  -1202  -1193   -630       C  
ATOM   1008  CG1 VAL A  68      17.637 -28.303 -30.874  1.00111.42           C  
ANISOU 1008  CG1 VAL A  68    17525  13771  11038  -1443  -1395   -554       C  
ATOM   1009  CG2 VAL A  68      16.510 -29.674 -32.624  1.00108.32           C  
ANISOU 1009  CG2 VAL A  68    16872  13358  10928  -1154  -1081   -568       C  
ATOM   1010  N   LEU A  69      14.712 -28.014 -28.660  1.00109.33           N  
ANISOU 1010  N   LEU A  69    17875  12959  10708   -979  -1216   -829       N  
ATOM   1011  CA  LEU A  69      14.547 -27.293 -27.404  1.00110.37           C  
ANISOU 1011  CA  LEU A  69    18287  12972  10675   -981  -1318   -900       C  
ATOM   1012  C   LEU A  69      14.173 -28.261 -26.283  1.00113.29           C  
ANISOU 1012  C   LEU A  69    18633  13397  11015   -761  -1199   -904       C  
ATOM   1013  O   LEU A  69      14.721 -28.133 -25.188  1.00114.61           O  
ANISOU 1013  O   LEU A  69    18888  13618  11038   -803  -1301   -898       O  
ATOM   1014  CB  LEU A  69      13.470 -26.203 -27.575  1.00110.69           C  
ANISOU 1014  CB  LEU A  69    18622  12740  10695   -938  -1330  -1018       C  
ATOM   1015  CG  LEU A  69      13.054 -25.389 -26.348  1.00117.06           C  
ANISOU 1015  CG  LEU A  69    19768  13383  11326   -885  -1416  -1121       C  
ATOM   1016  CD1 LEU A  69      14.230 -24.615 -25.752  1.00119.64           C  
ANISOU 1016  CD1 LEU A  69    20229  13740  11491  -1145  -1657  -1098       C  
ATOM   1017  CD2 LEU A  69      11.917 -24.456 -26.693  1.00118.53           C  
ANISOU 1017  CD2 LEU A  69    20211  13317  11507   -785  -1398  -1233       C  
ATOM   1018  N   VAL A  70      13.258 -29.233 -26.567  1.00107.47           N  
ANISOU 1018  N   VAL A  70    17777  12650  10406   -544   -989   -908       N  
ATOM   1019  CA  VAL A  70      12.802 -30.270 -25.626  1.00106.50           C  
ANISOU 1019  CA  VAL A  70    17618  12576  10270   -339   -855   -895       C  
ATOM   1020  C   VAL A  70      14.004 -31.135 -25.241  1.00112.78           C  
ANISOU 1020  C   VAL A  70    18220  13592  11039   -379   -896   -784       C  
ATOM   1021  O   VAL A  70      14.252 -31.336 -24.047  1.00113.11           O  
ANISOU 1021  O   VAL A  70    18331  13687  10958   -332   -931   -771       O  
ATOM   1022  CB  VAL A  70      11.613 -31.117 -26.173  1.00107.15           C  
ANISOU 1022  CB  VAL A  70    17605  12606  10500   -147   -636   -908       C  
ATOM   1023  CG1 VAL A  70      11.385 -32.368 -25.342  1.00106.40           C  
ANISOU 1023  CG1 VAL A  70    17429  12594  10403     18   -507   -856       C  
ATOM   1024  CG2 VAL A  70      10.334 -30.298 -26.220  1.00106.72           C  
ANISOU 1024  CG2 VAL A  70    17750  12367  10430    -59   -589  -1018       C  
ATOM   1025  N   MET A  71      14.767 -31.594 -26.248  1.00110.78           N  
ANISOU 1025  N   MET A  71    17730  13475  10884   -457   -899   -704       N  
ATOM   1026  CA  MET A  71      15.961 -32.416 -26.057  1.00112.48           C  
ANISOU 1026  CA  MET A  71    17735  13927  11075   -475   -938   -592       C  
ATOM   1027  C   MET A  71      17.033 -31.687 -25.246  1.00122.65           C  
ANISOU 1027  C   MET A  71    19085  15326  12188   -654  -1145   -564       C  
ATOM   1028  O   MET A  71      17.625 -32.302 -24.356  1.00124.24           O  
ANISOU 1028  O   MET A  71    19226  15674  12306   -597  -1168   -503       O  
ATOM   1029  CB  MET A  71      16.547 -32.851 -27.396  1.00113.92           C  
ANISOU 1029  CB  MET A  71    17667  14240  11378   -524   -911   -525       C  
ATOM   1030  CG  MET A  71      15.848 -34.017 -27.996  1.00115.94           C  
ANISOU 1030  CG  MET A  71    17808  14459  11783   -326   -715   -518       C  
ATOM   1031  SD  MET A  71      16.645 -34.517 -29.533  1.00119.56           S  
ANISOU 1031  SD  MET A  71    17984  15089  12354   -368   -696   -445       S  
ATOM   1032  CE  MET A  71      15.971 -33.314 -30.651  1.00115.44           C  
ANISOU 1032  CE  MET A  71    17558  14404  11902   -518   -720   -525       C  
ATOM   1033  N   PHE A  72      17.265 -30.385 -25.533  1.00121.63           N  
ANISOU 1033  N   PHE A  72    19091  15124  11997   -876  -1301   -606       N  
ATOM   1034  CA  PHE A  72      18.260 -29.569 -24.837  1.00124.65           C  
ANISOU 1034  CA  PHE A  72    19559  15595  12206  -1095  -1521   -583       C  
ATOM   1035  C   PHE A  72      17.968 -29.452 -23.331  1.00128.45           C  
ANISOU 1035  C   PHE A  72    20261  16007  12538  -1009  -1556   -639       C  
ATOM   1036  O   PHE A  72      18.888 -29.620 -22.534  1.00128.79           O  
ANISOU 1036  O   PHE A  72    20248  16227  12457  -1075  -1665   -577       O  
ATOM   1037  CB  PHE A  72      18.354 -28.167 -25.466  1.00128.32           C  
ANISOU 1037  CB  PHE A  72    20186  15931  12638  -1349  -1674   -628       C  
ATOM   1038  CG  PHE A  72      19.148 -27.157 -24.662  1.00133.95           C  
ANISOU 1038  CG  PHE A  72    21077  16662  13156  -1594  -1914   -631       C  
ATOM   1039  CD1 PHE A  72      20.538 -27.205 -24.628  1.00139.67           C  
ANISOU 1039  CD1 PHE A  72    21603  17666  13798  -1806  -2061   -513       C  
ATOM   1040  CD2 PHE A  72      18.506 -26.151 -23.944  1.00138.45           C  
ANISOU 1040  CD2 PHE A  72    22017  16977  13612  -1612  -1998   -752       C  
ATOM   1041  CE1 PHE A  72      21.272 -26.270 -23.886  1.00143.39           C  
ANISOU 1041  CE1 PHE A  72    22240  18160  14081  -2062  -2296   -513       C  
ATOM   1042  CE2 PHE A  72      19.242 -25.218 -23.196  1.00144.17           C  
ANISOU 1042  CE2 PHE A  72    22933  17698  14145  -1852  -2233   -762       C  
ATOM   1043  CZ  PHE A  72      20.619 -25.278 -23.181  1.00143.70           C  
ANISOU 1043  CZ  PHE A  72    22673  17916  14012  -2092  -2385   -640       C  
ATOM   1044  N   VAL A  73      16.711 -29.160 -22.952  1.00124.25           N  
ANISOU 1044  N   VAL A  73    19964  15239  12006   -858  -1465   -752       N  
ATOM   1045  CA  VAL A  73      16.327 -28.993 -21.550  1.00124.86           C  
ANISOU 1045  CA  VAL A  73    20265  15246  11928   -757  -1486   -816       C  
ATOM   1046  C   VAL A  73      16.216 -30.364 -20.849  1.00129.80           C  
ANISOU 1046  C   VAL A  73    20742  16003  12572   -538  -1338   -749       C  
ATOM   1047  O   VAL A  73      16.245 -30.405 -19.622  1.00131.24           O  
ANISOU 1047  O   VAL A  73    21048  16208  12609   -478  -1374   -763       O  
ATOM   1048  CB  VAL A  73      15.067 -28.117 -21.340  1.00127.91           C  
ANISOU 1048  CB  VAL A  73    20962  15361  12275   -662  -1452   -959       C  
ATOM   1049  CG1 VAL A  73      15.260 -26.721 -21.929  1.00128.57           C  
ANISOU 1049  CG1 VAL A  73    21240  15294  12318   -882  -1625  -1020       C  
ATOM   1050  CG2 VAL A  73      13.840 -28.765 -21.929  1.00125.54           C  
ANISOU 1050  CG2 VAL A  73    20586  14980  12135   -440  -1221   -983       C  
ATOM   1051  N   ILE A  74      16.157 -31.478 -21.609  1.00125.07           N  
ANISOU 1051  N   ILE A  74    19893  15491  12136   -429  -1186   -673       N  
ATOM   1052  CA  ILE A  74      16.162 -32.815 -21.011  1.00124.79           C  
ANISOU 1052  CA  ILE A  74    19729  15570  12116   -239  -1062   -595       C  
ATOM   1053  C   ILE A  74      17.646 -33.216 -20.770  1.00132.38           C  
ANISOU 1053  C   ILE A  74    20503  16791  13005   -329  -1188   -479       C  
ATOM   1054  O   ILE A  74      17.923 -34.176 -20.049  1.00132.26           O  
ANISOU 1054  O   ILE A  74    20410  16894  12948   -194  -1142   -405       O  
ATOM   1055  CB  ILE A  74      15.326 -33.832 -21.847  1.00125.32           C  
ANISOU 1055  CB  ILE A  74    19663  15580  12372    -71   -847   -576       C  
ATOM   1056  CG1 ILE A  74      13.838 -33.675 -21.474  1.00124.96           C  
ANISOU 1056  CG1 ILE A  74    19804  15343  12332     68   -715   -668       C  
ATOM   1057  CG2 ILE A  74      15.784 -35.298 -21.671  1.00125.04           C  
ANISOU 1057  CG2 ILE A  74    19436  15695  12380     69   -758   -460       C  
ATOM   1058  CD1 ILE A  74      12.840 -34.355 -22.381  1.00131.54           C  
ANISOU 1058  CD1 ILE A  74    20546  16092  13341    182   -526   -673       C  
ATOM   1059  N   VAL A  75      18.592 -32.416 -21.296  1.00131.87           N  
ANISOU 1059  N   VAL A  75    20380  16823  12903   -564  -1359   -460       N  
ATOM   1060  CA  VAL A  75      20.020 -32.665 -21.124  1.00134.02           C  
ANISOU 1060  CA  VAL A  75    20453  17379  13090   -672  -1493   -346       C  
ATOM   1061  C   VAL A  75      20.614 -31.636 -20.123  1.00143.11           C  
ANISOU 1061  C   VAL A  75    21778  18564  14032   -871  -1712   -372       C  
ATOM   1062  O   VAL A  75      21.098 -32.039 -19.065  1.00143.99           O  
ANISOU 1062  O   VAL A  75    21880  18812  14016   -818  -1762   -325       O  
ATOM   1063  CB  VAL A  75      20.758 -32.678 -22.500  1.00137.07           C  
ANISOU 1063  CB  VAL A  75    20588  17913  13578   -797  -1518   -277       C  
ATOM   1064  CG1 VAL A  75      22.273 -32.643 -22.336  1.00139.04           C  
ANISOU 1064  CG1 VAL A  75    20636  18486  13707   -956  -1688   -162       C  
ATOM   1065  CG2 VAL A  75      20.361 -33.891 -23.314  1.00134.71           C  
ANISOU 1065  CG2 VAL A  75    20110  17620  13453   -576  -1315   -240       C  
ATOM   1066  N   ARG A  76      20.551 -30.330 -20.458  1.00142.47           N  
ANISOU 1066  N   ARG A  76    21874  18348  13911  -1097  -1845   -448       N  
ATOM   1067  CA  ARG A  76      21.121 -29.221 -19.698  1.00145.60           C  
ANISOU 1067  CA  ARG A  76    22467  18741  14111  -1333  -2077   -482       C  
ATOM   1068  C   ARG A  76      20.413 -28.913 -18.386  1.00153.01           C  
ANISOU 1068  C   ARG A  76    23715  19511  14912  -1221  -2086   -587       C  
ATOM   1069  O   ARG A  76      21.070 -28.405 -17.478  1.00155.58           O  
ANISOU 1069  O   ARG A  76    24152  19909  15050  -1364  -2267   -588       O  
ATOM   1070  CB  ARG A  76      21.131 -27.948 -20.551  1.00146.72           C  
ANISOU 1070  CB  ARG A  76    22744  18738  14263  -1593  -2204   -535       C  
ATOM   1071  N   TYR A  77      19.096 -29.165 -18.277  1.00149.57           N  
ANISOU 1071  N   TYR A  77    23416  18864  14550   -980  -1900   -673       N  
ATOM   1072  CA  TYR A  77      18.379 -28.809 -17.053  1.00151.36           C  
ANISOU 1072  CA  TYR A  77    23937  18945  14628   -863  -1902   -776       C  
ATOM   1073  C   TYR A  77      17.804 -30.017 -16.285  1.00155.06           C  
ANISOU 1073  C   TYR A  77    24328  19464  15124   -568  -1700   -742       C  
ATOM   1074  O   TYR A  77      18.433 -30.431 -15.313  1.00155.32           O  
ANISOU 1074  O   TYR A  77    24334  19651  15031   -536  -1750   -686       O  
ATOM   1075  CB  TYR A  77      17.361 -27.695 -17.330  1.00153.25           C  
ANISOU 1075  CB  TYR A  77    24479  18886  14863   -864  -1905   -924       C  
ATOM   1076  CG  TYR A  77      18.025 -26.368 -17.628  1.00158.21           C  
ANISOU 1076  CG  TYR A  77    25278  19437  15398  -1171  -2147   -963       C  
ATOM   1077  CD1 TYR A  77      18.368 -26.019 -18.935  1.00159.83           C  
ANISOU 1077  CD1 TYR A  77    25363  19637  15729  -1353  -2187   -922       C  
ATOM   1078  CD2 TYR A  77      18.359 -25.485 -16.611  1.00162.03           C  
ANISOU 1078  CD2 TYR A  77    26046  19859  15660  -1297  -2345  -1033       C  
ATOM   1079  CE1 TYR A  77      18.998 -24.808 -19.217  1.00163.06           C  
ANISOU 1079  CE1 TYR A  77    25935  19975  16047  -1663  -2417   -942       C  
ATOM   1080  CE2 TYR A  77      18.985 -24.269 -16.879  1.00165.23           C  
ANISOU 1080  CE2 TYR A  77    26633  20177  15971  -1608  -2583  -1063       C  
ATOM   1081  CZ  TYR A  77      19.301 -23.931 -18.188  1.00173.83           C  
ANISOU 1081  CZ  TYR A  77    27600  21257  17191  -1797  -2618  -1012       C  
ATOM   1082  OH  TYR A  77      19.919 -22.730 -18.466  1.00178.24           O  
ANISOU 1082  OH  TYR A  77    28346  21724  17652  -2129  -2859  -1027       O  
ATOM   1083  N   THR A  78      16.646 -30.580 -16.701  1.00151.02           N  
ANISOU 1083  N   THR A  78    23781  18833  14765   -370  -1482   -765       N  
ATOM   1084  CA  THR A  78      16.087 -31.769 -16.030  1.00150.45           C  
ANISOU 1084  CA  THR A  78    23635  18806  14721   -121  -1291   -716       C  
ATOM   1085  C   THR A  78      16.804 -32.973 -16.641  1.00154.56           C  
ANISOU 1085  C   THR A  78    23846  19520  15359    -91  -1235   -572       C  
ATOM   1086  O   THR A  78      16.299 -33.555 -17.600  1.00152.86           O  
ANISOU 1086  O   THR A  78    23492  19265  15322     -2  -1082   -545       O  
ATOM   1087  CB  THR A  78      14.551 -31.918 -16.154  1.00154.40           C  
ANISOU 1087  CB  THR A  78    24214  19129  15321     66  -1085   -787       C  
ATOM   1088  OG1 THR A  78      13.953 -30.845 -16.847  1.00154.17           O  
ANISOU 1088  OG1 THR A  78    24371  18913  15293      2  -1129   -909       O  
ATOM   1089  CG2 THR A  78      13.870 -32.136 -14.812  1.00152.37           C  
ANISOU 1089  CG2 THR A  78    24063  18870  14959    269   -966   -793       C  
ATOM   1090  N   LYS A  79      18.006 -33.323 -16.092  1.00152.42           N  
ANISOU 1090  N   LYS A  79    23471  19463  14977   -157  -1364   -481       N  
ATOM   1091  CA  LYS A  79      18.799 -34.478 -16.545  1.00151.95           C  
ANISOU 1091  CA  LYS A  79    23129  19612  14994    -91  -1323   -340       C  
ATOM   1092  C   LYS A  79      17.800 -35.653 -16.459  1.00155.91           C  
ANISOU 1092  C   LYS A  79    23607  20038  15594    165  -1096   -305       C  
ATOM   1093  O   LYS A  79      16.927 -35.611 -15.587  1.00156.39           O  
ANISOU 1093  O   LYS A  79    23841  20013  15567    274  -1033   -343       O  
ATOM   1094  CB  LYS A  79      20.036 -34.556 -15.655  1.00155.93           C  
ANISOU 1094  CB  LYS A  79    23566  20356  15324   -160  -1490   -257       C  
ATOM   1095  N   MET A  80      17.844 -36.599 -17.420  1.00151.27           N  
ANISOU 1095  N   MET A  80    22829  19465  15182    246   -975   -244       N  
ATOM   1096  CA  MET A  80      16.930 -37.743 -17.534  1.00149.84           C  
ANISOU 1096  CA  MET A  80    22631  19185  15117    448   -766   -211       C  
ATOM   1097  C   MET A  80      17.082 -38.789 -16.397  1.00152.56           C  
ANISOU 1097  C   MET A  80    22988  19613  15367    613   -721   -113       C  
ATOM   1098  O   MET A  80      17.527 -39.923 -16.612  1.00151.56           O  
ANISOU 1098  O   MET A  80    22721  19568  15298    731   -666     -7       O  
ATOM   1099  CB  MET A  80      17.009 -38.432 -18.921  1.00151.21           C  
ANISOU 1099  CB  MET A  80    22613  19357  15484    481   -675   -172       C  
ATOM   1100  CG  MET A  80      18.412 -38.530 -19.514  1.00155.82           C  
ANISOU 1100  CG  MET A  80    22980  20158  16067    409   -795    -95       C  
ATOM   1101  SD  MET A  80      18.371 -38.382 -21.318  1.00158.65           S  
ANISOU 1101  SD  MET A  80    23184  20479  16616    334   -749   -125       S  
ATOM   1102  CE  MET A  80      20.099 -38.722 -21.706  1.00156.74           C  
ANISOU 1102  CE  MET A  80    22667  20564  16323    302   -876     -6       C  
ATOM   1103  N   LYS A  81      16.635 -38.401 -15.201  1.00149.32           N  
ANISOU 1103  N   LYS A  81    22764  19166  14805    634   -738   -152       N  
ATOM   1104  CA  LYS A  81      16.644 -39.233 -14.012  1.00149.69           C  
ANISOU 1104  CA  LYS A  81    22860  19278  14738    778   -698    -67       C  
ATOM   1105  C   LYS A  81      15.374 -40.098 -13.993  1.00151.63           C  
ANISOU 1105  C   LYS A  81    23162  19376  15074    927   -482    -48       C  
ATOM   1106  O   LYS A  81      15.412 -41.191 -13.427  1.00152.45           O  
ANISOU 1106  O   LYS A  81    23253  19520  15153   1059   -412     61       O  
ATOM   1107  CB  LYS A  81      16.771 -38.383 -12.737  1.00153.54           C  
ANISOU 1107  CB  LYS A  81    23524  19811  15003    725   -821   -120       C  
ATOM   1108  N   THR A  82      14.259 -39.626 -14.628  1.00144.74           N  
ANISOU 1108  N   THR A  82    22350  18342  14302    900   -381   -145       N  
ATOM   1109  CA  THR A  82      12.986 -40.361 -14.682  1.00142.50           C  
ANISOU 1109  CA  THR A  82    22104  17940  14101   1008   -181   -128       C  
ATOM   1110  C   THR A  82      12.842 -41.137 -15.980  1.00142.92           C  
ANISOU 1110  C   THR A  82    22013  17925  14365   1019    -85    -92       C  
ATOM   1111  O   THR A  82      13.499 -40.814 -16.972  1.00141.05           O  
ANISOU 1111  O   THR A  82    21664  17713  14218    938   -161   -118       O  
ATOM   1112  CB  THR A  82      11.766 -39.438 -14.499  1.00145.98           C  
ANISOU 1112  CB  THR A  82    22691  18274  14501    998   -119   -249       C  
ATOM   1113  OG1 THR A  82      11.836 -38.351 -15.416  1.00140.65           O  
ANISOU 1113  OG1 THR A  82    22013  17538  13891    881   -199   -359       O  
ATOM   1114  CG2 THR A  82      11.604 -38.943 -13.076  1.00147.12           C  
ANISOU 1114  CG2 THR A  82    23008  18468  14424   1042   -162   -277       C  
ATOM   1115  N   ALA A  83      11.949 -42.155 -15.967  1.00138.37           N  
ANISOU 1115  N   ALA A  83    21449  17267  13857   1111     81    -31       N  
ATOM   1116  CA  ALA A  83      11.637 -43.004 -17.118  1.00136.43           C  
ANISOU 1116  CA  ALA A  83    21105  16933  13800   1127    185      1       C  
ATOM   1117  C   ALA A  83      10.932 -42.199 -18.190  1.00137.13           C  
ANISOU 1117  C   ALA A  83    21166  16932  14005   1038    217   -115       C  
ATOM   1118  O   ALA A  83      11.245 -42.377 -19.366  1.00136.12           O  
ANISOU 1118  O   ALA A  83    20925  16779  14016   1004    213   -124       O  
ATOM   1119  CB  ALA A  83      10.778 -44.184 -16.700  1.00137.53           C  
ANISOU 1119  CB  ALA A  83    21300  16999  13956   1213    339     94       C  
ATOM   1120  N   THR A  84      10.065 -41.246 -17.786  1.00132.02           N  
ANISOU 1120  N   THR A  84    20624  16250  13286   1013    238   -206       N  
ATOM   1121  CA  THR A  84       9.314 -40.378 -18.702  1.00129.94           C  
ANISOU 1121  CA  THR A  84    20358  15903  13111    949    265   -319       C  
ATOM   1122  C   THR A  84      10.265 -39.459 -19.512  1.00130.85           C  
ANISOU 1122  C   THR A  84    20419  16037  13262    837    112   -383       C  
ATOM   1123  O   THR A  84      10.133 -39.399 -20.731  1.00128.71           O  
ANISOU 1123  O   THR A  84    20056  15713  13133    787    136   -413       O  
ATOM   1124  CB  THR A  84       8.239 -39.586 -17.954  1.00136.14           C  
ANISOU 1124  CB  THR A  84    21283  16666  13778    987    314   -396       C  
ATOM   1125  OG1 THR A  84       7.747 -40.377 -16.868  1.00136.34           O  
ANISOU 1125  OG1 THR A  84    21361  16734  13708   1079    413   -313       O  
ATOM   1126  CG2 THR A  84       7.083 -39.208 -18.858  1.00132.30           C  
ANISOU 1126  CG2 THR A  84    20774  16097  13399    978    414   -471       C  
ATOM   1127  N   ASN A  85      11.256 -38.825 -18.843  1.00126.80           N  
ANISOU 1127  N   ASN A  85    19953  15611  12613    787    -46   -390       N  
ATOM   1128  CA  ASN A  85      12.290 -37.950 -19.428  1.00125.59           C  
ANISOU 1128  CA  ASN A  85    19753  15507  12459    649   -213   -428       C  
ATOM   1129  C   ASN A  85      13.103 -38.651 -20.514  1.00124.83           C  
ANISOU 1129  C   ASN A  85    19456  15477  12498    625   -220   -358       C  
ATOM   1130  O   ASN A  85      13.665 -37.995 -21.395  1.00123.66           O  
ANISOU 1130  O   ASN A  85    19234  15354  12397    505   -312   -391       O  
ATOM   1131  CB  ASN A  85      13.246 -37.468 -18.329  1.00130.41           C  
ANISOU 1131  CB  ASN A  85    20437  16231  12882    603   -374   -414       C  
ATOM   1132  CG  ASN A  85      12.835 -36.202 -17.613  1.00159.89           C  
ANISOU 1132  CG  ASN A  85    24384  19897  16468    556   -454   -525       C  
ATOM   1133  OD1 ASN A  85      13.683 -35.386 -17.232  1.00156.24           O  
ANISOU 1133  OD1 ASN A  85    23987  19492  15885    437   -631   -551       O  
ATOM   1134  ND2 ASN A  85      11.534 -36.011 -17.390  1.00152.40           N  
ANISOU 1134  ND2 ASN A  85    23557  18836  15512    650   -330   -592       N  
ATOM   1135  N   ILE A  86      13.185 -39.978 -20.426  1.00119.35           N  
ANISOU 1135  N   ILE A  86    18685  14812  11852    744   -128   -260       N  
ATOM   1136  CA  ILE A  86      13.890 -40.807 -21.397  1.00117.96           C  
ANISOU 1136  CA  ILE A  86    18336  14692  11790    772   -117   -195       C  
ATOM   1137  C   ILE A  86      12.944 -41.053 -22.600  1.00118.95           C  
ANISOU 1137  C   ILE A  86    18427  14680  12090    772     11   -241       C  
ATOM   1138  O   ILE A  86      13.384 -40.905 -23.743  1.00118.26           O  
ANISOU 1138  O   ILE A  86    18220  14620  12096    716    -19   -258       O  
ATOM   1139  CB  ILE A  86      14.427 -42.100 -20.719  1.00121.45           C  
ANISOU 1139  CB  ILE A  86    18751  15208  12187    917    -89    -72       C  
ATOM   1140  CG1 ILE A  86      15.738 -41.791 -19.975  1.00123.22           C  
ANISOU 1140  CG1 ILE A  86    18929  15628  12259    895   -253    -22       C  
ATOM   1141  CG2 ILE A  86      14.640 -43.248 -21.709  1.00120.69           C  
ANISOU 1141  CG2 ILE A  86    18539  15094  12226   1010    -12    -15       C  
ATOM   1142  CD1 ILE A  86      15.900 -42.466 -18.656  1.00133.34           C  
ANISOU 1142  CD1 ILE A  86    20290  16962  13412   1011   -250     64       C  
ATOM   1143  N   TYR A  87      11.649 -41.364 -22.337  1.00112.46           N  
ANISOU 1143  N   TYR A  87    17701  13731  11297    823    148   -260       N  
ATOM   1144  CA  TYR A  87      10.633 -41.583 -23.368  1.00109.76           C  
ANISOU 1144  CA  TYR A  87    17331  13271  11104    813    268   -303       C  
ATOM   1145  C   TYR A  87      10.369 -40.312 -24.152  1.00111.21           C  
ANISOU 1145  C   TYR A  87    17511  13421  11325    705    218   -410       C  
ATOM   1146  O   TYR A  87      10.198 -40.390 -25.366  1.00110.46           O  
ANISOU 1146  O   TYR A  87    17327  13284  11358    671    252   -436       O  
ATOM   1147  CB  TYR A  87       9.325 -42.101 -22.769  1.00111.02           C  
ANISOU 1147  CB  TYR A  87    17584  13345  11255    872    412   -287       C  
ATOM   1148  CG  TYR A  87       9.264 -43.608 -22.613  1.00113.74           C  
ANISOU 1148  CG  TYR A  87    17922  13656  11639    956    503   -179       C  
ATOM   1149  CD1 TYR A  87       8.822 -44.424 -23.651  1.00114.64           C  
ANISOU 1149  CD1 TYR A  87    17982  13679  11898    955    591   -167       C  
ATOM   1150  CD2 TYR A  87       9.594 -44.212 -21.402  1.00116.12           C  
ANISOU 1150  CD2 TYR A  87    18295  14003  11824   1033    497    -89       C  
ATOM   1151  CE1 TYR A  87       8.759 -45.810 -23.504  1.00116.41           C  
ANISOU 1151  CE1 TYR A  87    18239  13840  12150   1024    663    -69       C  
ATOM   1152  CE2 TYR A  87       9.531 -45.596 -21.241  1.00117.63           C  
ANISOU 1152  CE2 TYR A  87    18511  14139  12043   1109    573     18       C  
ATOM   1153  CZ  TYR A  87       9.106 -46.391 -22.290  1.00126.22           C  
ANISOU 1153  CZ  TYR A  87    19563  15117  13275   1102    654     26       C  
ATOM   1154  OH  TYR A  87       9.034 -47.753 -22.099  1.00131.03           O  
ANISOU 1154  OH  TYR A  87    20237  15646  13902   1170    718    131       O  
ATOM   1155  N   ILE A  88      10.352 -39.144 -23.476  1.00107.10           N  
ANISOU 1155  N   ILE A  88    17101  12910  10684    654    130   -473       N  
ATOM   1156  CA  ILE A  88      10.150 -37.842 -24.130  1.00105.67           C  
ANISOU 1156  CA  ILE A  88    16958  12675  10516    553     61   -573       C  
ATOM   1157  C   ILE A  88      11.384 -37.531 -24.984  1.00108.28           C  
ANISOU 1157  C   ILE A  88    17170  13088  10885    439    -65   -556       C  
ATOM   1158  O   ILE A  88      11.202 -37.049 -26.103  1.00107.74           O  
ANISOU 1158  O   ILE A  88    17054  12973  10910    368    -69   -603       O  
ATOM   1159  CB  ILE A  88       9.825 -36.670 -23.155  1.00109.30           C  
ANISOU 1159  CB  ILE A  88    17609  13102  10820    540    -11   -650       C  
ATOM   1160  CG1 ILE A  88       8.654 -36.992 -22.221  1.00110.31           C  
ANISOU 1160  CG1 ILE A  88    17837  13194  10882    668    119   -657       C  
ATOM   1161  CG2 ILE A  88       9.557 -35.372 -23.918  1.00108.52           C  
ANISOU 1161  CG2 ILE A  88    17578  12916  10740    448    -81   -752       C  
ATOM   1162  CD1 ILE A  88       8.757 -36.321 -20.827  1.00120.24           C  
ANISOU 1162  CD1 ILE A  88    19271  14477  11937    698     41   -690       C  
ATOM   1163  N   PHE A  89      12.623 -37.844 -24.492  1.00103.35           N  
ANISOU 1163  N   PHE A  89    16481  12604  10183    425   -164   -481       N  
ATOM   1164  CA  PHE A  89      13.845 -37.601 -25.270  1.00102.38           C  
ANISOU 1164  CA  PHE A  89    16212  12608  10078    318   -281   -448       C  
ATOM   1165  C   PHE A  89      13.805 -38.381 -26.576  1.00103.89           C  
ANISOU 1165  C   PHE A  89    16246  12800  10428    360   -188   -425       C  
ATOM   1166  O   PHE A  89      14.125 -37.829 -27.625  1.00102.43           O  
ANISOU 1166  O   PHE A  89    15978  12642  10299    255   -238   -448       O  
ATOM   1167  CB  PHE A  89      15.129 -37.942 -24.491  1.00105.18           C  
ANISOU 1167  CB  PHE A  89    16498  13151  10316    322   -389   -359       C  
ATOM   1168  CG  PHE A  89      16.383 -37.666 -25.299  1.00106.86           C  
ANISOU 1168  CG  PHE A  89    16532  13538  10530    206   -508   -314       C  
ATOM   1169  CD1 PHE A  89      16.965 -36.404 -25.303  1.00110.80           C  
ANISOU 1169  CD1 PHE A  89    17062  14093  10943      4   -672   -342       C  
ATOM   1170  CD2 PHE A  89      16.942 -38.652 -26.106  1.00107.95           C  
ANISOU 1170  CD2 PHE A  89    16478  13786  10752    295   -454   -245       C  
ATOM   1171  CE1 PHE A  89      18.105 -36.145 -26.070  1.00111.83           C  
ANISOU 1171  CE1 PHE A  89    17011  14413  11068   -126   -779   -287       C  
ATOM   1172  CE2 PHE A  89      18.072 -38.385 -26.881  1.00111.06           C  
ANISOU 1172  CE2 PHE A  89    16687  14376  11137    196   -553   -200       C  
ATOM   1173  CZ  PHE A  89      18.655 -37.139 -26.843  1.00110.12           C  
ANISOU 1173  CZ  PHE A  89    16576  14336  10928    -23   -714   -213       C  
ATOM   1174  N   SER A  90      13.423 -39.663 -26.490  1.00100.38           N  
ANISOU 1174  N   SER A  90    15777  12321  10044    508    -60   -377       N  
ATOM   1175  CA  SER A  90      13.304 -40.592 -27.607  1.00 99.46           C  
ANISOU 1175  CA  SER A  90    15547  12179  10064    574     36   -358       C  
ATOM   1176  C   SER A  90      12.306 -40.064 -28.629  1.00103.03           C  
ANISOU 1176  C   SER A  90    16014  12506  10627    508     99   -444       C  
ATOM   1177  O   SER A  90      12.626 -39.984 -29.824  1.00101.59           O  
ANISOU 1177  O   SER A  90    15717  12356  10525    462     88   -456       O  
ATOM   1178  CB  SER A  90      12.865 -41.961 -27.099  1.00102.46           C  
ANISOU 1178  CB  SER A  90    15971  12493  10465    727    154   -299       C  
ATOM   1179  OG  SER A  90      13.206 -42.978 -28.020  1.00111.16           O  
ANISOU 1179  OG  SER A  90    16972  13604  11660    810    205   -262       O  
ATOM   1180  N   LEU A  91      11.118 -39.640 -28.139  1.00 99.84           N  
ANISOU 1180  N   LEU A  91    15744  11979  10211    507    159   -500       N  
ATOM   1181  CA  LEU A  91      10.046 -39.089 -28.959  1.00 98.85           C  
ANISOU 1181  CA  LEU A  91    15643  11745  10171    463    220   -580       C  
ATOM   1182  C   LEU A  91      10.513 -37.828 -29.695  1.00103.25           C  
ANISOU 1182  C   LEU A  91    16181  12324  10724    331    102   -632       C  
ATOM   1183  O   LEU A  91      10.351 -37.742 -30.916  1.00101.44           O  
ANISOU 1183  O   LEU A  91    15872  12075  10597    290    125   -658       O  
ATOM   1184  CB  LEU A  91       8.808 -38.784 -28.094  1.00 98.94           C  
ANISOU 1184  CB  LEU A  91    15797  11668  10128    508    292   -622       C  
ATOM   1185  CG  LEU A  91       7.487 -39.473 -28.506  1.00102.98           C  
ANISOU 1185  CG  LEU A  91    16296  12097  10736    562    450   -632       C  
ATOM   1186  CD1 LEU A  91       6.346 -38.919 -27.705  1.00103.54           C  
ANISOU 1186  CD1 LEU A  91    16483  12130  10729    602    505   -676       C  
ATOM   1187  CD2 LEU A  91       7.162 -39.277 -30.006  1.00104.17           C  
ANISOU 1187  CD2 LEU A  91    16356  12207  11017    506    472   -680       C  
ATOM   1188  N   ALA A  92      11.132 -36.879 -28.943  1.00100.96           N  
ANISOU 1188  N   ALA A  92    15976  12078  10308    254    -32   -641       N  
ATOM   1189  CA  ALA A  92      11.664 -35.608 -29.442  1.00100.53           C  
ANISOU 1189  CA  ALA A  92    15943  12035  10218     98   -171   -678       C  
ATOM   1190  C   ALA A  92      12.826 -35.823 -30.412  1.00103.43           C  
ANISOU 1190  C   ALA A  92    16121  12547  10631     16   -233   -618       C  
ATOM   1191  O   ALA A  92      12.978 -35.025 -31.332  1.00103.85           O  
ANISOU 1191  O   ALA A  92    16150  12594  10715   -107   -294   -642       O  
ATOM   1192  CB  ALA A  92      12.107 -34.726 -28.289  1.00102.53           C  
ANISOU 1192  CB  ALA A  92    16346  12300  10310     31   -305   -693       C  
ATOM   1193  N   LEU A  93      13.636 -36.883 -30.225  1.00 98.11           N  
ANISOU 1193  N   LEU A  93    15315  12009   9952     92   -217   -535       N  
ATOM   1194  CA  LEU A  93      14.737 -37.171 -31.138  1.00 97.53           C  
ANISOU 1194  CA  LEU A  93    15043  12106   9907     51   -263   -475       C  
ATOM   1195  C   LEU A  93      14.152 -37.602 -32.476  1.00101.23           C  
ANISOU 1195  C   LEU A  93    15432  12512  10520     93   -153   -505       C  
ATOM   1196  O   LEU A  93      14.561 -37.083 -33.519  1.00100.30           O  
ANISOU 1196  O   LEU A  93    15218  12460  10432    -13   -201   -506       O  
ATOM   1197  CB  LEU A  93      15.693 -38.239 -30.557  1.00 98.14           C  
ANISOU 1197  CB  LEU A  93    15011  12348   9929    168   -267   -382       C  
ATOM   1198  CG  LEU A  93      16.944 -38.622 -31.379  1.00101.99           C  
ANISOU 1198  CG  LEU A  93    15273  13064  10415    167   -313   -308       C  
ATOM   1199  CD1 LEU A  93      17.786 -37.413 -31.738  1.00102.72           C  
ANISOU 1199  CD1 LEU A  93    15294  13300  10437    -53   -467   -292       C  
ATOM   1200  CD2 LEU A  93      17.790 -39.604 -30.630  1.00102.90           C  
ANISOU 1200  CD2 LEU A  93    15311  13331  10454    313   -322   -220       C  
ATOM   1201  N   ALA A  94      13.138 -38.499 -32.427  1.00 97.53           N  
ANISOU 1201  N   ALA A  94    15015  11912  10131    229    -10   -528       N  
ATOM   1202  CA  ALA A  94      12.425 -39.022 -33.594  1.00 95.69           C  
ANISOU 1202  CA  ALA A  94    14730  11600  10030    272    100   -563       C  
ATOM   1203  C   ALA A  94      11.652 -37.914 -34.319  1.00 97.08           C  
ANISOU 1203  C   ALA A  94    14957  11680  10250    161     89   -639       C  
ATOM   1204  O   ALA A  94      11.650 -37.895 -35.548  1.00 96.16           O  
ANISOU 1204  O   ALA A  94    14747  11579  10210    128    108   -655       O  
ATOM   1205  CB  ALA A  94      11.477 -40.126 -33.170  1.00 95.93           C  
ANISOU 1205  CB  ALA A  94    14831  11508  10110    404    235   -563       C  
ATOM   1206  N   GLY A  95      11.043 -36.999 -33.554  1.00 92.00           N  
ANISOU 1206  N   GLY A  95    14467  10945   9544    119     55   -685       N  
ATOM   1207  CA  GLY A  95      10.283 -35.878 -34.084  1.00 90.65           C  
ANISOU 1207  CA  GLY A  95    14380  10670   9392     41     35   -757       C  
ATOM   1208  C   GLY A  95      11.140 -34.873 -34.829  1.00 94.12           C  
ANISOU 1208  C   GLY A  95    14779  11175   9807   -119    -97   -749       C  
ATOM   1209  O   GLY A  95      10.724 -34.380 -35.888  1.00 93.80           O  
ANISOU 1209  O   GLY A  95    14724  11085   9831   -171    -89   -784       O  
ATOM   1210  N   ALA A  96      12.357 -34.572 -34.285  1.00 89.27           N  
ANISOU 1210  N   ALA A  96    14142  10685   9091   -209   -224   -694       N  
ATOM   1211  CA  ALA A  96      13.327 -33.624 -34.855  1.00 88.08           C  
ANISOU 1211  CA  ALA A  96    13945  10629   8891   -399   -369   -662       C  
ATOM   1212  C   ALA A  96      13.936 -34.145 -36.138  1.00 90.44           C  
ANISOU 1212  C   ALA A  96    14026  11072   9265   -417   -340   -613       C  
ATOM   1213  O   ALA A  96      14.205 -33.350 -37.034  1.00 88.92           O  
ANISOU 1213  O   ALA A  96    13802  10907   9076   -561   -409   -607       O  
ATOM   1214  CB  ALA A  96      14.423 -33.333 -33.868  1.00 89.92           C  
ANISOU 1214  CB  ALA A  96    14189  10986   8989   -489   -504   -607       C  
ATOM   1215  N   LEU A  97      14.159 -35.477 -36.232  1.00 87.36           N  
ANISOU 1215  N   LEU A  97    13499  10771   8923   -265   -241   -577       N  
ATOM   1216  CA  LEU A  97      14.699 -36.107 -37.431  1.00 87.29           C  
ANISOU 1216  CA  LEU A  97    13292  10899   8974   -236   -198   -541       C  
ATOM   1217  C   LEU A  97      13.654 -36.097 -38.524  1.00 94.02           C  
ANISOU 1217  C   LEU A  97    14164  11618   9942   -215   -105   -608       C  
ATOM   1218  O   LEU A  97      13.989 -35.889 -39.692  1.00 93.79           O  
ANISOU 1218  O   LEU A  97    14019  11674   9942   -281   -118   -595       O  
ATOM   1219  CB  LEU A  97      15.150 -37.539 -37.147  1.00 87.12           C  
ANISOU 1219  CB  LEU A  97    13168  10974   8959    -50   -122   -495       C  
ATOM   1220  CG  LEU A  97      16.467 -37.690 -36.428  1.00 92.87           C  
ANISOU 1220  CG  LEU A  97    13797  11918   9570    -54   -216   -408       C  
ATOM   1221  CD1 LEU A  97      16.516 -38.999 -35.689  1.00 93.62           C  
ANISOU 1221  CD1 LEU A  97    13898  12013   9662    156   -139   -379       C  
ATOM   1222  CD2 LEU A  97      17.655 -37.525 -37.360  1.00 94.10           C  
ANISOU 1222  CD2 LEU A  97    13735  12331   9686   -129   -282   -341       C  
ATOM   1223  N   ALA A  98      12.379 -36.307 -38.135  1.00 92.01           N  
ANISOU 1223  N   ALA A  98    14045  11172   9741   -128    -13   -673       N  
ATOM   1224  CA  ALA A  98      11.229 -36.333 -39.033  1.00 91.24           C  
ANISOU 1224  CA  ALA A  98    13971  10949   9747   -100     79   -737       C  
ATOM   1225  C   ALA A  98      11.097 -35.012 -39.773  1.00 95.33           C  
ANISOU 1225  C   ALA A  98    14527  11435  10258   -246     -1   -763       C  
ATOM   1226  O   ALA A  98      11.073 -35.013 -41.003  1.00 94.15           O  
ANISOU 1226  O   ALA A  98    14284  11321  10169   -276     21   -768       O  
ATOM   1227  CB  ALA A  98       9.964 -36.622 -38.243  1.00 91.65           C  
ANISOU 1227  CB  ALA A  98    14157  10843   9821     -5    169   -786       C  
ATOM   1228  N   THR A  99      11.082 -33.887 -39.025  1.00 92.66           N  
ANISOU 1228  N   THR A  99    14339  11031   9836   -337   -103   -776       N  
ATOM   1229  CA  THR A  99      10.947 -32.537 -39.578  1.00 92.82           C  
ANISOU 1229  CA  THR A  99    14453  10984   9832   -478   -198   -798       C  
ATOM   1230  C   THR A  99      12.212 -32.074 -40.323  1.00 96.94           C  
ANISOU 1230  C   THR A  99    14854  11667  10313   -651   -310   -725       C  
ATOM   1231  O   THR A  99      12.101 -31.227 -41.205  1.00 95.86           O  
ANISOU 1231  O   THR A  99    14744  11493  10184   -764   -361   -728       O  
ATOM   1232  CB  THR A  99      10.559 -31.535 -38.487  1.00105.33           C  
ANISOU 1232  CB  THR A  99    16268  12430  11322   -505   -277   -840       C  
ATOM   1233  OG1 THR A  99      11.366 -31.758 -37.331  1.00109.58           O  
ANISOU 1233  OG1 THR A  99    16820  13047  11771   -518   -337   -800       O  
ATOM   1234  CG2 THR A  99       9.084 -31.612 -38.113  1.00103.09           C  
ANISOU 1234  CG2 THR A  99    16106  11991  11072   -350   -169   -920       C  
ATOM   1235  N   SER A 100      13.395 -32.647 -40.015  1.00 95.35           N  
ANISOU 1235  N   SER A 100    14509  11659  10062   -669   -345   -650       N  
ATOM   1236  CA  SER A 100      14.657 -32.275 -40.667  1.00 96.81           C  
ANISOU 1236  CA  SER A 100    14542  12051  10190   -834   -447   -564       C  
ATOM   1237  C   SER A 100      14.675 -32.674 -42.153  1.00103.58           C  
ANISOU 1237  C   SER A 100    15230  13001  11126   -814   -374   -553       C  
ATOM   1238  O   SER A 100      15.557 -32.223 -42.878  1.00104.08           O  
ANISOU 1238  O   SER A 100    15171  13233  11143   -962   -450   -483       O  
ATOM   1239  CB  SER A 100      15.847 -32.886 -39.933  1.00100.68           C  
ANISOU 1239  CB  SER A 100    14899  12755  10600   -820   -490   -486       C  
ATOM   1240  OG  SER A 100      16.002 -34.267 -40.215  1.00108.48           O  
ANISOU 1240  OG  SER A 100    15724  13849  11644   -626   -368   -473       O  
ATOM   1241  N   THR A 101      13.698 -33.497 -42.605  1.00101.19           N  
ANISOU 1241  N   THR A 101    14922  12595  10932   -642   -231   -618       N  
ATOM   1242  CA  THR A 101      13.563 -33.933 -43.998  1.00100.94           C  
ANISOU 1242  CA  THR A 101    14755  12623  10972   -604   -154   -625       C  
ATOM   1243  C   THR A 101      12.715 -32.930 -44.794  1.00106.38           C  
ANISOU 1243  C   THR A 101    15548  13173  11700   -699   -173   -668       C  
ATOM   1244  O   THR A 101      12.936 -32.787 -45.996  1.00106.68           O  
ANISOU 1244  O   THR A 101    15479  13301  11755   -757   -172   -647       O  
ATOM   1245  CB  THR A 101      12.964 -35.356 -44.096  1.00106.33           C  
ANISOU 1245  CB  THR A 101    15397  13261  11743   -390     -5   -673       C  
ATOM   1246  OG1 THR A 101      11.578 -35.359 -43.744  1.00104.23           O  
ANISOU 1246  OG1 THR A 101    15286  12775  11541   -324     64   -750       O  
ATOM   1247  CG2 THR A 101      13.730 -36.386 -43.263  1.00107.34           C  
ANISOU 1247  CG2 THR A 101    15456  13497  11830   -269     14   -630       C  
ATOM   1248  N   LEU A 102      11.741 -32.252 -44.123  1.00102.93           N  
ANISOU 1248  N   LEU A 102    15318  12525  11264   -696   -188   -728       N  
ATOM   1249  CA  LEU A 102      10.804 -31.289 -44.714  1.00102.03           C  
ANISOU 1249  CA  LEU A 102    15335  12257  11177   -743   -206   -775       C  
ATOM   1250  C   LEU A 102      11.482 -30.298 -45.645  1.00106.35           C  
ANISOU 1250  C   LEU A 102    15856  12874  11678   -938   -316   -715       C  
ATOM   1251  O   LEU A 102      11.046 -30.279 -46.786  1.00104.64           O  
ANISOU 1251  O   LEU A 102    15585  12656  11517   -930   -271   -729       O  
ATOM   1252  CB  LEU A 102       9.973 -30.541 -43.670  1.00102.34           C  
ANISOU 1252  CB  LEU A 102    15611  12098  11178   -714   -239   -832       C  
ATOM   1253  CG  LEU A 102       8.790 -31.318 -43.129  1.00106.69           C  
ANISOU 1253  CG  LEU A 102    16199  12551  11788   -521   -106   -902       C  
ATOM   1254  CD1 LEU A 102       8.347 -30.773 -41.792  1.00108.03           C  
ANISOU 1254  CD1 LEU A 102    16567  12595  11883   -478   -142   -939       C  
ATOM   1255  CD2 LEU A 102       7.649 -31.323 -44.111  1.00108.16           C  
ANISOU 1255  CD2 LEU A 102    16373  12666  12056   -454    -23   -953       C  
ATOM   1256  N   PRO A 103      12.573 -29.560 -45.278  1.00105.84           N  
ANISOU 1256  N   PRO A 103    15810  12895  11510  -1124   -458   -641       N  
ATOM   1257  CA  PRO A 103      13.201 -28.632 -46.251  1.00107.04           C  
ANISOU 1257  CA  PRO A 103    15931  13124  11614  -1338   -563   -568       C  
ATOM   1258  C   PRO A 103      13.533 -29.238 -47.632  1.00111.10           C  
ANISOU 1258  C   PRO A 103    16210  13829  12176  -1324   -489   -529       C  
ATOM   1259  O   PRO A 103      13.360 -28.556 -48.640  1.00109.97           O  
ANISOU 1259  O   PRO A 103    16084  13666  12034  -1425   -521   -509       O  
ATOM   1260  CB  PRO A 103      14.493 -28.186 -45.550  1.00110.32           C  
ANISOU 1260  CB  PRO A 103    16328  13678  11910  -1528   -706   -479       C  
ATOM   1261  CG  PRO A 103      14.597 -29.001 -44.303  1.00114.50           C  
ANISOU 1261  CG  PRO A 103    16849  14225  12431  -1388   -663   -505       C  
ATOM   1262  CD  PRO A 103      13.227 -29.440 -43.959  1.00108.49           C  
ANISOU 1262  CD  PRO A 103    16210  13252  11757  -1171   -541   -615       C  
ATOM   1263  N   PHE A 104      13.980 -30.507 -47.682  1.00108.37           N  
ANISOU 1263  N   PHE A 104    15661  13657  11857  -1187   -391   -521       N  
ATOM   1264  CA  PHE A 104      14.329 -31.209 -48.926  1.00108.32           C  
ANISOU 1264  CA  PHE A 104    15436  13839  11880  -1135   -313   -496       C  
ATOM   1265  C   PHE A 104      13.156 -31.611 -49.794  1.00111.72           C  
ANISOU 1265  C   PHE A 104    15904  14125  12418   -992   -196   -588       C  
ATOM   1266  O   PHE A 104      13.212 -31.405 -50.998  1.00110.71           O  
ANISOU 1266  O   PHE A 104    15697  14066  12303  -1031   -180   -575       O  
ATOM   1267  CB  PHE A 104      15.210 -32.436 -48.641  1.00110.95           C  
ANISOU 1267  CB  PHE A 104    15575  14387  12192  -1004   -254   -465       C  
ATOM   1268  CG  PHE A 104      16.403 -32.127 -47.773  1.00114.69           C  
ANISOU 1268  CG  PHE A 104    15994  15028  12555  -1125   -366   -374       C  
ATOM   1269  CD1 PHE A 104      17.582 -31.655 -48.327  1.00119.54           C  
ANISOU 1269  CD1 PHE A 104    16440  15910  13071  -1302   -453   -261       C  
ATOM   1270  CD2 PHE A 104      16.336 -32.278 -46.397  1.00117.71           C  
ANISOU 1270  CD2 PHE A 104    16490  15315  12920  -1074   -390   -395       C  
ATOM   1271  CE1 PHE A 104      18.679 -31.343 -47.520  1.00122.32           C  
ANISOU 1271  CE1 PHE A 104    16728  16437  13310  -1436   -567   -170       C  
ATOM   1272  CE2 PHE A 104      17.432 -31.958 -45.591  1.00122.39           C  
ANISOU 1272  CE2 PHE A 104    17033  16070  13401  -1198   -505   -311       C  
ATOM   1273  CZ  PHE A 104      18.595 -31.491 -46.158  1.00121.90           C  
ANISOU 1273  CZ  PHE A 104    16795  16277  13242  -1384   -596   -199       C  
ATOM   1274  N   GLN A 105      12.098 -32.176 -49.191  1.00110.15           N  
ANISOU 1274  N   GLN A 105    15819  13744  12288   -838   -118   -674       N  
ATOM   1275  CA  GLN A 105      10.871 -32.593 -49.887  1.00110.60           C  
ANISOU 1275  CA  GLN A 105    15911  13669  12442   -710     -9   -760       C  
ATOM   1276  C   GLN A 105       9.923 -31.384 -50.221  1.00118.48           C  
ANISOU 1276  C   GLN A 105    17051  14520  13447   -795    -60   -782       C  
ATOM   1277  O   GLN A 105       9.054 -31.476 -51.093  1.00116.77           O  
ANISOU 1277  O   GLN A 105    16810  14268  13288   -745      2   -824       O  
ATOM   1278  CB  GLN A 105      10.063 -33.592 -49.029  1.00111.63           C  
ANISOU 1278  CB  GLN A 105    16114  13674  12625   -548     80   -825       C  
ATOM   1279  CG  GLN A 105      10.760 -34.969 -48.836  1.00133.55           C  
ANISOU 1279  CG  GLN A 105    18770  16568  15405   -428    145   -809       C  
ATOM   1280  CD  GLN A 105      10.052 -35.974 -47.944  1.00158.01           C  
ANISOU 1280  CD  GLN A 105    21931  19541  18564   -274    249   -866       C  
ATOM   1281  OE1 GLN A 105      10.243 -37.193 -48.076  1.00152.55           O  
ANISOU 1281  OE1 GLN A 105    21168  18905  17889   -160    313   -865       O  
ATOM   1282  NE2 GLN A 105       9.202 -35.509 -47.045  1.00152.24           N  
ANISOU 1282  NE2 GLN A 105    21340  18645  17861   -263    267   -914       N  
ATOM   1283  N   SER A 106      10.147 -30.243 -49.522  1.00119.93           N  
ANISOU 1283  N   SER A 106    17393  14612  13561   -918   -178   -755       N  
ATOM   1284  CA  SER A 106       9.446 -28.965 -49.721  1.00121.55           C  
ANISOU 1284  CA  SER A 106    17774  14662  13749   -995   -251   -768       C  
ATOM   1285  C   SER A 106      10.082 -28.360 -50.964  1.00128.36           C  
ANISOU 1285  C   SER A 106    18558  15635  14577  -1158   -318   -692       C  
ATOM   1286  O   SER A 106       9.398 -27.679 -51.725  1.00128.65           O  
ANISOU 1286  O   SER A 106    18679  15576  14627  -1176   -334   -706       O  
ATOM   1287  CB  SER A 106       9.530 -27.973 -48.566  1.00126.88           C  
ANISOU 1287  CB  SER A 106    18670  15195  14344  -1069   -367   -765       C  
ATOM   1288  OG  SER A 106       9.032 -28.542 -47.366  1.00138.51           O  
ANISOU 1288  OG  SER A 106    20203  16593  15832   -921   -305   -825       O  
ATOM   1289  N   ALA A 107      11.398 -28.601 -51.157  1.00126.23           N  
ANISOU 1289  N   ALA A 107    18123  15585  14253  -1272   -357   -605       N  
ATOM   1290  CA  ALA A 107      12.164 -28.151 -52.317  1.00127.12           C  
ANISOU 1290  CA  ALA A 107    18118  15865  14317  -1437   -411   -514       C  
ATOM   1291  C   ALA A 107      11.762 -28.967 -53.533  1.00133.30           C  
ANISOU 1291  C   ALA A 107    18742  16740  15167  -1314   -289   -549       C  
ATOM   1292  O   ALA A 107      11.478 -28.392 -54.578  1.00132.65           O  
ANISOU 1292  O   ALA A 107    18670  16649  15081  -1382   -308   -529       O  
ATOM   1293  CB  ALA A 107      13.656 -28.286 -52.054  1.00128.75           C  
ANISOU 1293  CB  ALA A 107    18165  16319  14434  -1570   -475   -411       C  
ATOM   1294  N   ASP A 108      11.678 -30.305 -53.375  1.00132.20           N  
ANISOU 1294  N   ASP A 108    18478  16667  15084  -1128   -169   -605       N  
ATOM   1295  CA  ASP A 108      11.296 -31.242 -54.430  1.00132.80           C  
ANISOU 1295  CA  ASP A 108    18422  16816  15219   -996    -54   -654       C  
ATOM   1296  C   ASP A 108       9.878 -30.931 -54.955  1.00137.08           C  
ANISOU 1296  C   ASP A 108    19084  17170  15832   -941    -16   -730       C  
ATOM   1297  O   ASP A 108       9.666 -31.064 -56.155  1.00136.80           O  
ANISOU 1297  O   ASP A 108    18966  17202  15810   -932     21   -737       O  
ATOM   1298  CB  ASP A 108      11.412 -32.704 -53.948  1.00135.03           C  
ANISOU 1298  CB  ASP A 108    18614  17149  15542   -808     51   -704       C  
ATOM   1299  CG  ASP A 108      11.226 -33.756 -55.035  1.00152.27           C  
ANISOU 1299  CG  ASP A 108    20671  19420  17765   -678    157   -753       C  
ATOM   1300  OD1 ASP A 108      10.074 -33.974 -55.459  1.00154.13           O1-
ANISOU 1300  OD1 ASP A 108    20973  19517  18074   -609    216   -832       O1-
ATOM   1301  OD2 ASP A 108      12.240 -34.385 -55.446  1.00159.56           O1-
ANISOU 1301  OD2 ASP A 108    21430  20559  18635   -636    178   -714       O1-
ATOM   1302  N   TYR A 109       8.930 -30.491 -54.083  1.00133.53           N  
ANISOU 1302  N   TYR A 109    18818  16504  15412   -900    -29   -782       N  
ATOM   1303  CA  TYR A 109       7.566 -30.129 -54.506  1.00132.87           C  
ANISOU 1303  CA  TYR A 109    18837  16266  15379   -835      1   -847       C  
ATOM   1304  C   TYR A 109       7.609 -28.911 -55.431  1.00135.40           C  
ANISOU 1304  C   TYR A 109    19218  16576  15652   -969    -90   -792       C  
ATOM   1305  O   TYR A 109       6.949 -28.900 -56.471  1.00134.16           O  
ANISOU 1305  O   TYR A 109    19027  16422  15524   -934    -54   -815       O  
ATOM   1306  CB  TYR A 109       6.635 -29.854 -53.288  1.00134.95           C  
ANISOU 1306  CB  TYR A 109    19278  16336  15660   -749      4   -904       C  
ATOM   1307  CG  TYR A 109       5.334 -29.143 -53.646  1.00138.01           C  
ANISOU 1307  CG  TYR A 109    19786  16585  16066   -691      5   -951       C  
ATOM   1308  CD1 TYR A 109       4.298 -29.817 -54.286  1.00139.93           C  
ANISOU 1308  CD1 TYR A 109    19952  16837  16378   -578    106  -1012       C  
ATOM   1309  CD2 TYR A 109       5.154 -27.784 -53.369  1.00139.55           C  
ANISOU 1309  CD2 TYR A 109    20180  16643  16199   -748   -102   -931       C  
ATOM   1310  CE1 TYR A 109       3.116 -29.162 -54.647  1.00141.37           C  
ANISOU 1310  CE1 TYR A 109    20222  16926  16567   -515    104  -1047       C  
ATOM   1311  CE2 TYR A 109       3.980 -27.116 -53.734  1.00140.46           C  
ANISOU 1311  CE2 TYR A 109    20407  16643  16318   -666   -104   -970       C  
ATOM   1312  CZ  TYR A 109       2.961 -27.809 -54.372  1.00146.63           C  
ANISOU 1312  CZ  TYR A 109    21079  17466  17168   -545      3  -1026       C  
ATOM   1313  OH  TYR A 109       1.793 -27.164 -54.737  1.00145.72           O  
ANISOU 1313  OH  TYR A 109    21051  17268  17048   -451      1  -1058       O  
ATOM   1314  N   LEU A 110       8.389 -27.891 -55.035  1.00132.51           N  
ANISOU 1314  N   LEU A 110    18950  16193  15205  -1133   -216   -714       N  
ATOM   1315  CA  LEU A 110       8.519 -26.620 -55.745  1.00132.85           C  
ANISOU 1315  CA  LEU A 110    19096  16194  15186  -1292   -327   -644       C  
ATOM   1316  C   LEU A 110       9.238 -26.761 -57.089  1.00137.07           C  
ANISOU 1316  C   LEU A 110    19443  16944  15692  -1394   -321   -570       C  
ATOM   1317  O   LEU A 110       8.729 -26.234 -58.078  1.00137.18           O  
ANISOU 1317  O   LEU A 110    19493  16925  15703  -1416   -335   -559       O  
ATOM   1318  CB  LEU A 110       9.231 -25.556 -54.885  1.00133.78           C  
ANISOU 1318  CB  LEU A 110    19387  16231  15214  -1467   -475   -577       C  
ATOM   1319  CG  LEU A 110       8.512 -25.082 -53.621  1.00137.82           C  
ANISOU 1319  CG  LEU A 110    20138  16505  15721  -1381   -510   -647       C  
ATOM   1320  CD1 LEU A 110       9.473 -24.384 -52.700  1.00139.43           C  
ANISOU 1320  CD1 LEU A 110    20465  16680  15831  -1559   -647   -585       C  
ATOM   1321  CD2 LEU A 110       7.324 -24.187 -53.942  1.00139.01           C  
ANISOU 1321  CD2 LEU A 110    20498  16447  15874  -1305   -536   -691       C  
ATOM   1322  N   MET A 111      10.395 -27.457 -57.142  1.00133.04           N  
ANISOU 1322  N   MET A 111    18733  16666  15150  -1441   -300   -517       N  
ATOM   1323  CA  MET A 111      11.149 -27.592 -58.395  1.00132.94           C  
ANISOU 1323  CA  MET A 111    18528  16895  15090  -1526   -290   -441       C  
ATOM   1324  C   MET A 111      10.837 -28.900 -59.176  1.00135.04           C  
ANISOU 1324  C   MET A 111    18614  17280  15414  -1336   -146   -517       C  
ATOM   1325  O   MET A 111      11.376 -29.087 -60.272  1.00134.36           O  
ANISOU 1325  O   MET A 111    18370  17400  15283  -1372   -124   -470       O  
ATOM   1326  CB  MET A 111      12.664 -27.430 -58.162  1.00136.47           C  
ANISOU 1326  CB  MET A 111    18849  17569  15435  -1703   -364   -321       C  
ATOM   1327  CG  MET A 111      13.278 -28.446 -57.219  1.00139.51           C  
ANISOU 1327  CG  MET A 111    19118  18063  15827  -1596   -313   -344       C  
ATOM   1328  SD  MET A 111      14.706 -27.801 -56.301  1.00144.80           S  
ANISOU 1328  SD  MET A 111    19763  18877  16378  -1829   -453   -214       S  
ATOM   1329  CE  MET A 111      15.795 -27.280 -57.638  1.00142.85           C  
ANISOU 1329  CE  MET A 111    19317  18946  16014  -2052   -507    -59       C  
ATOM   1330  N   GLU A 112       9.962 -29.775 -58.625  1.00130.94           N  
ANISOU 1330  N   GLU A 112    18132  16632  14985  -1144    -54   -632       N  
ATOM   1331  CA  GLU A 112       9.492 -31.059 -59.203  1.00130.31           C  
ANISOU 1331  CA  GLU A 112    17940  16605  14968   -966     73   -721       C  
ATOM   1332  C   GLU A 112      10.630 -32.125 -59.429  1.00132.28           C  
ANISOU 1332  C   GLU A 112    17990  17096  15176   -904    128   -700       C  
ATOM   1333  O   GLU A 112      10.330 -33.313 -59.633  1.00132.09           O  
ANISOU 1333  O   GLU A 112    17910  17082  15197   -740    226   -782       O  
ATOM   1334  CB  GLU A 112       8.705 -30.840 -60.517  1.00131.86           C  
ANISOU 1334  CB  GLU A 112    18128  16793  15179   -958     96   -748       C  
ATOM   1335  CG  GLU A 112       7.323 -30.214 -60.332  1.00145.00           C  
ANISOU 1335  CG  GLU A 112    19965  18230  16899   -925     82   -802       C  
ATOM   1336  CD  GLU A 112       7.208 -28.707 -60.514  1.00166.65           C  
ANISOU 1336  CD  GLU A 112    22850  20880  19590  -1063    -33   -730       C  
ATOM   1337  OE1 GLU A 112       7.668 -28.187 -61.559  1.00153.13           O  
ANISOU 1337  OE1 GLU A 112    21083  19281  17817  -1175    -76   -656       O  
ATOM   1338  OE2 GLU A 112       6.589 -28.054 -59.641  1.00160.53           O1-
ANISOU 1338  OE2 GLU A 112    22253  19913  18828  -1047    -78   -751       O1-
ATOM   1339  N   THR A 113      11.916 -31.696 -59.344  1.00125.81           N  
ANISOU 1339  N   THR A 113    17072  16468  14261  -1033     60   -589       N  
ATOM   1340  CA  THR A 113      13.150 -32.482 -59.543  1.00123.35           C  
ANISOU 1340  CA  THR A 113    16554  16436  13877   -982     94   -543       C  
ATOM   1341  C   THR A 113      13.925 -32.616 -58.199  1.00120.42           C  
ANISOU 1341  C   THR A 113    16178  16098  13478   -992     53   -501       C  
ATOM   1342  O   THR A 113      13.755 -31.776 -57.309  1.00119.61           O  
ANISOU 1342  O   THR A 113    16220  15846  13381  -1112    -32   -476       O  
ATOM   1343  CB  THR A 113      13.982 -31.765 -60.636  1.00126.48           C  
ANISOU 1343  CB  THR A 113    16813  17077  14166  -1146     42   -428       C  
ATOM   1344  OG1 THR A 113      13.169 -31.609 -61.801  1.00126.11           O  
ANISOU 1344  OG1 THR A 113    16794  16976  14146  -1131     75   -470       O  
ATOM   1345  CG2 THR A 113      15.279 -32.479 -61.000  1.00121.60           C  
ANISOU 1345  CG2 THR A 113    15951  16803  13447  -1088     80   -368       C  
ATOM   1346  N   TRP A 114      14.759 -33.681 -58.067  1.00111.91           N  
ANISOU 1346  N   TRP A 114    14944  15214  12361   -850    111   -498       N  
ATOM   1347  CA  TRP A 114      15.597 -33.939 -56.894  1.00109.57           C  
ANISOU 1347  CA  TRP A 114    14608  14999  12023   -835     78   -452       C  
ATOM   1348  C   TRP A 114      17.062 -33.521 -57.183  1.00111.69           C  
ANISOU 1348  C   TRP A 114    14666  15618  12152   -971     11   -311       C  
ATOM   1349  O   TRP A 114      17.829 -34.289 -57.773  1.00110.79           O  
ANISOU 1349  O   TRP A 114    14355  15770  11971   -845     71   -290       O  
ATOM   1350  CB  TRP A 114      15.505 -35.407 -56.439  1.00107.20           C  
ANISOU 1350  CB  TRP A 114    14296  14669  11767   -572    181   -537       C  
ATOM   1351  CG  TRP A 114      16.354 -35.711 -55.238  1.00108.50           C  
ANISOU 1351  CG  TRP A 114    14420  14921  11883   -536    147   -486       C  
ATOM   1352  CD1 TRP A 114      17.629 -36.196 -55.236  1.00112.63           C  
ANISOU 1352  CD1 TRP A 114    14745  15749  12302   -467    146   -412       C  
ATOM   1353  CD2 TRP A 114      16.016 -35.466 -53.864  1.00107.76           C  
ANISOU 1353  CD2 TRP A 114    14481  14635  11828   -571    102   -497       C  
ATOM   1354  NE1 TRP A 114      18.087 -36.320 -53.946  1.00112.33           N  
ANISOU 1354  NE1 TRP A 114    14728  15712  12240   -454    103   -378       N  
ATOM   1355  CE2 TRP A 114      17.121 -35.869 -53.084  1.00112.62           C  
ANISOU 1355  CE2 TRP A 114    14985  15442  12363   -524     74   -429       C  
ATOM   1356  CE3 TRP A 114      14.878 -34.958 -53.212  1.00107.65           C  
ANISOU 1356  CE3 TRP A 114    14685  14321  11898   -623     85   -557       C  
ATOM   1357  CZ2 TRP A 114      17.121 -35.782 -51.686  1.00111.67           C  
ANISOU 1357  CZ2 TRP A 114    14973  15211  12248   -538     26   -423       C  
ATOM   1358  CZ3 TRP A 114      14.877 -34.885 -51.831  1.00108.92           C  
ANISOU 1358  CZ3 TRP A 114    14951  14376  12058   -627     45   -553       C  
ATOM   1359  CH2 TRP A 114      15.988 -35.293 -51.082  1.00110.50           C  
ANISOU 1359  CH2 TRP A 114    15045  14759  12180   -591     14   -487       C  
ATOM   1360  N   PRO A 115      17.471 -32.314 -56.738  1.00108.50           N  
ANISOU 1360  N   PRO A 115    14306  15225  11692  -1227   -118   -211       N  
ATOM   1361  CA  PRO A 115      18.841 -31.846 -57.026  1.00110.63           C  
ANISOU 1361  CA  PRO A 115    14368  15848  11819  -1402   -193    -60       C  
ATOM   1362  C   PRO A 115      19.952 -32.325 -56.070  1.00116.88           C  
ANISOU 1362  C   PRO A 115    15016  16862  12532  -1362   -219      3       C  
ATOM   1363  O   PRO A 115      21.130 -32.270 -56.416  1.00118.31           O  
ANISOU 1363  O   PRO A 115    14961  17406  12585  -1440   -249    122       O  
ATOM   1364  CB  PRO A 115      18.703 -30.327 -56.915  1.00112.44           C  
ANISOU 1364  CB  PRO A 115    14752  15947  12023  -1715   -334     16       C  
ATOM   1365  CG  PRO A 115      17.624 -30.121 -55.925  1.00114.70           C  
ANISOU 1365  CG  PRO A 115    15313  15853  12415  -1668   -350    -88       C  
ATOM   1366  CD  PRO A 115      16.680 -31.272 -56.047  1.00108.64           C  
ANISOU 1366  CD  PRO A 115    14575  14941  11761  -1377   -206   -229       C  
ATOM   1367  N   PHE A 116      19.580 -32.755 -54.871  1.00113.31           N  
ANISOU 1367  N   PHE A 116    14698  16212  12144  -1248   -212    -67       N  
ATOM   1368  CA  PHE A 116      20.473 -33.135 -53.777  1.00114.07           C  
ANISOU 1368  CA  PHE A 116    14707  16462  12174  -1211   -250    -15       C  
ATOM   1369  C   PHE A 116      21.280 -34.445 -54.021  1.00119.02           C  
ANISOU 1369  C   PHE A 116    15098  17381  12742   -945   -152     -8       C  
ATOM   1370  O   PHE A 116      22.269 -34.682 -53.322  1.00119.29           O  
ANISOU 1370  O   PHE A 116    14996  17644  12685   -927   -193     68       O  
ATOM   1371  CB  PHE A 116      19.649 -33.225 -52.483  1.00114.55           C  
ANISOU 1371  CB  PHE A 116    15011  16189  12326  -1149   -258   -104       C  
ATOM   1372  CG  PHE A 116      18.651 -32.093 -52.328  1.00115.13           C  
ANISOU 1372  CG  PHE A 116    15339  15943  12461  -1326   -327   -142       C  
ATOM   1373  CD1 PHE A 116      19.077 -30.806 -52.011  1.00119.02           C  
ANISOU 1373  CD1 PHE A 116    15902  16443  12877  -1618   -479    -52       C  
ATOM   1374  CD2 PHE A 116      17.291 -32.302 -52.551  1.00115.74           C  
ANISOU 1374  CD2 PHE A 116    15590  15725  12662  -1201   -245   -265       C  
ATOM   1375  CE1 PHE A 116      18.159 -29.754 -51.905  1.00119.33           C  
ANISOU 1375  CE1 PHE A 116    16203  16177  12961  -1753   -545    -92       C  
ATOM   1376  CE2 PHE A 116      16.370 -31.249 -52.437  1.00118.10           C  
ANISOU 1376  CE2 PHE A 116    16117  15753  13004  -1332   -306   -298       C  
ATOM   1377  CZ  PHE A 116      16.814 -29.983 -52.116  1.00117.12           C  
ANISOU 1377  CZ  PHE A 116    16079  15620  12800  -1593   -455   -215       C  
ATOM   1378  N   GLY A 117      20.886 -35.245 -55.013  1.00116.05           N  
ANISOU 1378  N   GLY A 117    14683  17006  12406   -741    -33    -86       N  
ATOM   1379  CA  GLY A 117      21.597 -36.476 -55.362  1.00117.52           C  
ANISOU 1379  CA  GLY A 117    14680  17446  12525   -462     60    -92       C  
ATOM   1380  C   GLY A 117      21.249 -37.705 -54.541  1.00121.47           C  
ANISOU 1380  C   GLY A 117    15292  17770  13092   -177    135   -190       C  
ATOM   1381  O   GLY A 117      20.553 -37.592 -53.531  1.00120.30           O  
ANISOU 1381  O   GLY A 117    15343  17334  13033   -211    110   -237       O  
ATOM   1382  N   GLU A 118      21.765 -38.890 -54.967  1.00118.41           N  
ANISOU 1382  N   GLU A 118    14781  17561  12647    114    225   -216       N  
ATOM   1383  CA  GLU A 118      21.520 -40.216 -54.379  1.00117.35           C  
ANISOU 1383  CA  GLU A 118    14756  17273  12557    417    302   -305       C  
ATOM   1384  C   GLU A 118      21.925 -40.337 -52.908  1.00121.36           C  
ANISOU 1384  C   GLU A 118    15296  17766  13048    434    246   -256       C  
ATOM   1385  O   GLU A 118      21.188 -40.947 -52.134  1.00119.63           O  
ANISOU 1385  O   GLU A 118    15279  17252  12921    546    280   -334       O  
ATOM   1386  CB  GLU A 118      22.218 -41.317 -55.181  1.00119.92           C  
ANISOU 1386  CB  GLU A 118    14933  17844  12785    719    389   -323       C  
ATOM   1387  CG  GLU A 118      21.464 -42.632 -55.124  1.00128.67           C  
ANISOU 1387  CG  GLU A 118    16248  18665  13977   1002    483   -460       C  
ATOM   1388  CD  GLU A 118      22.040 -43.719 -56.000  1.00155.98           C  
ANISOU 1388  CD  GLU A 118    19615  22316  17336   1318    566   -500       C  
ATOM   1389  OE1 GLU A 118      23.050 -44.338 -55.592  1.00156.84           O  
ANISOU 1389  OE1 GLU A 118    19601  22660  17331   1532    570   -446       O  
ATOM   1390  OE2 GLU A 118      21.476 -43.959 -57.091  1.00153.45           O1-
ANISOU 1390  OE2 GLU A 118    19350  21912  17043   1365    625   -588       O1-
ATOM   1391  N   LEU A 119      23.087 -39.787 -52.530  1.00119.89           N  
ANISOU 1391  N   LEU A 119    14907  17909  12736    319    160   -123       N  
ATOM   1392  CA  LEU A 119      23.605 -39.827 -51.154  1.00120.28           C  
ANISOU 1392  CA  LEU A 119    14958  17998  12745    317     91    -63       C  
ATOM   1393  C   LEU A 119      22.632 -39.123 -50.197  1.00117.10           C  
ANISOU 1393  C   LEU A 119    14808  17231  12454    119     33   -105       C  
ATOM   1394  O   LEU A 119      22.384 -39.648 -49.119  1.00115.41           O  
ANISOU 1394  O   LEU A 119    14724  16851  12275    232     39   -136       O  
ATOM   1395  CB  LEU A 119      25.013 -39.200 -51.071  1.00123.61           C  
ANISOU 1395  CB  LEU A 119    15093  18873  12999    171     -6     97       C  
ATOM   1396  CG  LEU A 119      25.985 -39.534 -52.227  1.00131.95           C  
ANISOU 1396  CG  LEU A 119    15856  20357  13920    295     42    161       C  
ATOM   1397  CD1 LEU A 119      26.897 -38.334 -52.565  1.00134.19           C  
ANISOU 1397  CD1 LEU A 119    15901  21006  14077    -34    -66    318       C  
ATOM   1398  CD2 LEU A 119      26.768 -40.833 -51.967  1.00137.28           C  
ANISOU 1398  CD2 LEU A 119    16406  21253  14502    677    107    167       C  
ATOM   1399  N   LEU A 120      22.049 -37.973 -50.612  1.00109.94           N  
ANISOU 1399  N   LEU A 120    13980  16195  11596   -153    -19   -109       N  
ATOM   1400  CA  LEU A 120      21.057 -37.232 -49.823  1.00107.12           C  
ANISOU 1400  CA  LEU A 120    13874  15493  11334   -320    -70   -158       C  
ATOM   1401  C   LEU A 120      19.637 -37.769 -50.045  1.00107.16           C  
ANISOU 1401  C   LEU A 120    14091  15140  11486   -188     34   -296       C  
ATOM   1402  O   LEU A 120      18.724 -37.379 -49.324  1.00105.52           O  
ANISOU 1402  O   LEU A 120    14089  14650  11355   -261     16   -348       O  
ATOM   1403  CB  LEU A 120      21.091 -35.727 -50.137  1.00107.24           C  
ANISOU 1403  CB  LEU A 120    13902  15524  11320   -658   -184    -95       C  
ATOM   1404  CG  LEU A 120      21.584 -34.826 -49.024  1.00112.86           C  
ANISOU 1404  CG  LEU A 120    14659  16261  11961   -881   -326    -18       C  
ATOM   1405  CD1 LEU A 120      21.746 -33.355 -49.480  1.00114.15           C  
ANISOU 1405  CD1 LEU A 120    14841  16454  12075  -1227   -450     57       C  
ATOM   1406  CD2 LEU A 120      21.065 -35.120 -47.621  1.00113.19           C  
ANISOU 1406  CD2 LEU A 120    14895  16060  12051   -793   -331    -78       C  
ATOM   1407  N   CYS A 121      19.454 -38.628 -51.063  1.00102.18           N  
ANISOU 1407  N   CYS A 121    13407  14535  10881     -3    137   -354       N  
ATOM   1408  CA  CYS A 121      18.193 -39.288 -51.405  1.00 99.63           C  
ANISOU 1408  CA  CYS A 121    13259  13915  10682    123    236   -479       C  
ATOM   1409  C   CYS A 121      18.028 -40.455 -50.456  1.00100.83           C  
ANISOU 1409  C   CYS A 121    13515  13934  10863    342    290   -521       C  
ATOM   1410  O   CYS A 121      16.959 -40.635 -49.872  1.00 98.23           O  
ANISOU 1410  O   CYS A 121    13381  13313  10631    348    320   -590       O  
ATOM   1411  CB  CYS A 121      18.207 -39.729 -52.867  1.00100.20           C  
ANISOU 1411  CB  CYS A 121    13233  14095  10745    220    307   -517       C  
ATOM   1412  SG  CYS A 121      16.804 -40.753 -53.370  1.00102.86           S  
ANISOU 1412  SG  CYS A 121    13764  14109  11210    387    423   -670       S  
ATOM   1413  N   LYS A 122      19.124 -41.215 -50.270  1.00 98.39           N  
ANISOU 1413  N   LYS A 122    13068  13858  10457    521    297   -469       N  
ATOM   1414  CA  LYS A 122      19.212 -42.359 -49.365  1.00 98.42           C  
ANISOU 1414  CA  LYS A 122    13158  13778  10461    749    337   -485       C  
ATOM   1415  C   LYS A 122      19.133 -41.887 -47.915  1.00101.21           C  
ANISOU 1415  C   LYS A 122    13603  14034  10817    638    268   -444       C  
ATOM   1416  O   LYS A 122      18.480 -42.541 -47.101  1.00100.83           O  
ANISOU 1416  O   LYS A 122    13730  13752  10829    737    307   -488       O  
ATOM   1417  CB  LYS A 122      20.505 -43.164 -49.600  1.00102.38           C  
ANISOU 1417  CB  LYS A 122    13471  14595  10834    980    352   -429       C  
ATOM   1418  CG  LYS A 122      20.482 -44.004 -50.870  1.00101.62           C  
ANISOU 1418  CG  LYS A 122    13345  14539  10728   1182    441   -497       C  
ATOM   1419  CD  LYS A 122      21.711 -44.876 -51.029  1.00102.36           C  
ANISOU 1419  CD  LYS A 122    13275  14934  10683   1463    463   -450       C  
ATOM   1420  CE  LYS A 122      21.733 -45.584 -52.357  1.00 99.80           C  
ANISOU 1420  CE  LYS A 122    12922  14670  10328   1659    545   -523       C  
ATOM   1421  NZ  LYS A 122      20.825 -46.763 -52.380  1.00102.36           N1+
ANISOU 1421  NZ  LYS A 122    13513  14641  10738   1854    620   -645       N1+
ATOM   1422  N   ALA A 123      19.772 -40.742 -47.608  1.00 96.21           N  
ANISOU 1422  N   ALA A 123    12864  13577  10115    420    161   -358       N  
ATOM   1423  CA  ALA A 123      19.763 -40.160 -46.280  1.00 95.03           C  
ANISOU 1423  CA  ALA A 123    12805  13353   9950    294     78   -321       C  
ATOM   1424  C   ALA A 123      18.358 -39.661 -45.913  1.00 97.58           C  
ANISOU 1424  C   ALA A 123    13367  13323  10387    181     92   -404       C  
ATOM   1425  O   ALA A 123      17.909 -39.950 -44.816  1.00 96.62           O  
ANISOU 1425  O   ALA A 123    13389  13032  10290    232    100   -424       O  
ATOM   1426  CB  ALA A 123      20.772 -39.030 -46.198  1.00 96.67           C  
ANISOU 1426  CB  ALA A 123    12854  13829  10045     63    -50   -213       C  
ATOM   1427  N   VAL A 124      17.642 -38.975 -46.837  1.00 93.65           N  
ANISOU 1427  N   VAL A 124    12906  12724   9952     51    102   -450       N  
ATOM   1428  CA  VAL A 124      16.304 -38.417 -46.588  1.00 91.68           C  
ANISOU 1428  CA  VAL A 124    12863  12175   9798    -43    114   -525       C  
ATOM   1429  C   VAL A 124      15.227 -39.532 -46.538  1.00 91.70           C  
ANISOU 1429  C   VAL A 124    12993  11949   9900    137    235   -614       C  
ATOM   1430  O   VAL A 124      14.455 -39.578 -45.574  1.00 88.41           O  
ANISOU 1430  O   VAL A 124    12732  11338   9523    145    250   -645       O  
ATOM   1431  CB  VAL A 124      15.949 -37.290 -47.610  1.00 95.84           C  
ANISOU 1431  CB  VAL A 124    13383  12688  10343   -233     75   -533       C  
ATOM   1432  CG1 VAL A 124      14.437 -37.119 -47.800  1.00 94.47           C  
ANISOU 1432  CG1 VAL A 124    13384  12230  10279   -236    133   -629       C  
ATOM   1433  CG2 VAL A 124      16.601 -35.961 -47.212  1.00 96.50           C  
ANISOU 1433  CG2 VAL A 124    13458  12867  10340   -470    -66   -454       C  
ATOM   1434  N   LEU A 125      15.175 -40.407 -47.561  1.00 89.44           N  
ANISOU 1434  N   LEU A 125    12648  11692   9645    271    315   -653       N  
ATOM   1435  CA  LEU A 125      14.166 -41.463 -47.608  1.00 89.45           C  
ANISOU 1435  CA  LEU A 125    12780  11473   9733    409    416   -734       C  
ATOM   1436  C   LEU A 125      14.236 -42.391 -46.386  1.00 98.33           C  
ANISOU 1436  C   LEU A 125    13999  12514  10847    548    440   -718       C  
ATOM   1437  O   LEU A 125      13.180 -42.746 -45.851  1.00 98.56           O  
ANISOU 1437  O   LEU A 125    14183  12320  10944    558    490   -762       O  
ATOM   1438  CB  LEU A 125      14.228 -42.283 -48.913  1.00 89.16           C  
ANISOU 1438  CB  LEU A 125    12679  11487   9710    533    484   -780       C  
ATOM   1439  CG  LEU A 125      13.639 -41.641 -50.200  1.00 92.24           C  
ANISOU 1439  CG  LEU A 125    13036  11868  10144    418    493   -826       C  
ATOM   1440  CD1 LEU A 125      13.607 -42.632 -51.334  1.00 92.16           C  
ANISOU 1440  CD1 LEU A 125    12999  11875  10141    564    564   -886       C  
ATOM   1441  CD2 LEU A 125      12.215 -41.181 -50.004  1.00 93.66           C  
ANISOU 1441  CD2 LEU A 125    13362  11806  10417    309    510   -884       C  
ATOM   1442  N   SER A 126      15.458 -42.742 -45.917  1.00 97.48           N  
ANISOU 1442  N   SER A 126    13792  12600  10645    648    403   -646       N  
ATOM   1443  CA  SER A 126      15.641 -43.635 -44.756  1.00 98.10           C  
ANISOU 1443  CA  SER A 126    13958  12618  10699    796    418   -618       C  
ATOM   1444  C   SER A 126      15.176 -42.983 -43.448  1.00101.67           C  
ANISOU 1444  C   SER A 126    14521  12955  11153    675    375   -599       C  
ATOM   1445  O   SER A 126      14.381 -43.587 -42.726  1.00100.35           O  
ANISOU 1445  O   SER A 126    14510  12589  11030    732    428   -623       O  
ATOM   1446  CB  SER A 126      17.091 -44.097 -44.630  1.00103.51           C  
ANISOU 1446  CB  SER A 126    14490  13570  11269    944    382   -540       C  
ATOM   1447  OG  SER A 126      17.988 -43.009 -44.478  1.00115.48           O  
ANISOU 1447  OG  SER A 126    15847  15329  12700    791    281   -465       O  
ATOM   1448  N   ILE A 127      15.651 -41.744 -43.166  1.00 98.81           N  
ANISOU 1448  N   ILE A 127    14091  12718  10734    502    277   -555       N  
ATOM   1449  CA  ILE A 127      15.307 -40.969 -41.971  1.00 97.91           C  
ANISOU 1449  CA  ILE A 127    14090  12512  10600    383    219   -544       C  
ATOM   1450  C   ILE A 127      13.793 -40.769 -41.901  1.00101.32           C  
ANISOU 1450  C   ILE A 127    14689  12682  11126    335    282   -623       C  
ATOM   1451  O   ILE A 127      13.227 -40.963 -40.837  1.00100.73           O  
ANISOU 1451  O   ILE A 127    14743  12478  11053    364    303   -628       O  
ATOM   1452  CB  ILE A 127      16.084 -39.623 -41.913  1.00101.09           C  
ANISOU 1452  CB  ILE A 127    14407  13082  10919    183     90   -491       C  
ATOM   1453  CG1 ILE A 127      17.617 -39.819 -41.824  1.00102.85           C  
ANISOU 1453  CG1 ILE A 127    14438  13610  11028    218     21   -395       C  
ATOM   1454  CG2 ILE A 127      15.593 -38.719 -40.801  1.00101.36           C  
ANISOU 1454  CG2 ILE A 127    14598  12985  10930     57     26   -502       C  
ATOM   1455  CD1 ILE A 127      18.167 -41.056 -41.028  1.00110.13           C  
ANISOU 1455  CD1 ILE A 127    15344  14596  11904    443     55   -354       C  
ATOM   1456  N   ASP A 128      13.148 -40.444 -43.033  1.00 97.85           N  
ANISOU 1456  N   ASP A 128    14236  12186  10756    274    315   -678       N  
ATOM   1457  CA  ASP A 128      11.698 -40.253 -43.091  1.00 96.64           C  
ANISOU 1457  CA  ASP A 128    14212  11822  10687    236    375   -749       C  
ATOM   1458  C   ASP A 128      10.943 -41.477 -42.531  1.00100.17           C  
ANISOU 1458  C   ASP A 128    14762  12118  11180    365    473   -769       C  
ATOM   1459  O   ASP A 128      10.166 -41.327 -41.580  1.00 99.50           O  
ANISOU 1459  O   ASP A 128    14794  11915  11098    347    492   -778       O  
ATOM   1460  CB  ASP A 128      11.259 -39.961 -44.528  1.00 97.61           C  
ANISOU 1460  CB  ASP A 128    14277  11940  10869    183    399   -796       C  
ATOM   1461  CG  ASP A 128       9.762 -39.780 -44.656  1.00105.18           C  
ANISOU 1461  CG  ASP A 128    15345  12718  11902    142    453   -863       C  
ATOM   1462  OD1 ASP A 128       9.162 -39.169 -43.748  1.00105.17           O1-
ANISOU 1462  OD1 ASP A 128    15440  12642  11880     81    421   -868       O1-
ATOM   1463  OD2 ASP A 128       9.204 -40.229 -45.667  1.00109.27           O  
ANISOU 1463  OD2 ASP A 128    15849  13182  12487    176    522   -910       O  
ATOM   1464  N   TYR A 129      11.222 -42.678 -43.080  1.00 96.45           N  
ANISOU 1464  N   TYR A 129    14258  11657  10730    494    529   -772       N  
ATOM   1465  CA  TYR A 129      10.598 -43.947 -42.692  1.00 95.67           C  
ANISOU 1465  CA  TYR A 129    14275  11405  10672    603    612   -783       C  
ATOM   1466  C   TYR A 129      11.021 -44.418 -41.305  1.00 97.08           C  
ANISOU 1466  C   TYR A 129    14522  11577  10788    683    599   -720       C  
ATOM   1467  O   TYR A 129      10.161 -44.851 -40.539  1.00 96.71           O  
ANISOU 1467  O   TYR A 129    14600  11382  10762    687    650   -719       O  
ATOM   1468  CB  TYR A 129      10.947 -45.030 -43.715  1.00 97.74           C  
ANISOU 1468  CB  TYR A 129    14506  11678  10954    727    654   -806       C  
ATOM   1469  CG  TYR A 129       9.984 -45.105 -44.867  1.00 99.46           C  
ANISOU 1469  CG  TYR A 129    14737  11801  11252    670    705   -882       C  
ATOM   1470  CD1 TYR A 129      10.163 -44.322 -46.003  1.00101.42           C  
ANISOU 1470  CD1 TYR A 129    14868  12160  11508    598    678   -911       C  
ATOM   1471  CD2 TYR A 129       8.908 -45.986 -44.844  1.00100.89           C  
ANISOU 1471  CD2 TYR A 129    15047  11791  11494    678    777   -918       C  
ATOM   1472  CE1 TYR A 129       9.287 -44.403 -47.085  1.00103.98           C  
ANISOU 1472  CE1 TYR A 129    15201  12408  11898    550    720   -981       C  
ATOM   1473  CE2 TYR A 129       8.027 -46.082 -45.920  1.00102.22           C  
ANISOU 1473  CE2 TYR A 129    15222  11889  11729    615    815   -987       C  
ATOM   1474  CZ  TYR A 129       8.217 -45.285 -47.041  1.00114.18           C  
ANISOU 1474  CZ  TYR A 129    16616  13517  13250    560    788  -1021       C  
ATOM   1475  OH  TYR A 129       7.359 -45.383 -48.118  1.00118.52           O  
ANISOU 1475  OH  TYR A 129    17167  14008  13857    502    821  -1088       O  
ATOM   1476  N   TYR A 130      12.339 -44.384 -41.003  1.00 91.92           N  
ANISOU 1476  N   TYR A 130    13777  11099  10049    748    532   -660       N  
ATOM   1477  CA  TYR A 130      12.916 -44.817 -39.730  1.00 91.60           C  
ANISOU 1477  CA  TYR A 130    13782  11089   9934    837    507   -591       C  
ATOM   1478  C   TYR A 130      12.362 -44.002 -38.556  1.00 92.75           C  
ANISOU 1478  C   TYR A 130    14015  11172  10053    726    478   -582       C  
ATOM   1479  O   TYR A 130      11.940 -44.591 -37.559  1.00 90.57           O  
ANISOU 1479  O   TYR A 130    13856  10792   9764    782    516   -557       O  
ATOM   1480  CB  TYR A 130      14.437 -44.713 -39.792  1.00 93.72           C  
ANISOU 1480  CB  TYR A 130    13895  11608  10107    902    428   -528       C  
ATOM   1481  CG  TYR A 130      15.159 -45.042 -38.509  1.00 96.23           C  
ANISOU 1481  CG  TYR A 130    14233  11999  10331    990    384   -450       C  
ATOM   1482  CD1 TYR A 130      15.313 -46.364 -38.088  1.00 99.11           C  
ANISOU 1482  CD1 TYR A 130    14681  12298  10680   1189    431   -417       C  
ATOM   1483  CD2 TYR A 130      15.763 -44.044 -37.758  1.00 96.89           C  
ANISOU 1483  CD2 TYR A 130    14258  12225  10331    878    284   -406       C  
ATOM   1484  CE1 TYR A 130      16.021 -46.679 -36.932  1.00100.16           C  
ANISOU 1484  CE1 TYR A 130    14827  12512  10718   1284    387   -338       C  
ATOM   1485  CE2 TYR A 130      16.487 -44.347 -36.613  1.00 99.10           C  
ANISOU 1485  CE2 TYR A 130    14543  12598  10514    960    235   -331       C  
ATOM   1486  CZ  TYR A 130      16.605 -45.666 -36.196  1.00108.37           C  
ANISOU 1486  CZ  TYR A 130    15789  13713  11676   1169    290   -296       C  
ATOM   1487  OH  TYR A 130      17.310 -45.957 -35.058  1.00112.52           O  
ANISOU 1487  OH  TYR A 130    16320  14335  12099   1258    239   -217       O  
ATOM   1488  N   SER A 131      12.339 -42.655 -38.699  1.00 89.67           N  
ANISOU 1488  N   SER A 131    13582  10840   9649    572    412   -603       N  
ATOM   1489  CA  SER A 131      11.792 -41.717 -37.721  1.00 89.37           C  
ANISOU 1489  CA  SER A 131    13642  10739   9574    472    377   -614       C  
ATOM   1490  C   SER A 131      10.265 -41.833 -37.644  1.00 94.68           C  
ANISOU 1490  C   SER A 131    14432  11225  10319    459    471   -669       C  
ATOM   1491  O   SER A 131       9.676 -41.332 -36.688  1.00 95.45           O  
ANISOU 1491  O   SER A 131    14629  11262  10377    428    469   -676       O  
ATOM   1492  CB  SER A 131      12.193 -40.280 -38.039  1.00 91.95           C  
ANISOU 1492  CB  SER A 131    13920  11156   9862    317    272   -625       C  
ATOM   1493  OG  SER A 131      11.471 -39.759 -39.144  1.00 98.95           O  
ANISOU 1493  OG  SER A 131    14795  11978  10825    242    299   -685       O  
ATOM   1494  N   MET A 132       9.623 -42.477 -38.637  1.00 91.17           N  
ANISOU 1494  N   MET A 132    13971  10704   9965    483    551   -707       N  
ATOM   1495  CA  MET A 132       8.184 -42.702 -38.580  1.00 90.48           C  
ANISOU 1495  CA  MET A 132    13971  10470   9938    463    641   -746       C  
ATOM   1496  C   MET A 132       7.921 -43.838 -37.624  1.00 93.66           C  
ANISOU 1496  C   MET A 132    14468  10793  10324    546    702   -698       C  
ATOM   1497  O   MET A 132       7.081 -43.708 -36.741  1.00 92.79           O  
ANISOU 1497  O   MET A 132    14440  10623  10192    524    740   -692       O  
ATOM   1498  CB  MET A 132       7.588 -42.988 -39.966  1.00 92.42           C  
ANISOU 1498  CB  MET A 132    14168  10670  10276    438    693   -800       C  
ATOM   1499  CG  MET A 132       6.079 -43.065 -39.953  1.00 95.86           C  
ANISOU 1499  CG  MET A 132    14665  10993  10764    392    773   -836       C  
ATOM   1500  SD  MET A 132       5.458 -43.889 -41.415  1.00100.04           S  
ANISOU 1500  SD  MET A 132    15159  11461  11392    378    837   -885       S  
ATOM   1501  CE  MET A 132       3.815 -44.283 -40.888  1.00 97.20           C  
ANISOU 1501  CE  MET A 132    14875  10997  11060    324    930   -887       C  
ATOM   1502  N   PHE A 133       8.693 -44.920 -37.760  1.00 91.19           N  
ANISOU 1502  N   PHE A 133    14149  10490  10009    651    707   -659       N  
ATOM   1503  CA  PHE A 133       8.552 -46.093 -36.922  1.00 92.61           C  
ANISOU 1503  CA  PHE A 133    14440  10579  10169    737    756   -604       C  
ATOM   1504  C   PHE A 133       9.024 -45.831 -35.494  1.00 98.21           C  
ANISOU 1504  C   PHE A 133    15191  11345  10778    768    712   -541       C  
ATOM   1505  O   PHE A 133       8.263 -46.135 -34.566  1.00 98.38           O  
ANISOU 1505  O   PHE A 133    15317  11284  10780    760    763   -512       O  
ATOM   1506  CB  PHE A 133       9.263 -47.301 -37.543  1.00 95.50           C  
ANISOU 1506  CB  PHE A 133    14811  10925  10550    867    765   -586       C  
ATOM   1507  CG  PHE A 133       8.397 -47.954 -38.587  1.00 97.62           C  
ANISOU 1507  CG  PHE A 133    15121  11062  10909    835    833   -640       C  
ATOM   1508  CD1 PHE A 133       7.466 -48.921 -38.230  1.00102.07           C  
ANISOU 1508  CD1 PHE A 133    15825  11456  11500    818    902   -620       C  
ATOM   1509  CD2 PHE A 133       8.457 -47.549 -39.919  1.00 99.80           C  
ANISOU 1509  CD2 PHE A 133    15295  11389  11234    800    822   -708       C  
ATOM   1510  CE1 PHE A 133       6.648 -49.506 -39.190  1.00103.26           C  
ANISOU 1510  CE1 PHE A 133    16019  11490  11726    762    951   -669       C  
ATOM   1511  CE2 PHE A 133       7.617 -48.115 -40.877  1.00102.57           C  
ANISOU 1511  CE2 PHE A 133    15687  11624  11661    759    877   -762       C  
ATOM   1512  CZ  PHE A 133       6.729 -49.098 -40.508  1.00101.49           C  
ANISOU 1512  CZ  PHE A 133    15694  11318  11550    738    938   -745       C  
ATOM   1513  N   THR A 134      10.230 -45.218 -35.303  1.00 94.49           N  
ANISOU 1513  N   THR A 134    14636  11030  10237    788    616   -519       N  
ATOM   1514  CA  THR A 134      10.743 -44.940 -33.949  1.00 94.21           C  
ANISOU 1514  CA  THR A 134    14639  11063  10094    809    560   -462       C  
ATOM   1515  C   THR A 134       9.808 -43.991 -33.193  1.00 96.76           C  
ANISOU 1515  C   THR A 134    15039  11338  10389    709    567   -494       C  
ATOM   1516  O   THR A 134       9.640 -44.163 -31.984  1.00 96.63           O  
ANISOU 1516  O   THR A 134    15112  11303  10300    741    576   -451       O  
ATOM   1517  CB  THR A 134      12.187 -44.412 -33.931  1.00 95.60           C  
ANISOU 1517  CB  THR A 134    14696  11436  10191    820    445   -429       C  
ATOM   1518  OG1 THR A 134      12.256 -43.155 -34.589  1.00 94.70           O  
ANISOU 1518  OG1 THR A 134    14506  11389  10088    682    384   -481       O  
ATOM   1519  CG2 THR A 134      13.191 -45.388 -34.508  1.00 92.22           C  
ANISOU 1519  CG2 THR A 134    14185  11095   9759    963    440   -387       C  
ATOM   1520  N   SER A 135       9.172 -43.030 -33.903  1.00 92.07           N  
ANISOU 1520  N   SER A 135    14418  10723   9843    606    566   -567       N  
ATOM   1521  CA  SER A 135       8.261 -42.067 -33.271  1.00 91.84           C  
ANISOU 1521  CA  SER A 135    14467  10651   9776    542    572   -608       C  
ATOM   1522  C   SER A 135       6.969 -42.719 -32.834  1.00 94.90           C  
ANISOU 1522  C   SER A 135    14933  10936  10188    567    690   -601       C  
ATOM   1523  O   SER A 135       6.470 -42.394 -31.754  1.00 94.85           O  
ANISOU 1523  O   SER A 135    15009  10926  10104    576    705   -593       O  
ATOM   1524  CB  SER A 135       7.947 -40.890 -34.192  1.00 94.39           C  
ANISOU 1524  CB  SER A 135    14753  10976  10137    447    535   -682       C  
ATOM   1525  OG  SER A 135       7.495 -39.781 -33.431  1.00103.05           O  
ANISOU 1525  OG  SER A 135    15943  12056  11156    411    497   -718       O  
ATOM   1526  N   ILE A 136       6.424 -43.622 -33.671  1.00 89.97           N  
ANISOU 1526  N   ILE A 136    14283  10240   9660    570    770   -604       N  
ATOM   1527  CA  ILE A 136       5.165 -44.291 -33.372  1.00 89.28           C  
ANISOU 1527  CA  ILE A 136    14256  10070   9597    557    879   -587       C  
ATOM   1528  C   ILE A 136       5.387 -45.296 -32.220  1.00 95.21           C  
ANISOU 1528  C   ILE A 136    15098  10793  10285    623    906   -496       C  
ATOM   1529  O   ILE A 136       4.653 -45.249 -31.233  1.00 94.62           O  
ANISOU 1529  O   ILE A 136    15086  10716  10147    616    955   -466       O  
ATOM   1530  CB  ILE A 136       4.548 -44.935 -34.648  1.00 90.90           C  
ANISOU 1530  CB  ILE A 136    14418  10205   9916    515    938   -618       C  
ATOM   1531  CG1 ILE A 136       4.020 -43.855 -35.621  1.00 88.95           C  
ANISOU 1531  CG1 ILE A 136    14092   9988   9716    447    926   -701       C  
ATOM   1532  CG2 ILE A 136       3.427 -45.888 -34.278  1.00 92.50           C  
ANISOU 1532  CG2 ILE A 136    14686  10327  10134    482   1039   -574       C  
ATOM   1533  CD1 ILE A 136       3.918 -44.267 -37.104  1.00 88.73           C  
ANISOU 1533  CD1 ILE A 136    13996   9926   9790    413    941   -743       C  
ATOM   1534  N   PHE A 137       6.426 -46.142 -32.318  1.00 93.48           N  
ANISOU 1534  N   PHE A 137    14885  10566  10067    701    871   -449       N  
ATOM   1535  CA  PHE A 137       6.688 -47.162 -31.316  1.00 95.37           C  
ANISOU 1535  CA  PHE A 137    15225  10765  10248    778    890   -357       C  
ATOM   1536  C   PHE A 137       7.122 -46.600 -29.957  1.00 99.81           C  
ANISOU 1536  C   PHE A 137    15822  11417  10685    812    841   -317       C  
ATOM   1537  O   PHE A 137       6.797 -47.245 -28.958  1.00100.33           O  
ANISOU 1537  O   PHE A 137    15984  11444  10692    841    885   -244       O  
ATOM   1538  CB  PHE A 137       7.681 -48.203 -31.829  1.00 98.98           C  
ANISOU 1538  CB  PHE A 137    15689  11191  10729    884    862   -322       C  
ATOM   1539  CG  PHE A 137       6.985 -49.200 -32.731  1.00102.28           C  
ANISOU 1539  CG  PHE A 137    16159  11463  11241    859    933   -334       C  
ATOM   1540  CD1 PHE A 137       6.191 -50.208 -32.195  1.00107.27           C  
ANISOU 1540  CD1 PHE A 137    16925  11961  11870    834   1004   -269       C  
ATOM   1541  CD2 PHE A 137       7.068 -49.088 -34.120  1.00104.10           C  
ANISOU 1541  CD2 PHE A 137    16309  11690  11555    840    925   -410       C  
ATOM   1542  CE1 PHE A 137       5.512 -51.098 -33.031  1.00108.40           C  
ANISOU 1542  CE1 PHE A 137    17132  11961  12092    779   1057   -282       C  
ATOM   1543  CE2 PHE A 137       6.386 -49.980 -34.956  1.00106.77           C  
ANISOU 1543  CE2 PHE A 137    16708  11889  11971    804    982   -430       C  
ATOM   1544  CZ  PHE A 137       5.617 -50.979 -34.407  1.00106.03           C  
ANISOU 1544  CZ  PHE A 137    16758  11654  11874    768   1043   -368       C  
ATOM   1545  N   THR A 138       7.788 -45.417 -29.862  1.00 95.76           N  
ANISOU 1545  N   THR A 138    15247  11015  10120    794    747   -361       N  
ATOM   1546  CA  THR A 138       8.083 -44.932 -28.498  1.00 96.02           C  
ANISOU 1546  CA  THR A 138    15341  11120  10022    817    700   -328       C  
ATOM   1547  C   THR A 138       6.811 -44.330 -27.925  1.00 99.11           C  
ANISOU 1547  C   THR A 138    15795  11484  10378    767    765   -361       C  
ATOM   1548  O   THR A 138       6.564 -44.453 -26.730  1.00100.50           O  
ANISOU 1548  O   THR A 138    16054  11677  10455    800    788   -314       O  
ATOM   1549  CB  THR A 138       9.269 -43.970 -28.357  1.00105.58           C  
ANISOU 1549  CB  THR A 138    16495  12458  11161    804    565   -347       C  
ATOM   1550  OG1 THR A 138       8.856 -42.628 -28.610  1.00108.16           O  
ANISOU 1550  OG1 THR A 138    16818  12795  11482    710    527   -434       O  
ATOM   1551  CG2 THR A 138      10.467 -44.360 -29.174  1.00104.15           C  
ANISOU 1551  CG2 THR A 138    16205  12352  11017    845    503   -325       C  
ATOM   1552  N   LEU A 139       5.996 -43.703 -28.785  1.00 93.04           N  
ANISOU 1552  N   LEU A 139    14983  10687   9682    700    799   -440       N  
ATOM   1553  CA  LEU A 139       4.710 -43.144 -28.393  1.00 92.14           C  
ANISOU 1553  CA  LEU A 139    14908  10568   9534    675    870   -475       C  
ATOM   1554  C   LEU A 139       3.838 -44.261 -27.833  1.00 97.46           C  
ANISOU 1554  C   LEU A 139    15625  11205  10201    684    987   -395       C  
ATOM   1555  O   LEU A 139       3.272 -44.079 -26.758  1.00 97.34           O  
ANISOU 1555  O   LEU A 139    15669  11233  10081    708   1029   -370       O  
ATOM   1556  CB  LEU A 139       4.072 -42.451 -29.609  1.00 90.94           C  
ANISOU 1556  CB  LEU A 139    14685  10396   9473    616    883   -562       C  
ATOM   1557  CG  LEU A 139       2.606 -41.968 -29.622  1.00 95.06           C  
ANISOU 1557  CG  LEU A 139    15206  10925   9987    603    970   -604       C  
ATOM   1558  CD1 LEU A 139       1.635 -43.000 -30.064  1.00 95.85           C  
ANISOU 1558  CD1 LEU A 139    15261  10992  10164    561   1084   -563       C  
ATOM   1559  CD2 LEU A 139       2.192 -41.159 -28.431  1.00 96.43           C  
ANISOU 1559  CD2 LEU A 139    15465  11154  10020    659    971   -621       C  
ATOM   1560  N   THR A 140       3.778 -45.427 -28.527  1.00 95.93           N  
ANISOU 1560  N   THR A 140    15414  10930  10105    662   1034   -352       N  
ATOM   1561  CA  THR A 140       2.993 -46.612 -28.115  1.00 97.34           C  
ANISOU 1561  CA  THR A 140    15651  11048  10284    636   1134   -263       C  
ATOM   1562  C   THR A 140       3.507 -47.178 -26.767  1.00103.11           C  
ANISOU 1562  C   THR A 140    16484  11792  10903    705   1125   -164       C  
ATOM   1563  O   THR A 140       2.702 -47.469 -25.870  1.00103.13           O  
ANISOU 1563  O   THR A 140    16539  11815  10831    685   1201    -99       O  
ATOM   1564  CB  THR A 140       3.008 -47.706 -29.218  1.00104.26           C  
ANISOU 1564  CB  THR A 140    16523  11808  11282    598   1157   -249       C  
ATOM   1565  OG1 THR A 140       2.881 -47.118 -30.515  1.00105.99           O  
ANISOU 1565  OG1 THR A 140    16645  12031  11597    555   1138   -346       O  
ATOM   1566  CG2 THR A 140       1.919 -48.720 -29.040  1.00 99.01           C  
ANISOU 1566  CG2 THR A 140    15916  11073  10630    515   1257   -175       C  
ATOM   1567  N   MET A 141       4.848 -47.310 -26.637  1.00100.44           N  
ANISOU 1567  N   MET A 141    16160  11462  10543    787   1031   -147       N  
ATOM   1568  CA  MET A 141       5.514 -47.798 -25.431  1.00101.77           C  
ANISOU 1568  CA  MET A 141    16414  11654  10599    870   1002    -54       C  
ATOM   1569  C   MET A 141       5.298 -46.849 -24.251  1.00106.01           C  
ANISOU 1569  C   MET A 141    16980  12300  11001    880    989    -66       C  
ATOM   1570  O   MET A 141       5.135 -47.308 -23.121  1.00106.01           O  
ANISOU 1570  O   MET A 141    17064  12318  10899    913   1022     20       O  
ATOM   1571  CB  MET A 141       7.013 -48.009 -25.681  1.00104.35           C  
ANISOU 1571  CB  MET A 141    16714  12006  10927    963    896    -43       C  
ATOM   1572  CG  MET A 141       7.362 -49.399 -26.152  1.00109.01           C  
ANISOU 1572  CG  MET A 141    17358  12483  11578   1026    915     24       C  
ATOM   1573  SD  MET A 141       6.555 -50.766 -25.264  1.00115.28           S  
ANISOU 1573  SD  MET A 141    18324  13145  12332   1020   1012    156       S  
ATOM   1574  CE  MET A 141       7.115 -50.459 -23.512  1.00113.03           C  
ANISOU 1574  CE  MET A 141    18095  12986  11864   1102    965    236       C  
ATOM   1575  N   MET A 142       5.249 -45.536 -24.531  1.00102.68           N  
ANISOU 1575  N   MET A 142    16503  11942  10570    853    941   -171       N  
ATOM   1576  CA  MET A 142       5.002 -44.489 -23.555  1.00103.68           C  
ANISOU 1576  CA  MET A 142    16677  12153  10563    870    918   -210       C  
ATOM   1577  C   MET A 142       3.604 -44.636 -22.962  1.00108.64           C  
ANISOU 1577  C   MET A 142    17340  12799  11139    859   1046   -183       C  
ATOM   1578  O   MET A 142       3.411 -44.306 -21.790  1.00109.99           O  
ANISOU 1578  O   MET A 142    17581  13042  11166    907   1055   -165       O  
ATOM   1579  CB  MET A 142       5.160 -43.133 -24.216  1.00105.74           C  
ANISOU 1579  CB  MET A 142    16895  12436  10844    835    840   -331       C  
ATOM   1580  CG  MET A 142       5.548 -42.057 -23.271  1.00111.35           C  
ANISOU 1580  CG  MET A 142    17684  13215  11408    862    750   -376       C  
ATOM   1581  SD  MET A 142       6.295 -40.686 -24.179  1.00116.11           S  
ANISOU 1581  SD  MET A 142    18254  13818  12044    793    607   -487       S  
ATOM   1582  CE  MET A 142       6.447 -39.510 -22.874  1.00114.27           C  
ANISOU 1582  CE  MET A 142    18170  13635  11613    820    515   -540       C  
ATOM   1583  N   CYS A 143       2.636 -45.144 -23.772  1.00104.03           N  
ANISOU 1583  N   CYS A 143    16699  12165  10661    794   1143   -177       N  
ATOM   1584  CA  CYS A 143       1.249 -45.422 -23.365  1.00103.74           C  
ANISOU 1584  CA  CYS A 143    16659  12173  10584    759   1273   -133       C  
ATOM   1585  C   CYS A 143       1.211 -46.685 -22.509  1.00105.64           C  
ANISOU 1585  C   CYS A 143    16975  12390  10771    750   1329     10       C  
ATOM   1586  O   CYS A 143       0.396 -46.782 -21.585  1.00105.18           O  
ANISOU 1586  O   CYS A 143    16943  12417  10604    748   1413     71       O  
ATOM   1587  CB  CYS A 143       0.325 -45.536 -24.577  1.00103.30           C  
ANISOU 1587  CB  CYS A 143    16507  12086  10655    671   1339   -170       C  
ATOM   1588  SG  CYS A 143      -0.078 -43.950 -25.349  1.00106.07           S  
ANISOU 1588  SG  CYS A 143    16783  12492  11027    693   1305   -323       S  
ATOM   1589  N   VAL A 144       2.104 -47.646 -22.817  1.00100.33           N  
ANISOU 1589  N   VAL A 144    16345  11609  10167    755   1282     68       N  
ATOM   1590  CA  VAL A 144       2.238 -48.900 -22.073  1.00100.36           C  
ANISOU 1590  CA  VAL A 144    16453  11555  10124    760   1314    209       C  
ATOM   1591  C   VAL A 144       2.835 -48.580 -20.689  1.00106.36           C  
ANISOU 1591  C   VAL A 144    17282  12408  10721    857   1269    250       C  
ATOM   1592  O   VAL A 144       2.383 -49.124 -19.679  1.00106.91           O  
ANISOU 1592  O   VAL A 144    17425  12509  10687    853   1333    357       O  
ATOM   1593  CB  VAL A 144       3.081 -49.910 -22.882  1.00102.21           C  
ANISOU 1593  CB  VAL A 144    16725  11641  10469    776   1264    239       C  
ATOM   1594  CG1 VAL A 144       3.508 -51.099 -22.029  1.00103.08           C  
ANISOU 1594  CG1 VAL A 144    16975  11680  10512    825   1265    382       C  
ATOM   1595  CG2 VAL A 144       2.321 -50.370 -24.116  1.00101.21           C  
ANISOU 1595  CG2 VAL A 144    16557  11416  10481    666   1319    212       C  
ATOM   1596  N   ASP A 145       3.822 -47.658 -20.660  1.00103.14           N  
ANISOU 1596  N   ASP A 145    16851  12054  10283    929   1156    166       N  
ATOM   1597  CA  ASP A 145       4.513 -47.197 -19.458  1.00103.92           C  
ANISOU 1597  CA  ASP A 145    17011  12248  10225   1012   1086    182       C  
ATOM   1598  C   ASP A 145       3.538 -46.508 -18.528  1.00109.63           C  
ANISOU 1598  C   ASP A 145    17763  13078  10814   1016   1154    164       C  
ATOM   1599  O   ASP A 145       3.565 -46.784 -17.329  1.00111.09           O  
ANISOU 1599  O   ASP A 145    18027  13324  10857   1063   1170    245       O  
ATOM   1600  CB  ASP A 145       5.656 -46.247 -19.832  1.00104.94           C  
ANISOU 1600  CB  ASP A 145    17094  12416  10362   1044    944     84       C  
ATOM   1601  CG  ASP A 145       6.664 -46.004 -18.726  1.00113.38           C  
ANISOU 1601  CG  ASP A 145    18221  13574  11282   1118    842    116       C  
ATOM   1602  OD1 ASP A 145       7.396 -46.966 -18.362  1.00115.00           O  
ANISOU 1602  OD1 ASP A 145    18461  13768  11466   1178    816    221       O  
ATOM   1603  OD2 ASP A 145       6.789 -44.834 -18.283  1.00114.39           O1-
ANISOU 1603  OD2 ASP A 145    18369  13781  11314   1118    775     32       O1-
ATOM   1604  N   ARG A 146       2.642 -45.650 -19.071  1.00105.77           N  
ANISOU 1604  N   ARG A 146    17210  12620  10356    981   1199     64       N  
ATOM   1605  CA  ARG A 146       1.623 -44.975 -18.258  1.00106.54           C  
ANISOU 1605  CA  ARG A 146    17328  12836  10315   1014   1275     40       C  
ATOM   1606  C   ARG A 146       0.552 -45.961 -17.796  1.00111.02           C  
ANISOU 1606  C   ARG A 146    17890  13445  10848    966   1421    167       C  
ATOM   1607  O   ARG A 146      -0.031 -45.745 -16.736  1.00111.72           O  
ANISOU 1607  O   ARG A 146    18014  13659  10777   1013   1483    200       O  
ATOM   1608  CB  ARG A 146       0.983 -43.794 -18.987  1.00107.42           C  
ANISOU 1608  CB  ARG A 146    17379  12973  10461   1016   1279    -99       C  
ATOM   1609  CG  ARG A 146       1.885 -42.561 -19.063  1.00125.60           C  
ANISOU 1609  CG  ARG A 146    19729  15262  12730   1062   1134   -223       C  
ATOM   1610  CD  ARG A 146       1.663 -41.586 -17.915  1.00138.80           C  
ANISOU 1610  CD  ARG A 146    21507  17029  14201   1159   1115   -280       C  
ATOM   1611  NE  ARG A 146       2.509 -41.882 -16.759  1.00145.24           N  
ANISOU 1611  NE  ARG A 146    22415  17881  14887   1198   1052   -216       N  
ATOM   1612  CZ  ARG A 146       2.350 -41.341 -15.558  1.00161.33           C  
ANISOU 1612  CZ  ARG A 146    24559  20010  16728   1285   1046   -236       C  
ATOM   1613  NH1 ARG A 146       1.361 -40.481 -15.334  1.00151.90           N  
ANISOU 1613  NH1 ARG A 146    23398  18881  15438   1358   1106   -321       N  
ATOM   1614  NH2 ARG A 146       3.169 -41.660 -14.564  1.00148.78           N1+
ANISOU 1614  NH2 ARG A 146    23048  18458  15026   1313    981   -173       N1+
ATOM   1615  N   TYR A 147       0.316 -47.060 -18.562  1.00106.85           N  
ANISOU 1615  N   TYR A 147    17327  12815  10456    865   1470    244       N  
ATOM   1616  CA  TYR A 147      -0.639 -48.091 -18.151  1.00107.32           C  
ANISOU 1616  CA  TYR A 147    17396  12898  10483    780   1594    384       C  
ATOM   1617  C   TYR A 147      -0.122 -48.766 -16.876  1.00111.17           C  
ANISOU 1617  C   TYR A 147    18004  13397  10837    827   1585    513       C  
ATOM   1618  O   TYR A 147      -0.897 -48.985 -15.956  1.00111.74           O  
ANISOU 1618  O   TYR A 147    18094  13584  10778    809   1678    603       O  
ATOM   1619  CB  TYR A 147      -0.898 -49.133 -19.268  1.00108.08           C  
ANISOU 1619  CB  TYR A 147    17466  12850  10749    649   1623    433       C  
ATOM   1620  CG  TYR A 147      -1.399 -50.462 -18.734  1.00111.06           C  
ANISOU 1620  CG  TYR A 147    17920  13189  11089    548   1703    609       C  
ATOM   1621  CD1 TYR A 147      -2.752 -50.678 -18.507  1.00113.92           C  
ANISOU 1621  CD1 TYR A 147    18219  13667  11398    431   1827    682       C  
ATOM   1622  CD2 TYR A 147      -0.513 -51.491 -18.409  1.00112.34           C  
ANISOU 1622  CD2 TYR A 147    18220  13209  11254    570   1650    711       C  
ATOM   1623  CE1 TYR A 147      -3.213 -51.885 -17.974  1.00116.61           C  
ANISOU 1623  CE1 TYR A 147    18639  13975  11692    309   1894    859       C  
ATOM   1624  CE2 TYR A 147      -0.962 -52.690 -17.850  1.00114.95           C  
ANISOU 1624  CE2 TYR A 147    18653  13486  11535    473   1714    882       C  
ATOM   1625  CZ  TYR A 147      -2.315 -52.887 -17.641  1.00123.42           C  
ANISOU 1625  CZ  TYR A 147    19668  14666  12559    327   1835    958       C  
ATOM   1626  OH  TYR A 147      -2.769 -54.083 -17.131  1.00125.44           O  
ANISOU 1626  OH  TYR A 147    20031  14865  12765    198   1892   1139       O  
ATOM   1627  N   ILE A 148       1.180 -49.133 -16.855  1.00107.28           N  
ANISOU 1627  N   ILE A 148    17587  12801  10373    888   1474    529       N  
ATOM   1628  CA  ILE A 148       1.870 -49.790 -15.730  1.00107.98           C  
ANISOU 1628  CA  ILE A 148    17795  12890  10343    954   1442    649       C  
ATOM   1629  C   ILE A 148       1.890 -48.809 -14.557  1.00115.98           C  
ANISOU 1629  C   ILE A 148    18829  14071  11165   1046   1426    608       C  
ATOM   1630  O   ILE A 148       1.568 -49.198 -13.435  1.00117.96           O  
ANISOU 1630  O   ILE A 148    19148  14403  11268   1061   1482    718       O  
ATOM   1631  CB  ILE A 148       3.289 -50.270 -16.159  1.00109.22           C  
ANISOU 1631  CB  ILE A 148    17996  12925  10580   1023   1318    654       C  
ATOM   1632  CG1 ILE A 148       3.171 -51.392 -17.225  1.00109.09           C  
ANISOU 1632  CG1 ILE A 148    17996  12727  10726    948   1346    704       C  
ATOM   1633  CG2 ILE A 148       4.135 -50.728 -14.959  1.00108.72           C  
ANISOU 1633  CG2 ILE A 148    18043  12892  10374   1123   1262    762       C  
ATOM   1634  CD1 ILE A 148       4.231 -51.427 -18.289  1.00110.78           C  
ANISOU 1634  CD1 ILE A 148    18175  12847  11068   1005   1245    630       C  
ATOM   1635  N   ALA A 149       2.187 -47.521 -14.838  1.00112.42           N  
ANISOU 1635  N   ALA A 149    18332  13672  10711   1098   1351    450       N  
ATOM   1636  CA  ALA A 149       2.195 -46.447 -13.851  1.00112.89           C  
ANISOU 1636  CA  ALA A 149    18435  13869  10590   1187   1320    380       C  
ATOM   1637  C   ALA A 149       0.827 -46.339 -13.134  1.00118.52           C  
ANISOU 1637  C   ALA A 149    19140  14722  11172   1189   1465    417       C  
ATOM   1638  O   ALA A 149       0.792 -46.360 -11.907  1.00119.71           O  
ANISOU 1638  O   ALA A 149    19365  14979  11139   1252   1485    477       O  
ATOM   1639  CB  ALA A 149       2.548 -45.131 -14.521  1.00112.18           C  
ANISOU 1639  CB  ALA A 149    18310  13771  10544   1209   1223    204       C  
ATOM   1640  N   VAL A 150      -0.285 -46.300 -13.897  1.00114.99           N  
ANISOU 1640  N   VAL A 150    18590  14290  10809   1120   1569    395       N  
ATOM   1641  CA  VAL A 150      -1.653 -46.188 -13.384  1.00116.23           C  
ANISOU 1641  CA  VAL A 150    18696  14617  10849   1119   1715    433       C  
ATOM   1642  C   VAL A 150      -2.149 -47.524 -12.777  1.00124.72           C  
ANISOU 1642  C   VAL A 150    19788  15724  11877   1024   1821    636       C  
ATOM   1643  O   VAL A 150      -2.420 -47.570 -11.580  1.00127.01           O  
ANISOU 1643  O   VAL A 150    20127  16154  11977   1077   1874    711       O  
ATOM   1644  CB  VAL A 150      -2.617 -45.670 -14.489  1.00118.36           C  
ANISOU 1644  CB  VAL A 150    18834  14911  11228   1077   1777    342       C  
ATOM   1645  CG1 VAL A 150      -4.087 -45.848 -14.124  1.00119.40           C  
ANISOU 1645  CG1 VAL A 150    18870  15238  11260   1047   1942    419       C  
ATOM   1646  CG2 VAL A 150      -2.338 -44.217 -14.799  1.00117.15           C  
ANISOU 1646  CG2 VAL A 150    18694  14758  11059   1190   1689    154       C  
ATOM   1647  N   CYS A 151      -2.283 -48.584 -13.588  1.00121.97           N  
ANISOU 1647  N   CYS A 151    19411  15243  11687    882   1848    724       N  
ATOM   1648  CA  CYS A 151      -2.874 -49.855 -13.193  1.00123.81           C  
ANISOU 1648  CA  CYS A 151    19671  15478  11891    753   1944    918       C  
ATOM   1649  C   CYS A 151      -2.036 -50.653 -12.199  1.00129.69           C  
ANISOU 1649  C   CYS A 151    20571  16162  12544    789   1898   1050       C  
ATOM   1650  O   CYS A 151      -2.629 -51.261 -11.309  1.00132.03           O  
ANISOU 1650  O   CYS A 151    20902  16555  12709    735   1988   1202       O  
ATOM   1651  CB  CYS A 151      -3.217 -50.694 -14.421  1.00123.70           C  
ANISOU 1651  CB  CYS A 151    19615  15312  12074    586   1964    955       C  
ATOM   1652  SG  CYS A 151      -4.540 -49.992 -15.443  1.00126.96           S  
ANISOU 1652  SG  CYS A 151    19828  15850  12562    509   2053    855       S  
ATOM   1653  N   HIS A 152      -0.701 -50.690 -12.336  1.00125.11           N  
ANISOU 1653  N   HIS A 152    20073  15440  12021    876   1762   1007       N  
ATOM   1654  CA  HIS A 152       0.119 -51.483 -11.408  1.00126.16           C  
ANISOU 1654  CA  HIS A 152    20350  15523  12061    928   1713   1139       C  
ATOM   1655  C   HIS A 152       1.143 -50.574 -10.708  1.00130.54           C  
ANISOU 1655  C   HIS A 152    20942  16155  12502   1092   1599   1046       C  
ATOM   1656  O   HIS A 152       2.326 -50.668 -11.028  1.00129.01           O  
ANISOU 1656  O   HIS A 152    20783  15856  12378   1155   1475   1014       O  
ATOM   1657  CB  HIS A 152       0.793 -52.636 -12.169  1.00126.53           C  
ANISOU 1657  CB  HIS A 152    20475  15333  12266    881   1655   1211       C  
ATOM   1658  CG  HIS A 152      -0.155 -53.399 -13.047  1.00130.12           C  
ANISOU 1658  CG  HIS A 152    20903  15688  12849    704   1742   1268       C  
ATOM   1659  ND1 HIS A 152      -1.098 -54.255 -12.513  1.00133.96           N  
ANISOU 1659  ND1 HIS A 152    21437  16200  13260    566   1849   1438       N  
ATOM   1660  CD2 HIS A 152      -0.301 -53.378 -14.395  1.00130.79           C  
ANISOU 1660  CD2 HIS A 152    20915  15661  13117    635   1730   1175       C  
ATOM   1661  CE1 HIS A 152      -1.769 -54.742 -13.544  1.00133.21           C  
ANISOU 1661  CE1 HIS A 152    21304  16004  13307    407   1892   1444       C  
ATOM   1662  NE2 HIS A 152      -1.327 -54.245 -14.697  1.00131.60           N  
ANISOU 1662  NE2 HIS A 152    21029  15714  13261    450   1824   1285       N  
ATOM   1663  N   PRO A 153       0.724 -49.663  -9.784  1.00128.68           N  
ANISOU 1663  N   PRO A 153    20697  16112  12084   1164   1631    995       N  
ATOM   1664  CA  PRO A 153       1.693 -48.709  -9.203  1.00128.33           C  
ANISOU 1664  CA  PRO A 153    20701  16127  11931   1299   1505    887       C  
ATOM   1665  C   PRO A 153       2.716 -49.333  -8.264  1.00134.10           C  
ANISOU 1665  C   PRO A 153    21548  16848  12556   1367   1423   1000       C  
ATOM   1666  O   PRO A 153       3.826 -48.803  -8.135  1.00133.47           O  
ANISOU 1666  O   PRO A 153    21494  16767  12449   1448   1282    923       O  
ATOM   1667  CB  PRO A 153       0.807 -47.705  -8.464  1.00130.52           C  
ANISOU 1667  CB  PRO A 153    20963  16600  12029   1360   1577    812       C  
ATOM   1668  CG  PRO A 153      -0.436 -48.453  -8.157  1.00136.15           C  
ANISOU 1668  CG  PRO A 153    21638  17403  12691   1277   1747    955       C  
ATOM   1669  CD  PRO A 153      -0.645 -49.399  -9.288  1.00131.13           C  
ANISOU 1669  CD  PRO A 153    20949  16604  12272   1132   1779   1023       C  
ATOM   1670  N   VAL A 154       2.347 -50.451  -7.621  1.00132.32           N  
ANISOU 1670  N   VAL A 154    21392  16622  12264   1327   1506   1188       N  
ATOM   1671  CA  VAL A 154       3.221 -51.152  -6.681  1.00133.34           C  
ANISOU 1671  CA  VAL A 154    21642  16742  12279   1399   1439   1320       C  
ATOM   1672  C   VAL A 154       4.339 -51.875  -7.465  1.00136.82           C  
ANISOU 1672  C   VAL A 154    22109  16995  12881   1421   1330   1346       C  
ATOM   1673  O   VAL A 154       5.501 -51.864  -7.036  1.00136.20           O  
ANISOU 1673  O   VAL A 154    22077  16932  12741   1530   1206   1354       O  
ATOM   1674  CB  VAL A 154       2.417 -52.110  -5.779  1.00138.90           C  
ANISOU 1674  CB  VAL A 154    22423  17497  12855   1340   1564   1522       C  
ATOM   1675  CG1 VAL A 154       3.277 -52.616  -4.630  1.00140.29           C  
ANISOU 1675  CG1 VAL A 154    22731  17703  12870   1440   1493   1647       C  
ATOM   1676  CG2 VAL A 154       1.156 -51.431  -5.239  1.00139.21           C  
ANISOU 1676  CG2 VAL A 154    22396  17744  12753   1314   1697   1494       C  
ATOM   1677  N   LYS A 155       3.979 -52.457  -8.634  1.00132.90           N  
ANISOU 1677  N   LYS A 155    21575  16340  12582   1325   1373   1351       N  
ATOM   1678  CA  LYS A 155       4.897 -53.157  -9.538  1.00131.99           C  
ANISOU 1678  CA  LYS A 155    21482  16042  12626   1355   1288   1363       C  
ATOM   1679  C   LYS A 155       5.703 -52.155 -10.390  1.00133.23           C  
ANISOU 1679  C   LYS A 155    21523  16216  12882   1407   1175   1178       C  
ATOM   1680  O   LYS A 155       6.871 -52.418 -10.687  1.00132.15           O  
ANISOU 1680  O   LYS A 155    21393  16029  12790   1498   1063   1179       O  
ATOM   1681  CB  LYS A 155       4.124 -54.133 -10.441  1.00134.78           C  
ANISOU 1681  CB  LYS A 155    21858  16219  13132   1222   1377   1432       C  
ATOM   1682  N   ALA A 156       5.080 -51.000 -10.759  1.00128.51           N  
ANISOU 1682  N   ALA A 156    20821  15700  12305   1355   1204   1029       N  
ATOM   1683  CA  ALA A 156       5.672 -49.917 -11.556  1.00126.94           C  
ANISOU 1683  CA  ALA A 156    20522  15519  12188   1374   1105    854       C  
ATOM   1684  C   ALA A 156       6.926 -49.350 -10.909  1.00132.63           C  
ANISOU 1684  C   ALA A 156    21262  16339  12795   1475    956    820       C  
ATOM   1685  O   ALA A 156       7.796 -48.848 -11.612  1.00130.91           O  
ANISOU 1685  O   ALA A 156    20971  16114  12654   1488    845    728       O  
ATOM   1686  CB  ALA A 156       4.662 -48.797 -11.755  1.00126.86           C  
ANISOU 1686  CB  ALA A 156    20444  15588  12169   1320   1169    724       C  
ATOM   1687  N   LEU A 157       7.021 -49.435  -9.576  1.00132.83           N  
ANISOU 1687  N   LEU A 157    21376  16467  12625   1535    950    900       N  
ATOM   1688  CA  LEU A 157       8.149 -48.943  -8.783  1.00134.19           C  
ANISOU 1688  CA  LEU A 157    21576  16754  12654   1622    806    882       C  
ATOM   1689  C   LEU A 157       9.475 -49.639  -9.137  1.00140.29           C  
ANISOU 1689  C   LEU A 157    22326  17488  13489   1693    692    948       C  
ATOM   1690  O   LEU A 157      10.550 -49.124  -8.835  1.00139.89           O  
ANISOU 1690  O   LEU A 157    22248  17545  13360   1744    551    911       O  
ATOM   1691  CB  LEU A 157       7.829 -49.140  -7.297  1.00135.92           C  
ANISOU 1691  CB  LEU A 157    21907  17083  12654   1672    848    981       C  
ATOM   1692  CG  LEU A 157       7.691 -47.854  -6.483  1.00140.81           C  
ANISOU 1692  CG  LEU A 157    22557  17851  13094   1692    805    862       C  
ATOM   1693  CD1 LEU A 157       6.375 -47.147  -6.769  1.00140.02           C  
ANISOU 1693  CD1 LEU A 157    22431  17761  13010   1639    926    761       C  
ATOM   1694  CD2 LEU A 157       7.814 -48.137  -5.000  1.00146.08           C  
ANISOU 1694  CD2 LEU A 157    23334  18639  13529   1769    801    969       C  
ATOM   1695  N   ASP A 158       9.385 -50.776  -9.818  1.00138.78           N  
ANISOU 1695  N   ASP A 158    22146  17150  13433   1698    750   1039       N  
ATOM   1696  CA  ASP A 158      10.524 -51.587 -10.196  1.00140.12           C  
ANISOU 1696  CA  ASP A 158    22308  17272  13657   1800    664   1111       C  
ATOM   1697  C   ASP A 158      10.699 -51.607 -11.694  1.00143.79           C  
ANISOU 1697  C   ASP A 158    22672  17635  14325   1768    656   1027       C  
ATOM   1698  O   ASP A 158      11.837 -51.648 -12.146  1.00143.57           O  
ANISOU 1698  O   ASP A 158    22571  17649  14329   1851    548   1014       O  
ATOM   1699  CB  ASP A 158      10.332 -53.000  -9.648  1.00144.49           C  
ANISOU 1699  CB  ASP A 158    23009  17721  14170   1860    729   1298       C  
ATOM   1700  CG  ASP A 158       9.756 -52.986  -8.240  1.00164.35           C  
ANISOU 1700  CG  ASP A 158    25625  20327  16491   1851    783   1385       C  
ATOM   1701  OD1 ASP A 158       8.517 -52.802  -8.103  1.00165.48           O1-
ANISOU 1701  OD1 ASP A 158    25786  20461  16627   1740    907   1376       O1-
ATOM   1702  OD2 ASP A 158      10.551 -53.050  -7.274  1.00175.29           O  
ANISOU 1702  OD2 ASP A 158    27056  21824  17720   1957    696   1453       O  
ATOM   1703  N   PHE A 159       9.589 -51.570 -12.471  1.00140.34           N  
ANISOU 1703  N   PHE A 159    22220  17087  14017   1652    768    973       N  
ATOM   1704  CA  PHE A 159       9.642 -51.570 -13.940  1.00139.04           C  
ANISOU 1704  CA  PHE A 159    21962  16822  14043   1613    769    888       C  
ATOM   1705  C   PHE A 159      10.055 -50.195 -14.489  1.00140.31           C  
ANISOU 1705  C   PHE A 159    21985  17093  14234   1569    683    727       C  
ATOM   1706  O   PHE A 159      10.903 -50.134 -15.386  1.00140.01           O  
ANISOU 1706  O   PHE A 159    21852  17059  14285   1600    606    681       O  
ATOM   1707  CB  PHE A 159       8.302 -52.011 -14.590  1.00140.89           C  
ANISOU 1707  CB  PHE A 159    22225  16911  14396   1492    910    890       C  
ATOM   1708  CG  PHE A 159       8.203 -51.670 -16.078  1.00141.67           C  
ANISOU 1708  CG  PHE A 159    22212  16941  14676   1430    910    768       C  
ATOM   1709  CD1 PHE A 159       8.810 -52.474 -17.044  1.00144.93           C  
ANISOU 1709  CD1 PHE A 159    22624  17237  15206   1487    880    783       C  
ATOM   1710  CD2 PHE A 159       7.547 -50.517 -16.506  1.00143.39           C  
ANISOU 1710  CD2 PHE A 159    22332  17217  14931   1333    934    635       C  
ATOM   1711  CE1 PHE A 159       8.758 -52.131 -18.410  1.00144.37           C  
ANISOU 1711  CE1 PHE A 159    22448  17120  15288   1435    878    669       C  
ATOM   1712  CE2 PHE A 159       7.514 -50.166 -17.869  1.00144.86           C  
ANISOU 1712  CE2 PHE A 159    22416  17349  15274   1280    926    527       C  
ATOM   1713  CZ  PHE A 159       8.108 -50.982 -18.810  1.00142.65           C  
ANISOU 1713  CZ  PHE A 159    22127  16963  15109   1324    900    547       C  
ATOM   1714  N   ARG A 160       9.414 -49.106 -14.014  1.00134.59           N  
ANISOU 1714  N   ARG A 160    21256  16450  13433   1497    700    641       N  
ATOM   1715  CA  ARG A 160       9.631 -47.750 -14.525  1.00132.53           C  
ANISOU 1715  CA  ARG A 160    20905  16258  13195   1436    622    487       C  
ATOM   1716  C   ARG A 160      10.996 -47.143 -14.077  1.00138.02           C  
ANISOU 1716  C   ARG A 160    21564  17095  13781   1479    452    467       C  
ATOM   1717  O   ARG A 160      11.084 -45.942 -13.810  1.00137.91           O  
ANISOU 1717  O   ARG A 160    21550  17161  13690   1424    377    365       O  
ATOM   1718  CB  ARG A 160       8.448 -46.838 -14.156  1.00129.39           C  
ANISOU 1718  CB  ARG A 160    20542  15883  12737   1371    696    403       C  
ATOM   1719  CG  ARG A 160       7.099 -47.317 -14.716  1.00130.38           C  
ANISOU 1719  CG  ARG A 160    20662  15909  12969   1309    855    417       C  
ATOM   1720  CD  ARG A 160       6.011 -46.269 -14.609  1.00136.29           C  
ANISOU 1720  CD  ARG A 160    21406  16707  13672   1267    918    312       C  
ATOM   1721  NE  ARG A 160       6.323 -45.094 -15.416  1.00151.78           N  
ANISOU 1721  NE  ARG A 160    23307  18668  15695   1233    831    163       N  
ATOM   1722  CZ  ARG A 160       6.138 -43.840 -15.021  1.00174.37           C  
ANISOU 1722  CZ  ARG A 160    26210  21593  18450   1240    785     51       C  
ATOM   1723  NH1 ARG A 160       5.613 -43.581 -13.830  1.00166.44           N1+
ANISOU 1723  NH1 ARG A 160    25298  20673  17269   1296    826     63       N1+
ATOM   1724  NH2 ARG A 160       6.466 -42.832 -15.819  1.00164.59           N  
ANISOU 1724  NH2 ARG A 160    24934  20329  17273   1195    696    -72       N  
ATOM   1725  N   THR A 161      12.063 -47.973 -14.086  1.00135.45           N  
ANISOU 1725  N   THR A 161    21210  16802  13455   1574    386    563       N  
ATOM   1726  CA  THR A 161      13.457 -47.638 -13.772  1.00136.13           C  
ANISOU 1726  CA  THR A 161    21228  17051  13446   1620    225    574       C  
ATOM   1727  C   THR A 161      14.071 -46.897 -14.973  1.00138.87           C  
ANISOU 1727  C   THR A 161    21426  17438  13899   1546    141    473       C  
ATOM   1728  O   THR A 161      13.868 -47.342 -16.111  1.00138.27           O  
ANISOU 1728  O   THR A 161    21291  17262  13984   1545    204    458       O  
ATOM   1729  CB  THR A 161      14.219 -48.941 -13.442  1.00147.73           C  
ANISOU 1729  CB  THR A 161    22716  18534  14880   1778    210    726       C  
ATOM   1730  OG1 THR A 161      13.582 -49.566 -12.326  1.00152.64           O  
ANISOU 1730  OG1 THR A 161    23488  19111  15396   1824    288    825       O  
ATOM   1731  CG2 THR A 161      15.707 -48.728 -13.141  1.00146.64           C  
ANISOU 1731  CG2 THR A 161    22478  18601  14636   1846     44    757       C  
ATOM   1732  N   PRO A 162      14.846 -45.799 -14.759  1.00134.54           N  
ANISOU 1732  N   PRO A 162    20821  17039  13261   1473     -4    408       N  
ATOM   1733  CA  PRO A 162      15.461 -45.096 -15.901  1.00132.78           C  
ANISOU 1733  CA  PRO A 162    20454  16867  13129   1380    -88    329       C  
ATOM   1734  C   PRO A 162      16.411 -45.989 -16.705  1.00134.52           C  
ANISOU 1734  C   PRO A 162    20534  17149  13428   1481   -109    405       C  
ATOM   1735  O   PRO A 162      16.576 -45.767 -17.900  1.00133.09           O  
ANISOU 1735  O   PRO A 162    20240  16959  13369   1430   -112    352       O  
ATOM   1736  CB  PRO A 162      16.209 -43.932 -15.246  1.00135.43           C  
ANISOU 1736  CB  PRO A 162    20785  17363  13312   1281   -255    282       C  
ATOM   1737  CG  PRO A 162      16.421 -44.358 -13.841  1.00142.00           C  
ANISOU 1737  CG  PRO A 162    21710  18272  13972   1374   -280    368       C  
ATOM   1738  CD  PRO A 162      15.199 -45.140 -13.486  1.00137.45           C  
ANISOU 1738  CD  PRO A 162    21262  17535  13430   1454   -106    406       C  
ATOM   1739  N   ALA A 163      17.002 -47.011 -16.057  1.00130.36           N  
ANISOU 1739  N   ALA A 163    20022  16684  12824   1640   -120    530       N  
ATOM   1740  CA  ALA A 163      17.871 -47.989 -16.704  1.00129.53           C  
ANISOU 1740  CA  ALA A 163    19812  16634  12769   1790   -131    610       C  
ATOM   1741  C   ALA A 163      17.038 -48.914 -17.593  1.00129.13           C  
ANISOU 1741  C   ALA A 163    19823  16358  12884   1847     16    610       C  
ATOM   1742  O   ALA A 163      17.477 -49.257 -18.692  1.00128.18           O  
ANISOU 1742  O   ALA A 163    19598  16244  12863   1901     18    599       O  
ATOM   1743  CB  ALA A 163      18.625 -48.791 -15.657  1.00132.38           C  
ANISOU 1743  CB  ALA A 163    20206  17107  12985   1960   -184    744       C  
ATOM   1744  N   LYS A 164      15.818 -49.283 -17.134  1.00123.46           N  
ANISOU 1744  N   LYS A 164    19270  15454  12186   1822    137    621       N  
ATOM   1745  CA  LYS A 164      14.892 -50.140 -17.882  1.00121.92           C  
ANISOU 1745  CA  LYS A 164    19153  15037  12135   1835    273    625       C  
ATOM   1746  C   LYS A 164      14.314 -49.369 -19.085  1.00122.99           C  
ANISOU 1746  C   LYS A 164    19204  15114  12414   1692    308    493       C  
ATOM   1747  O   LYS A 164      14.272 -49.916 -20.198  1.00121.16           O  
ANISOU 1747  O   LYS A 164    18937  14790  12310   1723    352    476       O  
ATOM   1748  CB  LYS A 164      13.775 -50.685 -16.966  1.00124.58           C  
ANISOU 1748  CB  LYS A 164    19672  15235  12429   1819    382    690       C  
ATOM   1749  CG  LYS A 164      14.228 -51.833 -16.052  1.00141.14           C  
ANISOU 1749  CG  LYS A 164    21884  17321  14421   1981    374    843       C  
ATOM   1750  CD  LYS A 164      13.051 -52.638 -15.467  1.00148.74           C  
ANISOU 1750  CD  LYS A 164    23031  18106  15376   1951    501    926       C  
ATOM   1751  CE  LYS A 164      13.447 -53.904 -14.736  1.00153.26           C  
ANISOU 1751  CE  LYS A 164    23749  18621  15863   2109    499   1088       C  
ATOM   1752  NZ  LYS A 164      12.272 -54.781 -14.464  1.00155.60           N1+
ANISOU 1752  NZ  LYS A 164    24224  18715  16180   2046    626   1173       N1+
ATOM   1753  N   ALA A 165      13.930 -48.079 -18.867  1.00118.18           N  
ANISOU 1753  N   ALA A 165    18572  14560  11771   1547    278    399       N  
ATOM   1754  CA  ALA A 165      13.399 -47.178 -19.905  1.00115.53           C  
ANISOU 1754  CA  ALA A 165    18166  14181  11549   1412    296    274       C  
ATOM   1755  C   ALA A 165      14.426 -46.964 -21.027  1.00116.97           C  
ANISOU 1755  C   ALA A 165    18184  14460  11797   1413    213    243       C  
ATOM   1756  O   ALA A 165      14.034 -46.895 -22.193  1.00115.50           O  
ANISOU 1756  O   ALA A 165    17945  14195  11745   1363    262    179       O  
ATOM   1757  CB  ALA A 165      12.996 -45.843 -19.297  1.00115.77           C  
ANISOU 1757  CB  ALA A 165    18233  14261  11492   1294    253    190       C  
ATOM   1758  N   LYS A 166      15.739 -46.900 -20.675  1.00112.31           N  
ANISOU 1758  N   LYS A 166    17504  14062  11105   1474     88    296       N  
ATOM   1759  CA  LYS A 166      16.840 -46.750 -21.626  1.00110.64           C  
ANISOU 1759  CA  LYS A 166    17111  14001  10925   1487      5    290       C  
ATOM   1760  C   LYS A 166      16.896 -47.963 -22.536  1.00114.29           C  
ANISOU 1760  C   LYS A 166    17554  14377  11494   1635     86    326       C  
ATOM   1761  O   LYS A 166      16.969 -47.781 -23.754  1.00113.28           O  
ANISOU 1761  O   LYS A 166    17323  14250  11469   1598     98    268       O  
ATOM   1762  CB  LYS A 166      18.186 -46.535 -20.919  1.00113.35           C  
ANISOU 1762  CB  LYS A 166    17356  14597  11114   1528   -141    359       C  
ATOM   1763  CG  LYS A 166      18.565 -45.067 -20.784  1.00128.19           C  
ANISOU 1763  CG  LYS A 166    19170  16613  12922   1329   -270    292       C  
ATOM   1764  CD  LYS A 166      19.426 -44.808 -19.545  1.00146.04           C  
ANISOU 1764  CD  LYS A 166    21426  19066  14995   1333   -401    356       C  
ATOM   1765  CE  LYS A 166      19.581 -43.333 -19.226  1.00157.33           C  
ANISOU 1765  CE  LYS A 166    22867  20573  16340   1112   -530    280       C  
ATOM   1766  NZ  LYS A 166      20.119 -43.109 -17.854  1.00164.83           N1+
ANISOU 1766  NZ  LYS A 166    23870  21658  17098   1109   -642    329       N1+
ATOM   1767  N   LEU A 167      16.794 -49.195 -21.959  1.00111.23           N  
ANISOU 1767  N   LEU A 167    17288  13897  11078   1799    144    420       N  
ATOM   1768  CA  LEU A 167      16.818 -50.454 -22.719  1.00110.66           C  
ANISOU 1768  CA  LEU A 167    17254  13703  11089   1958    215    456       C  
ATOM   1769  C   LEU A 167      15.719 -50.463 -23.806  1.00110.37           C  
ANISOU 1769  C   LEU A 167    17255  13467  11214   1852    319    367       C  
ATOM   1770  O   LEU A 167      16.053 -50.579 -24.980  1.00107.56           O  
ANISOU 1770  O   LEU A 167    16803  13127  10938   1886    321    323       O  
ATOM   1771  CB  LEU A 167      16.690 -51.679 -21.780  1.00112.20           C  
ANISOU 1771  CB  LEU A 167    17630  13784  11218   2115    256    573       C  
ATOM   1772  CG  LEU A 167      16.393 -53.049 -22.445  1.00117.46           C  
ANISOU 1772  CG  LEU A 167    18425  14235  11970   2255    341    608       C  
ATOM   1773  CD1 LEU A 167      17.643 -53.681 -23.055  1.00119.03           C  
ANISOU 1773  CD1 LEU A 167    18533  14552  12142   2484    283    643       C  
ATOM   1774  CD2 LEU A 167      15.766 -54.006 -21.465  1.00120.73           C  
ANISOU 1774  CD2 LEU A 167    19066  14469  12336   2305    402    710       C  
ATOM   1775  N   ILE A 168      14.435 -50.280 -23.399  1.00106.81           N  
ANISOU 1775  N   ILE A 168    16928  12860  10796   1725    403    341       N  
ATOM   1776  CA  ILE A 168      13.231 -50.254 -24.248  1.00105.00           C  
ANISOU 1776  CA  ILE A 168    16737  12456  10701   1607    504    265       C  
ATOM   1777  C   ILE A 168      13.428 -49.288 -25.422  1.00108.99           C  
ANISOU 1777  C   ILE A 168    17083  13042  11287   1511    467    157       C  
ATOM   1778  O   ILE A 168      13.228 -49.690 -26.574  1.00108.94           O  
ANISOU 1778  O   ILE A 168    17052  12951  11390   1520    512    116       O  
ATOM   1779  CB  ILE A 168      11.949 -49.895 -23.420  1.00106.95           C  
ANISOU 1779  CB  ILE A 168    17092  12617  10926   1480    578    259       C  
ATOM   1780  CG1 ILE A 168      11.724 -50.878 -22.233  1.00108.00           C  
ANISOU 1780  CG1 ILE A 168    17388  12679  10969   1560    619    382       C  
ATOM   1781  CG2 ILE A 168      10.702 -49.798 -24.318  1.00105.14           C  
ANISOU 1781  CG2 ILE A 168    16873  12249  10827   1355    677    184       C  
ATOM   1782  CD1 ILE A 168      11.055 -50.283 -21.006  1.00111.16           C  
ANISOU 1782  CD1 ILE A 168    17850  13122  11263   1483    642    397       C  
ATOM   1783  N   ASN A 169      13.855 -48.040 -25.137  1.00105.25           N  
ANISOU 1783  N   ASN A 169    16514  12727  10749   1417    378    115       N  
ATOM   1784  CA  ASN A 169      14.070 -47.028 -26.178  1.00104.37           C  
ANISOU 1784  CA  ASN A 169    16265  12693  10697   1305    330     25       C  
ATOM   1785  C   ASN A 169      15.240 -47.378 -27.121  1.00109.12           C  
ANISOU 1785  C   ASN A 169    16717  13426  11318   1399    277     43       C  
ATOM   1786  O   ASN A 169      15.134 -47.099 -28.312  1.00107.73           O  
ANISOU 1786  O   ASN A 169    16457  13241  11235   1344    293    -22       O  
ATOM   1787  CB  ASN A 169      14.244 -45.645 -25.578  1.00105.01           C  
ANISOU 1787  CB  ASN A 169    16321  12886  10691   1172    235    -16       C  
ATOM   1788  CG  ASN A 169      12.956 -45.116 -24.991  1.00132.59           C  
ANISOU 1788  CG  ASN A 169    19945  16254  14180   1084    300    -67       C  
ATOM   1789  OD1 ASN A 169      12.859 -44.855 -23.797  1.00127.84           O  
ANISOU 1789  OD1 ASN A 169    19430  15679  13464   1085    276    -43       O  
ATOM   1790  ND2 ASN A 169      11.914 -44.995 -25.803  1.00126.08           N  
ANISOU 1790  ND2 ASN A 169    19133  15302  13469   1020    388   -134       N  
ATOM   1791  N   ILE A 170      16.309 -48.037 -26.615  1.00107.02           N  
ANISOU 1791  N   ILE A 170    16416  13288  10958   1557    221    133       N  
ATOM   1792  CA  ILE A 170      17.447 -48.482 -27.431  1.00106.92           C  
ANISOU 1792  CA  ILE A 170    16254  13432  10938   1692    179    162       C  
ATOM   1793  C   ILE A 170      16.967 -49.580 -28.376  1.00110.47           C  
ANISOU 1793  C   ILE A 170    16778  13698  11498   1808    283    142       C  
ATOM   1794  O   ILE A 170      17.326 -49.555 -29.543  1.00110.27           O  
ANISOU 1794  O   ILE A 170    16636  13735  11526   1831    283    100       O  
ATOM   1795  CB  ILE A 170      18.641 -48.930 -26.545  1.00111.64           C  
ANISOU 1795  CB  ILE A 170    16802  14225  11392   1854     95    270       C  
ATOM   1796  CG1 ILE A 170      19.424 -47.696 -26.058  1.00111.89           C  
ANISOU 1796  CG1 ILE A 170    16691  14507  11316   1711    -39    276       C  
ATOM   1797  CG2 ILE A 170      19.571 -49.936 -27.268  1.00113.42           C  
ANISOU 1797  CG2 ILE A 170    16940  14548  11606   2093     97    317       C  
ATOM   1798  CD1 ILE A 170      20.232 -47.917 -24.804  1.00119.62           C  
ANISOU 1798  CD1 ILE A 170    17667  15646  12138   1807   -123    375       C  
ATOM   1799  N   CYS A 171      16.115 -50.494 -27.886  1.00107.36           N  
ANISOU 1799  N   CYS A 171    16585  13077  11131   1861    367    172       N  
ATOM   1800  CA  CYS A 171      15.528 -51.587 -28.656  1.00107.85           C  
ANISOU 1800  CA  CYS A 171    16768  12923  11288   1942    458    156       C  
ATOM   1801  C   CYS A 171      14.628 -51.066 -29.760  1.00108.86           C  
ANISOU 1801  C   CYS A 171    16863  12955  11544   1777    514     49       C  
ATOM   1802  O   CYS A 171      14.587 -51.674 -30.827  1.00106.94           O  
ANISOU 1802  O   CYS A 171    16629  12631  11372   1843    552     10       O  
ATOM   1803  CB  CYS A 171      14.767 -52.530 -27.738  1.00110.07           C  
ANISOU 1803  CB  CYS A 171    17276  12991  11553   1977    522    225       C  
ATOM   1804  SG  CYS A 171      15.792 -53.275 -26.453  1.00116.95           S  
ANISOU 1804  SG  CYS A 171    18212  13954  12267   2195    459    363       S  
ATOM   1805  N   ILE A 172      13.893 -49.959 -29.494  1.00105.19           N  
ANISOU 1805  N   ILE A 172    16373  12496  11100   1578    517     -1       N  
ATOM   1806  CA  ILE A 172      13.007 -49.294 -30.463  1.00103.89           C  
ANISOU 1806  CA  ILE A 172    16167  12262  11044   1419    562   -100       C  
ATOM   1807  C   ILE A 172      13.856 -48.750 -31.640  1.00108.12           C  
ANISOU 1807  C   ILE A 172    16521  12957  11604   1420    505   -150       C  
ATOM   1808  O   ILE A 172      13.529 -49.019 -32.799  1.00108.18           O  
ANISOU 1808  O   ILE A 172    16510  12891  11701   1416    551   -207       O  
ATOM   1809  CB  ILE A 172      12.145 -48.173 -29.790  1.00105.72           C  
ANISOU 1809  CB  ILE A 172    16420  12487  11261   1246    566   -136       C  
ATOM   1810  CG1 ILE A 172      11.076 -48.788 -28.860  1.00105.98           C  
ANISOU 1810  CG1 ILE A 172    16620  12366  11283   1232    651    -91       C  
ATOM   1811  CG2 ILE A 172      11.498 -47.250 -30.851  1.00104.37           C  
ANISOU 1811  CG2 ILE A 172    16173  12301  11183   1102    582   -238       C  
ATOM   1812  CD1 ILE A 172      10.663 -47.920 -27.723  1.00113.28           C  
ANISOU 1812  CD1 ILE A 172    17579  13340  12122   1153    636    -89       C  
ATOM   1813  N   TRP A 173      14.956 -48.029 -31.328  1.00103.95           N  
ANISOU 1813  N   TRP A 173    15857  12655  10985   1420    402   -122       N  
ATOM   1814  CA  TRP A 173      15.862 -47.444 -32.312  1.00103.44           C  
ANISOU 1814  CA  TRP A 173    15600  12786  10916   1400    338   -146       C  
ATOM   1815  C   TRP A 173      16.709 -48.510 -32.991  1.00106.93           C  
ANISOU 1815  C   TRP A 173    15983  13300  11346   1615    350   -113       C  
ATOM   1816  O   TRP A 173      17.058 -48.347 -34.155  1.00106.05           O  
ANISOU 1816  O   TRP A 173    15746  13279  11269   1617    348   -153       O  
ATOM   1817  CB  TRP A 173      16.720 -46.353 -31.670  1.00103.21           C  
ANISOU 1817  CB  TRP A 173    15457  12979  10780   1302    217   -113       C  
ATOM   1818  CG  TRP A 173      15.915 -45.114 -31.362  1.00103.54           C  
ANISOU 1818  CG  TRP A 173    15556  12948  10838   1089    197   -174       C  
ATOM   1819  CD1 TRP A 173      15.030 -44.947 -30.339  1.00106.22           C  
ANISOU 1819  CD1 TRP A 173    16051  13150  11160   1043    227   -183       C  
ATOM   1820  CD2 TRP A 173      15.834 -43.923 -32.155  1.00102.63           C  
ANISOU 1820  CD2 TRP A 173    15359  12878  10756    913    151   -236       C  
ATOM   1821  NE1 TRP A 173      14.424 -43.719 -30.430  1.00104.64           N  
ANISOU 1821  NE1 TRP A 173    15874  12910  10975    871    201   -254       N  
ATOM   1822  CE2 TRP A 173      14.906 -43.064 -31.530  1.00105.76           C  
ANISOU 1822  CE2 TRP A 173    15883  13151  11151    783    150   -286       C  
ATOM   1823  CE3 TRP A 173      16.496 -43.473 -33.306  1.00104.01           C  
ANISOU 1823  CE3 TRP A 173    15370  13199  10950    855    107   -249       C  
ATOM   1824  CZ2 TRP A 173      14.619 -41.785 -32.018  1.00104.72           C  
ANISOU 1824  CZ2 TRP A 173    15740  13011  11037    610    100   -350       C  
ATOM   1825  CZ3 TRP A 173      16.190 -42.218 -33.809  1.00105.05           C  
ANISOU 1825  CZ3 TRP A 173    15485  13323  11105    659     60   -305       C  
ATOM   1826  CH2 TRP A 173      15.267 -41.384 -33.163  1.00105.07           C  
ANISOU 1826  CH2 TRP A 173    15637  13178  11108    543     53   -356       C  
ATOM   1827  N   VAL A 174      16.968 -49.635 -32.319  1.00104.70           N  
ANISOU 1827  N   VAL A 174    15807  12961  11012   1806    368    -44       N  
ATOM   1828  CA  VAL A 174      17.710 -50.732 -32.939  1.00105.76           C  
ANISOU 1828  CA  VAL A 174    15925  13134  11124   2050    383    -19       C  
ATOM   1829  C   VAL A 174      16.760 -51.486 -33.887  1.00111.07           C  
ANISOU 1829  C   VAL A 174    16739  13548  11913   2067    480    -91       C  
ATOM   1830  O   VAL A 174      17.098 -51.675 -35.053  1.00110.56           O  
ANISOU 1830  O   VAL A 174    16595  13539  11875   2142    492   -138       O  
ATOM   1831  CB  VAL A 174      18.390 -51.657 -31.901  1.00110.28           C  
ANISOU 1831  CB  VAL A 174    16577  13737  11587   2270    356     84       C  
ATOM   1832  CG1 VAL A 174      18.791 -52.995 -32.515  1.00111.15           C  
ANISOU 1832  CG1 VAL A 174    16768  13777  11688   2547    394     96       C  
ATOM   1833  CG2 VAL A 174      19.606 -50.970 -31.293  1.00110.79           C  
ANISOU 1833  CG2 VAL A 174    16444  14129  11522   2283    246    152       C  
ATOM   1834  N   LEU A 175      15.567 -51.860 -33.395  1.00108.14           N  
ANISOU 1834  N   LEU A 175    16568  12917  11602   1981    544    -98       N  
ATOM   1835  CA  LEU A 175      14.557 -52.606 -34.137  1.00107.81           C  
ANISOU 1835  CA  LEU A 175    16682  12620  11663   1958    628   -154       C  
ATOM   1836  C   LEU A 175      14.122 -51.915 -35.436  1.00107.80           C  
ANISOU 1836  C   LEU A 175    16568  12638  11754   1821    649   -257       C  
ATOM   1837  O   LEU A 175      14.148 -52.549 -36.491  1.00107.04           O  
ANISOU 1837  O   LEU A 175    16498  12475  11696   1908    678   -306       O  
ATOM   1838  CB  LEU A 175      13.338 -52.859 -33.248  1.00108.17           C  
ANISOU 1838  CB  LEU A 175    16912  12448  11739   1832    684   -127       C  
ATOM   1839  CG  LEU A 175      12.258 -53.740 -33.846  1.00113.91           C  
ANISOU 1839  CG  LEU A 175    17815  12909  12555   1784    761   -163       C  
ATOM   1840  CD1 LEU A 175      12.462 -55.192 -33.457  1.00115.80           C  
ANISOU 1840  CD1 LEU A 175    18275  12972  12750   1963    772    -92       C  
ATOM   1841  CD2 LEU A 175      10.882 -53.235 -33.452  1.00117.80           C  
ANISOU 1841  CD2 LEU A 175    18350  13303  13104   1549    817   -178       C  
ATOM   1842  N   ALA A 176      13.739 -50.636 -35.370  1.00102.68           N  
ANISOU 1842  N   ALA A 176    15808  12074  11131   1619    630   -290       N  
ATOM   1843  CA  ALA A 176      13.277 -49.885 -36.547  1.00101.37           C  
ANISOU 1843  CA  ALA A 176    15544  11926  11048   1480    644   -380       C  
ATOM   1844  C   ALA A 176      14.346 -49.766 -37.666  1.00105.54           C  
ANISOU 1844  C   ALA A 176    15900  12647  11552   1575    606   -402       C  
ATOM   1845  O   ALA A 176      14.003 -49.305 -38.759  1.00104.50           O  
ANISOU 1845  O   ALA A 176    15697  12523  11485   1482    622   -473       O  
ATOM   1846  CB  ALA A 176      12.792 -48.501 -36.139  1.00100.87           C  
ANISOU 1846  CB  ALA A 176    15415  11919  10991   1276    616   -400       C  
ATOM   1847  N   SER A 177      15.605 -50.234 -37.428  1.00102.89           N  
ANISOU 1847  N   SER A 177    15497  12478  11118   1770    560   -339       N  
ATOM   1848  CA  SER A 177      16.654 -50.230 -38.455  1.00103.04           C  
ANISOU 1848  CA  SER A 177    15342  12716  11094   1888    532   -349       C  
ATOM   1849  C   SER A 177      16.409 -51.392 -39.454  1.00106.66           C  
ANISOU 1849  C   SER A 177    15914  13020  11594   2051    599   -406       C  
ATOM   1850  O   SER A 177      17.145 -51.550 -40.433  1.00105.99           O  
ANISOU 1850  O   SER A 177    15710  13089  11471   2178    595   -429       O  
ATOM   1851  CB  SER A 177      18.050 -50.281 -37.837  1.00108.47           C  
ANISOU 1851  CB  SER A 177    15895  13670  11647   2042    459   -256       C  
ATOM   1852  OG  SER A 177      18.397 -51.565 -37.347  1.00118.84           O  
ANISOU 1852  OG  SER A 177    17343  14906  12906   2299    478   -209       O  
ATOM   1853  N   GLY A 178      15.330 -52.145 -39.204  1.00103.15           N  
ANISOU 1853  N   GLY A 178    15702  12274  11218   2026    658   -430       N  
ATOM   1854  CA  GLY A 178      14.823 -53.209 -40.065  1.00103.26           C  
ANISOU 1854  CA  GLY A 178    15880  12074  11280   2118    715   -493       C  
ATOM   1855  C   GLY A 178      13.900 -52.633 -41.123  1.00105.11           C  
ANISOU 1855  C   GLY A 178    16075  12247  11616   1921    749   -587       C  
ATOM   1856  O   GLY A 178      13.389 -53.351 -41.982  1.00103.99           O  
ANISOU 1856  O   GLY A 178    16052  11941  11519   1952    789   -655       O  
ATOM   1857  N   VAL A 179      13.661 -51.316 -41.032  1.00101.74           N  
ANISOU 1857  N   VAL A 179    15496  11943  11217   1716    726   -592       N  
ATOM   1858  CA  VAL A 179      12.884 -50.472 -41.944  1.00100.59           C  
ANISOU 1858  CA  VAL A 179    15274  11791  11153   1522    744   -667       C  
ATOM   1859  C   VAL A 179      13.857 -49.438 -42.537  1.00105.74           C  
ANISOU 1859  C   VAL A 179    15688  12730  11759   1500    687   -662       C  
ATOM   1860  O   VAL A 179      13.797 -49.140 -43.732  1.00104.94           O  
ANISOU 1860  O   VAL A 179    15500  12684  11687   1461    697   -721       O  
ATOM   1861  CB  VAL A 179      11.663 -49.787 -41.268  1.00102.87           C  
ANISOU 1861  CB  VAL A 179    15621  11960  11507   1303    763   -670       C  
ATOM   1862  CG1 VAL A 179      10.723 -49.211 -42.317  1.00101.37           C  
ANISOU 1862  CG1 VAL A 179    15391  11724  11402   1144    792   -752       C  
ATOM   1863  CG2 VAL A 179      10.913 -50.746 -40.356  1.00103.35           C  
ANISOU 1863  CG2 VAL A 179    15889  11799  11580   1317    808   -635       C  
ATOM   1864  N   GLY A 180      14.748 -48.927 -41.679  1.00103.00           N  
ANISOU 1864  N   GLY A 180    15239  12565  11330   1515    624   -585       N  
ATOM   1865  CA  GLY A 180      15.779 -47.952 -42.012  1.00102.74           C  
ANISOU 1865  CA  GLY A 180    14980  12825  11230   1469    554   -553       C  
ATOM   1866  C   GLY A 180      16.774 -48.465 -43.028  1.00107.53           C  
ANISOU 1866  C   GLY A 180    15459  13620  11776   1652    557   -554       C  
ATOM   1867  O   GLY A 180      16.914 -47.862 -44.092  1.00107.09           O  
ANISOU 1867  O   GLY A 180    15269  13691  11728   1574    552   -586       O  
ATOM   1868  N   VAL A 181      17.448 -49.597 -42.722  1.00105.27           N  
ANISOU 1868  N   VAL A 181    15223  13355  11420   1910    568   -520       N  
ATOM   1869  CA  VAL A 181      18.429 -50.214 -43.625  1.00106.53           C  
ANISOU 1869  CA  VAL A 181    15274  13703  11498   2143    578   -523       C  
ATOM   1870  C   VAL A 181      17.745 -50.592 -44.970  1.00111.81           C  
ANISOU 1870  C   VAL A 181    16016  14231  12238   2153    642   -629       C  
ATOM   1871  O   VAL A 181      18.205 -50.070 -45.987  1.00111.84           O  
ANISOU 1871  O   VAL A 181    15838  14446  12212   2130    636   -647       O  
ATOM   1872  CB  VAL A 181      19.202 -51.420 -43.008  1.00111.40           C  
ANISOU 1872  CB  VAL A 181    15969  14339  12019   2455    578   -470       C  
ATOM   1873  CG1 VAL A 181      20.159 -52.041 -44.024  1.00112.65           C  
ANISOU 1873  CG1 VAL A 181    16019  14701  12082   2725    595   -485       C  
ATOM   1874  CG2 VAL A 181      19.953 -51.014 -41.744  1.00111.46           C  
ANISOU 1874  CG2 VAL A 181    15879  14528  11943   2447    507   -361       C  
ATOM   1875  N   PRO A 182      16.640 -51.404 -45.012  1.00108.23           N  
ANISOU 1875  N   PRO A 182    15812  13439  11870   2156    698   -696       N  
ATOM   1876  CA  PRO A 182      16.022 -51.745 -46.312  1.00107.63           C  
ANISOU 1876  CA  PRO A 182    15801  13244  11849   2153    746   -800       C  
ATOM   1877  C   PRO A 182      15.664 -50.548 -47.208  1.00109.92           C  
ANISOU 1877  C   PRO A 182    15927  13646  12190   1925    740   -838       C  
ATOM   1878  O   PRO A 182      15.877 -50.647 -48.417  1.00109.67           O  
ANISOU 1878  O   PRO A 182    15827  13704  12138   1989    760   -894       O  
ATOM   1879  CB  PRO A 182      14.750 -52.503 -45.908  1.00108.66           C  
ANISOU 1879  CB  PRO A 182    16209  13006  12070   2087    787   -840       C  
ATOM   1880  CG  PRO A 182      15.064 -53.083 -44.619  1.00113.76           C  
ANISOU 1880  CG  PRO A 182    16965  13587  12671   2199    771   -760       C  
ATOM   1881  CD  PRO A 182      15.940 -52.103 -43.911  1.00109.34           C  
ANISOU 1881  CD  PRO A 182    16189  13307  12050   2159    715   -675       C  
ATOM   1882  N   ILE A 183      15.119 -49.441 -46.634  1.00104.32           N  
ANISOU 1882  N   ILE A 183    15171  12927  11538   1677    712   -811       N  
ATOM   1883  CA  ILE A 183      14.726 -48.246 -47.390  1.00102.33           C  
ANISOU 1883  CA  ILE A 183    14794  12754  11332   1460    697   -839       C  
ATOM   1884  C   ILE A 183      15.994 -47.554 -47.896  1.00107.70           C  
ANISOU 1884  C   ILE A 183    15227  13778  11915   1478    648   -785       C  
ATOM   1885  O   ILE A 183      16.052 -47.168 -49.059  1.00107.62           O  
ANISOU 1885  O   ILE A 183    15111  13876  11902   1434    655   -820       O  
ATOM   1886  CB  ILE A 183      13.795 -47.301 -46.552  1.00103.65           C  
ANISOU 1886  CB  ILE A 183    15013  12800  11571   1225    678   -826       C  
ATOM   1887  CG1 ILE A 183      12.391 -47.914 -46.301  1.00103.35           C  
ANISOU 1887  CG1 ILE A 183    15182  12459  11626   1175    737   -880       C  
ATOM   1888  CG2 ILE A 183      13.677 -45.887 -47.137  1.00102.95           C  
ANISOU 1888  CG2 ILE A 183    14788  12831  11498   1019    637   -830       C  
ATOM   1889  CD1 ILE A 183      11.500 -48.283 -47.563  1.00106.95           C  
ANISOU 1889  CD1 ILE A 183    15694  12789  12152   1140    788   -975       C  
ATOM   1890  N   MET A 184      17.023 -47.465 -47.044  1.00105.89           N  
ANISOU 1890  N   MET A 184    14902  13735  11595   1548    597   -695       N  
ATOM   1891  CA  MET A 184      18.312 -46.854 -47.361  1.00107.29           C  
ANISOU 1891  CA  MET A 184    14828  14276  11661   1555    542   -621       C  
ATOM   1892  C   MET A 184      19.026 -47.642 -48.430  1.00112.74           C  
ANISOU 1892  C   MET A 184    15427  15133  12275   1791    584   -644       C  
ATOM   1893  O   MET A 184      19.825 -47.083 -49.175  1.00113.25           O  
ANISOU 1893  O   MET A 184    15270  15497  12261   1764    560   -605       O  
ATOM   1894  CB  MET A 184      19.169 -46.801 -46.104  1.00111.22           C  
ANISOU 1894  CB  MET A 184    15267  14917  12074   1599    480   -522       C  
ATOM   1895  CG  MET A 184      20.228 -45.752 -46.143  1.00116.51           C  
ANISOU 1895  CG  MET A 184    15687  15935  12646   1469    395   -431       C  
ATOM   1896  SD  MET A 184      21.673 -46.369 -45.272  1.00124.17           S  
ANISOU 1896  SD  MET A 184    16521  17196  13462   1697    350   -321       S  
ATOM   1897  CE  MET A 184      22.412 -47.486 -46.589  1.00122.81           C  
ANISOU 1897  CE  MET A 184    16237  17222  13205   2039    426   -350       C  
ATOM   1898  N   VAL A 185      18.733 -48.947 -48.499  1.00110.70           N  
ANISOU 1898  N   VAL A 185    15351  14680  12029   2021    644   -705       N  
ATOM   1899  CA  VAL A 185      19.288 -49.886 -49.468  1.00112.54           C  
ANISOU 1899  CA  VAL A 185    15567  15009  12185   2295    690   -750       C  
ATOM   1900  C   VAL A 185      18.693 -49.609 -50.863  1.00117.75           C  
ANISOU 1900  C   VAL A 185    16211  15635  12892   2199    727   -839       C  
ATOM   1901  O   VAL A 185      19.454 -49.472 -51.822  1.00117.66           O  
ANISOU 1901  O   VAL A 185    16018  15899  12790   2286    734   -834       O  
ATOM   1902  CB  VAL A 185      19.051 -51.350 -48.997  1.00117.14           C  
ANISOU 1902  CB  VAL A 185    16412  15329  12768   2550    728   -790       C  
ATOM   1903  CG1 VAL A 185      19.043 -52.342 -50.157  1.00118.17           C  
ANISOU 1903  CG1 VAL A 185    16643  15395  12862   2781    783   -888       C  
ATOM   1904  CG2 VAL A 185      20.076 -51.759 -47.948  1.00118.46           C  
ANISOU 1904  CG2 VAL A 185    16531  15649  12830   2749    693   -692       C  
ATOM   1905  N   MET A 186      17.349 -49.505 -50.966  1.00115.19           N  
ANISOU 1905  N   MET A 186    16063  15002  12700   2020    749   -913       N  
ATOM   1906  CA  MET A 186      16.673 -49.326 -52.248  1.00115.19           C  
ANISOU 1906  CA  MET A 186    16073  14946  12748   1933    782  -1001       C  
ATOM   1907  C   MET A 186      16.337 -47.865 -52.606  1.00115.18           C  
ANISOU 1907  C   MET A 186    15925  15045  12795   1639    747   -976       C  
ATOM   1908  O   MET A 186      15.763 -47.642 -53.672  1.00113.82           O  
ANISOU 1908  O   MET A 186    15750  14837  12658   1560    770  -1042       O  
ATOM   1909  CB  MET A 186      15.412 -50.201 -52.345  1.00117.99           C  
ANISOU 1909  CB  MET A 186    16702  14927  13201   1931    826  -1102       C  
ATOM   1910  CG  MET A 186      14.389 -49.985 -51.266  1.00121.58           C  
ANISOU 1910  CG  MET A 186    17297  15136  13763   1745    818  -1085       C  
ATOM   1911  SD  MET A 186      13.246 -51.388 -51.266  1.00127.61           S  
ANISOU 1911  SD  MET A 186    18383  15508  14595   1803    865  -1175       S  
ATOM   1912  CE  MET A 186      12.663 -51.301 -49.597  1.00124.01           C  
ANISOU 1912  CE  MET A 186    18038  14880  14199   1682    854  -1100       C  
ATOM   1913  N   ALA A 187      16.743 -46.879 -51.792  1.00110.21           N  
ANISOU 1913  N   ALA A 187    15178  14545  12151   1487    687   -881       N  
ATOM   1914  CA  ALA A 187      16.501 -45.478 -52.139  1.00108.60           C  
ANISOU 1914  CA  ALA A 187    14862  14424  11976   1219    642   -853       C  
ATOM   1915  C   ALA A 187      17.433 -45.071 -53.281  1.00114.42           C  
ANISOU 1915  C   ALA A 187    15374  15487  12613   1232    632   -819       C  
ATOM   1916  O   ALA A 187      18.645 -45.187 -53.124  1.00115.66           O  
ANISOU 1916  O   ALA A 187    15369  15924  12655   1345    610   -742       O  
ATOM   1917  CB  ALA A 187      16.718 -44.591 -50.929  1.00108.72           C  
ANISOU 1917  CB  ALA A 187    14849  14471  11987   1059    569   -767       C  
ATOM   1918  N   VAL A 188      16.888 -44.687 -54.455  1.00110.90           N  
ANISOU 1918  N   VAL A 188    14912  15027  12200   1138    653   -872       N  
ATOM   1919  CA  VAL A 188      17.729 -44.319 -55.606  1.00112.22           C  
ANISOU 1919  CA  VAL A 188    14865  15511  12262   1147    651   -836       C  
ATOM   1920  C   VAL A 188      17.209 -43.092 -56.351  1.00116.22           C  
ANISOU 1920  C   VAL A 188    15322  16028  12808    885    618   -825       C  
ATOM   1921  O   VAL A 188      16.001 -42.842 -56.376  1.00114.73           O  
ANISOU 1921  O   VAL A 188    15288  15572  12733    768    625   -890       O  
ATOM   1922  CB  VAL A 188      17.939 -45.476 -56.627  1.00117.42           C  
ANISOU 1922  CB  VAL A 188    15533  16222  12861   1417    726   -918       C  
ATOM   1923  CG1 VAL A 188      18.801 -46.599 -56.060  1.00118.97           C  
ANISOU 1923  CG1 VAL A 188    15735  16500  12970   1714    748   -906       C  
ATOM   1924  CG2 VAL A 188      16.617 -46.003 -57.183  1.00116.16           C  
ANISOU 1924  CG2 VAL A 188    15589  15739  12808   1415    774  -1049       C  
ATOM   1925  N   THR A 189      18.144 -42.364 -57.008  1.00114.18           N  
ANISOU 1925  N   THR A 189    14842  16098  12443    803    583   -736       N  
ATOM   1926  CA  THR A 189      17.862 -41.222 -57.880  1.00113.41           C  
ANISOU 1926  CA  THR A 189    14680  16059  12351    569    549   -707       C  
ATOM   1927  C   THR A 189      17.946 -41.712 -59.317  1.00118.09           C  
ANISOU 1927  C   THR A 189    15197  16785  12886    698    615   -762       C  
ATOM   1928  O   THR A 189      19.000 -42.195 -59.757  1.00118.95           O  
ANISOU 1928  O   THR A 189    15137  17193  12866    865    642   -726       O  
ATOM   1929  CB  THR A 189      18.763 -40.010 -57.626  1.00120.43           C  
ANISOU 1929  CB  THR A 189    15400  17201  13158    344    455   -562       C  
ATOM   1930  OG1 THR A 189      20.119 -40.428 -57.540  1.00125.20           O  
ANISOU 1930  OG1 THR A 189    15794  18154  13623    477    455   -480       O  
ATOM   1931  CG2 THR A 189      18.374 -39.247 -56.409  1.00116.33           C  
ANISOU 1931  CG2 THR A 189    15005  16488  12707    159    377   -529       C  
ATOM   1932  N   ARG A 190      16.800 -41.647 -60.013  1.00113.45           N  
ANISOU 1932  N   ARG A 190    14741  15978  12387    641    641   -854       N  
ATOM   1933  CA  ARG A 190      16.619 -42.108 -61.384  1.00113.31           C  
ANISOU 1933  CA  ARG A 190    14699  16024  12329    746    700   -928       C  
ATOM   1934  C   ARG A 190      16.042 -40.994 -62.290  1.00116.34           C  
ANISOU 1934  C   ARG A 190    15056  16412  12737    516    669   -909       C  
ATOM   1935  O   ARG A 190      15.226 -40.210 -61.808  1.00113.83           O  
ANISOU 1935  O   ARG A 190    14846  15886  12517    328    622   -900       O  
ATOM   1936  CB  ARG A 190      15.687 -43.341 -61.393  1.00111.68           C  
ANISOU 1936  CB  ARG A 190    14709  15522  12203    924    763  -1076       C  
ATOM   1937  CG  ARG A 190      16.302 -44.607 -60.792  1.00122.18           C  
ANISOU 1937  CG  ARG A 190    16086  16852  13485   1199    801  -1105       C  
ATOM   1938  CD  ARG A 190      17.133 -45.400 -61.796  1.00134.90           C  
ANISOU 1938  CD  ARG A 190    17601  18701  14955   1452    855  -1140       C  
ATOM   1939  NE  ARG A 190      18.155 -46.216 -61.134  1.00144.12           N  
ANISOU 1939  NE  ARG A 190    18727  19999  16031   1703    870  -1109       N  
ATOM   1940  CZ  ARG A 190      19.414 -45.833 -60.930  1.00155.84           C  
ANISOU 1940  CZ  ARG A 190    19973  21843  17394   1736    848   -987       C  
ATOM   1941  NH1 ARG A 190      19.832 -44.642 -61.343  1.00137.84           N1+
ANISOU 1941  NH1 ARG A 190    17484  19822  15068   1514    807   -882       N1+
ATOM   1942  NH2 ARG A 190      20.264 -46.637 -60.305  1.00144.34           N  
ANISOU 1942  NH2 ARG A 190    18490  20498  15855   1987    861   -964       N  
ATOM   1943  N   PRO A 191      16.418 -40.907 -63.595  1.00114.73           N  
ANISOU 1943  N   PRO A 191    14720  16436  12435    541    695   -901       N  
ATOM   1944  CA  PRO A 191      15.817 -39.872 -64.452  1.00114.69           C  
ANISOU 1944  CA  PRO A 191    14709  16416  12450    328    662   -879       C  
ATOM   1945  C   PRO A 191      14.472 -40.291 -65.066  1.00119.54           C  
ANISOU 1945  C   PRO A 191    15496  16765  13160    363    700  -1017       C  
ATOM   1946  O   PRO A 191      14.351 -41.388 -65.613  1.00118.41           O  
ANISOU 1946  O   PRO A 191    15397  16601  12992    564    765  -1123       O  
ATOM   1947  CB  PRO A 191      16.870 -39.641 -65.532  1.00118.02           C  
ANISOU 1947  CB  PRO A 191    14903  17229  12712    341    675   -800       C  
ATOM   1948  CG  PRO A 191      17.749 -40.866 -65.494  1.00123.38           C  
ANISOU 1948  CG  PRO A 191    15500  18086  13292    638    741   -836       C  
ATOM   1949  CD  PRO A 191      17.376 -41.739 -64.349  1.00117.93           C  
ANISOU 1949  CD  PRO A 191    14984  17127  12698    777    755   -913       C  
ATOM   1950  N   ARG A 192      13.461 -39.392 -64.963  1.00117.63           N  
ANISOU 1950  N   ARG A 192    15355  16323  13015    165    654  -1013       N  
ATOM   1951  CA  ARG A 192      12.106 -39.558 -65.511  1.00117.53           C  
ANISOU 1951  CA  ARG A 192    15481  16083  13091    153    674  -1121       C  
ATOM   1952  C   ARG A 192      11.689 -38.279 -66.246  1.00124.65           C  
ANISOU 1952  C   ARG A 192    16355  17019  13989    -49    622  -1060       C  
ATOM   1953  O   ARG A 192      11.553 -37.227 -65.613  1.00123.97           O  
ANISOU 1953  O   ARG A 192    16302  16861  13939   -216    555   -981       O  
ATOM   1954  CB  ARG A 192      11.070 -39.917 -64.418  1.00115.39           C  
ANISOU 1954  CB  ARG A 192    15394  15496  12955    155    677  -1188       C  
ATOM   1955  CG  ARG A 192      11.375 -41.170 -63.606  1.00124.47           C  
ANISOU 1955  CG  ARG A 192    16608  16569  14115    340    722  -1241       C  
ATOM   1956  CD  ARG A 192      11.192 -42.464 -64.369  1.00133.62           C  
ANISOU 1956  CD  ARG A 192    17828  17694  15248    526    785  -1360       C  
ATOM   1957  NE  ARG A 192      11.700 -43.602 -63.603  1.00142.38           N  
ANISOU 1957  NE  ARG A 192    19003  18752  16343    717    818  -1390       N  
ATOM   1958  CZ  ARG A 192      12.801 -44.281 -63.906  1.00158.40           C  
ANISOU 1958  CZ  ARG A 192    20952  20974  18257    915    848  -1389       C  
ATOM   1959  NH1 ARG A 192      13.515 -43.961 -64.977  1.00144.53           N1+
ANISOU 1959  NH1 ARG A 192    19034  19495  16385    944    857  -1359       N1+
ATOM   1960  NH2 ARG A 192      13.186 -45.300 -63.149  1.00149.84           N  
ANISOU 1960  NH2 ARG A 192    19954  19816  17163   1099    872  -1414       N  
ATOM   1961  N   ASP A 193      11.499 -38.382 -67.587  1.00124.22           N  
ANISOU 1961  N   ASP A 193    16253  17067  13878    -23    648  -1099       N  
ATOM   1962  CA  ASP A 193      11.110 -37.300 -68.506  1.00124.91           C  
ANISOU 1962  CA  ASP A 193    16313  17204  13942   -185    605  -1045       C  
ATOM   1963  C   ASP A 193      11.960 -36.036 -68.277  1.00127.25           C  
ANISOU 1963  C   ASP A 193    16516  17656  14177   -375    530   -880       C  
ATOM   1964  O   ASP A 193      11.436 -34.956 -67.978  1.00126.17           O  
ANISOU 1964  O   ASP A 193    16466  17384  14091   -544    460   -824       O  
ATOM   1965  CB  ASP A 193       9.593 -36.996 -68.421  1.00126.95           C  
ANISOU 1965  CB  ASP A 193    16729  17184  14320   -251    585  -1113       C  
ATOM   1966  CG  ASP A 193       8.694 -38.168 -68.826  1.00149.59           C  
ANISOU 1966  CG  ASP A 193    19682  19921  17235   -114    645  -1265       C  
ATOM   1967  OD1 ASP A 193       8.613 -38.473 -70.051  1.00152.18           O1-
ANISOU 1967  OD1 ASP A 193    19967  20358  17497    -67    670  -1314       O1-
ATOM   1968  OD2 ASP A 193       8.061 -38.769 -67.925  1.00159.32           O1-
ANISOU 1968  OD2 ASP A 193    21028  20944  18561    -67    662  -1332       O1-
ATOM   1969  N   GLY A 194      13.274 -36.211 -68.403  1.00124.03           N  
ANISOU 1969  N   GLY A 194    15938  17535  13650   -339    543   -803       N  
ATOM   1970  CA  GLY A 194      14.238 -35.128 -68.285  1.00124.61           C  
ANISOU 1970  CA  GLY A 194    15896  17813  13639   -535    470   -635       C  
ATOM   1971  C   GLY A 194      14.559 -34.683 -66.877  1.00128.32           C  
ANISOU 1971  C   GLY A 194    16416  18187  14154   -635    406   -570       C  
ATOM   1972  O   GLY A 194      15.638 -34.116 -66.652  1.00130.34           O  
ANISOU 1972  O   GLY A 194    16544  18664  14316   -763    353   -435       O  
ATOM   1973  N   ALA A 195      13.618 -34.931 -65.918  1.00121.17           N  
ANISOU 1973  N   ALA A 195    15692  16965  13382   -586    407   -662       N  
ATOM   1974  CA  ALA A 195      13.769 -34.590 -64.497  1.00118.60           C  
ANISOU 1974  CA  ALA A 195    15446  16513  13104   -656    350   -623       C  
ATOM   1975  C   ALA A 195      14.450 -35.724 -63.700  1.00117.60           C  
ANISOU 1975  C   ALA A 195    15259  16458  12966   -472    402   -655       C  
ATOM   1976  O   ALA A 195      14.720 -36.791 -64.259  1.00117.05           O  
ANISOU 1976  O   ALA A 195    15111  16505  12856   -276    482   -718       O  
ATOM   1977  CB  ALA A 195      12.418 -34.252 -63.874  1.00117.76           C  
ANISOU 1977  CB  ALA A 195    15556  16060  13129   -685    330   -696       C  
ATOM   1978  N   VAL A 196      14.767 -35.462 -62.410  1.00110.80           N  
ANISOU 1978  N   VAL A 196    14442  15530  12125   -530    349   -609       N  
ATOM   1979  CA  VAL A 196      15.419 -36.412 -61.499  1.00109.17           C  
ANISOU 1979  CA  VAL A 196    14193  15381  11905   -369    382   -622       C  
ATOM   1980  C   VAL A 196      14.426 -36.788 -60.385  1.00108.42           C  
ANISOU 1980  C   VAL A 196    14301  14957  11938   -307    396   -712       C  
ATOM   1981  O   VAL A 196      13.753 -35.904 -59.841  1.00106.91           O  
ANISOU 1981  O   VAL A 196    14242  14573  11807   -453    337   -702       O  
ATOM   1982  CB  VAL A 196      16.758 -35.869 -60.929  1.00113.72           C  
ANISOU 1982  CB  VAL A 196    14620  16216  12374   -487    308   -479       C  
ATOM   1983  CG1 VAL A 196      17.489 -36.932 -60.119  1.00113.82           C  
ANISOU 1983  CG1 VAL A 196    14565  16328  12354   -285    348   -489       C  
ATOM   1984  CG2 VAL A 196      17.663 -35.346 -62.038  1.00115.11           C  
ANISOU 1984  CG2 VAL A 196    14588  16732  12415   -595    289   -369       C  
ATOM   1985  N   VAL A 197      14.310 -38.102 -60.082  1.00102.89           N  
ANISOU 1985  N   VAL A 197    13636  14190  11268    -85    474   -799       N  
ATOM   1986  CA  VAL A 197      13.393 -38.598 -59.050  1.00100.98           C  
ANISOU 1986  CA  VAL A 197    13574  13659  11135    -23    497   -876       C  
ATOM   1987  C   VAL A 197      14.166 -39.347 -57.959  1.00101.59           C  
ANISOU 1987  C   VAL A 197    13635  13782  11183    106    505   -852       C  
ATOM   1988  O   VAL A 197      15.163 -40.001 -58.242  1.00 99.97           O  
ANISOU 1988  O   VAL A 197    13301  13795  10890    246    531   -829       O  
ATOM   1989  CB  VAL A 197      12.186 -39.452 -59.577  1.00104.57           C  
ANISOU 1989  CB  VAL A 197    14150  13907  11675     85    572  -1006       C  
ATOM   1990  CG1 VAL A 197      11.328 -38.686 -60.578  1.00103.90           C  
ANISOU 1990  CG1 VAL A 197    14085  13774  11619    -38    558  -1028       C  
ATOM   1991  CG2 VAL A 197      12.623 -40.776 -60.173  1.00105.33           C  
ANISOU 1991  CG2 VAL A 197    14207  14091  11724    302    644  -1069       C  
ATOM   1992  N   CYS A 198      13.691 -39.220 -56.710  1.00 97.13           N  
ANISOU 1992  N   CYS A 198    13200  13021  10682     69    481   -856       N  
ATOM   1993  CA  CYS A 198      14.215 -39.897 -55.527  1.00 96.92           C  
ANISOU 1993  CA  CYS A 198    13195  12989  10641    183    485   -837       C  
ATOM   1994  C   CYS A 198      13.129 -40.855 -55.076  1.00101.46           C  
ANISOU 1994  C   CYS A 198    13947  13289  11313    298    552   -936       C  
ATOM   1995  O   CYS A 198      12.110 -40.445 -54.515  1.00100.31           O  
ANISOU 1995  O   CYS A 198    13932  12936  11246    206    545   -963       O  
ATOM   1996  CB  CYS A 198      14.608 -38.904 -54.439  1.00 96.73           C  
ANISOU 1996  CB  CYS A 198    13177  12983  10591     25    393   -750       C  
ATOM   1997  SG  CYS A 198      15.143 -39.674 -52.890  1.00101.00           S  
ANISOU 1997  SG  CYS A 198    13758  13504  11112    155    391   -725       S  
ATOM   1998  N   MET A 199      13.324 -42.130 -55.394  1.00 99.34           N  
ANISOU 1998  N   MET A 199    13689  13027  11030    499    618   -988       N  
ATOM   1999  CA  MET A 199      12.340 -43.181 -55.194  1.00 99.07           C  
ANISOU 1999  CA  MET A 199    13827  12740  11074    598    680  -1080       C  
ATOM   2000  C   MET A 199      12.937 -44.446 -54.588  1.00103.81           C  
ANISOU 2000  C   MET A 199    14479  13327  11638    813    713  -1085       C  
ATOM   2001  O   MET A 199      14.125 -44.487 -54.272  1.00103.33           O  
ANISOU 2001  O   MET A 199    14304  13470  11488    901    689  -1015       O  
ATOM   2002  CB  MET A 199      11.730 -43.508 -56.560  1.00101.67           C  
ANISOU 2002  CB  MET A 199    14169  13038  11423    617    723  -1166       C  
ATOM   2003  CG  MET A 199      12.751 -43.416 -57.679  1.00106.95           C  
ANISOU 2003  CG  MET A 199    14669  13979  11988    681    721  -1144       C  
ATOM   2004  SD  MET A 199      12.443 -44.461 -59.101  1.00112.64           S  
ANISOU 2004  SD  MET A 199    15432  14680  12686    832    786  -1260       S  
ATOM   2005  CE  MET A 199      13.082 -46.026 -58.485  1.00110.83           C  
ANISOU 2005  CE  MET A 199    15303  14399  12410   1114    826  -1292       C  
ATOM   2006  N   LEU A 200      12.092 -45.486 -54.448  1.00101.77           N  
ANISOU 2006  N   LEU A 200    14397  12830  11441    894    764  -1162       N  
ATOM   2007  CA  LEU A 200      12.464 -46.790 -53.906  1.00103.19           C  
ANISOU 2007  CA  LEU A 200    14685  12931  11592   1101    795  -1175       C  
ATOM   2008  C   LEU A 200      12.470 -47.843 -55.023  1.00108.46           C  
ANISOU 2008  C   LEU A 200    15415  13568  12227   1265    839  -1265       C  
ATOM   2009  O   LEU A 200      11.443 -48.087 -55.666  1.00107.82           O  
ANISOU 2009  O   LEU A 200    15436  13322  12207   1195    863  -1346       O  
ATOM   2010  CB  LEU A 200      11.517 -47.210 -52.748  1.00102.68           C  
ANISOU 2010  CB  LEU A 200    14807  12599  11609   1052    809  -1180       C  
ATOM   2011  CG  LEU A 200      11.513 -46.330 -51.482  1.00106.25           C  
ANISOU 2011  CG  LEU A 200    15233  13060  12076    930    768  -1101       C  
ATOM   2012  CD1 LEU A 200      10.234 -46.504 -50.676  1.00105.37           C  
ANISOU 2012  CD1 LEU A 200    15284  12701  12050    834    794  -1121       C  
ATOM   2013  CD2 LEU A 200      12.728 -46.592 -50.626  1.00109.56           C  
ANISOU 2013  CD2 LEU A 200    15601  13615  12411   1063    740  -1023       C  
ATOM   2014  N   GLN A 201      13.641 -48.440 -55.265  1.00106.63           N  
ANISOU 2014  N   GLN A 201    15118  13510  11887   1488    847  -1250       N  
ATOM   2015  CA  GLN A 201      13.792 -49.473 -56.272  1.00108.28           C  
ANISOU 2015  CA  GLN A 201    15402  13700  12039   1688    885  -1339       C  
ATOM   2016  C   GLN A 201      13.518 -50.832 -55.628  1.00114.46           C  
ANISOU 2016  C   GLN A 201    16437  14217  12834   1849    906  -1382       C  
ATOM   2017  O   GLN A 201      14.436 -51.497 -55.123  1.00115.16           O  
ANISOU 2017  O   GLN A 201    16543  14371  12841   2074    906  -1347       O  
ATOM   2018  CB  GLN A 201      15.182 -49.414 -56.944  1.00111.23           C  
ANISOU 2018  CB  GLN A 201    15573  14422  12269   1871    887  -1304       C  
ATOM   2019  CG  GLN A 201      15.321 -50.270 -58.209  1.00133.02           C  
ANISOU 2019  CG  GLN A 201    18387  17202  14951   2073    929  -1407       C  
ATOM   2020  CD  GLN A 201      14.562 -49.720 -59.396  1.00157.28           C  
ANISOU 2020  CD  GLN A 201    21429  20269  18062   1905    936  -1471       C  
ATOM   2021  OE1 GLN A 201      13.322 -49.757 -59.449  1.00155.06           O  
ANISOU 2021  OE1 GLN A 201    21299  19726  17890   1745    936  -1533       O  
ATOM   2022  NE2 GLN A 201      15.298 -49.236 -60.398  1.00147.35           N  
ANISOU 2022  NE2 GLN A 201    19967  19316  16703   1946    943  -1453       N  
ATOM   2023  N   PHE A 202      12.233 -51.229 -55.632  1.00111.37           N  
ANISOU 2023  N   PHE A 202    16243  13532  12541   1723    919  -1450       N  
ATOM   2024  CA  PHE A 202      11.795 -52.515 -55.094  1.00112.47           C  
ANISOU 2024  CA  PHE A 202    16653  13382  12698   1821    932  -1488       C  
ATOM   2025  C   PHE A 202      12.274 -53.663 -56.001  1.00119.37           C  
ANISOU 2025  C   PHE A 202    17658  14220  13477   2081    948  -1578       C  
ATOM   2026  O   PHE A 202      12.371 -53.473 -57.223  1.00118.48           O  
ANISOU 2026  O   PHE A 202    17464  14232  13323   2103    957  -1643       O  
ATOM   2027  CB  PHE A 202      10.266 -52.545 -54.925  1.00113.23           C  
ANISOU 2027  CB  PHE A 202    16895  13213  12913   1580    937  -1525       C  
ATOM   2028  CG  PHE A 202       9.773 -51.670 -53.799  1.00113.37           C  
ANISOU 2028  CG  PHE A 202    16845  13224  13007   1384    927  -1439       C  
ATOM   2029  CD1 PHE A 202       9.922 -52.064 -52.473  1.00115.88           C  
ANISOU 2029  CD1 PHE A 202    17257  13445  13326   1428    924  -1369       C  
ATOM   2030  CD2 PHE A 202       9.158 -50.453 -54.062  1.00114.01           C  
ANISOU 2030  CD2 PHE A 202    16781  13392  13147   1170    918  -1431       C  
ATOM   2031  CE1 PHE A 202       9.483 -51.247 -51.432  1.00115.05           C  
ANISOU 2031  CE1 PHE A 202    17095  13343  13276   1263    916  -1297       C  
ATOM   2032  CE2 PHE A 202       8.711 -49.639 -53.012  1.00115.05           C  
ANISOU 2032  CE2 PHE A 202    16869  13513  13333   1017    908  -1361       C  
ATOM   2033  CZ  PHE A 202       8.878 -50.043 -51.707  1.00112.74           C  
ANISOU 2033  CZ  PHE A 202    16666  13135  13037   1064    908  -1298       C  
ATOM   2034  N   PRO A 203      12.600 -54.851 -55.431  1.00119.16           N  
ANISOU 2034  N   PRO A 203    17844  14027  13403   2293    948  -1583       N  
ATOM   2035  CA  PRO A 203      13.075 -55.967 -56.277  1.00121.77           C  
ANISOU 2035  CA  PRO A 203    18335  14305  13627   2572    958  -1677       C  
ATOM   2036  C   PRO A 203      11.997 -56.473 -57.221  1.00126.28           C  
ANISOU 2036  C   PRO A 203    19104  14638  14240   2460    958  -1801       C  
ATOM   2037  O   PRO A 203      10.823 -56.202 -56.988  1.00124.81           O  
ANISOU 2037  O   PRO A 203    18971  14282  14168   2179    951  -1801       O  
ATOM   2038  CB  PRO A 203      13.460 -57.051 -55.263  1.00125.28           C  
ANISOU 2038  CB  PRO A 203    19003  14567  14030   2781    949  -1642       C  
ATOM   2039  CG  PRO A 203      13.543 -56.347 -53.935  1.00127.90           C  
ANISOU 2039  CG  PRO A 203    19205  14971  14420   2649    937  -1512       C  
ATOM   2040  CD  PRO A 203      12.546 -55.248 -54.010  1.00120.93           C  
ANISOU 2040  CD  PRO A 203    18195  14097  13658   2300    938  -1504       C  
ATOM   2041  N   SER A 204      12.385 -57.186 -58.288  1.00124.67           N  
ANISOU 2041  N   SER A 204    19001  14438  13931   2679    964  -1905       N  
ATOM   2042  CA  SER A 204      11.414 -57.693 -59.256  1.00125.00           C  
ANISOU 2042  CA  SER A 204    19240  14262  13994   2575    954  -2032       C  
ATOM   2043  C   SER A 204      10.526 -58.762 -58.589  1.00129.24           C  
ANISOU 2043  C   SER A 204    20132  14386  14587   2493    926  -2055       C  
ATOM   2044  O   SER A 204      11.079 -59.671 -57.958  1.00131.09           O  
ANISOU 2044  O   SER A 204    20562  14487  14761   2717    917  -2037       O  
ATOM   2045  CB  SER A 204      12.119 -58.245 -60.493  1.00131.13           C  
ANISOU 2045  CB  SER A 204    20061  15140  14624   2857    964  -2142       C  
ATOM   2046  OG  SER A 204      11.286 -58.165 -61.639  1.00140.71           O  
ANISOU 2046  OG  SER A 204    21317  16291  15855   2700    955  -2249       O  
ATOM   2047  N   PRO A 205       9.167 -58.645 -58.628  1.00123.37           N  
ANISOU 2047  N   PRO A 205    19467  13452  13955   2168    909  -2076       N  
ATOM   2048  CA  PRO A 205       8.346 -57.615 -59.288  1.00120.46           C  
ANISOU 2048  CA  PRO A 205    18894  13209  13664   1893    914  -2092       C  
ATOM   2049  C   PRO A 205       8.067 -56.436 -58.356  1.00119.90           C  
ANISOU 2049  C   PRO A 205    18585  13277  13696   1685    928  -1969       C  
ATOM   2050  O   PRO A 205       7.422 -56.586 -57.315  1.00118.15           O  
ANISOU 2050  O   PRO A 205    18455  12889  13548   1540    924  -1906       O  
ATOM   2051  CB  PRO A 205       7.080 -58.387 -59.678  1.00122.98           C  
ANISOU 2051  CB  PRO A 205    19477  13224  14024   1698    880  -2177       C  
ATOM   2052  CG  PRO A 205       6.986 -59.550 -58.713  1.00129.37           C  
ANISOU 2052  CG  PRO A 205    20599  13726  14830   1751    859  -2151       C  
ATOM   2053  CD  PRO A 205       8.311 -59.657 -57.978  1.00125.89           C  
ANISOU 2053  CD  PRO A 205    20114  13400  14320   2055    879  -2080       C  
ATOM   2054  N   SER A 206       8.607 -55.267 -58.723  1.00115.18           N  
ANISOU 2054  N   SER A 206    17690  12986  13087   1682    943  -1932       N  
ATOM   2055  CA  SER A 206       8.530 -54.038 -57.945  1.00113.58           C  
ANISOU 2055  CA  SER A 206    17262  12938  12957   1518    948  -1823       C  
ATOM   2056  C   SER A 206       7.115 -53.750 -57.427  1.00118.58           C  
ANISOU 2056  C   SER A 206    17941  13405  13707   1229    943  -1803       C  
ATOM   2057  O   SER A 206       6.974 -53.536 -56.224  1.00117.74           O  
ANISOU 2057  O   SER A 206    17832  13257  13648   1163    947  -1717       O  
ATOM   2058  CB  SER A 206       9.062 -52.855 -58.741  1.00115.89           C  
ANISOU 2058  CB  SER A 206    17274  13541  13218   1501    951  -1807       C  
ATOM   2059  OG  SER A 206       8.404 -52.754 -59.990  1.00126.12           O  
ANISOU 2059  OG  SER A 206    18569  14836  14517   1408    948  -1897       O  
ATOM   2060  N   TRP A 207       6.076 -53.816 -58.301  1.00116.35           N  
ANISOU 2060  N   TRP A 207    17708  13040  13461   1069    935  -1881       N  
ATOM   2061  CA  TRP A 207       4.653 -53.571 -57.975  1.00115.51           C  
ANISOU 2061  CA  TRP A 207    17622  12815  13449    796    932  -1866       C  
ATOM   2062  C   TRP A 207       4.117 -54.471 -56.848  1.00117.65           C  
ANISOU 2062  C   TRP A 207    18106  12842  13755    736    933  -1825       C  
ATOM   2063  O   TRP A 207       3.132 -54.099 -56.206  1.00116.32           O  
ANISOU 2063  O   TRP A 207    17903  12636  13657    531    941  -1773       O  
ATOM   2064  CB  TRP A 207       3.771 -53.757 -59.215  1.00115.27           C  
ANISOU 2064  CB  TRP A 207    17634  12740  13423    672    914  -1966       C  
ATOM   2065  CG  TRP A 207       3.802 -55.148 -59.772  1.00118.78           C  
ANISOU 2065  CG  TRP A 207    18348  12977  13807    767    893  -2064       C  
ATOM   2066  CD1 TRP A 207       4.683 -55.644 -60.687  1.00122.95           C  
ANISOU 2066  CD1 TRP A 207    18938  13543  14236    991    887  -2148       C  
ATOM   2067  CD2 TRP A 207       2.942 -56.239 -59.408  1.00120.29           C  
ANISOU 2067  CD2 TRP A 207    18801  12883  14019    646    870  -2084       C  
ATOM   2068  NE1 TRP A 207       4.408 -56.970 -60.938  1.00124.65           N  
ANISOU 2068  NE1 TRP A 207    19459  13493  14408   1029    857  -2232       N  
ATOM   2069  CE2 TRP A 207       3.354 -57.365 -60.155  1.00126.16           C  
ANISOU 2069  CE2 TRP A 207    19784  13475  14675    806    842  -2190       C  
ATOM   2070  CE3 TRP A 207       1.867 -56.379 -58.510  1.00121.63           C  
ANISOU 2070  CE3 TRP A 207    19030  12919  14264    414    868  -2019       C  
ATOM   2071  CZ2 TRP A 207       2.708 -58.602 -60.061  1.00127.18           C  
ANISOU 2071  CZ2 TRP A 207    20231  13298  14794    720    802  -2234       C  
ATOM   2072  CZ3 TRP A 207       1.237 -57.610 -58.413  1.00124.66           C  
ANISOU 2072  CZ3 TRP A 207    19701  13026  14636    318    835  -2050       C  
ATOM   2073  CH2 TRP A 207       1.650 -58.699 -59.188  1.00127.19           C  
ANISOU 2073  CH2 TRP A 207    20278  13174  14874    459    797  -2157       C  
ATOM   2074  N   TYR A 208       4.719 -55.674 -56.656  1.00113.96           N  
ANISOU 2074  N   TYR A 208    17865  12207  13227    916    924  -1848       N  
ATOM   2075  CA  TYR A 208       4.311 -56.597 -55.598  1.00113.47           C  
ANISOU 2075  CA  TYR A 208    18030  11899  13183    869    919  -1798       C  
ATOM   2076  C   TYR A 208       4.946 -56.181 -54.265  1.00114.98           C  
ANISOU 2076  C   TYR A 208    18133  12172  13381    948    939  -1682       C  
ATOM   2077  O   TYR A 208       4.236 -56.014 -53.273  1.00112.57           O  
ANISOU 2077  O   TYR A 208    17832  11806  13131    785    951  -1604       O  
ATOM   2078  CB  TYR A 208       4.650 -58.061 -55.936  1.00116.38           C  
ANISOU 2078  CB  TYR A 208    18716  12025  13477   1032    890  -1870       C  
ATOM   2079  CG  TYR A 208       4.235 -59.007 -54.826  1.00119.02           C  
ANISOU 2079  CG  TYR A 208    19304  12092  13825    969    879  -1804       C  
ATOM   2080  CD1 TYR A 208       2.890 -59.259 -54.561  1.00121.09           C  
ANISOU 2080  CD1 TYR A 208    19660  12200  14150    668    869  -1781       C  
ATOM   2081  CD2 TYR A 208       5.183 -59.591 -53.990  1.00120.49           C  
ANISOU 2081  CD2 TYR A 208    19615  12209  13957   1201    880  -1749       C  
ATOM   2082  CE1 TYR A 208       2.500 -60.086 -53.510  1.00122.29           C  
ANISOU 2082  CE1 TYR A 208    20033  12124  14307    586    860  -1703       C  
ATOM   2083  CE2 TYR A 208       4.804 -60.422 -52.938  1.00122.37           C  
ANISOU 2083  CE2 TYR A 208    20088  12204  14203   1137    868  -1674       C  
ATOM   2084  CZ  TYR A 208       3.461 -60.664 -52.700  1.00129.91           C  
ANISOU 2084  CZ  TYR A 208    21139  13000  15219    821    860  -1649       C  
ATOM   2085  OH  TYR A 208       3.069 -61.478 -51.665  1.00134.28           O  
ANISOU 2085  OH  TYR A 208    21922  13325  15773    734    849  -1562       O  
ATOM   2086  N   TRP A 209       6.281 -56.002 -54.252  1.00112.14           N  
ANISOU 2086  N   TRP A 209    17684  11971  12955   1196    941  -1667       N  
ATOM   2087  CA  TRP A 209       7.039 -55.586 -53.077  1.00111.72           C  
ANISOU 2087  CA  TRP A 209    17533  12026  12890   1287    949  -1561       C  
ATOM   2088  C   TRP A 209       6.665 -54.169 -52.653  1.00115.36           C  
ANISOU 2088  C   TRP A 209    17749  12669  13414   1103    959  -1499       C  
ATOM   2089  O   TRP A 209       6.833 -53.835 -51.483  1.00114.98           O  
ANISOU 2089  O   TRP A 209    17662  12649  13375   1090    963  -1410       O  
ATOM   2090  CB  TRP A 209       8.534 -55.736 -53.326  1.00111.18           C  
ANISOU 2090  CB  TRP A 209    17403  12120  12719   1588    943  -1563       C  
ATOM   2091  CG  TRP A 209       8.887 -57.165 -53.616  1.00114.36           C  
ANISOU 2091  CG  TRP A 209    18082  12322  13048   1805    932  -1623       C  
ATOM   2092  CD1 TRP A 209       9.201 -57.697 -54.830  1.00118.48           C  
ANISOU 2092  CD1 TRP A 209    18679  12838  13500   1957    926  -1731       C  
ATOM   2093  CD2 TRP A 209       8.768 -58.276 -52.713  1.00115.74           C  
ANISOU 2093  CD2 TRP A 209    18536  12231  13210   1869    920  -1586       C  
ATOM   2094  NE1 TRP A 209       9.383 -59.058 -54.720  1.00120.14           N  
ANISOU 2094  NE1 TRP A 209    19205  12796  13647   2140    908  -1768       N  
ATOM   2095  CE2 TRP A 209       9.114 -59.441 -53.432  1.00121.82           C  
ANISOU 2095  CE2 TRP A 209    19553  12838  13896   2082    902  -1676       C  
ATOM   2096  CE3 TRP A 209       8.452 -58.395 -51.347  1.00116.71           C  
ANISOU 2096  CE3 TRP A 209    18732  12242  13371   1779    922  -1482       C  
ATOM   2097  CZ2 TRP A 209       9.162 -60.704 -52.834  1.00123.10           C  
ANISOU 2097  CZ2 TRP A 209    20045  12712  14015   2206    879  -1662       C  
ATOM   2098  CZ3 TRP A 209       8.492 -59.650 -50.759  1.00119.92           C  
ANISOU 2098  CZ3 TRP A 209    19448  12380  13737   1889    904  -1460       C  
ATOM   2099  CH2 TRP A 209       8.849 -60.783 -51.497  1.00122.72           C  
ANISOU 2099  CH2 TRP A 209    20057  12559  14012   2099    880  -1547       C  
ATOM   2100  N   ASP A 210       6.089 -53.370 -53.573  1.00111.95           N  
ANISOU 2100  N   ASP A 210    17177  12339  13020    960    960  -1548       N  
ATOM   2101  CA  ASP A 210       5.563 -52.044 -53.270  1.00110.68           C  
ANISOU 2101  CA  ASP A 210    16824  12314  12916    783    964  -1502       C  
ATOM   2102  C   ASP A 210       4.323 -52.235 -52.398  1.00114.11           C  
ANISOU 2102  C   ASP A 210    17355  12590  13413    600    981  -1465       C  
ATOM   2103  O   ASP A 210       4.270 -51.708 -51.286  1.00113.93           O  
ANISOU 2103  O   ASP A 210    17282  12603  13405    559    990  -1386       O  
ATOM   2104  CB  ASP A 210       5.234 -51.268 -54.555  1.00112.60           C  
ANISOU 2104  CB  ASP A 210    16924  12687  13172    698    957  -1565       C  
ATOM   2105  CG  ASP A 210       4.984 -49.786 -54.329  1.00131.97           C  
ANISOU 2105  CG  ASP A 210    19182  15300  15662    570    950  -1515       C  
ATOM   2106  OD1 ASP A 210       3.950 -49.445 -53.702  1.00133.61           O1-
ANISOU 2106  OD1 ASP A 210    19397  15445  15925    418    961  -1486       O1-
ATOM   2107  OD2 ASP A 210       5.805 -48.962 -54.807  1.00140.68           O  
ANISOU 2107  OD2 ASP A 210    20129  16596  16728    621    931  -1502       O  
ATOM   2108  N   THR A 211       3.376 -53.068 -52.878  1.00110.05           N  
ANISOU 2108  N   THR A 211    16988  11905  12922    494    984  -1518       N  
ATOM   2109  CA  THR A 211       2.129 -53.456 -52.222  1.00109.72           C  
ANISOU 2109  CA  THR A 211    17045  11718  12924    300   1000  -1482       C  
ATOM   2110  C   THR A 211       2.428 -54.095 -50.838  1.00113.09           C  
ANISOU 2110  C   THR A 211    17611  12026  13333    359   1011  -1394       C  
ATOM   2111  O   THR A 211       1.797 -53.701 -49.858  1.00112.19           O  
ANISOU 2111  O   THR A 211    17453  11929  13245    241   1035  -1320       O  
ATOM   2112  CB  THR A 211       1.361 -54.397 -53.153  1.00122.14           C  
ANISOU 2112  CB  THR A 211    18772  13134  14501    198    983  -1561       C  
ATOM   2113  OG1 THR A 211       1.158 -53.748 -54.406  1.00124.97           O  
ANISOU 2113  OG1 THR A 211    18990  13625  14867    159    971  -1638       O  
ATOM   2114  CG2 THR A 211       0.050 -54.853 -52.582  1.00120.47           C  
ANISOU 2114  CG2 THR A 211    18652  12797  14325    -33    994  -1517       C  
ATOM   2115  N   VAL A 212       3.410 -55.041 -50.755  1.00109.17           N  
ANISOU 2115  N   VAL A 212    17276  11423  12781    559    995  -1400       N  
ATOM   2116  CA  VAL A 212       3.834 -55.710 -49.507  1.00108.36           C  
ANISOU 2116  CA  VAL A 212    17320  11205  12646    650    998  -1315       C  
ATOM   2117  C   VAL A 212       4.171 -54.651 -48.453  1.00107.02           C  
ANISOU 2117  C   VAL A 212    16969  11214  12481    658   1013  -1229       C  
ATOM   2118  O   VAL A 212       3.518 -54.601 -47.415  1.00106.60           O  
ANISOU 2118  O   VAL A 212    16943  11114  12445    540   1034  -1155       O  
ATOM   2119  CB  VAL A 212       5.013 -56.689 -49.743  1.00114.01           C  
ANISOU 2119  CB  VAL A 212    18200  11834  13287    921    973  -1343       C  
ATOM   2120  CG1 VAL A 212       5.676 -57.114 -48.429  1.00114.71           C  
ANISOU 2120  CG1 VAL A 212    18383  11870  13332   1057    972  -1243       C  
ATOM   2121  CG2 VAL A 212       4.550 -57.910 -50.534  1.00115.57           C  
ANISOU 2121  CG2 VAL A 212    18659  11784  13469    901    951  -1422       C  
ATOM   2122  N   THR A 213       5.133 -53.771 -48.767  1.00100.64           N  
ANISOU 2122  N   THR A 213    15974  10616  11649    779    998  -1241       N  
ATOM   2123  CA  THR A 213       5.600 -52.661 -47.933  1.00 98.79           C  
ANISOU 2123  CA  THR A 213    15568  10563  11406    786    994  -1174       C  
ATOM   2124  C   THR A 213       4.415 -51.804 -47.459  1.00101.84           C  
ANISOU 2124  C   THR A 213    15873  10974  11845    572   1017  -1149       C  
ATOM   2125  O   THR A 213       4.324 -51.502 -46.261  1.00100.28           O  
ANISOU 2125  O   THR A 213    15674  10792  11638    547   1026  -1075       O  
ATOM   2126  CB  THR A 213       6.627 -51.847 -48.722  1.00 98.05           C  
ANISOU 2126  CB  THR A 213    15286  10690  11279    889    966  -1204       C  
ATOM   2127  OG1 THR A 213       7.715 -52.712 -49.034  1.00 99.97           O  
ANISOU 2127  OG1 THR A 213    15599  10931  11455   1115    953  -1218       O  
ATOM   2128  CG2 THR A 213       7.144 -50.653 -47.961  1.00 92.64           C  
ANISOU 2128  CG2 THR A 213    14436  10186  10576    870    945  -1139       C  
ATOM   2129  N   LYS A 214       3.496 -51.465 -48.394  1.00 98.45           N  
ANISOU 2129  N   LYS A 214    15386  10556  11464    433   1026  -1210       N  
ATOM   2130  CA  LYS A 214       2.295 -50.671 -48.118  1.00 97.72           C  
ANISOU 2130  CA  LYS A 214    15208  10508  11414    253   1050  -1195       C  
ATOM   2131  C   LYS A 214       1.375 -51.399 -47.100  1.00101.91           C  
ANISOU 2131  C   LYS A 214    15868  10905  11950    147   1087  -1133       C  
ATOM   2132  O   LYS A 214       0.971 -50.780 -46.111  1.00102.26           O  
ANISOU 2132  O   LYS A 214    15857  11012  11987     97   1109  -1074       O  
ATOM   2133  CB  LYS A 214       1.522 -50.333 -49.417  1.00100.26           C  
ANISOU 2133  CB  LYS A 214    15450  10870  11774    144   1049  -1272       C  
ATOM   2134  CG  LYS A 214       2.293 -49.560 -50.512  1.00115.98           C  
ANISOU 2134  CG  LYS A 214    17307  13005  13755    220   1016  -1327       C  
ATOM   2135  CD  LYS A 214       2.691 -48.151 -50.118  1.00128.07           C  
ANISOU 2135  CD  LYS A 214    18687  14699  15276    228    997  -1290       C  
ATOM   2136  CE  LYS A 214       3.337 -47.379 -51.242  1.00139.67           C  
ANISOU 2136  CE  LYS A 214    20027  16309  16730    262    962  -1330       C  
ATOM   2137  NZ  LYS A 214       2.373 -47.045 -52.327  1.00148.77           N1+
ANISOU 2137  NZ  LYS A 214    21125  17481  17918    154    966  -1388       N1+
ATOM   2138  N   ILE A 215       1.094 -52.711 -47.311  1.00 97.75           N  
ANISOU 2138  N   ILE A 215    15524  10195  11423    118   1089  -1141       N  
ATOM   2139  CA  ILE A 215       0.253 -53.536 -46.420  1.00 97.55           C  
ANISOU 2139  CA  ILE A 215    15641  10031  11394     -6   1117  -1069       C  
ATOM   2140  C   ILE A 215       0.962 -53.733 -45.077  1.00102.26           C  
ANISOU 2140  C   ILE A 215    16310  10601  11945    109   1123   -980       C  
ATOM   2141  O   ILE A 215       0.299 -53.992 -44.080  1.00102.27           O  
ANISOU 2141  O   ILE A 215    16368  10557  11932      9   1155   -899       O  
ATOM   2142  CB  ILE A 215      -0.151 -54.912 -47.064  1.00101.18           C  
ANISOU 2142  CB  ILE A 215    16314  10274  11855    -81   1100  -1102       C  
ATOM   2143  CG1 ILE A 215      -0.820 -54.720 -48.439  1.00100.46           C  
ANISOU 2143  CG1 ILE A 215    16149  10220  11799   -195   1086  -1197       C  
ATOM   2144  CG2 ILE A 215      -1.068 -55.727 -46.138  1.00102.09           C  
ANISOU 2144  CG2 ILE A 215    16575  10255  11960   -250   1124  -1011       C  
ATOM   2145  CD1 ILE A 215      -0.788 -55.868 -49.288  1.00103.60           C  
ANISOU 2145  CD1 ILE A 215    16748  10429  12185   -201   1050  -1261       C  
ATOM   2146  N   CYS A 216       2.289 -53.582 -45.047  1.00 99.63           N  
ANISOU 2146  N   CYS A 216    15959  10318  11579    313   1093   -988       N  
ATOM   2147  CA  CYS A 216       3.063 -53.750 -43.828  1.00100.72           C  
ANISOU 2147  CA  CYS A 216    16153  10451  11663    438   1088   -905       C  
ATOM   2148  C   CYS A 216       3.112 -52.486 -42.996  1.00103.41           C  
ANISOU 2148  C   CYS A 216    16328  10973  11992    420   1095   -865       C  
ATOM   2149  O   CYS A 216       2.867 -52.558 -41.791  1.00103.45           O  
ANISOU 2149  O   CYS A 216    16382  10960  11965    394   1116   -784       O  
ATOM   2150  CB  CYS A 216       4.456 -54.249 -44.152  1.00101.99           C  
ANISOU 2150  CB  CYS A 216    16368  10604  11780    671   1048   -925       C  
ATOM   2151  SG  CYS A 216       4.474 -55.967 -44.673  1.00108.29           S  
ANISOU 2151  SG  CYS A 216    17457  11128  12561    741   1036   -951       S  
ATOM   2152  N   VAL A 217       3.418 -51.334 -43.617  1.00 97.94           N  
ANISOU 2152  N   VAL A 217    15456  10445  11313    431   1073   -918       N  
ATOM   2153  CA  VAL A 217       3.479 -50.064 -42.884  1.00 96.21           C  
ANISOU 2153  CA  VAL A 217    15107  10376  11072    412   1065   -890       C  
ATOM   2154  C   VAL A 217       2.072 -49.670 -42.389  1.00 98.76           C  
ANISOU 2154  C   VAL A 217    15411  10700  11412    255   1114   -871       C  
ATOM   2155  O   VAL A 217       1.968 -48.907 -41.433  1.00 98.34           O  
ANISOU 2155  O   VAL A 217    15316  10727  11322    251   1118   -833       O  
ATOM   2156  CB  VAL A 217       4.162 -48.905 -43.661  1.00 98.80           C  
ANISOU 2156  CB  VAL A 217    15273  10866  11403    445   1018   -942       C  
ATOM   2157  CG1 VAL A 217       5.610 -49.236 -43.998  1.00 98.74           C  
ANISOU 2157  CG1 VAL A 217    15250  10912  11355    607    974   -941       C  
ATOM   2158  CG2 VAL A 217       3.393 -48.555 -44.917  1.00 98.19           C  
ANISOU 2158  CG2 VAL A 217    15123  10803  11382    346   1029  -1016       C  
ATOM   2159  N   PHE A 218       1.001 -50.219 -42.987  1.00 94.38           N  
ANISOU 2159  N   PHE A 218    14889  10069  10900    130   1149   -894       N  
ATOM   2160  CA  PHE A 218      -0.333 -49.910 -42.498  1.00 93.50           C  
ANISOU 2160  CA  PHE A 218    14738   9997  10790    -11   1200   -863       C  
ATOM   2161  C   PHE A 218      -0.633 -50.740 -41.241  1.00 99.10           C  
ANISOU 2161  C   PHE A 218    15574  10624  11456    -42   1238   -766       C  
ATOM   2162  O   PHE A 218      -1.169 -50.196 -40.275  1.00 98.63           O  
ANISOU 2162  O   PHE A 218    15469  10651  11355    -73   1273   -716       O  
ATOM   2163  CB  PHE A 218      -1.407 -50.099 -43.574  1.00 94.56           C  
ANISOU 2163  CB  PHE A 218    14831  10123  10975   -153   1218   -913       C  
ATOM   2164  CG  PHE A 218      -2.803 -49.880 -43.046  1.00 95.61           C  
ANISOU 2164  CG  PHE A 218    14904  10328  11093   -294   1275   -869       C  
ATOM   2165  CD1 PHE A 218      -3.245 -48.607 -42.713  1.00 98.01           C  
ANISOU 2165  CD1 PHE A 218    15070  10793  11375   -277   1291   -874       C  
ATOM   2166  CD2 PHE A 218      -3.656 -50.951 -42.830  1.00 98.11           C  
ANISOU 2166  CD2 PHE A 218    15310  10560  11407   -440   1309   -814       C  
ATOM   2167  CE1 PHE A 218      -4.530 -48.410 -42.209  1.00 99.37           C  
ANISOU 2167  CE1 PHE A 218    15174  11065  11517   -378   1350   -830       C  
ATOM   2168  CE2 PHE A 218      -4.943 -50.750 -42.341  1.00101.24           C  
ANISOU 2168  CE2 PHE A 218    15622  11067  11776   -575   1365   -761       C  
ATOM   2169  CZ  PHE A 218      -5.366 -49.485 -42.014  1.00 98.84           C  
ANISOU 2169  CZ  PHE A 218    15163  10948  11445   -528   1390   -769       C  
ATOM   2170  N   LEU A 219      -0.257 -52.031 -41.240  1.00 97.09           N  
ANISOU 2170  N   LEU A 219    15488  10201  11199    -21   1228   -737       N  
ATOM   2171  CA  LEU A 219      -0.486 -52.906 -40.089  1.00 98.59           C  
ANISOU 2171  CA  LEU A 219    15825  10292  11343    -56   1257   -633       C  
ATOM   2172  C   LEU A 219       0.432 -52.537 -38.927  1.00104.32           C  
ANISOU 2172  C   LEU A 219    16557  11074  12006     92   1243   -578       C  
ATOM   2173  O   LEU A 219      -0.066 -52.265 -37.839  1.00104.91           O  
ANISOU 2173  O   LEU A 219    16618  11210  12032     47   1281   -508       O  
ATOM   2174  CB  LEU A 219      -0.316 -54.393 -40.450  1.00 99.86           C  
ANISOU 2174  CB  LEU A 219    16203  10228  11511    -66   1237   -619       C  
ATOM   2175  CG  LEU A 219      -1.237 -54.940 -41.548  1.00104.81           C  
ANISOU 2175  CG  LEU A 219    16866  10770  12187   -236   1239   -669       C  
ATOM   2176  CD1 LEU A 219      -0.794 -56.290 -41.993  1.00106.50           C  
ANISOU 2176  CD1 LEU A 219    17321  10745  12397   -198   1199   -679       C  
ATOM   2177  CD2 LEU A 219      -2.685 -54.999 -41.108  1.00108.13           C  
ANISOU 2177  CD2 LEU A 219    17248  11236  12601   -470   1291   -602       C  
ATOM   2178  N   PHE A 220       1.748 -52.444 -39.177  1.00100.89           N  
ANISOU 2178  N   PHE A 220    16122  10649  11563    265   1188   -610       N  
ATOM   2179  CA  PHE A 220       2.755 -52.146 -38.169  1.00100.68           C  
ANISOU 2179  CA  PHE A 220    16096  10688  11470    406   1159   -559       C  
ATOM   2180  C   PHE A 220       2.789 -50.723 -37.639  1.00106.02           C  
ANISOU 2180  C   PHE A 220    16623  11545  12117    405   1150   -571       C  
ATOM   2181  O   PHE A 220       3.005 -50.583 -36.433  1.00107.77           O  
ANISOU 2181  O   PHE A 220    16876  11803  12269    445   1150   -504       O  
ATOM   2182  CB  PHE A 220       4.145 -52.479 -38.686  1.00102.34           C  
ANISOU 2182  CB  PHE A 220    16325  10889  11669    588   1100   -586       C  
ATOM   2183  CG  PHE A 220       4.488 -53.906 -38.394  1.00105.41           C  
ANISOU 2183  CG  PHE A 220    16922  11098  12030    675   1097   -530       C  
ATOM   2184  CD1 PHE A 220       4.963 -54.280 -37.141  1.00109.76           C  
ANISOU 2184  CD1 PHE A 220    17566  11631  12508    763   1090   -434       C  
ATOM   2185  CD2 PHE A 220       4.282 -54.893 -39.347  1.00107.73           C  
ANISOU 2185  CD2 PHE A 220    17344  11227  12361    667   1097   -572       C  
ATOM   2186  CE1 PHE A 220       5.246 -55.612 -36.854  1.00112.30           C  
ANISOU 2186  CE1 PHE A 220    18105  11766  12796    851   1083   -374       C  
ATOM   2187  CE2 PHE A 220       4.564 -56.222 -39.060  1.00112.53           C  
ANISOU 2187  CE2 PHE A 220    18185  11637  12933    752   1087   -520       C  
ATOM   2188  CZ  PHE A 220       5.046 -56.574 -37.816  1.00111.91           C  
ANISOU 2188  CZ  PHE A 220    18199  11538  12785    847   1080   -418       C  
ATOM   2189  N   ALA A 221       2.676 -49.674 -38.505  1.00100.87           N  
ANISOU 2189  N   ALA A 221    15827  10996  11504    371   1132   -652       N  
ATOM   2190  CA  ALA A 221       2.785 -48.269 -38.056  1.00 99.28           C  
ANISOU 2190  CA  ALA A 221    15517  10939  11265    376   1106   -670       C  
ATOM   2191  C   ALA A 221       1.426 -47.540 -37.954  1.00102.41           C  
ANISOU 2191  C   ALA A 221    15854  11389  11667    265   1158   -689       C  
ATOM   2192  O   ALA A 221       1.377 -46.300 -37.950  1.00101.21           O  
ANISOU 2192  O   ALA A 221    15622  11336  11496    269   1132   -730       O  
ATOM   2193  CB  ALA A 221       3.727 -47.499 -38.964  1.00 98.91           C  
ANISOU 2193  CB  ALA A 221    15366  10979  11236    427   1038   -732       C  
ATOM   2194  N   PHE A 222       0.329 -48.316 -37.838  1.00 99.46           N  
ANISOU 2194  N   PHE A 222    15526  10955  11308    168   1227   -653       N  
ATOM   2195  CA  PHE A 222      -1.021 -47.776 -37.679  1.00 98.70           C  
ANISOU 2195  CA  PHE A 222    15359  10942  11202     72   1285   -655       C  
ATOM   2196  C   PHE A 222      -1.928 -48.714 -36.848  1.00102.53           C  
ANISOU 2196  C   PHE A 222    15915  11392  11651    -19   1359   -562       C  
ATOM   2197  O   PHE A 222      -2.270 -48.381 -35.708  1.00102.16           O  
ANISOU 2197  O   PHE A 222    15869  11422  11524     -3   1395   -509       O  
ATOM   2198  CB  PHE A 222      -1.672 -47.453 -39.041  1.00 99.36           C  
ANISOU 2198  CB  PHE A 222    15343  11053  11357     -3   1287   -731       C  
ATOM   2199  CG  PHE A 222      -2.997 -46.750 -38.896  1.00100.51           C  
ANISOU 2199  CG  PHE A 222    15391  11321  11479    -68   1341   -734       C  
ATOM   2200  CD1 PHE A 222      -3.055 -45.406 -38.544  1.00102.98           C  
ANISOU 2200  CD1 PHE A 222    15642  11743  11743      8   1327   -768       C  
ATOM   2201  CD2 PHE A 222      -4.188 -47.442 -39.053  1.00103.06           C  
ANISOU 2201  CD2 PHE A 222    15691  11656  11813   -203   1404   -698       C  
ATOM   2202  CE1 PHE A 222      -4.283 -44.757 -38.397  1.00104.05           C  
ANISOU 2202  CE1 PHE A 222    15691  12003  11840    -14   1379   -773       C  
ATOM   2203  CE2 PHE A 222      -5.416 -46.795 -38.903  1.00106.18           C  
ANISOU 2203  CE2 PHE A 222    15969  12203  12169   -245   1458   -693       C  
ATOM   2204  CZ  PHE A 222      -5.457 -45.458 -38.572  1.00103.71           C  
ANISOU 2204  CZ  PHE A 222    15594  12004  11806   -133   1449   -733       C  
ATOM   2205  N   VAL A 223      -2.300 -49.876 -37.422  1.00 98.12           N  
ANISOU 2205  N   VAL A 223    15423  10718  11140   -122   1376   -541       N  
ATOM   2206  CA  VAL A 223      -3.214 -50.849 -36.830  1.00 98.46           C  
ANISOU 2206  CA  VAL A 223    15540  10716  11153   -256   1436   -445       C  
ATOM   2207  C   VAL A 223      -2.700 -51.368 -35.473  1.00103.33           C  
ANISOU 2207  C   VAL A 223    16285  11284  11694   -194   1445   -345       C  
ATOM   2208  O   VAL A 223      -3.410 -51.221 -34.478  1.00104.25           O  
ANISOU 2208  O   VAL A 223    16378  11496  11737   -241   1503   -272       O  
ATOM   2209  CB  VAL A 223      -3.515 -51.999 -37.810  1.00102.31           C  
ANISOU 2209  CB  VAL A 223    16115  11053  11705   -381   1426   -452       C  
ATOM   2210  CG1 VAL A 223      -4.626 -52.889 -37.275  1.00103.91           C  
ANISOU 2210  CG1 VAL A 223    16378  11231  11873   -572   1483   -347       C  
ATOM   2211  CG2 VAL A 223      -3.903 -51.450 -39.167  1.00100.96           C  
ANISOU 2211  CG2 VAL A 223    15818  10941  11602   -426   1409   -555       C  
ATOM   2212  N   VAL A 224      -1.490 -51.960 -35.436  1.00 99.23           N  
ANISOU 2212  N   VAL A 224    15890  10633  11180    -77   1390   -339       N  
ATOM   2213  CA  VAL A 224      -0.870 -52.505 -34.220  1.00 99.54           C  
ANISOU 2213  CA  VAL A 224    16059  10618  11145      4   1385   -244       C  
ATOM   2214  C   VAL A 224      -0.709 -51.379 -33.152  1.00102.98           C  
ANISOU 2214  C   VAL A 224    16407  11221  11498     88   1392   -234       C  
ATOM   2215  O   VAL A 224      -1.243 -51.567 -32.050  1.00104.46           O  
ANISOU 2215  O   VAL A 224    16634  11450  11607     47   1443   -143       O  
ATOM   2216  CB  VAL A 224       0.465 -53.270 -34.478  1.00103.27           C  
ANISOU 2216  CB  VAL A 224    16663  10945  11630    150   1317   -247       C  
ATOM   2217  CG1 VAL A 224       1.039 -53.823 -33.182  1.00104.22           C  
ANISOU 2217  CG1 VAL A 224    16914  11020  11663    239   1312   -139       C  
ATOM   2218  CG2 VAL A 224       0.274 -54.409 -35.474  1.00103.70           C  
ANISOU 2218  CG2 VAL A 224    16842  10812  11747     83   1308   -264       C  
ATOM   2219  N   PRO A 225      -0.068 -50.209 -33.435  1.00 96.57           N  
ANISOU 2219  N   PRO A 225    15489  10510  10692    188   1342   -321       N  
ATOM   2220  CA  PRO A 225       0.048 -49.171 -32.396  1.00 95.98           C  
ANISOU 2220  CA  PRO A 225    15370  10570  10527    257   1337   -316       C  
ATOM   2221  C   PRO A 225      -1.292 -48.724 -31.816  1.00102.91           C  
ANISOU 2221  C   PRO A 225    16190  11563  11350    177   1419   -292       C  
ATOM   2222  O   PRO A 225      -1.342 -48.497 -30.608  1.00103.93           O  
ANISOU 2222  O   PRO A 225    16352  11761  11375    221   1441   -238       O  
ATOM   2223  CB  PRO A 225       0.733 -48.018 -33.126  1.00 95.87           C  
ANISOU 2223  CB  PRO A 225    15259  10622  10546    322   1265   -421       C  
ATOM   2224  CG  PRO A 225       1.465 -48.654 -34.205  1.00 99.68           C  
ANISOU 2224  CG  PRO A 225    15754  11010  11109    343   1223   -452       C  
ATOM   2225  CD  PRO A 225       0.615 -49.779 -34.668  1.00 96.17           C  
ANISOU 2225  CD  PRO A 225    15369  10455  10717    237   1280   -421       C  
ATOM   2226  N   ILE A 226      -2.376 -48.645 -32.636  1.00100.58           N  
ANISOU 2226  N   ILE A 226    15805  11303  11108     66   1467   -324       N  
ATOM   2227  CA  ILE A 226      -3.706 -48.236 -32.159  1.00101.62           C  
ANISOU 2227  CA  ILE A 226    15852  11582  11177      2   1550   -297       C  
ATOM   2228  C   ILE A 226      -4.264 -49.284 -31.198  1.00107.46           C  
ANISOU 2228  C   ILE A 226    16667  12313  11850    -88   1620   -163       C  
ATOM   2229  O   ILE A 226      -4.685 -48.913 -30.107  1.00107.56           O  
ANISOU 2229  O   ILE A 226    16664  12452  11752    -54   1670   -114       O  
ATOM   2230  CB  ILE A 226      -4.700 -47.912 -33.305  1.00104.80           C  
ANISOU 2230  CB  ILE A 226    16123  12050  11646    -90   1577   -357       C  
ATOM   2231  CG1 ILE A 226      -4.381 -46.524 -33.888  1.00104.89           C  
ANISOU 2231  CG1 ILE A 226    16054  12123  11675     18   1523   -474       C  
ATOM   2232  CG2 ILE A 226      -6.165 -47.943 -32.821  1.00106.18           C  
ANISOU 2232  CG2 ILE A 226    16207  12387  11750   -185   1677   -291       C  
ATOM   2233  CD1 ILE A 226      -4.687 -46.389 -35.309  1.00114.00           C  
ANISOU 2233  CD1 ILE A 226    17124  13265  12927    -43   1505   -546       C  
ATOM   2234  N   LEU A 227      -4.229 -50.573 -31.575  1.00105.30           N  
ANISOU 2234  N   LEU A 227    16492  11886  11632   -197   1618   -104       N  
ATOM   2235  CA  LEU A 227      -4.747 -51.649 -30.728  1.00107.52           C  
ANISOU 2235  CA  LEU A 227    16870  12132  11851   -312   1674     37       C  
ATOM   2236  C   LEU A 227      -4.079 -51.682 -29.358  1.00109.50           C  
ANISOU 2236  C   LEU A 227    17219  12391  11997   -197   1671    110       C  
ATOM   2237  O   LEU A 227      -4.788 -51.789 -28.360  1.00110.86           O  
ANISOU 2237  O   LEU A 227    17383  12673  12067   -249   1742    207       O  
ATOM   2238  CB  LEU A 227      -4.620 -53.011 -31.403  1.00109.50           C  
ANISOU 2238  CB  LEU A 227    17263  12166  12176   -430   1646     76       C  
ATOM   2239  CG  LEU A 227      -5.317 -53.163 -32.758  1.00116.25           C  
ANISOU 2239  CG  LEU A 227    18045  12999  13125   -571   1643     12       C  
ATOM   2240  CD1 LEU A 227      -5.093 -54.557 -33.325  1.00118.19           C  
ANISOU 2240  CD1 LEU A 227    18482  12999  13425   -674   1604     47       C  
ATOM   2241  CD2 LEU A 227      -6.810 -52.812 -32.682  1.00121.48           C  
ANISOU 2241  CD2 LEU A 227    18542  13870  13746   -728   1725     50       C  
ATOM   2242  N   ILE A 228      -2.741 -51.532 -29.299  1.00102.66           N  
ANISOU 2242  N   ILE A 228    16425  11438  11144    -38   1589     67       N  
ATOM   2243  CA  ILE A 228      -1.976 -51.512 -28.042  1.00101.57           C  
ANISOU 2243  CA  ILE A 228    16374  11314  10903     84   1569    128       C  
ATOM   2244  C   ILE A 228      -2.439 -50.339 -27.123  1.00105.87           C  
ANISOU 2244  C   ILE A 228    16824  12067  11335    141   1609    111       C  
ATOM   2245  O   ILE A 228      -2.785 -50.573 -25.960  1.00105.90           O  
ANISOU 2245  O   ILE A 228    16873  12140  11224    135   1661    209       O  
ATOM   2246  CB  ILE A 228      -0.456 -51.448 -28.329  1.00102.41           C  
ANISOU 2246  CB  ILE A 228    16535  11331  11046    239   1466     73       C  
ATOM   2247  CG1 ILE A 228       0.026 -52.726 -29.039  1.00101.84           C  
ANISOU 2247  CG1 ILE A 228    16590  11053  11051    224   1433    102       C  
ATOM   2248  CG2 ILE A 228       0.333 -51.191 -27.040  1.00103.40           C  
ANISOU 2248  CG2 ILE A 228    16718  11515  11054    368   1433    122       C  
ATOM   2249  CD1 ILE A 228       1.381 -52.647 -29.635  1.00102.82           C  
ANISOU 2249  CD1 ILE A 228    16722  11124  11219    375   1342     34       C  
ATOM   2250  N   ILE A 229      -2.461 -49.101 -27.665  1.00101.72           N  
ANISOU 2250  N   ILE A 229    16182  11634  10834    201   1582    -13       N  
ATOM   2251  CA  ILE A 229      -2.855 -47.881 -26.953  1.00101.95           C  
ANISOU 2251  CA  ILE A 229    16146  11833  10756    282   1604    -57       C  
ATOM   2252  C   ILE A 229      -4.355 -47.952 -26.528  1.00109.21           C  
ANISOU 2252  C   ILE A 229    16986  12906  11601    196   1724      7       C  
ATOM   2253  O   ILE A 229      -4.681 -47.541 -25.406  1.00110.80           O  
ANISOU 2253  O   ILE A 229    17193  13241  11664    262   1769     41       O  
ATOM   2254  CB  ILE A 229      -2.521 -46.626 -27.813  1.00103.28           C  
ANISOU 2254  CB  ILE A 229    16238  12024  10978    353   1535   -201       C  
ATOM   2255  CG1 ILE A 229      -0.988 -46.471 -27.974  1.00101.69           C  
ANISOU 2255  CG1 ILE A 229    16101  11728  10810    435   1418   -242       C  
ATOM   2256  CG2 ILE A 229      -3.128 -45.341 -27.216  1.00105.32           C  
ANISOU 2256  CG2 ILE A 229    16452  12441  11125    439   1559   -259       C  
ATOM   2257  CD1 ILE A 229      -0.544 -45.549 -29.060  1.00 96.84           C  
ANISOU 2257  CD1 ILE A 229    15419  11103  10274    457   1343   -359       C  
ATOM   2258  N   THR A 230      -5.241 -48.499 -27.404  1.00105.66           N  
ANISOU 2258  N   THR A 230    16461  12452  11232     48   1773     26       N  
ATOM   2259  CA  THR A 230      -6.678 -48.684 -27.136  1.00106.04           C  
ANISOU 2259  CA  THR A 230    16405  12671  11214    -65   1884    101       C  
ATOM   2260  C   THR A 230      -6.847 -49.677 -25.988  1.00109.64           C  
ANISOU 2260  C   THR A 230    16953  13132  11572   -139   1940    260       C  
ATOM   2261  O   THR A 230      -7.610 -49.392 -25.072  1.00110.37           O  
ANISOU 2261  O   THR A 230    16984  13421  11529   -125   2022    320       O  
ATOM   2262  CB  THR A 230      -7.428 -49.134 -28.400  1.00112.09           C  
ANISOU 2262  CB  THR A 230    17081  13416  12094   -229   1900     89       C  
ATOM   2263  OG1 THR A 230      -7.211 -48.171 -29.429  1.00109.43           O  
ANISOU 2263  OG1 THR A 230    16666  13076  11837   -147   1845    -53       O  
ATOM   2264  CG2 THR A 230      -8.922 -49.302 -28.180  1.00112.11           C  
ANISOU 2264  CG2 THR A 230    16944  13632  12021   -362   2009    174       C  
ATOM   2265  N   VAL A 231      -6.116 -50.810 -26.028  1.00105.41           N  
ANISOU 2265  N   VAL A 231    16572  12386  11094   -201   1894    328       N  
ATOM   2266  CA  VAL A 231      -6.139 -51.843 -24.988  1.00107.19           C  
ANISOU 2266  CA  VAL A 231    16923  12571  11232   -273   1930    488       C  
ATOM   2267  C   VAL A 231      -5.672 -51.206 -23.650  1.00113.34           C  
ANISOU 2267  C   VAL A 231    17737  13461  11866   -102   1934    502       C  
ATOM   2268  O   VAL A 231      -6.357 -51.359 -22.632  1.00114.67           O  
ANISOU 2268  O   VAL A 231    17892  13777  11900   -140   2017    611       O  
ATOM   2269  CB  VAL A 231      -5.324 -53.115 -25.390  1.00110.65           C  
ANISOU 2269  CB  VAL A 231    17551  12731  11760   -330   1862    539       C  
ATOM   2270  CG1 VAL A 231      -5.016 -54.009 -24.186  1.00111.96           C  
ANISOU 2270  CG1 VAL A 231    17884  12831  11823   -336   1874    694       C  
ATOM   2271  CG2 VAL A 231      -6.056 -53.912 -26.471  1.00110.60           C  
ANISOU 2271  CG2 VAL A 231    17539  12630  11855   -541   1873    557       C  
ATOM   2272  N   CYS A 232      -4.562 -50.438 -23.673  1.00109.43           N  
ANISOU 2272  N   CYS A 232    17274  12916  11387     76   1845    392       N  
ATOM   2273  CA  CYS A 232      -4.049 -49.744 -22.488  1.00109.97           C  
ANISOU 2273  CA  CYS A 232    17384  13080  11318    233   1827    385       C  
ATOM   2274  C   CYS A 232      -5.157 -48.892 -21.875  1.00117.41           C  
ANISOU 2274  C   CYS A 232    18213  14267  12129    263   1920    375       C  
ATOM   2275  O   CYS A 232      -5.432 -49.048 -20.687  1.00118.72           O  
ANISOU 2275  O   CYS A 232    18415  14547  12147    285   1977    469       O  
ATOM   2276  CB  CYS A 232      -2.823 -48.905 -22.829  1.00108.34           C  
ANISOU 2276  CB  CYS A 232    17200  12806  11157    380   1709    255       C  
ATOM   2277  SG  CYS A 232      -1.324 -49.874 -23.095  1.00111.76           S  
ANISOU 2277  SG  CYS A 232    17771  13019  11675    415   1603    290       S  
ATOM   2278  N   TYR A 233      -5.838 -48.060 -22.707  1.00115.19           N  
ANISOU 2278  N   TYR A 233    17795  14077  11896    267   1940    270       N  
ATOM   2279  CA  TYR A 233      -6.946 -47.178 -22.321  1.00116.99           C  
ANISOU 2279  CA  TYR A 233    17900  14548  12004    328   2027    242       C  
ATOM   2280  C   TYR A 233      -8.103 -47.958 -21.704  1.00123.31           C  
ANISOU 2280  C   TYR A 233    18631  15514  12705    197   2155    398       C  
ATOM   2281  O   TYR A 233      -8.594 -47.571 -20.643  1.00124.51           O  
ANISOU 2281  O   TYR A 233    18759  15864  12685    283   2226    437       O  
ATOM   2282  CB  TYR A 233      -7.450 -46.370 -23.537  1.00118.31           C  
ANISOU 2282  CB  TYR A 233    17937  14751  12264    339   2017    118       C  
ATOM   2283  CG  TYR A 233      -8.709 -45.555 -23.298  1.00122.75           C  
ANISOU 2283  CG  TYR A 233    18358  15576  12707    411   2113     95       C  
ATOM   2284  CD1 TYR A 233      -8.690 -44.424 -22.487  1.00125.58           C  
ANISOU 2284  CD1 TYR A 233    18749  16049  12916    617   2112     20       C  
ATOM   2285  CD2 TYR A 233      -9.908 -45.884 -23.925  1.00124.37           C  
ANISOU 2285  CD2 TYR A 233    18396  15918  12940    283   2197    143       C  
ATOM   2286  CE1 TYR A 233      -9.840 -43.663 -22.274  1.00127.99           C  
ANISOU 2286  CE1 TYR A 233    18932  16602  13096    722   2201     -7       C  
ATOM   2287  CE2 TYR A 233     -11.060 -45.119 -23.739  1.00126.35           C  
ANISOU 2287  CE2 TYR A 233    18496  16440  13070    374   2285    124       C  
ATOM   2288  CZ  TYR A 233     -11.021 -44.003 -22.916  1.00134.39           C  
ANISOU 2288  CZ  TYR A 233    19556  17570  13936    609   2290     47       C  
ATOM   2289  OH  TYR A 233     -12.156 -43.243 -22.726  1.00134.50           O  
ANISOU 2289  OH  TYR A 233    19431  17859  13816    736   2380     24       O  
ATOM   2290  N   GLY A 234      -8.521 -49.029 -22.380  1.00120.22           N  
ANISOU 2290  N   GLY A 234    18215  15048  12416    -12   2179    485       N  
ATOM   2291  CA  GLY A 234      -9.612 -49.901 -21.958  1.00122.19           C  
ANISOU 2291  CA  GLY A 234    18400  15438  12588   -198   2287    651       C  
ATOM   2292  C   GLY A 234      -9.381 -50.546 -20.609  1.00128.36           C  
ANISOU 2292  C   GLY A 234    19303  16235  13234   -206   2321    796       C  
ATOM   2293  O   GLY A 234     -10.300 -50.611 -19.791  1.00129.64           O  
ANISOU 2293  O   GLY A 234    19379  16635  13243   -249   2428    904       O  
ATOM   2294  N   LEU A 235      -8.139 -51.002 -20.367  1.00125.15           N  
ANISOU 2294  N   LEU A 235    19086  15594  12871   -152   2230    802       N  
ATOM   2295  CA  LEU A 235      -7.734 -51.607 -19.099  1.00126.80           C  
ANISOU 2295  CA  LEU A 235    19435  15789  12955   -135   2242    935       C  
ATOM   2296  C   LEU A 235      -7.578 -50.534 -18.034  1.00131.62           C  
ANISOU 2296  C   LEU A 235    20029  16583  13399     79   2258    878       C  
ATOM   2297  O   LEU A 235      -7.921 -50.774 -16.879  1.00133.21           O  
ANISOU 2297  O   LEU A 235    20252  16927  13433     80   2329    997       O  
ATOM   2298  CB  LEU A 235      -6.427 -52.392 -19.250  1.00126.27           C  
ANISOU 2298  CB  LEU A 235    19568  15424  12983   -116   2131    951       C  
ATOM   2299  CG  LEU A 235      -6.423 -53.596 -20.186  1.00131.20           C  
ANISOU 2299  CG  LEU A 235    20277  15821  13754   -303   2101   1011       C  
ATOM   2300  CD1 LEU A 235      -5.013 -54.076 -20.426  1.00130.57           C  
ANISOU 2300  CD1 LEU A 235    20374  15475  13759   -200   1984    982       C  
ATOM   2301  CD2 LEU A 235      -7.283 -54.727 -19.645  1.00136.05           C  
ANISOU 2301  CD2 LEU A 235    20943  16459  14291   -526   2181   1214       C  
ATOM   2302  N   MET A 236      -7.065 -49.350 -18.429  1.00126.40           N  
ANISOU 2302  N   MET A 236    19340  15913  12773    254   2188    697       N  
ATOM   2303  CA  MET A 236      -6.878 -48.223 -17.526  1.00126.30           C  
ANISOU 2303  CA  MET A 236    19340  16043  12604    461   2183    615       C  
ATOM   2304  C   MET A 236      -8.218 -47.735 -17.008  1.00133.02           C  
ANISOU 2304  C   MET A 236    20050  17195  13297    489   2315    642       C  
ATOM   2305  O   MET A 236      -8.310 -47.466 -15.818  1.00134.05           O  
ANISOU 2305  O   MET A 236    20219  17475  13239    597   2358    680       O  
ATOM   2306  CB  MET A 236      -6.088 -47.088 -18.186  1.00126.50           C  
ANISOU 2306  CB  MET A 236    19382  15972  12709    604   2068    422       C  
ATOM   2307  CG  MET A 236      -4.590 -47.203 -17.961  1.00128.93           C  
ANISOU 2307  CG  MET A 236    19842  16093  13051    669   1938    398       C  
ATOM   2308  SD  MET A 236      -3.643 -45.775 -18.558  1.00130.50           S  
ANISOU 2308  SD  MET A 236    20063  16216  13303    813   1797    190       S  
ATOM   2309  CE  MET A 236      -3.309 -46.283 -20.193  1.00125.58           C  
ANISOU 2309  CE  MET A 236    19384  15406  12923    692   1746    156       C  
ATOM   2310  N   LEU A 237      -9.269 -47.694 -17.861  1.00130.94           N  
ANISOU 2310  N   LEU A 237    19617  17039  13094    393   2384    636       N  
ATOM   2311  CA  LEU A 237     -10.603 -47.268 -17.422  1.00133.32           C  
ANISOU 2311  CA  LEU A 237    19752  17668  13235    427   2517    673       C  
ATOM   2312  C   LEU A 237     -11.294 -48.370 -16.601  1.00141.85           C  
ANISOU 2312  C   LEU A 237    20799  18895  14201    254   2628    891       C  
ATOM   2313  O   LEU A 237     -12.049 -48.066 -15.674  1.00142.64           O  
ANISOU 2313  O   LEU A 237    20817  19281  14099    331   2734    949       O  
ATOM   2314  CB  LEU A 237     -11.498 -46.805 -18.597  1.00132.73           C  
ANISOU 2314  CB  LEU A 237    19490  17692  13249    394   2549    597       C  
ATOM   2315  CG  LEU A 237     -11.934 -47.810 -19.666  1.00137.16           C  
ANISOU 2315  CG  LEU A 237    19968  18172  13973    126   2557    677       C  
ATOM   2316  CD1 LEU A 237     -13.265 -48.483 -19.304  1.00139.58           C  
ANISOU 2316  CD1 LEU A 237    20109  18757  14168    -52   2695    852       C  
ATOM   2317  CD2 LEU A 237     -12.095 -47.124 -20.990  1.00138.09           C  
ANISOU 2317  CD2 LEU A 237    19988  18249  14229    159   2510    531       C  
ATOM   2318  N   LEU A 238     -11.037 -49.636 -16.960  1.00141.08           N  
ANISOU 2318  N   LEU A 238    20777  18603  14225     23   2600   1013       N  
ATOM   2319  CA  LEU A 238     -11.590 -50.821 -16.313  1.00144.59           C  
ANISOU 2319  CA  LEU A 238    21230  19122  14586   -190   2682   1235       C  
ATOM   2320  C   LEU A 238     -10.998 -51.000 -14.906  1.00153.84           C  
ANISOU 2320  C   LEU A 238    22553  20304  15595    -89   2686   1319       C  
ATOM   2321  O   LEU A 238     -11.738 -51.305 -13.968  1.00155.76           O  
ANISOU 2321  O   LEU A 238    22740  20784  15660   -147   2795   1468       O  
ATOM   2322  CB  LEU A 238     -11.304 -52.052 -17.204  1.00144.19           C  
ANISOU 2322  CB  LEU A 238    21277  18787  14723   -438   2618   1309       C  
ATOM   2323  CG  LEU A 238     -11.571 -53.460 -16.668  1.00150.85           C  
ANISOU 2323  CG  LEU A 238    22220  19578  15518   -688   2657   1540       C  
ATOM   2324  CD1 LEU A 238     -13.056 -53.750 -16.577  1.00153.29           C  
ANISOU 2324  CD1 LEU A 238    22327  20191  15724   -902   2786   1682       C  
ATOM   2325  CD2 LEU A 238     -10.919 -54.493 -17.557  1.00152.34           C  
ANISOU 2325  CD2 LEU A 238    22582  19403  15898   -843   2554   1557       C  
ATOM   2326  N   ARG A 239      -9.674 -50.796 -14.763  1.00152.20           N  
ANISOU 2326  N   ARG A 239    22523  19864  15440     58   2566   1228       N  
ATOM   2327  CA  ARG A 239      -8.961 -50.958 -13.493  1.00154.44           C  
ANISOU 2327  CA  ARG A 239    22963  20136  15581    163   2546   1296       C  
ATOM   2328  C   ARG A 239      -8.978 -49.660 -12.643  1.00159.55           C  
ANISOU 2328  C   ARG A 239    23576  20997  16047    421   2566   1176       C  
ATOM   2329  O   ARG A 239      -8.425 -49.639 -11.538  1.00159.98           O  
ANISOU 2329  O   ARG A 239    23749  21081  15956    530   2550   1213       O  
ATOM   2330  CB  ARG A 239      -7.531 -51.514 -13.707  1.00155.96           C  
ANISOU 2330  CB  ARG A 239    23359  19996  15904    182   2405   1281       C  
ATOM   2331  CG  ARG A 239      -7.534 -53.008 -14.105  1.00169.31           C  
ANISOU 2331  CG  ARG A 239    25146  21483  17701    -54   2398   1444       C  
ATOM   2332  CD  ARG A 239      -6.207 -53.562 -14.617  1.00178.21           C  
ANISOU 2332  CD  ARG A 239    26452  22281  18980    -17   2261   1410       C  
ATOM   2333  NE  ARG A 239      -6.403 -54.844 -15.304  1.00187.91           N  
ANISOU 2333  NE  ARG A 239    27764  23304  20328   -237   2255   1523       N  
ATOM   2334  CZ  ARG A 239      -5.446 -55.730 -15.570  1.00198.04           C  
ANISOU 2334  CZ  ARG A 239    29240  24303  21705   -236   2160   1561       C  
ATOM   2335  NH1 ARG A 239      -4.195 -55.494 -15.196  1.00184.32           N1+
ANISOU 2335  NH1 ARG A 239    27604  22474  19954    -31   2065   1504       N1+
ATOM   2336  NH2 ARG A 239      -5.730 -56.859 -16.202  1.00180.57           N  
ANISOU 2336  NH2 ARG A 239    27123  21898  19586   -436   2155   1656       N  
ATOM   2337  N   LEU A 240      -9.683 -48.620 -13.130  1.00156.43           N  
ANISOU 2337  N   LEU A 240    23029  20762  15647    517   2604   1042       N  
ATOM   2338  CA  LEU A 240      -9.953 -47.380 -12.402  1.00157.37           C  
ANISOU 2338  CA  LEU A 240    23116  21099  15578    763   2638    927       C  
ATOM   2339  C   LEU A 240     -11.398 -47.439 -11.911  1.00165.86           C  
ANISOU 2339  C   LEU A 240    24011  22536  16472    733   2810   1042       C  
ATOM   2340  O   LEU A 240     -11.738 -46.817 -10.905  1.00166.83           O  
ANISOU 2340  O   LEU A 240    24131  22887  16370    912   2873   1030       O  
ATOM   2341  CB  LEU A 240      -9.738 -46.134 -13.261  1.00155.42           C  
ANISOU 2341  CB  LEU A 240    22843  20784  15425    914   2561    705       C  
ATOM   2342  CG  LEU A 240      -9.826 -44.815 -12.508  1.00159.46           C  
ANISOU 2342  CG  LEU A 240    23498  21266  15822   1162   2473    548       C  
ATOM   2343  CD1 LEU A 240      -8.666 -43.914 -12.853  1.00157.28           C  
ANISOU 2343  CD1 LEU A 240    23353  20684  15722   1162   2303    438       C  
ATOM   2344  CD2 LEU A 240     -11.132 -44.114 -12.794  1.00162.22           C  
ANISOU 2344  CD2 LEU A 240    23768  21811  16056   1364   2520    408       C  
ATOM   2345  N   ARG A 241     -12.234 -48.233 -12.621  1.00164.87           N  
ANISOU 2345  N   ARG A 241    23735  22470  16436    497   2881   1160       N  
ATOM   2346  CA  ARG A 241     -13.630 -48.539 -12.298  1.00168.04           C  
ANISOU 2346  CA  ARG A 241    23933  23227  16688    392   3042   1312       C  
ATOM   2347  C   ARG A 241     -13.628 -49.460 -11.073  1.00177.57           C  
ANISOU 2347  C   ARG A 241    25218  24514  17736    285   3104   1523       C  
ATOM   2348  O   ARG A 241     -14.581 -49.444 -10.296  1.00179.86           O  
ANISOU 2348  O   ARG A 241    25371  25155  17814    291   3241   1635       O  
ATOM   2349  CB  ARG A 241     -14.340 -49.216 -13.480  1.00166.93           C  
ANISOU 2349  CB  ARG A 241    23642  23070  16714    124   3064   1379       C  
ATOM   2350  CG  ARG A 241     -15.859 -49.276 -13.375  1.00176.83           C  
ANISOU 2350  CG  ARG A 241    24626  24737  17824     29   3221   1499       C  
ATOM   2351  CD  ARG A 241     -16.493 -49.348 -14.754  1.00185.62           C  
ANISOU 2351  CD  ARG A 241    25571  25851  19106   -127   3213   1464       C  
ATOM   2352  NE  ARG A 241     -16.350 -48.085 -15.486  1.00189.33           N  
ANISOU 2352  NE  ARG A 241    26001  26293  19643    126   3159   1232       N  
ATOM   2353  CZ  ARG A 241     -16.537 -47.937 -16.794  1.00195.86           C  
ANISOU 2353  CZ  ARG A 241    26740  27030  20648     55   3110   1145       C  
ATOM   2354  NH1 ARG A 241     -16.872 -48.978 -17.546  1.00181.59           N1+
ANISOU 2354  NH1 ARG A 241    24877  25147  18973   -262   3103   1259       N1+
ATOM   2355  NH2 ARG A 241     -16.385 -46.750 -17.361  1.00178.36           N  
ANISOU 2355  NH2 ARG A 241    24508  24789  18472    297   3060    943       N  
ATOM   2356  N   SER A 242     -12.552 -50.262 -10.913  1.00175.56           N  
ANISOU 2356  N   SER A 242    25182  23947  17577    197   3004   1581       N  
ATOM   2357  CA  SER A 242     -12.345 -51.171  -9.785  1.00178.29           C  
ANISOU 2357  CA  SER A 242    25650  24303  17789    105   3036   1779       C  
ATOM   2358  C   SER A 242     -12.009 -50.375  -8.511  1.00186.12           C  
ANISOU 2358  C   SER A 242    26712  25454  18552    377   3051   1723       C  
ATOM   2359  O   SER A 242     -12.462 -50.744  -7.427  1.00188.23           O  
ANISOU 2359  O   SER A 242    26965  25943  18609    350   3149   1883       O  
ATOM   2360  CB  SER A 242     -11.239 -52.170 -10.103  1.00180.41           C  
ANISOU 2360  CB  SER A 242    26140  24175  18233    -23   2910   1832       C  
ATOM   2361  OG  SER A 242     -10.001 -51.516 -10.328  1.00185.79           O  
ANISOU 2361  OG  SER A 242    26955  24627  19009    183   2772   1646       O  
ATOM   2362  N   VAL A 243     -11.222 -49.282  -8.651  1.00183.04           N  
ANISOU 2362  N   VAL A 243    26402  24951  18192    626   2949   1500       N  
ATOM   2363  CA  VAL A 243     -10.836 -48.363  -7.563  1.00184.35           C  
ANISOU 2363  CA  VAL A 243    26660  25235  18149    897   2936   1403       C  
ATOM   2364  C   VAL A 243     -12.099 -47.557  -7.146  1.00192.55           C  
ANISOU 2364  C   VAL A 243    27513  26676  18971   1041   3084   1376       C  
ATOM   2365  O   VAL A 243     -12.340 -47.333  -5.953  1.00193.80           O  
ANISOU 2365  O   VAL A 243    27691  27067  18877   1174   3158   1423       O  
ATOM   2366  CB  VAL A 243      -9.650 -47.440  -7.998  1.00185.59           C  
ANISOU 2366  CB  VAL A 243    26960  25136  18420   1076   2767   1173       C  
ATOM   2367  CG1 VAL A 243      -9.277 -46.436  -6.908  1.00186.06           C  
ANISOU 2367  CG1 VAL A 243    27133  25307  18255   1341   2739   1060       C  
ATOM   2368  CG2 VAL A 243      -8.426 -48.258  -8.408  1.00183.82           C  
ANISOU 2368  CG2 VAL A 243    26889  24564  18390    953   2632   1210       C  
ATOM   2369  N   ARG A 244     -12.906 -47.166  -8.157  1.00190.58           N  
ANISOU 2369  N   ARG A 244    27080  26515  18817   1020   3128   1306       N  
ATOM   2370  CA  ARG A 244     -14.163 -46.421  -8.053  1.00192.81           C  
ANISOU 2370  CA  ARG A 244    27152  27178  18929   1159   3264   1274       C  
ATOM   2371  C   ARG A 244     -15.232 -47.244  -7.314  1.00201.57           C  
ANISOU 2371  C   ARG A 244    28095  28639  19853   1004   3435   1518       C  
ATOM   2372  O   ARG A 244     -15.889 -46.709  -6.417  1.00202.97           O  
ANISOU 2372  O   ARG A 244    28191  29162  19767   1192   3548   1528       O  
ATOM   2373  CB  ARG A 244     -14.648 -46.054  -9.470  1.00191.97           C  
ANISOU 2373  CB  ARG A 244    26893  27033  19012   1117   3249   1170       C  
ATOM   2374  CG  ARG A 244     -15.725 -44.977  -9.540  1.00204.23           C  
ANISOU 2374  CG  ARG A 244    28262  28924  20413   1347   3349   1069       C  
ATOM   2375  CD  ARG A 244     -16.269 -44.839 -10.953  1.00211.91           C  
ANISOU 2375  CD  ARG A 244    29066  29875  21576   1256   3340   1011       C  
ATOM   2376  NE  ARG A 244     -17.248 -45.882 -11.270  1.00219.11           N  
ANISOU 2376  NE  ARG A 244    29752  30987  22512    960   3448   1221       N  
ATOM   2377  CZ  ARG A 244     -17.656 -46.184 -12.497  1.00229.08           C  
ANISOU 2377  CZ  ARG A 244    30878  32199  23965    773   3432   1227       C  
ATOM   2378  NH1 ARG A 244     -17.166 -45.534 -13.546  1.00214.55           N  
ANISOU 2378  NH1 ARG A 244    29095  30112  22310    860   3318   1039       N  
ATOM   2379  NH2 ARG A 244     -18.551 -47.144 -12.688  1.00214.86           N1+
ANISOU 2379  NH2 ARG A 244    28884  30593  22162    483   3523   1426       N1+
ATOM   2380  N   LEU A 245     -15.387 -48.544  -7.690  1.00200.34           N  
ANISOU 2380  N   LEU A 245    27902  28391  19826    660   3449   1717       N  
ATOM   2381  CA  LEU A 245     -16.345 -49.503  -7.114  1.00203.95           C  
ANISOU 2381  CA  LEU A 245    28216  29138  20138    428   3592   1982       C  
ATOM   2382  C   LEU A 245     -16.086 -49.720  -5.616  1.00212.59           C  
ANISOU 2382  C   LEU A 245    29428  30357  20988    509   3640   2098       C  
ATOM   2383  O   LEU A 245     -17.034 -49.952  -4.861  1.00215.11           O  
ANISOU 2383  O   LEU A 245    29591  31061  21081    462   3790   2263       O  
ATOM   2384  CB  LEU A 245     -16.289 -50.851  -7.862  1.00203.59           C  
ANISOU 2384  CB  LEU A 245    28198  28853  20305     38   3549   2147       C  
ATOM   2385  CG  LEU A 245     -17.604 -51.631  -7.979  1.00210.55           C  
ANISOU 2385  CG  LEU A 245    28842  30039  21117   -263   3682   2372       C  
ATOM   2386  CD1 LEU A 245     -18.336 -51.285  -9.266  1.00209.68           C  
ANISOU 2386  CD1 LEU A 245    28515  30005  21147   -327   3690   2282       C  
ATOM   2387  CD2 LEU A 245     -17.354 -53.126  -7.945  1.00213.66           C  
ANISOU 2387  CD2 LEU A 245    29382  30201  21598   -627   3646   2599       C  
ATOM   2388  N   LEU A 246     -14.806 -49.626  -5.194  1.00209.82           N  
ANISOU 2388  N   LEU A 246    29342  29706  20674    631   3511   2014       N  
ATOM   2389  CA  LEU A 246     -14.373 -49.751  -3.800  1.00212.23           C  
ANISOU 2389  CA  LEU A 246    29793  30088  20758    735   3528   2096       C  
ATOM   2390  C   LEU A 246     -14.830 -48.536  -2.986  1.00220.48           C  
ANISOU 2390  C   LEU A 246    30773  31472  21530   1070   3610   1969       C  
ATOM   2391  O   LEU A 246     -15.151 -48.680  -1.803  1.00222.59           O  
ANISOU 2391  O   LEU A 246    31034  32006  21536   1125   3708   2093       O  
ATOM   2392  CB  LEU A 246     -12.839 -49.898  -3.713  1.00210.17           C  
ANISOU 2392  CB  LEU A 246    29816  29414  20624    786   3349   2018       C  
ATOM   2393  CG  LEU A 246     -12.251 -51.269  -4.051  1.00214.20           C  
ANISOU 2393  CG  LEU A 246    30458  29609  21319    502   3276   2187       C  
ATOM   2394  CD1 LEU A 246     -10.804 -51.143  -4.491  1.00211.71           C  
ANISOU 2394  CD1 LEU A 246    30352  28892  21194    590   3088   2040       C  
ATOM   2395  CD2 LEU A 246     -12.366 -52.229  -2.873  1.00218.93           C  
ANISOU 2395  CD2 LEU A 246    31132  30322  21730    378   3346   2443       C  
ATOM   2396  N   SER A 247     -14.895 -47.348  -3.647  1.00217.40           N  
ANISOU 2396  N   SER A 247    30339  31072  21193   1296   3570   1726       N  
ATOM   2397  CA  SER A 247     -15.286 -46.031  -3.112  1.00218.78           C  
ANISOU 2397  CA  SER A 247    30487  31504  21137   1655   3621   1553       C  
ATOM   2398  C   SER A 247     -14.374 -45.635  -1.928  1.00224.41           C  
ANISOU 2398  C   SER A 247    31447  32146  21671   1862   3550   1484       C  
ATOM   2399  O   SER A 247     -14.844 -45.414  -0.805  1.00227.01           O  
ANISOU 2399  O   SER A 247    31756  32791  21704   2017   3657   1534       O  
ATOM   2400  CB  SER A 247     -16.772 -45.987  -2.736  1.00224.85           C  
ANISOU 2400  CB  SER A 247    30977  32783  21673   1688   3828   1673       C  
ATOM   2401  OG  SER A 247     -17.090 -46.765  -1.593  1.00235.67           O  
ANISOU 2401  OG  SER A 247    32319  34399  22824   1585   3940   1903       O  
ATOM   2402  N   GLY A 248     -13.073 -45.558  -2.215  1.00218.68           N  
ANISOU 2402  N   GLY A 248    30946  31021  21123   1857   3366   1371       N  
ATOM   2403  CA  GLY A 248     -12.040 -45.221  -1.242  1.00218.61           C  
ANISOU 2403  CA  GLY A 248    31182  30896  20985   2015   3262   1299       C  
ATOM   2404  C   GLY A 248     -11.580 -43.779  -1.295  1.00221.83           C  
ANISOU 2404  C   GLY A 248    31729  31214  21344   2309   3153   1015       C  
ATOM   2405  O   GLY A 248     -12.118 -42.931  -0.576  1.00223.48           O  
ANISOU 2405  O   GLY A 248    31944  31678  21292   2566   3223    926       O  
ATOM   2406  N   SER A 249     -10.566 -43.497  -2.140  1.00215.38           N  
ANISOU 2406  N   SER A 249    31035  30034  20766   2272   2976    875       N  
ATOM   2407  CA  SER A 249      -9.989 -42.160  -2.292  1.00213.89           C  
ANISOU 2407  CA  SER A 249    31008  29701  20559   2500   2841    613       C  
ATOM   2408  C   SER A 249     -10.662 -41.388  -3.424  1.00216.72           C  
ANISOU 2408  C   SER A 249    31247  30063  21032   2572   2860    472       C  
ATOM   2409  O   SER A 249     -10.741 -41.876  -4.556  1.00214.33           O  
ANISOU 2409  O   SER A 249    30823  29629  20984   2380   2852    514       O  
ATOM   2410  CB  SER A 249      -8.483 -42.241  -2.528  1.00214.64           C  
ANISOU 2410  CB  SER A 249    31295  29434  20825   2414   2635    550       C  
ATOM   2411  OG  SER A 249      -7.872 -40.970  -2.377  1.00221.77           O  
ANISOU 2411  OG  SER A 249    32387  30227  21649   2619   2498    320       O  
ATOM   2412  N   LYS A 250     -11.161 -40.185  -3.100  1.00214.14           N  
ANISOU 2412  N   LYS A 250    30969  29890  20505   2862   2885    304       N  
ATOM   2413  CA  LYS A 250     -11.819 -39.293  -4.050  1.00213.09           C  
ANISOU 2413  CA  LYS A 250    30753  29776  20434   2992   2899    155       C  
ATOM   2414  C   LYS A 250     -10.777 -38.493  -4.837  1.00214.29           C  
ANISOU 2414  C   LYS A 250    31098  29553  20769   3009   2691    -46       C  
ATOM   2415  O   LYS A 250     -10.960 -38.276  -6.036  1.00211.78           O  
ANISOU 2415  O   LYS A 250    30691  29122  20654   2952   2665   -105       O  
ATOM   2416  CB  LYS A 250     -12.790 -38.349  -3.322  1.00217.88           C  
ANISOU 2416  CB  LYS A 250    31354  30707  20725   3327   3012     62       C  
ATOM   2417  N   GLU A 251      -9.678 -38.074  -4.164  1.00211.01           N  
ANISOU 2417  N   GLU A 251    30939  28959  20276   3072   2541   -140       N  
ATOM   2418  CA  GLU A 251      -8.603 -37.269  -4.760  1.00208.92           C  
ANISOU 2418  CA  GLU A 251    30874  28360  20148   3074   2330   -322       C  
ATOM   2419  C   GLU A 251      -7.639 -38.074  -5.658  1.00209.59           C  
ANISOU 2419  C   GLU A 251    30918  28172  20544   2786   2223   -247       C  
ATOM   2420  O   GLU A 251      -7.265 -37.571  -6.719  1.00207.49           O  
ANISOU 2420  O   GLU A 251    30675  27697  20466   2743   2116   -359       O  
ATOM   2421  CB  GLU A 251      -7.798 -36.563  -3.660  1.00211.50           C  
ANISOU 2421  CB  GLU A 251    31481  28624  20255   3224   2204   -438       C  
ATOM   2422  N   LYS A 252      -7.238 -39.297  -5.225  1.00205.35           N  
ANISOU 2422  N   LYS A 252    30333  27643  20047   2606   2249    -58       N  
ATOM   2423  CA  LYS A 252      -6.307 -40.180  -5.946  1.00202.65           C  
ANISOU 2423  CA  LYS A 252    29965  27062  19969   2363   2156     28       C  
ATOM   2424  C   LYS A 252      -6.919 -40.766  -7.226  1.00203.83           C  
ANISOU 2424  C   LYS A 252    29907  27179  20359   2201   2231     95       C  
ATOM   2425  O   LYS A 252      -6.201 -40.904  -8.220  1.00200.92           O  
ANISOU 2425  O   LYS A 252    29541  26576  20225   2074   2123     61       O  
ATOM   2426  CB  LYS A 252      -5.818 -41.319  -5.040  1.00206.00           C  
ANISOU 2426  CB  LYS A 252    30418  27518  20335   2254   2172    215       C  
ATOM   2427  N   ASP A 253      -8.229 -41.118  -7.197  1.00201.02           N  
ANISOU 2427  N   ASP A 253    29368  27074  19936   2200   2413    194       N  
ATOM   2428  CA  ASP A 253      -8.966 -41.671  -8.346  1.00199.53           C  
ANISOU 2428  CA  ASP A 253    28970  26898  19943   2040   2494    264       C  
ATOM   2429  C   ASP A 253      -9.173 -40.611  -9.437  1.00200.74           C  
ANISOU 2429  C   ASP A 253    29099  26969  20204   2136   2440     79       C  
ATOM   2430  O   ASP A 253      -9.188 -40.958 -10.622  1.00198.66           O  
ANISOU 2430  O   ASP A 253    28732  26577  20171   1983   2420     89       O  
ATOM   2431  CB  ASP A 253     -10.331 -42.250  -7.911  1.00203.45           C  
ANISOU 2431  CB  ASP A 253    29269  27731  20300   2011   2699    425       C  
ATOM   2432  CG  ASP A 253     -11.107 -42.952  -9.022  1.00210.52           C  
ANISOU 2432  CG  ASP A 253    29946  28657  21384   1804   2778    522       C  
ATOM   2433  OD1 ASP A 253     -11.879 -42.266  -9.737  1.00209.81           O  
ANISOU 2433  OD1 ASP A 253    29731  28672  21315   1892   2820    428       O  
ATOM   2434  OD2 ASP A 253     -10.951 -44.184  -9.168  1.00215.84           O  
ANISOU 2434  OD2 ASP A 253    30585  29249  22174   1559   2793    692       O  
ATOM   2435  N   ARG A 254      -9.352 -39.329  -9.041  1.00196.82           N  
ANISOU 2435  N   ARG A 254    28711  26540  19531   2395   2415    -89       N  
ATOM   2436  CA  ARG A 254      -9.581 -38.252 -10.004  1.00194.80           C  
ANISOU 2436  CA  ARG A 254    28462  26202  19350   2510   2360   -264       C  
ATOM   2437  C   ARG A 254      -8.278 -37.870 -10.700  1.00194.12           C  
ANISOU 2437  C   ARG A 254    28535  25773  19451   2428   2159   -377       C  
ATOM   2438  O   ARG A 254      -8.322 -37.493 -11.871  1.00192.25           O  
ANISOU 2438  O   ARG A 254    28248  25413  19384   2392   2111   -454       O  
ATOM   2439  CB  ARG A 254     -10.236 -37.030  -9.343  1.00197.06           C  
ANISOU 2439  CB  ARG A 254    28839  26663  19370   2829   2397   -403       C  
ATOM   2440  N   SER A 255      -7.129 -37.995  -9.992  1.00188.58           N  
ANISOU 2440  N   SER A 255    28005  24936  18709   2392   2042   -375       N  
ATOM   2441  CA  SER A 255      -5.776 -37.694 -10.478  1.00185.58           C  
ANISOU 2441  CA  SER A 255    27767  24272  18474   2302   1845   -460       C  
ATOM   2442  C   SER A 255      -5.345 -38.678 -11.586  1.00184.62           C  
ANISOU 2442  C   SER A 255    27509  24002  18636   2063   1825   -363       C  
ATOM   2443  O   SER A 255      -4.690 -38.282 -12.564  1.00182.67           O  
ANISOU 2443  O   SER A 255    27288  23560  18557   1997   1705   -451       O  
ATOM   2444  CB  SER A 255      -4.783 -37.737  -9.317  1.00189.82           C  
ANISOU 2444  CB  SER A 255    28484  24772  18867   2321   1748   -450       C  
ATOM   2445  OG  SER A 255      -3.434 -37.723  -9.762  1.00197.13           O  
ANISOU 2445  OG  SER A 255    29495  25466  19938   2193   1569   -484       O  
ATOM   2446  N   LEU A 256      -5.701 -39.961 -11.402  1.00178.75           N  
ANISOU 2446  N   LEU A 256    26636  23351  17931   1934   1940   -181       N  
ATOM   2447  CA  LEU A 256      -5.376 -41.025 -12.342  1.00175.61           C  
ANISOU 2447  CA  LEU A 256    26132  22818  17775   1719   1933    -79       C  
ATOM   2448  C   LEU A 256      -6.377 -41.042 -13.499  1.00175.57           C  
ANISOU 2448  C   LEU A 256    25949  22856  17905   1663   2020    -88       C  
ATOM   2449  O   LEU A 256      -6.041 -41.540 -14.570  1.00173.63           O  
ANISOU 2449  O   LEU A 256    25640  22456  17875   1514   1978    -71       O  
ATOM   2450  CB  LEU A 256      -5.311 -42.392 -11.642  1.00176.62           C  
ANISOU 2450  CB  LEU A 256    26236  22993  17876   1600   2003    122       C  
ATOM   2451  CG  LEU A 256      -4.211 -42.562 -10.575  1.00182.04           C  
ANISOU 2451  CG  LEU A 256    27089  23628  18452   1636   1908    154       C  
ATOM   2452  CD1 LEU A 256      -4.589 -43.629  -9.565  1.00184.08           C  
ANISOU 2452  CD1 LEU A 256    27334  24023  18586   1587   2020    347       C  
ATOM   2453  CD2 LEU A 256      -2.833 -42.854 -11.204  1.00182.91           C  
ANISOU 2453  CD2 LEU A 256    27258  23497  18742   1542   1750    137       C  
ATOM   2454  N   ARG A 257      -7.583 -40.462 -13.308  1.00171.01           N  
ANISOU 2454  N   ARG A 257    25289  22497  17190   1795   2134   -121       N  
ATOM   2455  CA  ARG A 257      -8.620 -40.361 -14.344  1.00169.46           C  
ANISOU 2455  CA  ARG A 257    24910  22387  17090   1768   2217   -134       C  
ATOM   2456  C   ARG A 257      -8.220 -39.350 -15.422  1.00169.37           C  
ANISOU 2456  C   ARG A 257    24951  22196  17207   1822   2096   -306       C  
ATOM   2457  O   ARG A 257      -8.714 -39.419 -16.545  1.00167.57           O  
ANISOU 2457  O   ARG A 257    24587  21955  17126   1748   2121   -315       O  
ATOM   2458  CB  ARG A 257      -9.966 -39.970 -13.737  1.00172.46           C  
ANISOU 2458  CB  ARG A 257    25184  23087  17256   1928   2370   -119       C  
ATOM   2459  CG  ARG A 257     -11.149 -40.590 -14.462  1.00185.91           C  
ANISOU 2459  CG  ARG A 257    26635  24967  19034   1804   2503    -15       C  
ATOM   2460  CD  ARG A 257     -12.279 -40.853 -13.489  1.00204.80           C  
ANISOU 2460  CD  ARG A 257    28899  27716  21199   1869   2674    103       C  
ATOM   2461  NE  ARG A 257     -13.332 -41.689 -14.069  1.00217.06           N  
ANISOU 2461  NE  ARG A 257    30203  29452  22819   1682   2797    246       N  
ATOM   2462  CZ  ARG A 257     -14.300 -42.269 -13.365  1.00233.46           C  
ANISOU 2462  CZ  ARG A 257    32126  31844  24735   1635   2951    405       C  
ATOM   2463  NH1 ARG A 257     -14.354 -42.123 -12.047  1.00220.04           N1+
ANISOU 2463  NH1 ARG A 257    30494  30313  22796   1778   3009    441       N1+
ATOM   2464  NH2 ARG A 257     -15.216 -43.010 -13.975  1.00221.72           N  
ANISOU 2464  NH2 ARG A 257    30414  30514  23317   1432   3043    534       N  
ATOM   2465  N   ARG A 258      -7.323 -38.413 -15.065  1.00164.75           N  
ANISOU 2465  N   ARG A 258    24569  21474  16555   1940   1959   -437       N  
ATOM   2466  CA  ARG A 258      -6.754 -37.377 -15.927  1.00162.68           C  
ANISOU 2466  CA  ARG A 258    24405  21018  16387   1980   1819   -596       C  
ATOM   2467  C   ARG A 258      -5.797 -38.020 -16.943  1.00161.11           C  
ANISOU 2467  C   ARG A 258    24169  20607  16438   1766   1725   -561       C  
ATOM   2468  O   ARG A 258      -5.817 -37.658 -18.121  1.00159.22           O  
ANISOU 2468  O   ARG A 258    23879  20271  16347   1725   1681   -628       O  
ATOM   2469  CB  ARG A 258      -6.018 -36.333 -15.051  1.00165.78           C  
ANISOU 2469  CB  ARG A 258    25046  21336  16609   2129   1694   -719       C  
ATOM   2470  CG  ARG A 258      -5.475 -35.113 -15.804  1.00180.03           C  
ANISOU 2470  CG  ARG A 258    26991  22943  18469   2173   1538   -884       C  
ATOM   2471  CD  ARG A 258      -4.092 -34.707 -15.318  1.00191.75           C  
ANISOU 2471  CD  ARG A 258    28684  24257  19915   2131   1358   -941       C  
ATOM   2472  NE  ARG A 258      -3.040 -35.576 -15.855  1.00199.28           N  
ANISOU 2472  NE  ARG A 258    29566  25089  21063   1912   1286   -855       N  
ATOM   2473  CZ  ARG A 258      -1.760 -35.517 -15.500  1.00213.21           C  
ANISOU 2473  CZ  ARG A 258    31448  26742  22818   1836   1138   -863       C  
ATOM   2474  NH1 ARG A 258      -1.352 -34.632 -14.600  1.00203.94           N  
ANISOU 2474  NH1 ARG A 258    30485  25548  21456   1934   1037   -954       N  
ATOM   2475  NH2 ARG A 258      -0.878 -36.347 -16.041  1.00197.05           N1+
ANISOU 2475  NH2 ARG A 258    29313  24614  20942   1667   1088   -780       N1+
ATOM   2476  N   ILE A 259      -4.967 -38.975 -16.471  1.00154.88           N  
ANISOU 2476  N   ILE A 259    23408  19759  15682   1648   1695   -456       N  
ATOM   2477  CA  ILE A 259      -3.977 -39.720 -17.258  1.00151.79           C  
ANISOU 2477  CA  ILE A 259    22991  19187  15495   1475   1612   -409       C  
ATOM   2478  C   ILE A 259      -4.698 -40.668 -18.244  1.00151.92           C  
ANISOU 2478  C   ILE A 259    22827  19218  15679   1336   1713   -321       C  
ATOM   2479  O   ILE A 259      -4.235 -40.855 -19.371  1.00150.36           O  
ANISOU 2479  O   ILE A 259    22586  18880  15666   1234   1652   -345       O  
ATOM   2480  CB  ILE A 259      -3.004 -40.478 -16.316  1.00155.45           C  
ANISOU 2480  CB  ILE A 259    23543  19614  15905   1433   1564   -313       C  
ATOM   2481  CG1 ILE A 259      -2.365 -39.512 -15.282  1.00157.18           C  
ANISOU 2481  CG1 ILE A 259    23943  19841  15936   1563   1460   -402       C  
ATOM   2482  CG2 ILE A 259      -1.918 -41.217 -17.110  1.00154.45           C  
ANISOU 2482  CG2 ILE A 259    23396  19316  15971   1293   1473   -270       C  
ATOM   2483  CD1 ILE A 259      -2.073 -40.102 -13.894  1.00167.43           C  
ANISOU 2483  CD1 ILE A 259    25318  21226  17071   1594   1481   -301       C  
ATOM   2484  N   THR A 260      -5.834 -41.241 -17.824  1.00147.42           N  
ANISOU 2484  N   THR A 260    22152  18829  15031   1325   1864   -221       N  
ATOM   2485  CA  THR A 260      -6.654 -42.131 -18.652  1.00146.21           C  
ANISOU 2485  CA  THR A 260    21832  18716  15006   1174   1962   -130       C  
ATOM   2486  C   THR A 260      -7.399 -41.293 -19.724  1.00148.72           C  
ANISOU 2486  C   THR A 260    22043  19075  15389   1220   1975   -239       C  
ATOM   2487  O   THR A 260      -7.635 -41.804 -20.817  1.00147.43           O  
ANISOU 2487  O   THR A 260    21772  18857  15390   1084   1986   -216       O  
ATOM   2488  CB  THR A 260      -7.587 -42.978 -17.773  1.00152.10           C  
ANISOU 2488  CB  THR A 260    22502  19663  15627   1126   2109     27       C  
ATOM   2489  OG1 THR A 260      -6.805 -43.583 -16.739  1.00151.08           O  
ANISOU 2489  OG1 THR A 260    22500  19483  15421   1114   2080    114       O  
ATOM   2490  CG2 THR A 260      -8.344 -44.051 -18.551  1.00148.88           C  
ANISOU 2490  CG2 THR A 260    21943  19280  15344    921   2194    143       C  
ATOM   2491  N   ARG A 261      -7.734 -40.009 -19.441  1.00144.93           N  
ANISOU 2491  N   ARG A 261    21611  18678  14776   1419   1963   -361       N  
ATOM   2492  CA  ARG A 261      -8.373 -39.182 -20.463  1.00143.65           C  
ANISOU 2492  CA  ARG A 261    21369  18539  14670   1483   1962   -463       C  
ATOM   2493  C   ARG A 261      -7.322 -38.703 -21.469  1.00144.51           C  
ANISOU 2493  C   ARG A 261    21563  18401  14943   1435   1809   -566       C  
ATOM   2494  O   ARG A 261      -7.656 -38.519 -22.634  1.00143.12           O  
ANISOU 2494  O   ARG A 261    21293  18194  14892   1393   1803   -607       O  
ATOM   2495  CB  ARG A 261      -9.178 -38.013 -19.894  1.00145.94           C  
ANISOU 2495  CB  ARG A 261    21692  19000  14759   1730   2007   -554       C  
ATOM   2496  CG  ARG A 261     -10.415 -37.779 -20.768  1.00161.24           C  
ANISOU 2496  CG  ARG A 261    23440  21096  16726   1764   2095   -566       C  
ATOM   2497  CD  ARG A 261     -10.997 -36.376 -20.730  1.00179.93           C  
ANISOU 2497  CD  ARG A 261    25866  23547  18952   2033   2089   -702       C  
ATOM   2498  NE  ARG A 261     -11.882 -36.133 -21.878  1.00192.98           N  
ANISOU 2498  NE  ARG A 261    27350  25285  20687   2043   2130   -725       N  
ATOM   2499  CZ  ARG A 261     -13.198 -36.339 -21.888  1.00210.45           C  
ANISOU 2499  CZ  ARG A 261    29350  27793  22819   2093   2272   -659       C  
ATOM   2500  NH1 ARG A 261     -13.815 -36.792 -20.802  1.00201.85           N1+
ANISOU 2500  NH1 ARG A 261    28185  26950  21558   2134   2397   -560       N1+
ATOM   2501  NH2 ARG A 261     -13.908 -36.092 -22.981  1.00195.63           N  
ANISOU 2501  NH2 ARG A 261    27323  25985  21022   2098   2290   -683       N  
ATOM   2502  N   MET A 262      -6.047 -38.567 -21.053  1.00140.20           N  
ANISOU 2502  N   MET A 262    21177  17698  14394   1426   1687   -595       N  
ATOM   2503  CA  MET A 262      -4.989 -38.141 -21.973  1.00138.36           C  
ANISOU 2503  CA  MET A 262    21008  17261  14303   1364   1541   -675       C  
ATOM   2504  C   MET A 262      -4.537 -39.276 -22.908  1.00137.88           C  
ANISOU 2504  C   MET A 262    20843  17099  14444   1174   1536   -596       C  
ATOM   2505  O   MET A 262      -4.100 -38.967 -24.021  1.00136.78           O  
ANISOU 2505  O   MET A 262    20685  16846  14441   1120   1458   -658       O  
ATOM   2506  CB  MET A 262      -3.791 -37.525 -21.247  1.00141.52           C  
ANISOU 2506  CB  MET A 262    21599  17556  14617   1410   1402   -733       C  
ATOM   2507  CG  MET A 262      -3.502 -36.085 -21.693  1.00146.01           C  
ANISOU 2507  CG  MET A 262    22291  18025  15162   1490   1280   -881       C  
ATOM   2508  SD  MET A 262      -4.735 -34.819 -21.197  1.00152.69           S  
ANISOU 2508  SD  MET A 262    23222  18987  15806   1736   1336   -989       S  
ATOM   2509  CE  MET A 262      -4.398 -34.700 -19.391  1.00151.06           C  
ANISOU 2509  CE  MET A 262    23192  18850  15355   1851   1324   -983       C  
ATOM   2510  N   VAL A 263      -4.674 -40.573 -22.503  1.00131.35           N  
ANISOU 2510  N   VAL A 263    19961  16312  13634   1077   1617   -461       N  
ATOM   2511  CA  VAL A 263      -4.331 -41.680 -23.414  1.00128.67           C  
ANISOU 2511  CA  VAL A 263    19550  15863  13475    915   1613   -394       C  
ATOM   2512  C   VAL A 263      -5.417 -41.724 -24.546  1.00129.13           C  
ANISOU 2512  C   VAL A 263    19456  15976  13631    851   1686   -409       C  
ATOM   2513  O   VAL A 263      -5.091 -42.065 -25.688  1.00127.18           O  
ANISOU 2513  O   VAL A 263    19163  15616  13543    753   1644   -426       O  
ATOM   2514  CB  VAL A 263      -4.086 -43.043 -22.700  1.00132.75           C  
ANISOU 2514  CB  VAL A 263    20095  16365  13979    830   1659   -248       C  
ATOM   2515  CG1 VAL A 263      -5.341 -43.560 -22.032  1.00134.12           C  
ANISOU 2515  CG1 VAL A 263    20198  16713  14050    805   1804   -146       C  
ATOM   2516  CG2 VAL A 263      -3.487 -44.099 -23.637  1.00131.39           C  
ANISOU 2516  CG2 VAL A 263    19904  16036  13982    696   1624   -200       C  
ATOM   2517  N   LEU A 264      -6.665 -41.284 -24.244  1.00124.32           N  
ANISOU 2517  N   LEU A 264    18766  15554  12914    925   1786   -412       N  
ATOM   2518  CA  LEU A 264      -7.722 -41.185 -25.251  1.00122.75           C  
ANISOU 2518  CA  LEU A 264    18412  15444  12784    886   1847   -430       C  
ATOM   2519  C   LEU A 264      -7.399 -40.024 -26.190  1.00124.95           C  
ANISOU 2519  C   LEU A 264    18717  15632  13125    966   1750   -571       C  
ATOM   2520  O   LEU A 264      -7.565 -40.162 -27.400  1.00124.76           O  
ANISOU 2520  O   LEU A 264    18603  15561  13238    879   1737   -592       O  
ATOM   2521  CB  LEU A 264      -9.121 -41.021 -24.634  1.00124.00           C  
ANISOU 2521  CB  LEU A 264    18457  15866  12789    961   1982   -386       C  
ATOM   2522  CG  LEU A 264     -10.322 -41.107 -25.600  1.00127.89           C  
ANISOU 2522  CG  LEU A 264    18753  16502  13339    898   2057   -374       C  
ATOM   2523  CD1 LEU A 264     -10.450 -42.485 -26.229  1.00127.72           C  
ANISOU 2523  CD1 LEU A 264    18648  16428  13454    648   2087   -265       C  
ATOM   2524  CD2 LEU A 264     -11.610 -40.756 -24.912  1.00130.89           C  
ANISOU 2524  CD2 LEU A 264    19014  17180  13538   1015   2182   -338       C  
ATOM   2525  N   VAL A 265      -6.890 -38.902 -25.643  1.00119.45           N  
ANISOU 2525  N   VAL A 265    18162  14898  12326   1120   1672   -664       N  
ATOM   2526  CA  VAL A 265      -6.464 -37.744 -26.440  1.00117.64           C  
ANISOU 2526  CA  VAL A 265    18001  14556  12142   1183   1561   -790       C  
ATOM   2527  C   VAL A 265      -5.413 -38.220 -27.453  1.00117.18           C  
ANISOU 2527  C   VAL A 265    17935  14323  12266   1029   1470   -788       C  
ATOM   2528  O   VAL A 265      -5.602 -38.023 -28.649  1.00115.72           O  
ANISOU 2528  O   VAL A 265    17674  14102  12193    984   1451   -828       O  
ATOM   2529  CB  VAL A 265      -5.934 -36.583 -25.549  1.00122.70           C  
ANISOU 2529  CB  VAL A 265    18839  15153  12630   1339   1473   -878       C  
ATOM   2530  CG1 VAL A 265      -5.199 -35.521 -26.363  1.00121.64           C  
ANISOU 2530  CG1 VAL A 265    18808  14854  12554   1347   1329   -988       C  
ATOM   2531  CG2 VAL A 265      -7.063 -35.952 -24.749  1.00124.46           C  
ANISOU 2531  CG2 VAL A 265    19072  15554  12664   1534   1563   -906       C  
ATOM   2532  N   VAL A 266      -4.363 -38.911 -26.965  1.00111.52           N  
ANISOU 2532  N   VAL A 266    17283  13519  11568    959   1423   -733       N  
ATOM   2533  CA  VAL A 266      -3.239 -39.453 -27.731  1.00109.23           C  
ANISOU 2533  CA  VAL A 266    16992  13090  11422    842   1339   -720       C  
ATOM   2534  C   VAL A 266      -3.708 -40.348 -28.909  1.00109.87           C  
ANISOU 2534  C   VAL A 266    16936  13155  11656    721   1396   -683       C  
ATOM   2535  O   VAL A 266      -3.224 -40.149 -30.029  1.00107.68           O  
ANISOU 2535  O   VAL A 266    16629  12794  11491    672   1329   -733       O  
ATOM   2536  CB  VAL A 266      -2.280 -40.212 -26.775  1.00113.79           C  
ANISOU 2536  CB  VAL A 266    17648  13628  11958    822   1310   -643       C  
ATOM   2537  CG1 VAL A 266      -1.383 -41.211 -27.525  1.00113.23           C  
ANISOU 2537  CG1 VAL A 266    17542  13451  12029    715   1270   -596       C  
ATOM   2538  CG2 VAL A 266      -1.443 -39.236 -25.958  1.00113.63           C  
ANISOU 2538  CG2 VAL A 266    17769  13588  11819    905   1202   -700       C  
ATOM   2539  N   VAL A 267      -4.644 -41.301 -28.658  1.00106.16           N  
ANISOU 2539  N   VAL A 267    16388  12771  11179    664   1514   -595       N  
ATOM   2540  CA  VAL A 267      -5.145 -42.244 -29.665  1.00105.36           C  
ANISOU 2540  CA  VAL A 267    16178  12651  11204    527   1564   -553       C  
ATOM   2541  C   VAL A 267      -6.085 -41.546 -30.699  1.00107.36           C  
ANISOU 2541  C   VAL A 267    16314  12980  11498    534   1586   -623       C  
ATOM   2542  O   VAL A 267      -6.027 -41.879 -31.886  1.00105.54           O  
ANISOU 2542  O   VAL A 267    16023  12684  11395    442   1563   -643       O  
ATOM   2543  CB  VAL A 267      -5.791 -43.501 -29.009  1.00110.74           C  
ANISOU 2543  CB  VAL A 267    16836  13389  11852    432   1667   -424       C  
ATOM   2544  CG1 VAL A 267      -7.178 -43.217 -28.451  1.00111.94           C  
ANISOU 2544  CG1 VAL A 267    16892  13753  11886    463   1778   -391       C  
ATOM   2545  CG2 VAL A 267      -5.817 -44.695 -29.957  1.00110.37           C  
ANISOU 2545  CG2 VAL A 267    16753  13241  11942    269   1676   -376       C  
ATOM   2546  N   VAL A 268      -6.920 -40.584 -30.261  1.00103.70           N  
ANISOU 2546  N   VAL A 268    15826  12657  10919    659   1626   -662       N  
ATOM   2547  CA  VAL A 268      -7.808 -39.857 -31.174  1.00103.01           C  
ANISOU 2547  CA  VAL A 268    15634  12655  10852    699   1642   -725       C  
ATOM   2548  C   VAL A 268      -6.945 -38.948 -32.082  1.00105.69           C  
ANISOU 2548  C   VAL A 268    16041  12850  11267    733   1518   -828       C  
ATOM   2549  O   VAL A 268      -7.182 -38.917 -33.289  1.00104.55           O  
ANISOU 2549  O   VAL A 268    15811  12689  11223    674   1504   -858       O  
ATOM   2550  CB  VAL A 268      -8.914 -39.081 -30.432  1.00107.63           C  
ANISOU 2550  CB  VAL A 268    16181  13439  11275    858   1719   -737       C  
ATOM   2551  CG1 VAL A 268      -9.726 -38.205 -31.388  1.00107.38           C  
ANISOU 2551  CG1 VAL A 268    16057  13489  11254    938   1719   -809       C  
ATOM   2552  CG2 VAL A 268      -9.826 -40.044 -29.685  1.00108.50           C  
ANISOU 2552  CG2 VAL A 268    16186  13726  11313    791   1848   -617       C  
ATOM   2553  N   ALA A 269      -5.917 -38.271 -31.499  1.00101.24           N  
ANISOU 2553  N   ALA A 269    15631  12187  10650    806   1425   -872       N  
ATOM   2554  CA  ALA A 269      -4.933 -37.443 -32.205  1.00 99.03           C  
ANISOU 2554  CA  ALA A 269    15430  11771  10424    807   1295   -950       C  
ATOM   2555  C   ALA A 269      -4.164 -38.296 -33.197  1.00102.05           C  
ANISOU 2555  C   ALA A 269    15754  12059  10960    662   1259   -924       C  
ATOM   2556  O   ALA A 269      -4.038 -37.903 -34.356  1.00100.94           O  
ANISOU 2556  O   ALA A 269    15574  11876  10903    628   1210   -972       O  
ATOM   2557  CB  ALA A 269      -3.972 -36.806 -31.225  1.00 99.85           C  
ANISOU 2557  CB  ALA A 269    15702  11808  10428    872   1206   -976       C  
ATOM   2558  N   PHE A 270      -3.710 -39.499 -32.756  1.00 97.84           N  
ANISOU 2558  N   PHE A 270    15220  11499  10455    589   1289   -845       N  
ATOM   2559  CA  PHE A 270      -2.982 -40.435 -33.596  1.00 96.02           C  
ANISOU 2559  CA  PHE A 270    14953  11179  10351    481   1262   -818       C  
ATOM   2560  C   PHE A 270      -3.813 -40.811 -34.827  1.00 97.53           C  
ANISOU 2560  C   PHE A 270    15025  11391  10642    402   1310   -830       C  
ATOM   2561  O   PHE A 270      -3.295 -40.719 -35.937  1.00 96.03           O  
ANISOU 2561  O   PHE A 270    14805  11139  10542    361   1252   -871       O  
ATOM   2562  CB  PHE A 270      -2.557 -41.686 -32.811  1.00 98.63           C  
ANISOU 2562  CB  PHE A 270    15327  11477  10673    443   1295   -726       C  
ATOM   2563  CG  PHE A 270      -1.641 -42.614 -33.588  1.00100.69           C  
ANISOU 2563  CG  PHE A 270    15582  11632  11042    376   1254   -707       C  
ATOM   2564  CD1 PHE A 270      -0.264 -42.433 -33.572  1.00102.94           C  
ANISOU 2564  CD1 PHE A 270    15916  11866  11329    409   1157   -718       C  
ATOM   2565  CD2 PHE A 270      -2.162 -43.670 -34.347  1.00104.68           C  
ANISOU 2565  CD2 PHE A 270    16037  12101  11635    282   1310   -677       C  
ATOM   2566  CE1 PHE A 270       0.576 -43.287 -34.307  1.00105.82           C  
ANISOU 2566  CE1 PHE A 270    16269  12160  11778    379   1126   -702       C  
ATOM   2567  CE2 PHE A 270      -1.324 -44.517 -35.084  1.00105.24           C  
ANISOU 2567  CE2 PHE A 270    16125  12069  11792    248   1272   -671       C  
ATOM   2568  CZ  PHE A 270       0.037 -44.321 -35.062  1.00104.10           C  
ANISOU 2568  CZ  PHE A 270    16019  11889  11644    311   1185   -683       C  
ATOM   2569  N   VAL A 271      -5.091 -41.192 -34.640  1.00 94.11           N  
ANISOU 2569  N   VAL A 271    14514  11062  10181    378   1412   -791       N  
ATOM   2570  CA  VAL A 271      -5.970 -41.623 -35.732  1.00 93.82           C  
ANISOU 2570  CA  VAL A 271    14356  11067  10225    283   1457   -793       C  
ATOM   2571  C   VAL A 271      -6.278 -40.466 -36.685  1.00 99.05           C  
ANISOU 2571  C   VAL A 271    14963  11765  10906    341   1415   -880       C  
ATOM   2572  O   VAL A 271      -6.076 -40.625 -37.892  1.00 97.73           O  
ANISOU 2572  O   VAL A 271    14749  11545  10839    272   1379   -912       O  
ATOM   2573  CB  VAL A 271      -7.264 -42.289 -35.208  1.00 98.39           C  
ANISOU 2573  CB  VAL A 271    14852  11783  10751    224   1571   -715       C  
ATOM   2574  CG1 VAL A 271      -8.312 -42.442 -36.304  1.00 97.97           C  
ANISOU 2574  CG1 VAL A 271    14654  11817  10754    135   1608   -726       C  
ATOM   2575  CG2 VAL A 271      -6.959 -43.641 -34.580  1.00 98.80           C  
ANISOU 2575  CG2 VAL A 271    14967  11762  10810    123   1603   -618       C  
ATOM   2576  N   VAL A 272      -6.736 -39.312 -36.156  1.00 97.47           N  
ANISOU 2576  N   VAL A 272    14785  11647  10603    476   1416   -918       N  
ATOM   2577  CA  VAL A 272      -7.103 -38.142 -36.969  1.00 97.40           C  
ANISOU 2577  CA  VAL A 272    14751  11665  10593    555   1374   -996       C  
ATOM   2578  C   VAL A 272      -5.912 -37.636 -37.830  1.00103.90           C  
ANISOU 2578  C   VAL A 272    15644  12342  11493    527   1256  -1050       C  
ATOM   2579  O   VAL A 272      -6.147 -37.164 -38.940  1.00103.03           O  
ANISOU 2579  O   VAL A 272    15480  12233  11433    518   1225  -1093       O  
ATOM   2580  CB  VAL A 272      -7.760 -36.989 -36.172  1.00100.70           C  
ANISOU 2580  CB  VAL A 272    15219  12176  10867    736   1390  -1031       C  
ATOM   2581  CG1 VAL A 272      -9.118 -37.392 -35.596  1.00101.21           C  
ANISOU 2581  CG1 VAL A 272    15162  12444  10850    770   1517   -976       C  
ATOM   2582  CG2 VAL A 272      -6.849 -36.391 -35.121  1.00100.60           C  
ANISOU 2582  CG2 VAL A 272    15384  12073  10767    819   1324  -1054       C  
ATOM   2583  N   CYS A 273      -4.657 -37.800 -37.351  1.00102.66           N  
ANISOU 2583  N   CYS A 273    15587  12080  11338    504   1192  -1039       N  
ATOM   2584  CA  CYS A 273      -3.439 -37.376 -38.047  1.00102.40           C  
ANISOU 2584  CA  CYS A 273    15603  11945  11360    464   1081  -1072       C  
ATOM   2585  C   CYS A 273      -2.905 -38.422 -38.998  1.00103.10           C  
ANISOU 2585  C   CYS A 273    15615  11993  11565    353   1081  -1049       C  
ATOM   2586  O   CYS A 273      -2.262 -38.056 -39.980  1.00102.58           O  
ANISOU 2586  O   CYS A 273    15534  11888  11553    317   1011  -1081       O  
ATOM   2587  CB  CYS A 273      -2.361 -36.996 -37.043  1.00104.17           C  
ANISOU 2587  CB  CYS A 273    15957  12113  11510    496   1006  -1066       C  
ATOM   2588  SG  CYS A 273      -2.762 -35.555 -36.030  1.00109.84           S  
ANISOU 2588  SG  CYS A 273    16819  12840  12074    636    970  -1117       S  
ATOM   2589  N   TRP A 274      -3.077 -39.703 -38.678  1.00 98.10           N  
ANISOU 2589  N   TRP A 274    14952  11361  10959    303   1151   -993       N  
ATOM   2590  CA  TRP A 274      -2.480 -40.744 -39.482  1.00 97.74           C  
ANISOU 2590  CA  TRP A 274    14874  11254  11008    222   1143   -978       C  
ATOM   2591  C   TRP A 274      -3.429 -41.429 -40.467  1.00 99.86           C  
ANISOU 2591  C   TRP A 274    15049  11544  11348    139   1202   -984       C  
ATOM   2592  O   TRP A 274      -2.966 -41.781 -41.560  1.00 98.13           O  
ANISOU 2592  O   TRP A 274    14801  11280  11204     92   1169  -1010       O  
ATOM   2593  CB  TRP A 274      -1.810 -41.773 -38.582  1.00 98.11           C  
ANISOU 2593  CB  TRP A 274    14990  11249  11038    220   1157   -914       C  
ATOM   2594  CG  TRP A 274      -0.472 -41.298 -38.096  1.00 99.68           C  
ANISOU 2594  CG  TRP A 274    15255  11422  11196    273   1070   -913       C  
ATOM   2595  CD1 TRP A 274      -0.141 -40.896 -36.832  1.00103.25           C  
ANISOU 2595  CD1 TRP A 274    15788  11889  11553    331   1049   -889       C  
ATOM   2596  CD2 TRP A 274       0.696 -41.107 -38.900  1.00 99.10           C  
ANISOU 2596  CD2 TRP A 274    15163  11328  11163    263    987   -936       C  
ATOM   2597  NE1 TRP A 274       1.183 -40.513 -36.789  1.00102.29           N  
ANISOU 2597  NE1 TRP A 274    15699  11755  11414    345    951   -893       N  
ATOM   2598  CE2 TRP A 274       1.719 -40.632 -38.047  1.00103.00           C  
ANISOU 2598  CE2 TRP A 274    15719  11832  11584    303    914   -916       C  
ATOM   2599  CE3 TRP A 274       0.989 -41.326 -40.259  1.00 99.86           C  
ANISOU 2599  CE3 TRP A 274    15189  11414  11339    222    967   -967       C  
ATOM   2600  CZ2 TRP A 274       3.007 -40.366 -38.514  1.00101.93           C  
ANISOU 2600  CZ2 TRP A 274    15560  11715  11454    292    823   -918       C  
ATOM   2601  CZ3 TRP A 274       2.259 -41.046 -40.721  1.00101.06           C  
ANISOU 2601  CZ3 TRP A 274    15321  11583  11494    227    884   -971       C  
ATOM   2602  CH2 TRP A 274       3.256 -40.590 -39.851  1.00101.91           C  
ANISOU 2602  CH2 TRP A 274    15475  11718  11529    257    814   -942       C  
ATOM   2603  N   ALA A 275      -4.731 -41.610 -40.123  1.00 96.06           N  
ANISOU 2603  N   ALA A 275    14515  11148  10835    118   1283   -958       N  
ATOM   2604  CA  ALA A 275      -5.705 -42.240 -41.038  1.00 95.38           C  
ANISOU 2604  CA  ALA A 275    14330  11105  10806     15   1330   -958       C  
ATOM   2605  C   ALA A 275      -5.754 -41.525 -42.418  1.00 97.97           C  
ANISOU 2605  C   ALA A 275    14589  11450  11187     16   1280  -1029       C  
ATOM   2606  O   ALA A 275      -5.585 -42.232 -43.405  1.00 96.31           O  
ANISOU 2606  O   ALA A 275    14354  11189  11050    -68   1268  -1045       O  
ATOM   2607  CB  ALA A 275      -7.094 -42.302 -40.416  1.00 96.96           C  
ANISOU 2607  CB  ALA A 275    14455  11444  10940     -2   1419   -913       C  
ATOM   2608  N   PRO A 276      -5.842 -40.158 -42.521  1.00 95.92           N  
ANISOU 2608  N   PRO A 276    14321  11238  10885    113   1241  -1074       N  
ATOM   2609  CA  PRO A 276      -5.839 -39.496 -43.841  1.00 95.85           C  
ANISOU 2609  CA  PRO A 276    14260  11237  10921    109   1188  -1130       C  
ATOM   2610  C   PRO A 276      -4.762 -39.971 -44.843  1.00102.28           C  
ANISOU 2610  C   PRO A 276    15085  11960  11815     45   1132  -1152       C  
ATOM   2611  O   PRO A 276      -5.109 -40.365 -45.966  1.00100.76           O  
ANISOU 2611  O   PRO A 276    14822  11785  11679    -23   1136  -1176       O  
ATOM   2612  CB  PRO A 276      -5.604 -38.032 -43.468  1.00 96.92           C  
ANISOU 2612  CB  PRO A 276    14465  11372  10987    229   1131  -1161       C  
ATOM   2613  CG  PRO A 276      -6.298 -37.878 -42.203  1.00101.79           C  
ANISOU 2613  CG  PRO A 276    15106  12055  11514    307   1190  -1134       C  
ATOM   2614  CD  PRO A 276      -6.025 -39.145 -41.455  1.00 97.79           C  
ANISOU 2614  CD  PRO A 276    14615  11520  11021    236   1241  -1075       C  
ATOM   2615  N   ILE A 277      -3.469 -39.937 -44.444  1.00101.34           N  
ANISOU 2615  N   ILE A 277    15049  11766  11690     71   1079  -1143       N  
ATOM   2616  CA  ILE A 277      -2.376 -40.348 -45.321  1.00101.18           C  
ANISOU 2616  CA  ILE A 277    15025  11694  11723     37   1030  -1157       C  
ATOM   2617  C   ILE A 277      -2.401 -41.867 -45.529  1.00106.15           C  
ANISOU 2617  C   ILE A 277    15657  12274  12402    -21   1077  -1141       C  
ATOM   2618  O   ILE A 277      -2.102 -42.300 -46.639  1.00106.79           O  
ANISOU 2618  O   ILE A 277    15707  12336  12531    -55   1060  -1172       O  
ATOM   2619  CB  ILE A 277      -0.972 -39.822 -44.870  1.00104.22           C  
ANISOU 2619  CB  ILE A 277    15473  12052  12073     79    954  -1144       C  
ATOM   2620  CG1 ILE A 277       0.105 -40.005 -45.980  1.00103.71           C  
ANISOU 2620  CG1 ILE A 277    15368  11988  12048     54    901  -1158       C  
ATOM   2621  CG2 ILE A 277      -0.505 -40.394 -43.519  1.00105.73           C  
ANISOU 2621  CG2 ILE A 277    15741  12210  12223    114    971  -1094       C  
ATOM   2622  CD1 ILE A 277      -0.101 -39.132 -47.254  1.00106.83           C  
ANISOU 2622  CD1 ILE A 277    15702  12426  12463     22    860  -1198       C  
ATOM   2623  N   HIS A 278      -2.785 -42.672 -44.506  1.00102.61           N  
ANISOU 2623  N   HIS A 278    15257  11798  11933    -34   1134  -1092       N  
ATOM   2624  CA  HIS A 278      -2.826 -44.138 -44.667  1.00102.25           C  
ANISOU 2624  CA  HIS A 278    15252  11672  11925    -98   1169  -1071       C  
ATOM   2625  C   HIS A 278      -3.929 -44.540 -45.658  1.00104.32           C  
ANISOU 2625  C   HIS A 278    15447  11961  12228   -203   1199  -1098       C  
ATOM   2626  O   HIS A 278      -3.757 -45.511 -46.391  1.00103.54           O  
ANISOU 2626  O   HIS A 278    15384  11785  12172   -257   1193  -1117       O  
ATOM   2627  CB  HIS A 278      -2.981 -44.875 -43.316  1.00103.54           C  
ANISOU 2627  CB  HIS A 278    15497  11795  12047   -101   1217   -997       C  
ATOM   2628  CG  HIS A 278      -1.686 -45.033 -42.578  1.00106.62           C  
ANISOU 2628  CG  HIS A 278    15973  12129  12409    -12   1180   -968       C  
ATOM   2629  ND1 HIS A 278      -0.682 -45.849 -43.053  1.00108.33           N  
ANISOU 2629  ND1 HIS A 278    16243  12263  12654     21   1148   -974       N  
ATOM   2630  CD2 HIS A 278      -1.261 -44.445 -41.435  1.00108.43           C  
ANISOU 2630  CD2 HIS A 278    16238  12388  12574     59   1166   -936       C  
ATOM   2631  CE1 HIS A 278       0.313 -45.740 -42.188  1.00107.80           C  
ANISOU 2631  CE1 HIS A 278    16224  12193  12541    108   1117   -938       C  
ATOM   2632  NE2 HIS A 278       0.009 -44.911 -41.194  1.00108.12           N  
ANISOU 2632  NE2 HIS A 278    16260  12296  12526    123   1123   -914       N  
ATOM   2633  N   ILE A 279      -5.029 -43.763 -45.703  1.00100.26           N  
ANISOU 2633  N   ILE A 279    14839  11561  11693   -221   1224  -1105       N  
ATOM   2634  CA  ILE A 279      -6.150 -43.967 -46.609  1.00100.37           C  
ANISOU 2634  CA  ILE A 279    14761  11644  11732   -319   1246  -1126       C  
ATOM   2635  C   ILE A 279      -5.697 -43.568 -47.995  1.00106.71           C  
ANISOU 2635  C   ILE A 279    15525  12442  12578   -308   1188  -1195       C  
ATOM   2636  O   ILE A 279      -5.940 -44.297 -48.956  1.00106.21           O  
ANISOU 2636  O   ILE A 279    15448  12353  12552   -395   1183  -1224       O  
ATOM   2637  CB  ILE A 279      -7.378 -43.167 -46.119  1.00103.26           C  
ANISOU 2637  CB  ILE A 279    15027  12165  12042   -301   1291  -1103       C  
ATOM   2638  CG1 ILE A 279      -8.090 -43.926 -44.993  1.00104.63           C  
ANISOU 2638  CG1 ILE A 279    15210  12372  12172   -366   1363  -1025       C  
ATOM   2639  CG2 ILE A 279      -8.344 -42.862 -47.253  1.00104.09           C  
ANISOU 2639  CG2 ILE A 279    15005  12381  12163   -355   1288  -1139       C  
ATOM   2640  CD1 ILE A 279      -8.767 -43.047 -43.946  1.00112.90           C  
ANISOU 2640  CD1 ILE A 279    16207  13559  13132   -271   1409   -993       C  
ATOM   2641  N   PHE A 280      -5.002 -42.423 -48.084  1.00105.84           N  
ANISOU 2641  N   PHE A 280    15410  12351  12451   -210   1140  -1217       N  
ATOM   2642  CA  PHE A 280      -4.473 -41.867 -49.325  1.00106.55           C  
ANISOU 2642  CA  PHE A 280    15463  12453  12567   -195   1081  -1268       C  
ATOM   2643  C   PHE A 280      -3.580 -42.853 -50.043  1.00114.15           C  
ANISOU 2643  C   PHE A 280    16467  13336  13567   -220   1062  -1292       C  
ATOM   2644  O   PHE A 280      -3.862 -43.158 -51.195  1.00114.74           O  
ANISOU 2644  O   PHE A 280    16501  13425  13671   -272   1053  -1335       O  
ATOM   2645  CB  PHE A 280      -3.696 -40.578 -49.058  1.00107.82           C  
ANISOU 2645  CB  PHE A 280    15648  12625  12693   -107   1025  -1267       C  
ATOM   2646  CG  PHE A 280      -4.102 -39.420 -49.924  1.00109.14           C  
ANISOU 2646  CG  PHE A 280    15757  12859  12850    -90    985  -1297       C  
ATOM   2647  CD1 PHE A 280      -3.751 -39.380 -51.267  1.00111.84           C  
ANISOU 2647  CD1 PHE A 280    16054  13217  13224   -124    947  -1331       C  
ATOM   2648  CD2 PHE A 280      -4.789 -38.339 -49.386  1.00111.85           C  
ANISOU 2648  CD2 PHE A 280    16106  13250  13142    -23    983  -1291       C  
ATOM   2649  CE1 PHE A 280      -4.105 -38.289 -52.064  1.00112.72           C  
ANISOU 2649  CE1 PHE A 280    16123  13385  13319   -107    906  -1349       C  
ATOM   2650  CE2 PHE A 280      -5.140 -37.247 -50.182  1.00114.60           C  
ANISOU 2650  CE2 PHE A 280    16426  13644  13475     10    940  -1315       C  
ATOM   2651  CZ  PHE A 280      -4.798 -37.231 -51.518  1.00112.20           C  
ANISOU 2651  CZ  PHE A 280    16075  13350  13207    -39    900  -1339       C  
ATOM   2652  N   VAL A 281      -2.551 -43.402 -49.358  1.00113.11           N  
ANISOU 2652  N   VAL A 281    16420  13127  13428   -171   1056  -1265       N  
ATOM   2653  CA  VAL A 281      -1.605 -44.360 -49.948  1.00114.71           C  
ANISOU 2653  CA  VAL A 281    16675  13262  13650   -151   1039  -1287       C  
ATOM   2654  C   VAL A 281      -2.332 -45.646 -50.453  1.00123.95           C  
ANISOU 2654  C   VAL A 281    17891  14355  14849   -237   1072  -1310       C  
ATOM   2655  O   VAL A 281      -1.824 -46.283 -51.373  1.00125.14           O  
ANISOU 2655  O   VAL A 281    18075  14462  15011   -223   1052  -1356       O  
ATOM   2656  CB  VAL A 281      -0.394 -44.705 -49.036  1.00118.72           C  
ANISOU 2656  CB  VAL A 281    17259  13721  14130    -61   1026  -1245       C  
ATOM   2657  CG1 VAL A 281       0.357 -43.446 -48.609  1.00117.73           C  
ANISOU 2657  CG1 VAL A 281    17093  13672  13967     -7    978  -1223       C  
ATOM   2658  CG2 VAL A 281      -0.805 -45.534 -47.822  1.00119.61           C  
ANISOU 2658  CG2 VAL A 281    17463  13751  14231    -76   1073  -1192       C  
ATOM   2659  N   ILE A 282      -3.518 -45.994 -49.888  1.00122.47           N  
ANISOU 2659  N   ILE A 282    17708  14163  14662   -332   1117  -1279       N  
ATOM   2660  CA  ILE A 282      -4.318 -47.158 -50.303  1.00123.60           C  
ANISOU 2660  CA  ILE A 282    17901  14238  14824   -458   1137  -1290       C  
ATOM   2661  C   ILE A 282      -5.028 -46.832 -51.630  1.00128.13           C  
ANISOU 2661  C   ILE A 282    18374  14894  15415   -531   1117  -1350       C  
ATOM   2662  O   ILE A 282      -4.916 -47.599 -52.589  1.00128.08           O  
ANISOU 2662  O   ILE A 282    18421  14821  15424   -573   1094  -1403       O  
ATOM   2663  CB  ILE A 282      -5.322 -47.583 -49.180  1.00127.54           C  
ANISOU 2663  CB  ILE A 282    18418  14738  15303   -555   1191  -1215       C  
ATOM   2664  CG1 ILE A 282      -4.598 -48.208 -47.947  1.00128.60           C  
ANISOU 2664  CG1 ILE A 282    18685  14762  15416   -495   1207  -1153       C  
ATOM   2665  CG2 ILE A 282      -6.455 -48.486 -49.697  1.00129.07           C  
ANISOU 2665  CG2 ILE A 282    18619  14916  15508   -738   1203  -1216       C  
ATOM   2666  CD1 ILE A 282      -3.657 -49.487 -48.192  1.00139.56           C  
ANISOU 2666  CD1 ILE A 282    20248  15966  16815   -458   1180  -1168       C  
ATOM   2667  N   VAL A 283      -5.737 -45.682 -51.674  1.00124.50           N  
ANISOU 2667  N   VAL A 283    17781  14579  14945   -530   1123  -1344       N  
ATOM   2668  CA  VAL A 283      -6.513 -45.218 -52.825  1.00124.24           C  
ANISOU 2668  CA  VAL A 283    17636  14652  14919   -586   1104  -1388       C  
ATOM   2669  C   VAL A 283      -5.581 -44.828 -53.974  1.00129.91           C  
ANISOU 2669  C   VAL A 283    18346  15367  15647   -515   1053  -1449       C  
ATOM   2670  O   VAL A 283      -5.950 -45.026 -55.129  1.00130.63           O  
ANISOU 2670  O   VAL A 283    18399  15489  15745   -575   1031  -1499       O  
ATOM   2671  CB  VAL A 283      -7.487 -44.077 -52.450  1.00127.25           C  
ANISOU 2671  CB  VAL A 283    17891  15189  15271   -565   1125  -1357       C  
ATOM   2672  CG1 VAL A 283      -8.418 -43.746 -53.607  1.00127.01           C  
ANISOU 2672  CG1 VAL A 283    17740  15279  15240   -627   1107  -1393       C  
ATOM   2673  CG2 VAL A 283      -8.309 -44.450 -51.221  1.00128.01           C  
ANISOU 2673  CG2 VAL A 283    17982  15317  15339   -617   1185  -1288       C  
ATOM   2674  N   TRP A 284      -4.374 -44.322 -53.675  1.00127.07           N  
ANISOU 2674  N   TRP A 284    18020  14983  15279   -400   1031  -1439       N  
ATOM   2675  CA  TRP A 284      -3.395 -43.974 -54.708  1.00127.33           C  
ANISOU 2675  CA  TRP A 284    18034  15039  15308   -339    986  -1480       C  
ATOM   2676  C   TRP A 284      -2.933 -45.232 -55.433  1.00135.42           C  
ANISOU 2676  C   TRP A 284    19137  15978  16338   -347    981  -1531       C  
ATOM   2677  O   TRP A 284      -2.812 -45.219 -56.661  1.00134.92           O  
ANISOU 2677  O   TRP A 284    19040  15956  16268   -352    956  -1585       O  
ATOM   2678  CB  TRP A 284      -2.183 -43.232 -54.120  1.00125.13           C  
ANISOU 2678  CB  TRP A 284    17767  14771  15008   -238    960  -1444       C  
ATOM   2679  CG  TRP A 284      -1.476 -42.370 -55.129  1.00125.35           C  
ANISOU 2679  CG  TRP A 284    17729  14881  15017   -206    910  -1462       C  
ATOM   2680  CD1 TRP A 284      -0.552 -42.771 -56.050  1.00128.27           C  
ANISOU 2680  CD1 TRP A 284    18093  15271  15373   -170    890  -1493       C  
ATOM   2681  CD2 TRP A 284      -1.645 -40.958 -55.315  1.00124.55           C  
ANISOU 2681  CD2 TRP A 284    17568  14858  14898   -205    873  -1444       C  
ATOM   2682  NE1 TRP A 284      -0.133 -41.697 -56.799  1.00126.98           N  
ANISOU 2682  NE1 TRP A 284    17854  15208  15186   -166    846  -1486       N  
ATOM   2683  CE2 TRP A 284      -0.793 -40.572 -56.376  1.00128.11           C  
ANISOU 2683  CE2 TRP A 284    17974  15373  15328   -193    830  -1455       C  
ATOM   2684  CE3 TRP A 284      -2.420 -39.971 -54.676  1.00125.65           C  
ANISOU 2684  CE3 TRP A 284    17699  15016  15025   -202    871  -1417       C  
ATOM   2685  CZ2 TRP A 284      -0.701 -39.246 -56.818  1.00127.18           C  
ANISOU 2685  CZ2 TRP A 284    17816  15323  15185   -202    779  -1433       C  
ATOM   2686  CZ3 TRP A 284      -2.335 -38.658 -55.124  1.00126.78           C  
ANISOU 2686  CZ3 TRP A 284    17817  15213  15142   -188    818  -1406       C  
ATOM   2687  CH2 TRP A 284      -1.481 -38.305 -56.177  1.00127.34           C  
ANISOU 2687  CH2 TRP A 284    17855  15330  15198   -200    769  -1410       C  
ATOM   2688  N   THR A 285      -2.709 -46.323 -54.659  1.00135.31           N  
ANISOU 2688  N   THR A 285    19244  15841  16327   -343   1005  -1512       N  
ATOM   2689  CA  THR A 285      -2.249 -47.642 -55.111  1.00137.24           C  
ANISOU 2689  CA  THR A 285    19617  15962  16565   -325   1000  -1557       C  
ATOM   2690  C   THR A 285      -3.233 -48.253 -56.122  1.00144.05           C  
ANISOU 2690  C   THR A 285    20495  16800  17435   -453    990  -1618       C  
ATOM   2691  O   THR A 285      -2.815 -48.710 -57.196  1.00144.21           O  
ANISOU 2691  O   THR A 285    20559  16797  17437   -420    964  -1689       O  
ATOM   2692  CB  THR A 285      -2.038 -48.562 -53.876  1.00146.26           C  
ANISOU 2692  CB  THR A 285    20899  16969  17706   -307   1025  -1505       C  
ATOM   2693  OG1 THR A 285      -0.912 -48.095 -53.145  1.00146.71           O  
ANISOU 2693  OG1 THR A 285    20944  17056  17742   -172   1021  -1462       O  
ATOM   2694  CG2 THR A 285      -1.817 -50.021 -54.234  1.00145.66           C  
ANISOU 2694  CG2 THR A 285    21000  16725  17617   -302   1016  -1547       C  
ATOM   2695  N   LEU A 286      -4.529 -48.239 -55.777  1.00142.24           N  
ANISOU 2695  N   LEU A 286    20225  16597  17222   -598   1009  -1588       N  
ATOM   2696  CA  LEU A 286      -5.582 -48.851 -56.577  1.00143.76           C  
ANISOU 2696  CA  LEU A 286    20425  16782  17414   -756    994  -1630       C  
ATOM   2697  C   LEU A 286      -6.179 -47.871 -57.613  1.00148.16           C  
ANISOU 2697  C   LEU A 286    20816  17510  17969   -786    972  -1663       C  
ATOM   2698  O   LEU A 286      -5.909 -48.013 -58.813  1.00148.37           O  
ANISOU 2698  O   LEU A 286    20850  17544  17981   -773    937  -1736       O  
ATOM   2699  CB  LEU A 286      -6.683 -49.424 -55.646  1.00144.92           C  
ANISOU 2699  CB  LEU A 286    20599  16898  17566   -914   1024  -1564       C  
ATOM   2700  CG  LEU A 286      -6.215 -50.159 -54.361  1.00150.02           C  
ANISOU 2700  CG  LEU A 286    21391  17399  18210   -885   1053  -1501       C  
ATOM   2701  CD1 LEU A 286      -7.303 -50.184 -53.316  1.00150.69           C  
ANISOU 2701  CD1 LEU A 286    21426  17539  18289  -1017   1096  -1412       C  
ATOM   2702  CD2 LEU A 286      -5.716 -51.573 -54.653  1.00153.30           C  
ANISOU 2702  CD2 LEU A 286    22033  17599  18615   -897   1024  -1542       C  
ATOM   2703  N   VAL A 287      -6.969 -46.883 -57.147  1.00144.33           N  
ANISOU 2703  N   VAL A 287    20189  17164  17487   -807    993  -1610       N  
ATOM   2704  CA  VAL A 287      -7.668 -45.896 -57.977  1.00144.06           C  
ANISOU 2704  CA  VAL A 287    19998  17295  17442   -823    974  -1626       C  
ATOM   2705  C   VAL A 287      -6.676 -44.919 -58.635  1.00148.44           C  
ANISOU 2705  C   VAL A 287    20516  17895  17989   -685    943  -1651       C  
ATOM   2706  O   VAL A 287      -5.718 -44.480 -57.993  1.00147.39           O  
ANISOU 2706  O   VAL A 287    20416  17727  17857   -576    949  -1621       O  
ATOM   2707  CB  VAL A 287      -8.742 -45.130 -57.137  1.00147.84           C  
ANISOU 2707  CB  VAL A 287    20356  17907  17910   -844   1008  -1557       C  
ATOM   2708  CG1 VAL A 287      -9.577 -44.186 -58.003  1.00147.68           C  
ANISOU 2708  CG1 VAL A 287    20181  18062  17869   -847    985  -1570       C  
ATOM   2709  CG2 VAL A 287      -9.662 -46.092 -56.390  1.00148.85           C  
ANISOU 2709  CG2 VAL A 287    20506  18017  18034   -993   1044  -1512       C  
ATOM   2710  N   ASP A 288      -6.907 -44.604 -59.934  1.00146.11           N  
ANISOU 2710  N   ASP A 288    20152  17685  17678   -706    907  -1701       N  
ATOM   2711  CA  ASP A 288      -6.122 -43.616 -60.680  1.00145.50           C  
ANISOU 2711  CA  ASP A 288    20026  17676  17583   -605    875  -1712       C  
ATOM   2712  C   ASP A 288      -6.752 -42.242 -60.469  1.00147.80           C  
ANISOU 2712  C   ASP A 288    20208  18085  17865   -572    869  -1663       C  
ATOM   2713  O   ASP A 288      -7.753 -41.922 -61.125  1.00147.62           O  
ANISOU 2713  O   ASP A 288    20093  18169  17827   -621    854  -1673       O  
ATOM   2714  CB  ASP A 288      -6.037 -43.935 -62.195  1.00148.41           C  
ANISOU 2714  CB  ASP A 288    20382  18082  17925   -633    838  -1785       C  
ATOM   2715  CG  ASP A 288      -5.898 -45.391 -62.578  1.00162.68           C  
ANISOU 2715  CG  ASP A 288    22310  19775  19726   -687    836  -1853       C  
ATOM   2716  OD1 ASP A 288      -6.936 -46.082 -62.657  1.00164.64           O1-
ANISOU 2716  OD1 ASP A 288    22572  20005  19977   -821    832  -1872       O1-
ATOM   2717  OD2 ASP A 288      -4.755 -45.827 -62.848  1.00168.92           O  
ANISOU 2717  OD2 ASP A 288    23183  20502  20497   -594    833  -1887       O  
ATOM   2718  N   ILE A 289      -6.182 -41.422 -59.561  1.00143.41           N  
ANISOU 2718  N   ILE A 289    19671  17509  17308   -483    873  -1611       N  
ATOM   2719  CA  ILE A 289      -6.691 -40.064 -59.297  1.00142.86           C  
ANISOU 2719  CA  ILE A 289    19542  17520  17217   -426    859  -1569       C  
ATOM   2720  C   ILE A 289      -5.650 -39.111 -59.919  1.00145.15           C  
ANISOU 2720  C   ILE A 289    19844  17821  17486   -361    807  -1558       C  
ATOM   2721  O   ILE A 289      -4.448 -39.323 -59.717  1.00144.64           O  
ANISOU 2721  O   ILE A 289    19836  17697  17422   -336    799  -1550       O  
ATOM   2722  CB  ILE A 289      -7.070 -39.823 -57.801  1.00146.05           C  
ANISOU 2722  CB  ILE A 289    19971  17901  17619   -387    898  -1519       C  
ATOM   2723  CG1 ILE A 289      -7.862 -38.493 -57.616  1.00146.76           C  
ANISOU 2723  CG1 ILE A 289    20009  18084  17671   -309    885  -1490       C  
ATOM   2724  CG2 ILE A 289      -5.871 -39.930 -56.833  1.00145.53           C  
ANISOU 2724  CG2 ILE A 289    20006  17726  17561   -337    902  -1494       C  
ATOM   2725  CD1 ILE A 289      -9.251 -38.380 -58.386  1.00153.02           C  
ANISOU 2725  CD1 ILE A 289    20675  19023  18443   -340    887  -1502       C  
ATOM   2726  N   ASP A 290      -6.095 -38.100 -60.711  1.00140.60           N  
ANISOU 2726  N   ASP A 290    19212  17331  16881   -339    769  -1550       N  
ATOM   2727  CA  ASP A 290      -5.211 -37.169 -61.442  1.00139.69           C  
ANISOU 2727  CA  ASP A 290    19110  17233  16735   -308    711  -1529       C  
ATOM   2728  C   ASP A 290      -4.345 -36.350 -60.469  1.00140.06           C  
ANISOU 2728  C   ASP A 290    19239  17208  16768   -262    686  -1477       C  
ATOM   2729  O   ASP A 290      -4.753 -35.324 -59.918  1.00139.30           O  
ANISOU 2729  O   ASP A 290    19186  17094  16648   -209    661  -1443       O  
ATOM   2730  CB  ASP A 290      -5.946 -36.267 -62.471  1.00142.30           C  
ANISOU 2730  CB  ASP A 290    19383  17654  17029   -289    669  -1521       C  
ATOM   2731  CG  ASP A 290      -7.025 -35.322 -61.971  1.00155.50           C  
ANISOU 2731  CG  ASP A 290    21041  19361  18683   -221    672  -1497       C  
ATOM   2732  OD1 ASP A 290      -7.338 -35.356 -60.752  1.00157.86           O  
ANISOU 2732  OD1 ASP A 290    21346  19636  18995   -204    720  -1493       O  
ATOM   2733  OD2 ASP A 290      -7.571 -34.557 -62.802  1.00158.86           O1-
ANISOU 2733  OD2 ASP A 290    21446  19845  19067   -174    628  -1480       O1-
ATOM   2734  N   ARG A 291      -3.115 -36.830 -60.327  1.00134.48           N  
ANISOU 2734  N   ARG A 291    18560  16468  16068   -277    688  -1474       N  
ATOM   2735  CA  ARG A 291      -2.029 -36.319 -59.495  1.00133.24           C  
ANISOU 2735  CA  ARG A 291    18466  16266  15894   -261    659  -1426       C  
ATOM   2736  C   ARG A 291      -1.722 -34.838 -59.732  1.00135.44           C  
ANISOU 2736  C   ARG A 291    18780  16555  16126   -265    585  -1374       C  
ATOM   2737  O   ARG A 291      -1.018 -34.228 -58.925  1.00135.32           O  
ANISOU 2737  O   ARG A 291    18836  16490  16087   -265    548  -1330       O  
ATOM   2738  CB  ARG A 291      -0.790 -37.153 -59.858  1.00133.31           C  
ANISOU 2738  CB  ARG A 291    18454  16300  15897   -271    667  -1433       C  
ATOM   2739  N   ARG A 292      -2.259 -34.264 -60.823  1.00130.43           N  
ANISOU 2739  N   ARG A 292    18108  15978  15471   -275    555  -1377       N  
ATOM   2740  CA  ARG A 292      -2.037 -32.874 -61.191  1.00129.72           C  
ANISOU 2740  CA  ARG A 292    18072  15885  15332   -287    476  -1323       C  
ATOM   2741  C   ARG A 292      -3.146 -31.938 -60.697  1.00132.72           C  
ANISOU 2741  C   ARG A 292    18523  16210  15693   -212    456  -1317       C  
ATOM   2742  O   ARG A 292      -2.872 -30.744 -60.540  1.00133.23           O  
ANISOU 2742  O   ARG A 292    18695  16214  15712   -206    384  -1270       O  
ATOM   2743  CB  ARG A 292      -1.858 -32.740 -62.705  1.00130.19           C  
ANISOU 2743  CB  ARG A 292    18062  16042  15363   -332    450  -1318       C  
ATOM   2744  CG  ARG A 292      -0.494 -33.250 -63.177  1.00142.34           C  
ANISOU 2744  CG  ARG A 292    19549  17652  16883   -389    449  -1301       C  
ATOM   2745  CD  ARG A 292       0.109 -32.391 -64.277  1.00152.83           C  
ANISOU 2745  CD  ARG A 292    20859  19062  18148   -453    386  -1241       C  
ATOM   2746  NE  ARG A 292      -0.516 -32.623 -65.581  1.00155.11           N  
ANISOU 2746  NE  ARG A 292    21073  19437  18424   -448    398  -1277       N  
ATOM   2747  CZ  ARG A 292      -0.095 -33.520 -66.465  1.00165.08           C  
ANISOU 2747  CZ  ARG A 292    22246  20806  19673   -455    434  -1315       C  
ATOM   2748  NH1 ARG A 292       0.953 -34.287 -66.197  1.00152.77           N  
ANISOU 2748  NH1 ARG A 292    20654  19282  18108   -451    466  -1321       N  
ATOM   2749  NH2 ARG A 292      -0.721 -33.659 -67.624  1.00150.83           N1+
ANISOU 2749  NH2 ARG A 292    20386  19076  17848   -454    436  -1351       N1+
ATOM   2750  N   ASP A 293      -4.368 -32.456 -60.420  1.00128.10           N  
ANISOU 2750  N   ASP A 293    17888  15650  15135   -153    516  -1361       N  
ATOM   2751  CA  ASP A 293      -5.504 -31.648 -59.947  1.00128.43           C  
ANISOU 2751  CA  ASP A 293    17972  15680  15146    -50    510  -1358       C  
ATOM   2752  C   ASP A 293      -5.135 -30.802 -58.709  1.00132.64           C  
ANISOU 2752  C   ASP A 293    18657  16097  15643      6    475  -1329       C  
ATOM   2753  O   ASP A 293      -4.461 -31.317 -57.812  1.00132.67           O  
ANISOU 2753  O   ASP A 293    18689  16053  15668    -25    498  -1328       O  
ATOM   2754  CB  ASP A 293      -6.716 -32.535 -59.627  1.00130.65           C  
ANISOU 2754  CB  ASP A 293    18150  16037  15454    -18    591  -1397       C  
ATOM   2755  CG  ASP A 293      -8.032 -31.789 -59.492  1.00144.15           C  
ANISOU 2755  CG  ASP A 293    19847  17807  17117    103    591  -1394       C  
ATOM   2756  OD1 ASP A 293      -8.268 -31.182 -58.421  1.00143.31           O  
ANISOU 2756  OD1 ASP A 293    19828  17648  16974    204    593  -1382       O  
ATOM   2757  OD2 ASP A 293      -8.830 -31.817 -60.453  1.00155.34           O1-
ANISOU 2757  OD2 ASP A 293    21164  19335  18525    107    589  -1405       O1-
ATOM   2758  N   PRO A 294      -5.549 -29.510 -58.640  1.00129.10           N  
ANISOU 2758  N   PRO A 294    18322  15596  15133     95    413  -1307       N  
ATOM   2759  CA  PRO A 294      -5.172 -28.680 -57.476  1.00128.48           C  
ANISOU 2759  CA  PRO A 294    18420  15389  15008    146    367  -1290       C  
ATOM   2760  C   PRO A 294      -5.827 -29.113 -56.158  1.00127.96           C  
ANISOU 2760  C   PRO A 294    18355  15324  14941    242    440  -1321       C  
ATOM   2761  O   PRO A 294      -5.201 -28.960 -55.110  1.00127.64           O  
ANISOU 2761  O   PRO A 294    18423  15193  14881    238    423  -1314       O  
ATOM   2762  CB  PRO A 294      -5.616 -27.269 -57.877  1.00131.61           C  
ANISOU 2762  CB  PRO A 294    18951  15723  15331    236    283  -1268       C  
ATOM   2763  CG  PRO A 294      -6.679 -27.475 -58.896  1.00136.93           C  
ANISOU 2763  CG  PRO A 294    19488  16527  16013    291    318  -1283       C  
ATOM   2764  CD  PRO A 294      -6.320 -28.731 -59.632  1.00131.65           C  
ANISOU 2764  CD  PRO A 294    18640  15964  15418    157    372  -1298       C  
ATOM   2765  N   LEU A 295      -7.064 -29.648 -56.205  1.00120.86           N  
ANISOU 2765  N   LEU A 295    17329  14540  14052    316    518  -1348       N  
ATOM   2766  CA  LEU A 295      -7.785 -30.108 -55.017  1.00119.16           C  
ANISOU 2766  CA  LEU A 295    17088  14364  13825    398    596  -1365       C  
ATOM   2767  C   LEU A 295      -7.077 -31.375 -54.508  1.00117.84           C  
ANISOU 2767  C   LEU A 295    16874  14181  13718    286    651  -1367       C  
ATOM   2768  O   LEU A 295      -6.943 -31.521 -53.289  1.00117.47           O  
ANISOU 2768  O   LEU A 295    16895  14091  13648    329    677  -1364       O  
ATOM   2769  CB  LEU A 295      -9.245 -30.412 -55.372  1.00119.95           C  
ANISOU 2769  CB  LEU A 295    17034  14630  13914    472    660  -1378       C  
ATOM   2770  CG  LEU A 295     -10.129 -30.962 -54.263  1.00125.54           C  
ANISOU 2770  CG  LEU A 295    17673  15429  14599    540    751  -1382       C  
ATOM   2771  CD1 LEU A 295     -10.977 -29.877 -53.649  1.00126.34           C  
ANISOU 2771  CD1 LEU A 295    17845  15560  14596    754    746  -1384       C  
ATOM   2772  CD2 LEU A 295     -10.996 -32.098 -54.789  1.00129.74           C  
ANISOU 2772  CD2 LEU A 295    17997  16127  15172    453    823  -1385       C  
ATOM   2773  N   VAL A 296      -6.616 -32.275 -55.423  1.00110.18           N  
ANISOU 2773  N   VAL A 296    15803  13244  12815    157    667  -1372       N  
ATOM   2774  CA  VAL A 296      -5.892 -33.494 -55.022  1.00108.09           C  
ANISOU 2774  CA  VAL A 296    15514  12953  12602     71    713  -1373       C  
ATOM   2775  C   VAL A 296      -4.528 -33.121 -54.377  1.00110.86           C  
ANISOU 2775  C   VAL A 296    15981  13201  12940     42    654  -1348       C  
ATOM   2776  O   VAL A 296      -4.205 -33.645 -53.315  1.00110.21           O  
ANISOU 2776  O   VAL A 296    15931  13080  12863     38    684  -1340       O  
ATOM   2777  CB  VAL A 296      -5.813 -34.652 -56.077  1.00110.55           C  
ANISOU 2777  CB  VAL A 296    15708  13319  12975    -32    751  -1396       C  
ATOM   2778  CG1 VAL A 296      -4.973 -35.828 -55.588  1.00110.73           C  
ANISOU 2778  CG1 VAL A 296    15623  13453  12997    -34    762  -1417       C  
ATOM   2779  CG2 VAL A 296      -7.181 -35.108 -56.585  1.00109.42           C  
ANISOU 2779  CG2 VAL A 296    15581  13140  12853   -104    709  -1393       C  
ATOM   2780  N   VAL A 297      -3.771 -32.182 -54.986  1.00107.14           N  
ANISOU 2780  N   VAL A 297    15571  12697  12442     15    568  -1328       N  
ATOM   2781  CA  VAL A 297      -2.506 -31.700 -54.416  1.00107.22           C  
ANISOU 2781  CA  VAL A 297    15680  12634  12426    -38    499  -1293       C  
ATOM   2782  C   VAL A 297      -2.654 -31.014 -53.009  1.00111.85           C  
ANISOU 2782  C   VAL A 297    16411  13132  12955     40    479  -1290       C  
ATOM   2783  O   VAL A 297      -1.818 -31.231 -52.124  1.00111.82           O  
ANISOU 2783  O   VAL A 297    16458  13088  12941      8    466  -1273       O  
ATOM   2784  CB  VAL A 297      -1.838 -30.796 -55.489  1.00111.29           C  
ANISOU 2784  CB  VAL A 297    16224  13148  12914   -109    408  -1259       C  
ATOM   2785  CG1 VAL A 297      -0.712 -29.935 -54.911  1.00111.57           C  
ANISOU 2785  CG1 VAL A 297    16393  13105  12895   -173    313  -1211       C  
ATOM   2786  CG2 VAL A 297      -1.319 -31.644 -56.644  1.00110.58           C  
ANISOU 2786  CG2 VAL A 297    15995  13156  12866   -189    432  -1259       C  
ATOM   2787  N   ALA A 298      -3.747 -30.247 -52.803  1.00107.62           N  
ANISOU 2787  N   ALA A 298    15936  12579  12373    157    479  -1309       N  
ATOM   2788  CA  ALA A 298      -4.057 -29.591 -51.532  1.00106.74           C  
ANISOU 2788  CA  ALA A 298    15969  12395  12192    265    467  -1319       C  
ATOM   2789  C   ALA A 298      -4.411 -30.623 -50.472  1.00107.73           C  
ANISOU 2789  C   ALA A 298    16031  12568  12335    299    565  -1330       C  
ATOM   2790  O   ALA A 298      -3.992 -30.483 -49.331  1.00107.41           O  
ANISOU 2790  O   ALA A 298    16094  12465  12251    323    552  -1326       O  
ATOM   2791  CB  ALA A 298      -5.208 -28.623 -51.714  1.00108.33           C  
ANISOU 2791  CB  ALA A 298    16232  12596  12331    414    454  -1339       C  
ATOM   2792  N   ALA A 299      -5.164 -31.665 -50.851  1.00102.30           N  
ANISOU 2792  N   ALA A 299    15180  11987  11703    288    657  -1340       N  
ATOM   2793  CA  ALA A 299      -5.557 -32.726 -49.932  1.00101.10           C  
ANISOU 2793  CA  ALA A 299    14966  11881  11566    294    751  -1337       C  
ATOM   2794  C   ALA A 299      -4.357 -33.575 -49.555  1.00103.40           C  
ANISOU 2794  C   ALA A 299    15268  12120  11898    197    749  -1317       C  
ATOM   2795  O   ALA A 299      -4.132 -33.764 -48.372  1.00102.53           O  
ANISOU 2795  O   ALA A 299    15221  11979  11758    225    767  -1304       O  
ATOM   2796  CB  ALA A 299      -6.646 -33.584 -50.543  1.00101.79           C  
ANISOU 2796  CB  ALA A 299    14890  12090  11695    273    831  -1345       C  
ATOM   2797  N   LEU A 300      -3.551 -34.026 -50.538  1.00100.34           N  
ANISOU 2797  N   LEU A 300    14825  11734  11567     99    722  -1313       N  
ATOM   2798  CA  LEU A 300      -2.362 -34.856 -50.321  1.00 99.89           C  
ANISOU 2798  CA  LEU A 300    14764  11651  11540     31    718  -1293       C  
ATOM   2799  C   LEU A 300      -1.364 -34.187 -49.382  1.00104.95           C  
ANISOU 2799  C   LEU A 300    15521  12230  12126     36    650  -1266       C  
ATOM   2800  O   LEU A 300      -1.001 -34.805 -48.381  1.00105.17           O  
ANISOU 2800  O   LEU A 300    15574  12240  12147     47    678  -1250       O  
ATOM   2801  CB  LEU A 300      -1.673 -35.228 -51.652  1.00 99.27           C  
ANISOU 2801  CB  LEU A 300    14606  11607  11506    -45    694  -1297       C  
ATOM   2802  CG  LEU A 300      -0.309 -35.933 -51.571  1.00103.61           C  
ANISOU 2802  CG  LEU A 300    15145  12156  12067    -87    679  -1274       C  
ATOM   2803  CD1 LEU A 300      -0.403 -37.285 -50.878  1.00103.78           C  
ANISOU 2803  CD1 LEU A 300    15158  12156  12118    -68    754  -1275       C  
ATOM   2804  CD2 LEU A 300       0.294 -36.106 -52.934  1.00106.69           C  
ANISOU 2804  CD2 LEU A 300    15456  12607  12476   -137    656  -1279       C  
ATOM   2805  N   HIS A 301      -0.947 -32.934 -49.684  1.00101.64           N  
ANISOU 2805  N   HIS A 301    15182  11775  11661     20    556  -1258       N  
ATOM   2806  CA  HIS A 301       0.040 -32.188 -48.900  1.00101.61           C  
ANISOU 2806  CA  HIS A 301    15301  11711  11594     -9    468  -1231       C  
ATOM   2807  C   HIS A 301      -0.472 -31.815 -47.497  1.00103.50           C  
ANISOU 2807  C   HIS A 301    15663  11892  11769     85    479  -1246       C  
ATOM   2808  O   HIS A 301       0.332 -31.650 -46.578  1.00101.72           O  
ANISOU 2808  O   HIS A 301    15524  11629  11497     64    431  -1227       O  
ATOM   2809  CB  HIS A 301       0.555 -30.976 -49.683  1.00103.15           C  
ANISOU 2809  CB  HIS A 301    15564  11876  11753    -79    357  -1211       C  
ATOM   2810  CG  HIS A 301       1.508 -31.393 -50.766  1.00107.13           C  
ANISOU 2810  CG  HIS A 301    15948  12462  12294   -188    337  -1178       C  
ATOM   2811  ND1 HIS A 301       1.051 -31.828 -52.000  1.00109.24           N  
ANISOU 2811  ND1 HIS A 301    16098  12794  12615   -190    383  -1195       N  
ATOM   2812  CD2 HIS A 301       2.855 -31.538 -50.728  1.00109.64           C  
ANISOU 2812  CD2 HIS A 301    16234  12831  12595   -282    286  -1131       C  
ATOM   2813  CE1 HIS A 301       2.132 -32.177 -52.683  1.00108.87           C  
ANISOU 2813  CE1 HIS A 301    15963  12826  12575   -275    360  -1162       C  
ATOM   2814  NE2 HIS A 301       3.241 -32.025 -51.954  1.00109.56           N  
ANISOU 2814  NE2 HIS A 301    16087  12919  12620   -329    304  -1119       N  
ATOM   2815  N   LEU A 302      -1.800 -31.780 -47.320  1.00100.51           N  
ANISOU 2815  N   LEU A 302    15276  11530  11383    192    548  -1278       N  
ATOM   2816  CA  LEU A 302      -2.437 -31.538 -46.025  1.00101.00           C  
ANISOU 2816  CA  LEU A 302    15429  11571  11373    307    581  -1294       C  
ATOM   2817  C   LEU A 302      -2.436 -32.819 -45.196  1.00104.57           C  
ANISOU 2817  C   LEU A 302    15811  12070  11852    300    670  -1274       C  
ATOM   2818  O   LEU A 302      -2.440 -32.766 -43.965  1.00104.92           O  
ANISOU 2818  O   LEU A 302    15940  12093  11831    357    680  -1271       O  
ATOM   2819  CB  LEU A 302      -3.872 -31.070 -46.224  1.00101.51           C  
ANISOU 2819  CB  LEU A 302    15477  11682  11409    433    630  -1326       C  
ATOM   2820  CG  LEU A 302      -4.567 -30.616 -44.978  1.00107.54           C  
ANISOU 2820  CG  LEU A 302    16397  12404  12060    582    613  -1353       C  
ATOM   2821  CD1 LEU A 302      -5.533 -29.504 -45.302  1.00108.76           C  
ANISOU 2821  CD1 LEU A 302    16646  12514  12164    674    550  -1380       C  
ATOM   2822  CD2 LEU A 302      -5.241 -31.790 -44.268  1.00109.96           C  
ANISOU 2822  CD2 LEU A 302    16623  12819  12338    682    736  -1353       C  
ATOM   2823  N   CYS A 303      -2.447 -33.973 -45.878  1.00 99.54           N  
ANISOU 2823  N   CYS A 303    15033  11487  11301    232    732  -1261       N  
ATOM   2824  CA  CYS A 303      -2.433 -35.271 -45.236  1.00 99.20           C  
ANISOU 2824  CA  CYS A 303    14940  11465  11286    213    809  -1235       C  
ATOM   2825  C   CYS A 303      -1.026 -35.593 -44.804  1.00 99.28           C  
ANISOU 2825  C   CYS A 303    14993  11435  11295    166    758  -1205       C  
ATOM   2826  O   CYS A 303      -0.853 -36.112 -43.690  1.00 99.88           O  
ANISOU 2826  O   CYS A 303    15110  11501  11341    191    788  -1180       O  
ATOM   2827  CB  CYS A 303      -2.997 -36.351 -46.146  1.00100.25           C  
ANISOU 2827  CB  CYS A 303    14942  11648  11500    158    879  -1238       C  
ATOM   2828  SG  CYS A 303      -4.797 -36.296 -46.316  1.00105.27           S  
ANISOU 2828  SG  CYS A 303    15493  12381  12124    205    960  -1254       S  
ATOM   2829  N   ILE A 304      -0.023 -35.287 -45.680  1.00 91.31           N  
ANISOU 2829  N   ILE A 304    13964  10423  10308     98    682  -1200       N  
ATOM   2830  CA  ILE A 304       1.402 -35.507 -45.408  1.00 89.80           C  
ANISOU 2830  CA  ILE A 304    13784  10236  10103     51    623  -1164       C  
ATOM   2831  C   ILE A 304       1.806 -34.711 -44.167  1.00 96.74           C  
ANISOU 2831  C   ILE A 304    14791  11074  10892     71    560  -1151       C  
ATOM   2832  O   ILE A 304       2.481 -35.243 -43.280  1.00 96.72           O  
ANISOU 2832  O   ILE A 304    14807  11080  10864     77    558  -1119       O  
ATOM   2833  CB  ILE A 304       2.288 -35.140 -46.621  1.00 91.39           C  
ANISOU 2833  CB  ILE A 304    13924  10477  10322    -28    553  -1154       C  
ATOM   2834  CG1 ILE A 304       2.018 -36.053 -47.820  1.00 91.19           C  
ANISOU 2834  CG1 ILE A 304    13780  10495  10374    -39    614  -1173       C  
ATOM   2835  CG2 ILE A 304       3.770 -35.152 -46.248  1.00 91.32           C  
ANISOU 2835  CG2 ILE A 304    13914  10510  10273    -76    481  -1106       C  
ATOM   2836  CD1 ILE A 304       2.409 -35.449 -49.144  1.00 98.10           C  
ANISOU 2836  CD1 ILE A 304    14599  11418  11257   -101    559  -1174       C  
ATOM   2837  N   ALA A 305       1.370 -33.436 -44.111  1.00 95.05           N  
ANISOU 2837  N   ALA A 305    14681  10811  10622     89    503  -1178       N  
ATOM   2838  CA  ALA A 305       1.667 -32.524 -43.014  1.00 95.29           C  
ANISOU 2838  CA  ALA A 305    14871  10782  10553    108    427  -1181       C  
ATOM   2839  C   ALA A 305       1.028 -33.001 -41.710  1.00 99.38           C  
ANISOU 2839  C   ALA A 305    15432  11299  11028    209    504  -1188       C  
ATOM   2840  O   ALA A 305       1.684 -32.935 -40.675  1.00100.04           O  
ANISOU 2840  O   ALA A 305    15597  11367  11046    207    461  -1170       O  
ATOM   2841  CB  ALA A 305       1.210 -31.114 -43.351  1.00 96.05           C  
ANISOU 2841  CB  ALA A 305    15094  10804  10596    126    353  -1216       C  
ATOM   2842  N   LEU A 306      -0.211 -33.523 -41.760  1.00 95.25           N  
ANISOU 2842  N   LEU A 306    14844  10811  10535    286    616  -1204       N  
ATOM   2843  CA  LEU A 306      -0.914 -34.011 -40.567  1.00 95.75           C  
ANISOU 2843  CA  LEU A 306    14930  10900  10550    374    701  -1198       C  
ATOM   2844  C   LEU A 306      -0.107 -35.096 -39.823  1.00101.15           C  
ANISOU 2844  C   LEU A 306    15592  11597  11244    337    722  -1147       C  
ATOM   2845  O   LEU A 306      -0.042 -35.082 -38.591  1.00100.31           O  
ANISOU 2845  O   LEU A 306    15569  11486  11057    388    727  -1134       O  
ATOM   2846  CB  LEU A 306      -2.313 -34.539 -40.935  1.00 95.19           C  
ANISOU 2846  CB  LEU A 306    14750  10900  10516    421    817  -1206       C  
ATOM   2847  CG  LEU A 306      -3.438 -33.523 -40.895  1.00 98.53           C  
ANISOU 2847  CG  LEU A 306    15220  11348  10871    539    828  -1249       C  
ATOM   2848  CD1 LEU A 306      -4.705 -34.125 -41.452  1.00 97.95           C  
ANISOU 2848  CD1 LEU A 306    14993  11381  10840    556    934  -1244       C  
ATOM   2849  CD2 LEU A 306      -3.647 -32.988 -39.479  1.00 99.63           C  
ANISOU 2849  CD2 LEU A 306    15493  11479  10882    656    830  -1261       C  
ATOM   2850  N   GLY A 307       0.526 -35.984 -40.592  1.00 99.03           N  
ANISOU 2850  N   GLY A 307    15223  11344  11062    262    729  -1120       N  
ATOM   2851  CA  GLY A 307       1.387 -37.041 -40.074  1.00 99.09           C  
ANISOU 2851  CA  GLY A 307    15211  11359  11080    245    740  -1069       C  
ATOM   2852  C   GLY A 307       2.602 -36.460 -39.380  1.00102.83           C  
ANISOU 2852  C   GLY A 307    15761  11829  11479    228    635  -1050       C  
ATOM   2853  O   GLY A 307       2.940 -36.873 -38.269  1.00103.10           O  
ANISOU 2853  O   GLY A 307    15844  11869  11459    261    641  -1016       O  
ATOM   2854  N   TYR A 308       3.232 -35.449 -40.015  1.00 98.27           N  
ANISOU 2854  N   TYR A 308    15200  11248  10888    164    531  -1066       N  
ATOM   2855  CA  TYR A 308       4.381 -34.750 -39.464  1.00 97.96           C  
ANISOU 2855  CA  TYR A 308    15233  11216  10769    109    411  -1045       C  
ATOM   2856  C   TYR A 308       3.993 -34.061 -38.159  1.00102.13           C  
ANISOU 2856  C   TYR A 308    15922  11693  11191    166    387  -1068       C  
ATOM   2857  O   TYR A 308       4.761 -34.114 -37.195  1.00102.44           O  
ANISOU 2857  O   TYR A 308    16013  11751  11158    156    334  -1038       O  
ATOM   2858  CB  TYR A 308       4.925 -33.733 -40.473  1.00 99.02           C  
ANISOU 2858  CB  TYR A 308    15366  11350  10905      6    307  -1052       C  
ATOM   2859  CG  TYR A 308       5.910 -34.291 -41.473  1.00101.42           C  
ANISOU 2859  CG  TYR A 308    15520  11749  11266    -66    290  -1010       C  
ATOM   2860  CD1 TYR A 308       7.192 -34.667 -41.085  1.00103.97           C  
ANISOU 2860  CD1 TYR A 308    15790  12164  11551   -104    235   -953       C  
ATOM   2861  CD2 TYR A 308       5.594 -34.358 -42.830  1.00102.47           C  
ANISOU 2861  CD2 TYR A 308    15562  11899  11475    -89    321  -1027       C  
ATOM   2862  CE1 TYR A 308       8.118 -35.161 -42.008  1.00106.47           C  
ANISOU 2862  CE1 TYR A 308    15956  12596  11900   -145    223   -913       C  
ATOM   2863  CE2 TYR A 308       6.512 -34.855 -43.766  1.00103.95           C  
ANISOU 2863  CE2 TYR A 308    15610  12188  11697   -139    308   -992       C  
ATOM   2864  CZ  TYR A 308       7.780 -35.241 -43.352  1.00114.33           C  
ANISOU 2864  CZ  TYR A 308    16868  13604  12968   -161    261   -935       C  
ATOM   2865  OH  TYR A 308       8.706 -35.710 -44.260  1.00114.79           O  
ANISOU 2865  OH  TYR A 308    16780  13793  13042   -185    252   -898       O  
ATOM   2866  N   ILE A 309       2.775 -33.456 -38.121  1.00 98.23           N  
ANISOU 2866  N   ILE A 309    15500  11148  10676    241    428  -1121       N  
ATOM   2867  CA  ILE A 309       2.218 -32.735 -36.963  1.00 98.06           C  
ANISOU 2867  CA  ILE A 309    15640  11081  10538    333    418  -1157       C  
ATOM   2868  C   ILE A 309       2.102 -33.681 -35.768  1.00101.02           C  
ANISOU 2868  C   ILE A 309    16005  11503  10876    397    497  -1122       C  
ATOM   2869  O   ILE A 309       2.528 -33.303 -34.683  1.00100.71           O  
ANISOU 2869  O   ILE A 309    16087  11449  10731    417    439  -1124       O  
ATOM   2870  CB  ILE A 309       0.854 -32.033 -37.292  1.00100.58           C  
ANISOU 2870  CB  ILE A 309    16005  11369  10841    436    466  -1217       C  
ATOM   2871  CG1 ILE A 309       1.078 -30.804 -38.200  1.00 99.93           C  
ANISOU 2871  CG1 ILE A 309    16008  11208  10753    383    353  -1251       C  
ATOM   2872  CG2 ILE A 309       0.099 -31.610 -36.019  1.00101.80           C  
ANISOU 2872  CG2 ILE A 309    16295  11515  10869    578    498  -1252       C  
ATOM   2873  CD1 ILE A 309      -0.039 -30.504 -39.151  1.00100.04           C  
ANISOU 2873  CD1 ILE A 309    15975  11225  10812    451    408  -1284       C  
ATOM   2874  N   ASN A 310       1.573 -34.904 -35.968  1.00 97.46           N  
ANISOU 2874  N   ASN A 310    15424  11103  10505    417    619  -1087       N  
ATOM   2875  CA  ASN A 310       1.402 -35.845 -34.865  1.00 98.42           C  
ANISOU 2875  CA  ASN A 310    15545  11261  10588    467    697  -1041       C  
ATOM   2876  C   ASN A 310       2.736 -36.256 -34.234  1.00105.44           C  
ANISOU 2876  C   ASN A 310    16455  12160  11445    427    626   -990       C  
ATOM   2877  O   ASN A 310       2.790 -36.400 -33.019  1.00105.82           O  
ANISOU 2877  O   ASN A 310    16580  12225  11404    478    634   -968       O  
ATOM   2878  CB  ASN A 310       0.622 -37.088 -35.288  1.00 98.88           C  
ANISOU 2878  CB  ASN A 310    15479  11352  10737    464    825  -1005       C  
ATOM   2879  CG  ASN A 310       0.293 -38.030 -34.151  1.00127.60           C  
ANISOU 2879  CG  ASN A 310    19132  15022  14328    504    910   -946       C  
ATOM   2880  OD1 ASN A 310       0.858 -39.131 -34.054  1.00128.24           O  
ANISOU 2880  OD1 ASN A 310    19181  15094  14450    472    928   -887       O  
ATOM   2881  ND2 ASN A 310      -0.594 -37.605 -33.245  1.00115.59           N  
ANISOU 2881  ND2 ASN A 310    17669  13544  12707    586    960   -958       N  
ATOM   2882  N   SER A 311       3.799 -36.438 -35.029  1.00103.40           N  
ANISOU 2882  N   SER A 311    16124  11914  11248    347    559   -969       N  
ATOM   2883  CA  SER A 311       5.075 -36.884 -34.468  1.00103.94           C  
ANISOU 2883  CA  SER A 311    16185  12028  11280    324    495   -912       C  
ATOM   2884  C   SER A 311       5.948 -35.727 -33.939  1.00107.76           C  
ANISOU 2884  C   SER A 311    16767  12519  11657    267    350   -926       C  
ATOM   2885  O   SER A 311       6.765 -35.952 -33.046  1.00107.79           O  
ANISOU 2885  O   SER A 311    16798  12570  11587    267    298   -883       O  
ATOM   2886  CB  SER A 311       5.848 -37.710 -35.488  1.00107.89           C  
ANISOU 2886  CB  SER A 311    16548  12572  11874    286    496   -875       C  
ATOM   2887  OG  SER A 311       5.320 -39.026 -35.546  1.00117.83           O  
ANISOU 2887  OG  SER A 311    17760  13812  13197    342    611   -846       O  
ATOM   2888  N   SER A 312       5.780 -34.512 -34.474  1.00103.75           N  
ANISOU 2888  N   SER A 312    16326  11962  11134    212    277   -980       N  
ATOM   2889  CA  SER A 312       6.576 -33.376 -34.028  1.00103.97           C  
ANISOU 2889  CA  SER A 312    16477  11973  11055    130    125   -993       C  
ATOM   2890  C   SER A 312       5.893 -32.628 -32.846  1.00108.49           C  
ANISOU 2890  C   SER A 312    17249  12471  11503    211    111  -1049       C  
ATOM   2891  O   SER A 312       6.607 -32.103 -31.995  1.00109.06           O  
ANISOU 2891  O   SER A 312    17434  12541  11461    165      1  -1047       O  
ATOM   2892  CB  SER A 312       6.882 -32.441 -35.195  1.00106.64           C  
ANISOU 2892  CB  SER A 312    16811  12281  11425     13     34  -1012       C  
ATOM   2893  OG  SER A 312       5.717 -31.841 -35.737  1.00112.25           O  
ANISOU 2893  OG  SER A 312    17586  12900  12164     68     80  -1076       O  
ATOM   2894  N   LEU A 313       4.537 -32.698 -32.716  1.00104.62           N  
ANISOU 2894  N   LEU A 313    16789  11943  11020    338    229  -1091       N  
ATOM   2895  CA  LEU A 313       3.769 -32.040 -31.634  1.00104.93           C  
ANISOU 2895  CA  LEU A 313    17006  11936  10929    454    238  -1148       C  
ATOM   2896  C   LEU A 313       3.567 -32.916 -30.388  1.00109.60           C  
ANISOU 2896  C   LEU A 313    17591  12594  11457    543    323  -1109       C  
ATOM   2897  O   LEU A 313       3.471 -32.363 -29.298  1.00109.32           O  
ANISOU 2897  O   LEU A 313    17714  12541  11283    609    286  -1143       O  
ATOM   2898  CB  LEU A 313       2.395 -31.560 -32.133  1.00104.47           C  
ANISOU 2898  CB  LEU A 313    16971  11838  10886    563    318  -1209       C  
ATOM   2899  CG  LEU A 313       2.069 -30.064 -32.000  1.00109.33           C  
ANISOU 2899  CG  LEU A 313    17808  12344  11390    617    222  -1295       C  
ATOM   2900  CD1 LEU A 313       3.040 -29.181 -32.786  1.00109.30           C  
ANISOU 2900  CD1 LEU A 313    17876  12253  11402    457     60  -1301       C  
ATOM   2901  CD2 LEU A 313       0.664 -29.787 -32.461  1.00110.61           C  
ANISOU 2901  CD2 LEU A 313    17956  12506  11564    761    322  -1342       C  
ATOM   2902  N   ASN A 314       3.493 -34.258 -30.536  1.00107.35           N  
ANISOU 2902  N   ASN A 314    17145  12378  11265    547    432  -1039       N  
ATOM   2903  CA  ASN A 314       3.337 -35.185 -29.400  1.00108.74           C  
ANISOU 2903  CA  ASN A 314    17318  12613  11386    616    513   -983       C  
ATOM   2904  C   ASN A 314       4.476 -35.038 -28.360  1.00115.87           C  
ANISOU 2904  C   ASN A 314    18312  13538  12177    589    402   -958       C  
ATOM   2905  O   ASN A 314       4.136 -34.982 -27.173  1.00117.91           O  
ANISOU 2905  O   ASN A 314    18672  13817  12312    672    426   -961       O  
ATOM   2906  CB  ASN A 314       3.216 -36.652 -29.842  1.00108.53           C  
ANISOU 2906  CB  ASN A 314    17134  12624  11479    601    623   -906       C  
ATOM   2907  CG  ASN A 314       1.808 -37.131 -30.157  1.00128.65           C  
ANISOU 2907  CG  ASN A 314    19614  15188  14079    649    769   -906       C  
ATOM   2908  OD1 ASN A 314       0.882 -36.327 -30.266  1.00121.98           O  
ANISOU 2908  OD1 ASN A 314    18681  14360  13306    632    858   -843       O  
ATOM   2909  ND2 ASN A 314       1.591 -38.440 -30.286  1.00120.60           N  
ANISOU 2909  ND2 ASN A 314    18636  14166  13020    709    791   -974       N  
ATOM   2910  N   PRO A 315       5.792 -34.929 -28.723  1.00111.97           N  
ANISOU 2910  N   PRO A 315    17781  13060  11702    477    278   -931       N  
ATOM   2911  CA  PRO A 315       6.817 -34.742 -27.680  1.00112.59           C  
ANISOU 2911  CA  PRO A 315    17939  13184  11658    447    165   -904       C  
ATOM   2912  C   PRO A 315       6.815 -33.321 -27.117  1.00116.55           C  
ANISOU 2912  C   PRO A 315    18646  13619  12020    426     45   -986       C  
ATOM   2913  O   PRO A 315       7.033 -33.150 -25.921  1.00116.87           O  
ANISOU 2913  O   PRO A 315    18805  13678  11923    461      0   -989       O  
ATOM   2914  CB  PRO A 315       8.138 -35.041 -28.406  1.00114.01           C  
ANISOU 2914  CB  PRO A 315    17984  13432  11901    332     77   -846       C  
ATOM   2915  CG  PRO A 315       7.762 -35.536 -29.762  1.00117.43           C  
ANISOU 2915  CG  PRO A 315    18275  13849  12492    323    161   -842       C  
ATOM   2916  CD  PRO A 315       6.424 -34.965 -30.054  1.00112.71           C  
ANISOU 2916  CD  PRO A 315    17749  13160  11914    374    234   -917       C  
ATOM   2917  N   VAL A 316       6.560 -32.313 -27.975  1.00112.49           N  
ANISOU 2917  N   VAL A 316    18190  13017  11534    374    -10  -1052       N  
ATOM   2918  CA  VAL A 316       6.533 -30.898 -27.612  1.00113.26           C  
ANISOU 2918  CA  VAL A 316    18518  13013  11504    352   -137  -1137       C  
ATOM   2919  C   VAL A 316       5.382 -30.623 -26.643  1.00119.70           C  
ANISOU 2919  C   VAL A 316    19487  13789  12205    534    -56  -1203       C  
ATOM   2920  O   VAL A 316       5.606 -29.976 -25.626  1.00121.38           O  
ANISOU 2920  O   VAL A 316    19892  13969  12259    554   -146  -1246       O  
ATOM   2921  CB  VAL A 316       6.460 -29.995 -28.868  1.00115.89           C  
ANISOU 2921  CB  VAL A 316    18877  13252  11905    264   -202  -1179       C  
ATOM   2922  CG1 VAL A 316       6.053 -28.574 -28.513  1.00116.56           C  
ANISOU 2922  CG1 VAL A 316    19240  13190  11858    294   -303  -1278       C  
ATOM   2923  CG2 VAL A 316       7.785 -29.994 -29.617  1.00115.43           C  
ANISOU 2923  CG2 VAL A 316    18705  13251  11904     62   -320  -1115       C  
ATOM   2924  N   LEU A 317       4.174 -31.124 -26.932  1.00116.28           N  
ANISOU 2924  N   LEU A 317    18965  13378  11838    664    109  -1207       N  
ATOM   2925  CA  LEU A 317       3.023 -30.882 -26.070  1.00117.50           C  
ANISOU 2925  CA  LEU A 317    19231  13538  11874    849    200  -1261       C  
ATOM   2926  C   LEU A 317       3.123 -31.620 -24.746  1.00124.35           C  
ANISOU 2926  C   LEU A 317    20105  14500  12642    911    252  -1212       C  
ATOM   2927  O   LEU A 317       2.810 -31.019 -23.720  1.00125.28           O  
ANISOU 2927  O   LEU A 317    20402  14608  12592   1019    232  -1269       O  
ATOM   2928  CB  LEU A 317       1.713 -31.227 -26.770  1.00116.66           C  
ANISOU 2928  CB  LEU A 317    18999  13468  11858    951    360  -1265       C  
ATOM   2929  CG  LEU A 317       1.148 -30.113 -27.643  1.00121.30           C  
ANISOU 2929  CG  LEU A 317    19674  13959  12456    990    319  -1349       C  
ATOM   2930  CD1 LEU A 317       0.324 -30.674 -28.752  1.00120.15           C  
ANISOU 2930  CD1 LEU A 317    19329  13864  12458   1002    442  -1322       C  
ATOM   2931  CD2 LEU A 317       0.298 -29.156 -26.836  1.00125.78           C  
ANISOU 2931  CD2 LEU A 317    20450  14493  12846   1183    322  -1441       C  
ATOM   2932  N   TYR A 318       3.586 -32.891 -24.748  1.00122.25           N  
ANISOU 2932  N   TYR A 318    19664  14319  12466    852    312  -1107       N  
ATOM   2933  CA  TYR A 318       3.731 -33.682 -23.515  1.00123.66           C  
ANISOU 2933  CA  TYR A 318    19847  14586  12554    906    360  -1043       C  
ATOM   2934  C   TYR A 318       4.670 -33.002 -22.532  1.00127.17           C  
ANISOU 2934  C   TYR A 318    20463  15017  12838    875    205  -1072       C  
ATOM   2935  O   TYR A 318       4.380 -32.958 -21.338  1.00127.38           O  
ANISOU 2935  O   TYR A 318    20601  15084  12712    976    228  -1082       O  
ATOM   2936  CB  TYR A 318       4.243 -35.108 -23.804  1.00125.25           C  
ANISOU 2936  CB  TYR A 318    19861  14850  12880    843    421   -926       C  
ATOM   2937  CG  TYR A 318       4.122 -36.032 -22.608  1.00129.96           C  
ANISOU 2937  CG  TYR A 318    20460  15528  13391    915    500   -846       C  
ATOM   2938  CD1 TYR A 318       5.099 -36.051 -21.612  1.00133.32           C  
ANISOU 2938  CD1 TYR A 318    20963  15993  13699    902    401   -815       C  
ATOM   2939  CD2 TYR A 318       3.029 -36.879 -22.463  1.00131.48           C  
ANISOU 2939  CD2 TYR A 318    20578  15769  13610    984    669   -795       C  
ATOM   2940  CE1 TYR A 318       4.969 -36.865 -20.484  1.00136.05           C  
ANISOU 2940  CE1 TYR A 318    21324  16415  13954    975    472   -738       C  
ATOM   2941  CE2 TYR A 318       2.900 -37.718 -21.352  1.00133.74           C  
ANISOU 2941  CE2 TYR A 318    20878  16130  13809   1038    741   -710       C  
ATOM   2942  CZ  TYR A 318       3.876 -37.713 -20.366  1.00142.13           C  
ANISOU 2942  CZ  TYR A 318    22027  17221  14754   1041    644   -682       C  
ATOM   2943  OH  TYR A 318       3.747 -38.550 -19.276  1.00141.40           O  
ANISOU 2943  OH  TYR A 318    21954  17203  14570   1097    715   -590       O  
ATOM   2944  N   ALA A 319       5.802 -32.501 -23.052  1.00123.31           N  
ANISOU 2944  N   ALA A 319    19986  14487  12380    724     46  -1078       N  
ATOM   2945  CA  ALA A 319       6.873 -31.836 -22.329  1.00123.96           C  
ANISOU 2945  CA  ALA A 319    20209  14564  12326    635   -133  -1096       C  
ATOM   2946  C   ALA A 319       6.393 -30.556 -21.682  1.00128.88           C  
ANISOU 2946  C   ALA A 319    21104  15086  12780    703   -207  -1214       C  
ATOM   2947  O   ALA A 319       6.385 -30.464 -20.457  1.00130.01           O  
ANISOU 2947  O   ALA A 319    21379  15260  12759    778   -225  -1233       O  
ATOM   2948  CB  ALA A 319       8.028 -31.543 -23.275  1.00124.12           C  
ANISOU 2948  CB  ALA A 319    20151  14578  12430    440   -273  -1069       C  
ATOM   2949  N   PHE A 320       5.939 -29.596 -22.486  1.00125.38           N  
ANISOU 2949  N   PHE A 320    20753  14519  12365    696   -243  -1296       N  
ATOM   2950  CA  PHE A 320       5.493 -28.289 -22.013  1.00127.23           C  
ANISOU 2950  CA  PHE A 320    21280  14625  12437    774   -328  -1419       C  
ATOM   2951  C   PHE A 320       4.227 -28.374 -21.126  1.00132.66           C  
ANISOU 2951  C   PHE A 320    22046  15350  13007   1026   -181  -1469       C  
ATOM   2952  O   PHE A 320       3.904 -27.398 -20.442  1.00133.96           O  
ANISOU 2952  O   PHE A 320    22472  15431  12995   1133   -247  -1573       O  
ATOM   2953  CB  PHE A 320       5.307 -27.330 -23.197  1.00128.75           C  
ANISOU 2953  CB  PHE A 320    21546  14673  12702    714   -397  -1479       C  
ATOM   2954  CG  PHE A 320       6.620 -26.826 -23.752  1.00130.58           C  
ANISOU 2954  CG  PHE A 320    21799  14853  12961    455   -592  -1452       C  
ATOM   2955  CD1 PHE A 320       7.402 -27.627 -24.577  1.00132.72           C  
ANISOU 2955  CD1 PHE A 320    21805  15230  13391    302   -582  -1346       C  
ATOM   2956  CD2 PHE A 320       7.090 -25.566 -23.424  1.00134.72           C  
ANISOU 2956  CD2 PHE A 320    22614  15234  13340    361   -789  -1528       C  
ATOM   2957  CE1 PHE A 320       8.631 -27.176 -25.062  1.00134.00           C  
ANISOU 2957  CE1 PHE A 320    21961  15390  13564     61   -758  -1308       C  
ATOM   2958  CE2 PHE A 320       8.312 -25.110 -23.922  1.00138.21           C  
ANISOU 2958  CE2 PHE A 320    23063  15653  13799     91   -973  -1487       C  
ATOM   2959  CZ  PHE A 320       9.077 -25.920 -24.733  1.00134.96           C  
ANISOU 2959  CZ  PHE A 320    22355  15383  13542    -57   -952  -1372       C  
ATOM   2960  N   LEU A 321       3.566 -29.549 -21.074  1.00128.74           N  
ANISOU 2960  N   LEU A 321    21334  14989  12591   1116      9  -1390       N  
ATOM   2961  CA  LEU A 321       2.423 -29.754 -20.189  1.00130.01           C  
ANISOU 2961  CA  LEU A 321    21529  15237  12632   1333    157  -1409       C  
ATOM   2962  C   LEU A 321       2.819 -30.610 -18.954  1.00137.60           C  
ANISOU 2962  C   LEU A 321    22462  16322  13499   1345    190  -1332       C  
ATOM   2963  O   LEU A 321       2.059 -30.645 -17.979  1.00138.37           O  
ANISOU 2963  O   LEU A 321    22630  16499  13446   1514    282  -1350       O  
ATOM   2964  CB  LEU A 321       1.219 -30.354 -20.923  1.00128.76           C  
ANISOU 2964  CB  LEU A 321    21172  15153  12597   1425    348  -1375       C  
ATOM   2965  CG  LEU A 321       0.375 -29.389 -21.762  1.00133.14           C  
ANISOU 2965  CG  LEU A 321    21796  15624  13168   1519    354  -1469       C  
ATOM   2966  CD1 LEU A 321      -0.754 -30.118 -22.452  1.00132.21           C  
ANISOU 2966  CD1 LEU A 321    21447  15618  13170   1585    540  -1418       C  
ATOM   2967  CD2 LEU A 321      -0.212 -28.266 -20.921  1.00137.93           C  
ANISOU 2967  CD2 LEU A 321    22670  16185  13550   1723    320  -1590       C  
ATOM   2968  N   ASP A 322       4.020 -31.256 -18.979  1.00135.61           N  
ANISOU 2968  N   ASP A 322    22111  16097  13316   1179    111  -1245       N  
ATOM   2969  CA  ASP A 322       4.557 -32.030 -17.852  1.00137.16           C  
ANISOU 2969  CA  ASP A 322    22291  16402  13420   1182    115  -1164       C  
ATOM   2970  C   ASP A 322       4.996 -31.055 -16.776  1.00144.22           C  
ANISOU 2970  C   ASP A 322    23445  17259  14091   1205    -33  -1251       C  
ATOM   2971  O   ASP A 322       5.756 -30.133 -17.076  1.00144.06           O  
ANISOU 2971  O   ASP A 322    23553  17134  14048   1082   -212  -1315       O  
ATOM   2972  CB  ASP A 322       5.729 -32.934 -18.285  1.00138.69           C  
ANISOU 2972  CB  ASP A 322    22307  16641  13749   1022     63  -1051       C  
ATOM   2973  CG  ASP A 322       6.346 -33.768 -17.166  1.00155.86           C  
ANISOU 2973  CG  ASP A 322    24461  18929  15829   1034     58   -957       C  
ATOM   2974  OD1 ASP A 322       7.050 -33.185 -16.300  1.00158.02           O1-
ANISOU 2974  OD1 ASP A 322    24887  19213  15941   1005    -83   -992       O1-
ATOM   2975  OD2 ASP A 322       6.168 -35.011 -17.184  1.00163.24           O  
ANISOU 2975  OD2 ASP A 322    25238  19936  16851   1062    185   -846       O  
ATOM   2976  N   LYS A 323       4.533 -31.270 -15.525  1.00143.24           N  
ANISOU 2976  N   LYS A 323    23404  17224  13795   1350     38  -1249       N  
ATOM   2977  CA  LYS A 323       4.807 -30.406 -14.371  1.00145.43           C  
ANISOU 2977  CA  LYS A 323    23947  17478  13831   1405    -85  -1339       C  
ATOM   2978  C   LYS A 323       6.313 -30.282 -14.054  1.00149.59           C  
ANISOU 2978  C   LYS A 323    24524  17998  14316   1214   -291  -1312       C  
ATOM   2979  O   LYS A 323       6.797 -29.154 -13.883  1.00150.35           O  
ANISOU 2979  O   LYS A 323    24847  17984  14295   1146   -472  -1415       O  
ATOM   2980  CB  LYS A 323       4.041 -30.893 -13.125  1.00149.45           C  
ANISOU 2980  CB  LYS A 323    24485  18125  14173   1595     54  -1314       C  
ATOM   2981  CG  LYS A 323       2.545 -30.552 -13.116  1.00162.80           C  
ANISOU 2981  CG  LYS A 323    26213  19843  15802   1814    214  -1382       C  
ATOM   2982  CD  LYS A 323       1.858 -31.096 -11.856  1.00170.09           C  
ANISOU 2982  CD  LYS A 323    27140  20941  16547   1985    356  -1337       C  
ATOM   2983  CE  LYS A 323       0.380 -31.360 -12.043  1.00174.27           C  
ANISOU 2983  CE  LYS A 323    27548  21584  17083   2157    572  -1323       C  
ATOM   2984  NZ  LYS A 323      -0.132 -32.377 -11.080  1.00177.30           N1+
ANISOU 2984  NZ  LYS A 323    27822  22172  17373   2234    733  -1203       N1+
ATOM   2985  N   ASN A 324       7.047 -31.419 -13.995  1.00145.01           N  
ANISOU 2985  N   ASN A 324    23740  17535  13822   1129   -271  -1174       N  
ATOM   2986  CA  ASN A 324       8.483 -31.437 -13.683  1.00145.56           C  
ANISOU 2986  CA  ASN A 324    23807  17651  13848    962   -454  -1127       C  
ATOM   2987  C   ASN A 324       9.312 -30.731 -14.768  1.00148.44           C  
ANISOU 2987  C   ASN A 324    24157  17926  14317    757   -615  -1156       C  
ATOM   2988  O   ASN A 324      10.264 -30.020 -14.441  1.00148.87           O  
ANISOU 2988  O   ASN A 324    24336  17968  14261    613   -816  -1188       O  
ATOM   2989  CB  ASN A 324       8.981 -32.869 -13.472  1.00147.89           C  
ANISOU 2989  CB  ASN A 324    23879  18095  14219    958   -378   -966       C  
ATOM   2990  CG  ASN A 324       8.331 -33.607 -12.314  1.00175.53           C  
ANISOU 2990  CG  ASN A 324    27401  21695  17599   1125   -240   -913       C  
ATOM   2991  OD1 ASN A 324       7.782 -34.706 -12.478  1.00171.13           O  
ANISOU 2991  OD1 ASN A 324    26685  21191  17146   1195    -69   -813       O  
ATOM   2992  ND2 ASN A 324       8.396 -33.041 -11.111  1.00166.59           N  
ANISOU 2992  ND2 ASN A 324    26471  20590  16236   1183   -316   -973       N  
ATOM   2993  N   PHE A 325       8.923 -30.902 -16.045  1.00143.56           N  
ANISOU 2993  N   PHE A 325    23393  17255  13900    734   -531  -1143       N  
ATOM   2994  CA  PHE A 325       9.562 -30.273 -17.207  1.00142.81           C  
ANISOU 2994  CA  PHE A 325    23264  17082  13916    549   -656  -1161       C  
ATOM   2995  C   PHE A 325       9.324 -28.744 -17.203  1.00148.72           C  
ANISOU 2995  C   PHE A 325    24305  17656  14545    517   -791  -1305       C  
ATOM   2996  O   PHE A 325      10.277 -27.980 -17.383  1.00148.85           O  
ANISOU 2996  O   PHE A 325    24413  17627  14516    317   -990  -1324       O  
ATOM   2997  CB  PHE A 325       9.029 -30.906 -18.505  1.00142.21           C  
ANISOU 2997  CB  PHE A 325    22969  16996  14068    568   -508  -1116       C  
ATOM   2998  CG  PHE A 325       9.706 -30.479 -19.789  1.00142.64           C  
ANISOU 2998  CG  PHE A 325    22938  17005  14252    384   -611  -1109       C  
ATOM   2999  CD1 PHE A 325       9.320 -29.314 -20.447  1.00145.88           C  
ANISOU 2999  CD1 PHE A 325    23503  17260  14665    339   -677  -1208       C  
ATOM   3000  CD2 PHE A 325      10.692 -31.265 -20.365  1.00143.72           C  
ANISOU 3000  CD2 PHE A 325    22841  17262  14503    271   -633   -999       C  
ATOM   3001  CE1 PHE A 325       9.924 -28.934 -21.646  1.00146.02           C  
ANISOU 3001  CE1 PHE A 325    23439  17245  14797    161   -767  -1190       C  
ATOM   3002  CE2 PHE A 325      11.287 -30.891 -21.568  1.00146.05           C  
ANISOU 3002  CE2 PHE A 325    23041  17543  14907    107   -715   -986       C  
ATOM   3003  CZ  PHE A 325      10.893 -29.730 -22.204  1.00144.31           C  
ANISOU 3003  CZ  PHE A 325    22972  17170  14690     42   -780  -1078       C  
ATOM   3004  N   LYS A 326       8.052 -28.312 -17.008  1.00146.34           N  
ANISOU 3004  N   LYS A 326    24153  17263  14185    713   -684  -1401       N  
ATOM   3005  CA  LYS A 326       7.617 -26.910 -16.941  1.00147.78           C  
ANISOU 3005  CA  LYS A 326    24648  17263  14238    753   -786  -1548       C  
ATOM   3006  C   LYS A 326       8.522 -26.100 -16.010  1.00155.82           C  
ANISOU 3006  C   LYS A 326    25923  18233  15049    635  -1009  -1605       C  
ATOM   3007  O   LYS A 326       8.853 -24.954 -16.323  1.00155.96           O  
ANISOU 3007  O   LYS A 326    26164  18085  15008    510  -1185  -1686       O  
ATOM   3008  CB  LYS A 326       6.166 -26.834 -16.432  1.00149.98           C  
ANISOU 3008  CB  LYS A 326    25025  17533  14428   1043   -616  -1624       C  
ATOM   3009  CG  LYS A 326       5.090 -26.891 -17.509  1.00150.83           C  
ANISOU 3009  CG  LYS A 326    25016  17605  14689   1151   -464  -1635       C  
ATOM   3010  CD  LYS A 326       3.799 -27.590 -17.025  1.00154.32           C  
ANISOU 3010  CD  LYS A 326    25355  18178  15102   1400   -231  -1618       C  
ATOM   3011  CE  LYS A 326       2.966 -26.820 -16.020  1.00159.05           C  
ANISOU 3011  CE  LYS A 326    26214  18755  15463   1638   -211  -1737       C  
ATOM   3012  NZ  LYS A 326       1.896 -27.666 -15.430  1.00163.67           N1+
ANISOU 3012  NZ  LYS A 326    26651  19527  16007   1842     14  -1685       N1+
ATOM   3013  N   ARG A 327       8.929 -26.727 -14.872  1.00155.08           N  
ANISOU 3013  N   ARG A 327    25800  18283  14840    664  -1007  -1554       N  
ATOM   3014  CA  ARG A 327       9.794 -26.176 -13.828  1.00157.67           C  
ANISOU 3014  CA  ARG A 327    26339  18612  14957    560  -1206  -1592       C  
ATOM   3015  C   ARG A 327      11.169 -25.743 -14.377  1.00163.67           C  
ANISOU 3015  C   ARG A 327    27068  19363  15756    240  -1430  -1548       C  
ATOM   3016  O   ARG A 327      11.549 -24.580 -14.193  1.00165.61           O  
ANISOU 3016  O   ARG A 327    27596  19466  15864    106  -1634  -1640       O  
ATOM   3017  CB  ARG A 327       9.964 -27.191 -12.681  1.00157.34           C  
ANISOU 3017  CB  ARG A 327    26189  18765  14827    654  -1129  -1510       C  
ATOM   3018  N   CYS A 328      11.878 -26.652 -15.100  1.00158.84           N  
ANISOU 3018  N   CYS A 328    26124  18902  15327    118  -1393  -1407       N  
ATOM   3019  CA  CYS A 328      13.210 -26.416 -15.684  1.00158.79           C  
ANISOU 3019  CA  CYS A 328    26011  18956  15365   -178  -1579  -1336       C  
ATOM   3020  C   CYS A 328      13.128 -25.533 -16.950  1.00161.26           C  
ANISOU 3020  C   CYS A 328    26389  19102  15779   -320  -1650  -1381       C  
ATOM   3021  O   CYS A 328      13.838 -25.767 -17.933  1.00159.99           O  
ANISOU 3021  O   CYS A 328    26009  19023  15756   -498  -1688  -1290       O  
ATOM   3022  CB  CYS A 328      13.902 -27.742 -15.986  1.00157.91           C  
ANISOU 3022  CB  CYS A 328    25527  19077  15396   -200  -1494  -1176       C  
ATOM   3023  SG  CYS A 328      14.287 -28.731 -14.519  1.00162.74           S  
ANISOU 3023  SG  CYS A 328    26065  19884  15883    -55  -1435  -1099       S  
ATOM   3024  N   PHE A 329      12.284 -24.497 -16.893  1.00157.63           N  
ANISOU 3024  N   PHE A 329    26243  18415  15235   -233  -1674  -1520       N  
ATOM   3025  CA  PHE A 329      12.053 -23.545 -17.965  1.00167.37           C  
ANISOU 3025  CA  PHE A 329    27607  19453  16533   -332  -1745  -1578       C  
ATOM   3026  C   PHE A 329      11.836 -22.152 -17.335  1.00174.40           C  
ANISOU 3026  C   PHE A 329    28955  20105  17206   -340  -1918  -1729       C  
ATOM   3027  O   PHE A 329      12.403 -21.826 -16.281  1.00122.12           O  
ANISOU 3027  O   PHE A 329    22515  13493  10391   -415  -2067  -1762       O  
ATOM   3028  CB  PHE A 329      10.843 -23.997 -18.814  1.00166.95           C  
ANISOU 3028  CB  PHE A 329    27414  19364  16655   -111  -1511  -1585       C  
ATOM   3029  CG  PHE A 329      10.914 -23.707 -20.296  1.00167.39           C  
ANISOU 3029  CG  PHE A 329    27367  19351  16885   -245  -1524  -1554       C  
ATOM   3030  CD1 PHE A 329      11.688 -24.496 -21.140  1.00169.06           C  
ANISOU 3030  CD1 PHE A 329    27241  19731  17263   -399  -1500  -1422       C  
ATOM   3031  CD2 PHE A 329      10.162 -22.681 -20.859  1.00170.14           C  
ANISOU 3031  CD2 PHE A 329    27952  19472  17222   -191  -1550  -1655       C  
ATOM   3032  CE1 PHE A 329      11.741 -24.233 -22.516  1.00168.99           C  
ANISOU 3032  CE1 PHE A 329    27134  19671  17403   -518  -1506  -1393       C  
ATOM   3033  CE2 PHE A 329      10.217 -22.417 -22.234  1.00171.79           C  
ANISOU 3033  CE2 PHE A 329    28067  19621  17585   -314  -1562  -1620       C  
ATOM   3034  CZ  PHE A 329      11.013 -23.189 -23.051  1.00168.40           C  
ANISOU 3034  CZ  PHE A 329    27300  19369  17316   -485  -1540  -1489       C  
TER    3035      PHE A 329                                                      
ATOM   3036  N   LEU B1003      -1.640 -23.418  -7.419  1.00202.98           N  
ANISOU 3036  N   LEU B1003    36221  20473  20430   3355    167    304       N  
ATOM   3037  CA  LEU B1003      -1.313 -24.833  -7.559  1.00203.91           C  
ANISOU 3037  CA  LEU B1003    36477  20500  20499   3517    283    360       C  
ATOM   3038  C   LEU B1003      -2.143 -25.462  -8.679  1.00206.98           C  
ANISOU 3038  C   LEU B1003    36695  20852  21096   3346    584    319       C  
ATOM   3039  O   LEU B1003      -3.320 -25.132  -8.837  1.00205.50           O  
ANISOU 3039  O   LEU B1003    36487  20590  21005   3147    810    266       O  
ATOM   3040  CB  LEU B1003      -1.535 -25.580  -6.226  1.00205.97           C  
ANISOU 3040  CB  LEU B1003    37203  20534  20524   3685    417    422       C  
ATOM   3041  CG  LEU B1003      -0.849 -26.946  -6.067  1.00209.40           C  
ANISOU 3041  CG  LEU B1003    37164  21195  21202   3701    412    497       C  
ATOM   3042  CD1 LEU B1003       0.588 -26.795  -5.589  1.00210.31           C  
ANISOU 3042  CD1 LEU B1003    37090  21538  21281   3856     39    565       C  
ATOM   3043  CD2 LEU B1003      -1.600 -27.819  -5.086  1.00210.64           C  
ANISOU 3043  CD2 LEU B1003    37186  21343  21503   3589    653    525       C  
ATOM   3044  N   GLU B1004      -1.509 -26.354  -9.463  1.00203.92           N  
ANISOU 3044  N   GLU B1004    36181  20521  20779   3425    580    342       N  
ATOM   3045  CA  GLU B1004      -2.105 -27.083 -10.585  1.00202.72           C  
ANISOU 3045  CA  GLU B1004    35879  20342  20805   3280    836    304       C  
ATOM   3046  C   GLU B1004      -3.202 -28.022 -10.085  1.00207.59           C  
ANISOU 3046  C   GLU B1004    36855  20676  21342   3257   1216    305       C  
ATOM   3047  O   GLU B1004      -4.301 -28.044 -10.647  1.00205.95           O  
ANISOU 3047  O   GLU B1004    36553  20419  21279   3033   1461    242       O  
ATOM   3048  CB  GLU B1004      -1.022 -27.873 -11.341  1.00204.49           C  
ANISOU 3048  CB  GLU B1004    35958  20664  21074   3417    736    341       C  
ATOM   3049  N   ASP B1005      -2.902 -28.764  -8.999  1.00206.42           N  
ANISOU 3049  N   ASP B1005    37122  20346  20962   3490   1259    379       N  
ATOM   3050  CA  ASP B1005      -3.803 -29.714  -8.356  1.00206.32           C  
ANISOU 3050  CA  ASP B1005    37183  20198  21010   3409   1568    384       C  
ATOM   3051  C   ASP B1005      -5.017 -28.998  -7.745  1.00208.23           C  
ANISOU 3051  C   ASP B1005    37241  20476  21403   3163   1686    330       C  
ATOM   3052  O   ASP B1005      -6.136 -29.489  -7.899  1.00207.66           O  
ANISOU 3052  O   ASP B1005    37229  20259  21413   3013   2005    287       O  
ATOM   3053  CB  ASP B1005      -3.057 -30.539  -7.288  1.00208.12           C  
ANISOU 3053  CB  ASP B1005    37149  20597  21329   3507   1433    466       C  
ATOM   3054  CG  ASP B1005      -1.917 -31.401  -7.817  1.00216.23           C  
ANISOU 3054  CG  ASP B1005    37166  22135  22855   3373   1198    498       C  
ATOM   3055  OD1 ASP B1005      -2.067 -31.980  -8.919  1.00216.61           O  
ANISOU 3055  OD1 ASP B1005    37163  22145  22995   3319   1339    461       O  
ATOM   3056  OD2 ASP B1005      -0.894 -31.529  -7.110  1.00220.96           O1-
ANISOU 3056  OD2 ASP B1005    37169  23096  23689   3343    918    570       O1-
ATOM   3057  N   ASN B1006      -4.800 -27.827  -7.094  1.00205.69           N  
ANISOU 3057  N   ASN B1006    37250  20073  20829   3278   1517    343       N  
ATOM   3058  CA  ASN B1006      -5.860 -27.018  -6.476  1.00205.05           C  
ANISOU 3058  CA  ASN B1006    37280  19894  20737   3144   1656    305       C  
ATOM   3059  C   ASN B1006      -6.817 -26.451  -7.542  1.00206.57           C  
ANISOU 3059  C   ASN B1006    37318  20079  21091   2912   1820    228       C  
ATOM   3060  O   ASN B1006      -8.032 -26.559  -7.373  1.00205.86           O  
ANISOU 3060  O   ASN B1006    37300  19848  21070   2766   2124    195       O  
ATOM   3061  CB  ASN B1006      -5.274 -25.884  -5.615  1.00206.45           C  
ANISOU 3061  CB  ASN B1006    37314  20251  20876   3175   1335    320       C  
ATOM   3062  CG  ASN B1006      -5.051 -26.221  -4.150  1.00224.73           C  
ANISOU 3062  CG  ASN B1006    37430  23661  24296   2626   1015    327       C  
ATOM   3063  OD1 ASN B1006      -5.887 -26.845  -3.478  1.00221.54           O  
ANISOU 3063  OD1 ASN B1006    37398  23003  23774   2668   1264    332       O  
ATOM   3064  ND2 ASN B1006      -3.950 -25.733  -3.595  1.00219.61           N  
ANISOU 3064  ND2 ASN B1006    37383  22849  23210   2913    801    389       N  
ATOM   3065  N   TRP B1007      -6.269 -25.890  -8.647  1.00201.31           N  
ANISOU 3065  N   TRP B1007    36262  19650  20578   2837   1599    197       N  
ATOM   3066  CA  TRP B1007      -7.021 -25.338  -9.784  1.00198.98           C  
ANISOU 3066  CA  TRP B1007    35574  19487  20543   2576   1671    126       C  
ATOM   3067  C   TRP B1007      -7.876 -26.431 -10.440  1.00203.12           C  
ANISOU 3067  C   TRP B1007    36100  19895  21181   2450   2001     93       C  
ATOM   3068  O   TRP B1007      -8.979 -26.144 -10.913  1.00201.66           O  
ANISOU 3068  O   TRP B1007    35750  19710  21162   2232   2184     38       O  
ATOM   3069  CB  TRP B1007      -6.061 -24.705 -10.807  1.00196.00           C  
ANISOU 3069  CB  TRP B1007    34785  19392  20293   2550   1353    110       C  
ATOM   3070  N   GLU B1008      -7.379 -27.691 -10.420  1.00201.00           N  
ANISOU 3070  N   GLU B1008    36034  19520  20817   2590   2080    129       N  
ATOM   3071  CA  GLU B1008      -8.078 -28.864 -10.946  1.00201.17           C  
ANISOU 3071  CA  GLU B1008    36121  19401  20912   2487   2400     99       C  
ATOM   3072  C   GLU B1008      -9.295 -29.197 -10.064  1.00206.10           C  
ANISOU 3072  C   GLU B1008    37066  19764  21477   2424   2747     90       C  
ATOM   3073  O   GLU B1008     -10.401 -29.281 -10.601  1.00205.25           O  
ANISOU 3073  O   GLU B1008    36821  19627  21537   2193   2981     26       O  
ATOM   3074  CB  GLU B1008      -7.132 -30.069 -11.064  1.00203.74           C  
ANISOU 3074  CB  GLU B1008    36613  19667  21132   2682   2389    148       C  
ATOM   3075  N   THR B1009      -9.102 -29.308  -8.715  1.00203.73           N  
ANISOU 3075  N   THR B1009    37172  19289  20946   2620   2768    153       N  
ATOM   3076  CA  THR B1009     -10.147 -29.599  -7.709  1.00203.04           C  
ANISOU 3076  CA  THR B1009    37120  19097  20927   2528   3008    144       C  
ATOM   3077  C   THR B1009     -11.257 -28.542  -7.744  1.00204.49           C  
ANISOU 3077  C   THR B1009    37128  19313  21257   2319   3103     90       C  
ATOM   3078  O   THR B1009     -12.432 -28.882  -7.591  1.00203.73           O  
ANISOU 3078  O   THR B1009    37049  19092  21265   2166   3411     53       O  
ATOM   3079  CB  THR B1009      -9.547 -29.684  -6.287  1.00208.08           C  
ANISOU 3079  CB  THR B1009    37178  20103  21782   2563   2675    189       C  
ATOM   3080  OG1 THR B1009      -8.256 -30.293  -6.326  1.00208.35           O  
ANISOU 3080  OG1 THR B1009    37187  20233  21744   2746   2459    248       O  
ATOM   3081  CG2 THR B1009     -10.444 -30.442  -5.312  1.00207.11           C  
ANISOU 3081  CG2 THR B1009    37115  19860  21717   2508   2922    188       C  
ATOM   3082  N   LEU B1010     -10.871 -27.267  -7.948  1.00200.90           N  
ANISOU 3082  N   LEU B1010    36711  18917  20707   2358   2896     94       N  
ATOM   3083  CA  LEU B1010     -11.770 -26.119  -8.034  1.00199.78           C  
ANISOU 3083  CA  LEU B1010    36352  18842  20713   2179   2935     52       C  
ATOM   3084  C   LEU B1010     -12.741 -26.260  -9.197  1.00202.84           C  
ANISOU 3084  C   LEU B1010    36391  19306  21372   1920   3115    -16       C  
ATOM   3085  O   LEU B1010     -13.929 -25.983  -9.045  1.00202.46           O  
ANISOU 3085  O   LEU B1010    36315  19176  21433   1770   3356    -46       O  
ATOM   3086  CB  LEU B1010     -10.954 -24.821  -8.195  1.00198.48           C  
ANISOU 3086  CB  LEU B1010    35946  18913  20555   2218   2554     58       C  
ATOM   3087  CG  LEU B1010     -10.426 -24.186  -6.912  1.00204.46           C  
ANISOU 3087  CG  LEU B1010    37009  19599  21076   2396   2400    105       C  
ATOM   3088  CD1 LEU B1010      -9.202 -23.338  -7.191  1.00203.73           C  
ANISOU 3088  CD1 LEU B1010    36700  19747  20961   2472   1980    114       C  
ATOM   3089  CD2 LEU B1010     -11.499 -23.358  -6.228  1.00207.02           C  
ANISOU 3089  CD2 LEU B1010    37310  19870  21477   2279   2558     86       C  
ATOM   3090  N   ASN B1011     -12.231 -26.702 -10.353  1.00198.50           N  
ANISOU 3090  N   ASN B1011    35580  18912  20928   1870   2998    -41       N  
ATOM   3091  CA  ASN B1011     -13.014 -26.868 -11.569  1.00197.28           C  
ANISOU 3091  CA  ASN B1011    35087  18856  21016   1625   3119   -109       C  
ATOM   3092  C   ASN B1011     -13.726 -28.231 -11.608  1.00201.73           C  
ANISOU 3092  C   ASN B1011    35844  19212  21592   1544   3471   -138       C  
ATOM   3093  O   ASN B1011     -14.757 -28.345 -12.273  1.00200.52           O  
ANISOU 3093  O   ASN B1011    35484  19077  21628   1313   3657   -200       O  
ATOM   3094  CB  ASN B1011     -12.123 -26.668 -12.807  1.00198.52           C  
ANISOU 3094  CB  ASN B1011    34890  19271  21269   1603   2833   -125       C  
ATOM   3095  CG  ASN B1011     -11.475 -25.293 -12.901  1.00222.08           C  
ANISOU 3095  CG  ASN B1011    37397  22595  24390   1608   2434   -114       C  
ATOM   3096  OD1 ASN B1011     -12.098 -24.254 -12.663  1.00215.62           O  
ANISOU 3096  OD1 ASN B1011    36724  21685  23518   1567   2499   -116       O  
ATOM   3097  ND2 ASN B1011     -10.206 -25.250 -13.271  1.00215.76           N  
ANISOU 3097  ND2 ASN B1011    36753  21808  23417   1771   2223    -84       N  
ATOM   3098  N   ASP B1012     -13.197 -29.243 -10.885  1.00200.26           N  
ANISOU 3098  N   ASP B1012    36056  18829  21203   1729   3564    -92       N  
ATOM   3099  CA  ASP B1012     -13.753 -30.603 -10.819  1.00201.84           C  
ANISOU 3099  CA  ASP B1012    36506  18801  21384   1677   3908   -113       C  
ATOM   3100  C   ASP B1012     -15.090 -30.636 -10.068  1.00205.31           C  
ANISOU 3100  C   ASP B1012    36810  19202  21997   1519   4134   -145       C  
ATOM   3101  O   ASP B1012     -16.054 -31.220 -10.569  1.00205.25           O  
ANISOU 3101  O   ASP B1012    36699  19142  22145   1308   4385   -209       O  
ATOM   3102  CB  ASP B1012     -12.758 -31.577 -10.165  1.00204.18           C  
ANISOU 3102  CB  ASP B1012    36928  19086  21566   1902   3799    -53       C  
ATOM   3103  N   ASN B1013     -15.144 -30.016  -8.872  1.00202.43           N  
ANISOU 3103  N   ASN B1013    36800  18672  21443   1663   4181    -90       N  
ATOM   3104  CA  ASN B1013     -16.358 -29.945  -8.051  1.00202.07           C  
ANISOU 3104  CA  ASN B1013    36697  18555  21525   1546   4410   -109       C  
ATOM   3105  C   ASN B1013     -17.362 -28.941  -8.642  1.00204.38           C  
ANISOU 3105  C   ASN B1013    36662  18959  22035   1328   4461   -160       C  
ATOM   3106  O   ASN B1013     -18.554 -29.029  -8.340  1.00204.23           O  
ANISOU 3106  O   ASN B1013    36533  18887  22179   1177   4701   -192       O  
ATOM   3107  CB  ASN B1013     -16.016 -29.551  -6.606  1.00201.93           C  
ANISOU 3107  CB  ASN B1013    36752  18560  21412   1721   4258    -48       C  
ATOM   3108  CG  ASN B1013     -15.494 -30.666  -5.737  1.00212.78           C  
ANISOU 3108  CG  ASN B1013    36902  20624  23322   1668   3707    -57       C  
ATOM   3109  OD1 ASN B1013     -16.244 -31.535  -5.284  1.00208.43           O  
ANISOU 3109  OD1 ASN B1013    36763  19762  22668   1659   4076    -60       O  
ATOM   3110  ND2 ASN B1013     -14.211 -30.613  -5.408  1.00205.88           N  
ANISOU 3110  ND2 ASN B1013    36908  19393  21922   1990   3746     33       N  
ATOM   3111  N   LEU B1014     -16.874 -27.986  -9.476  1.00199.98           N  
ANISOU 3111  N   LEU B1014    36068  18489  21425   1334   4284   -159       N  
ATOM   3112  CA  LEU B1014     -17.664 -26.922 -10.114  1.00198.03           C  
ANISOU 3112  CA  LEU B1014    35405  18425  21414   1144   4244   -197       C  
ATOM   3113  C   LEU B1014     -18.733 -27.500 -11.052  1.00202.38           C  
ANISOU 3113  C   LEU B1014    35696  18998  22200    879   4471   -271       C  
ATOM   3114  O   LEU B1014     -19.795 -26.895 -11.227  1.00201.36           O  
ANISOU 3114  O   LEU B1014    35334  18916  22259    716   4591   -298       O  
ATOM   3115  CB  LEU B1014     -16.737 -25.956 -10.872  1.00195.53           C  
ANISOU 3115  CB  LEU B1014    34765  18396  21134   1184   3835   -188       C  
ATOM   3116  CG  LEU B1014     -17.235 -24.536 -11.216  1.00198.27           C  
ANISOU 3116  CG  LEU B1014    34765  18924  21646   1081   3716   -196       C  
ATOM   3117  CD1 LEU B1014     -18.072 -23.902 -10.105  1.00199.25           C  
ANISOU 3117  CD1 LEU B1014    35076  18887  21745   1101   3918   -172       C  
ATOM   3118  CD2 LEU B1014     -16.067 -23.631 -11.505  1.00199.72           C  
ANISOU 3118  CD2 LEU B1014    34800  19314  21771   1194   3324   -169       C  
ATOM   3119  N   LYS B1015     -18.462 -28.679 -11.629  1.00200.02           N  
ANISOU 3119  N   LYS B1015    35447  18661  21888    838   4535   -304       N  
ATOM   3120  CA  LYS B1015     -19.408 -29.373 -12.496  1.00200.61           C  
ANISOU 3120  CA  LYS B1015    35322  18741  22160    578   4751   -384       C  
ATOM   3121  C   LYS B1015     -20.327 -30.289 -11.656  1.00206.50           C  
ANISOU 3121  C   LYS B1015    36258  19266  22935    516   5104   -401       C  
ATOM   3122  O   LYS B1015     -21.409 -30.658 -12.120  1.00206.99           O  
ANISOU 3122  O   LYS B1015    36096  19345  23206    278   5299   -469       O  
ATOM   3123  CB  LYS B1015     -18.667 -30.169 -13.584  1.00202.67           C  
ANISOU 3123  CB  LYS B1015    35481  19105  22421    546   4618   -419       C  
ATOM   3124  N   VAL B1016     -19.904 -30.629 -10.414  1.00203.57           N  
ANISOU 3124  N   VAL B1016    36270  18710  22366    728   5163   -340       N  
ATOM   3125  CA  VAL B1016     -20.665 -31.481  -9.496  1.00214.30           C  
ANISOU 3125  CA  VAL B1016    36376  20722  24326    633   4683   -369       C  
ATOM   3126  C   VAL B1016     -21.868 -30.707  -8.952  1.00208.78           C  
ANISOU 3126  C   VAL B1016    36146  19654  23525    560   5159   -364       C  
ATOM   3127  O   VAL B1016     -22.909 -31.295  -8.658  1.00163.36           O  
ANISOU 3127  O   VAL B1016    31794  12934  17342    462   6273   -384       O  
ATOM   3128  CB  VAL B1016     -19.774 -32.019  -8.353  1.00216.47           C  
ANISOU 3128  CB  VAL B1016    36520  21146  24583    836   4400   -317       C  
ATOM   3129  N   ALA B1023     -29.379 -30.729  -2.252  1.00200.00           N  
ANISOU 3129  N   ALA B1023    34989  17900  23102    249   6691   -318       N  
ATOM   3130  CA  ALA B1023     -28.554 -29.814  -1.460  1.00199.28           C  
ANISOU 3130  CA  ALA B1023    35162  17759  22797    465   6555   -258       C  
ATOM   3131  C   ALA B1023     -27.368 -30.522  -0.781  1.00201.29           C  
ANISOU 3131  C   ALA B1023    35432  18140  22910    643   6200   -232       C  
ATOM   3132  O   ALA B1023     -26.344 -29.879  -0.541  1.00200.27           O  
ANISOU 3132  O   ALA B1023    35584  17957  22551    814   6069   -190       O  
ATOM   3133  CB  ALA B1023     -29.405 -29.116  -0.415  1.00199.91           C  
ANISOU 3133  CB  ALA B1023    35094  17877  22987    482   6590   -230       C  
ATOM   3134  N   ALA B1024     -27.506 -31.831  -0.471  1.00199.64           N  
ANISOU 3134  N   ALA B1024    35356  17818  22679    621   6342   -248       N  
ATOM   3135  CA  ALA B1024     -26.468 -32.659   0.159  1.00199.37           C  
ANISOU 3135  CA  ALA B1024    35515  17770  22464    786   6176   -218       C  
ATOM   3136  C   ALA B1024     -25.208 -32.719  -0.714  1.00202.10           C  
ANISOU 3136  C   ALA B1024    35730  18305  22754    856   5837   -218       C  
ATOM   3137  O   ALA B1024     -24.098 -32.605  -0.195  1.00201.45           O  
ANISOU 3137  O   ALA B1024    35881  18203  22459   1048   5665   -169       O  
ATOM   3138  CB  ALA B1024     -27.001 -34.065   0.410  1.00200.11           C  
ANISOU 3138  CB  ALA B1024    35442  17897  22693    698   6230   -248       C  
ATOM   3139  N   GLN B1025     -25.396 -32.863  -2.041  1.00200.26           N  
ANISOU 3139  N   GLN B1025    35609  17953  22528    722   6050   -262       N  
ATOM   3140  CA  GLN B1025     -24.325 -32.892  -3.029  1.00200.01           C  
ANISOU 3140  CA  GLN B1025    35722  17920  22352    778   5934   -263       C  
ATOM   3141  C   GLN B1025     -23.798 -31.476  -3.296  1.00202.56           C  
ANISOU 3141  C   GLN B1025    35880  18422  22662    847   5656   -237       C  
ATOM   3142  O   GLN B1025     -22.586 -31.304  -3.431  1.00201.98           O  
ANISOU 3142  O   GLN B1025    36029  18337  22376   1007   5479   -201       O  
ATOM   3143  CB  GLN B1025     -24.814 -33.532  -4.337  1.00201.35           C  
ANISOU 3143  CB  GLN B1025    35626  18168  22711    560   6006   -337       C  
ATOM   3144  N   VAL B1026     -24.707 -30.472  -3.376  1.00200.63           N  
ANISOU 3144  N   VAL B1026    35726  18047  22457    756   5910   -242       N  
ATOM   3145  CA  VAL B1026     -24.395 -29.058  -3.658  1.00200.53           C  
ANISOU 3145  CA  VAL B1026    35793  18041  22359    813   5832   -216       C  
ATOM   3146  C   VAL B1026     -23.516 -28.441  -2.543  1.00203.25           C  
ANISOU 3146  C   VAL B1026    36028  18577  22621   1017   5434   -160       C  
ATOM   3147  O   VAL B1026     -22.547 -27.748  -2.863  1.00203.07           O  
ANISOU 3147  O   VAL B1026    36163  18570  22426   1131   5253   -133       O  
ATOM   3148  CB  VAL B1026     -25.661 -28.184  -3.903  1.00203.44           C  
ANISOU 3148  CB  VAL B1026    35680  18581  23039    640   5866   -240       C  
ATOM   3149  CG1 VAL B1026     -25.297 -26.855  -4.564  1.00203.16           C  
ANISOU 3149  CG1 VAL B1026    35734  18539  22920    670   5816   -222       C  
ATOM   3150  CG2 VAL B1026     -26.706 -28.924  -4.735  1.00203.92           C  
ANISOU 3150  CG2 VAL B1026    35478  18665  23337    401   6071   -304       C  
ATOM   3151  N   LYS B1027     -23.857 -28.684  -1.254  1.00200.68           N  
ANISOU 3151  N   LYS B1027    35956  18083  22209   1092   5598   -132       N  
ATOM   3152  CA  LYS B1027     -23.116 -28.160  -0.096  1.00200.00           C  
ANISOU 3152  CA  LYS B1027    36086  17982  21924   1286   5424    -77       C  
ATOM   3153  C   LYS B1027     -21.713 -28.773   0.001  1.00201.14           C  
ANISOU 3153  C   LYS B1027    36269  18238  21917   1438   5110    -49       C  
ATOM   3154  O   LYS B1027     -20.755 -28.051   0.280  1.00201.06           O  
ANISOU 3154  O   LYS B1027    36402  18267  21726   1582   4885    -10       O  
ATOM   3155  CB  LYS B1027     -23.889 -28.403   1.212  1.00201.94           C  
ANISOU 3155  CB  LYS B1027    36054  18333  22340   1259   5403    -77       C  
ATOM   3156  N   ASP B1028     -21.604 -30.095  -0.247  1.00197.28           N  
ANISOU 3156  N   ASP B1028    36170  17500  21288   1459   5367    -50       N  
ATOM   3157  CA  ASP B1028     -20.368 -30.884  -0.224  1.00196.29           C  
ANISOU 3157  CA  ASP B1028    36274  17351  20957   1625   5211    -12       C  
ATOM   3158  C   ASP B1028     -19.334 -30.353  -1.244  1.00196.86           C  
ANISOU 3158  C   ASP B1028    36394  17496  20908   1695   4996     -2       C  
ATOM   3159  O   ASP B1028     -18.154 -30.238  -0.903  1.00196.39           O  
ANISOU 3159  O   ASP B1028    36517  17466  20638   1888   4755     51       O  
ATOM   3160  CB  ASP B1028     -20.707 -32.362  -0.505  1.00197.78           C  
ANISOU 3160  CB  ASP B1028    36213  17602  21331   1518   5278    -51       C  
ATOM   3161  CG  ASP B1028     -19.522 -33.282  -0.710  1.00204.92           C  
ANISOU 3161  CG  ASP B1028    36431  18984  22447   1554   4732    -51       C  
ATOM   3162  OD1 ASP B1028     -18.931 -33.719   0.299  1.00205.04           O  
ANISOU 3162  OD1 ASP B1028    36491  19033  22381   1687   4600     -3       O  
ATOM   3163  OD2 ASP B1028     -19.216 -33.603  -1.881  1.00209.29           O1-
ANISOU 3163  OD2 ASP B1028    36505  19806  23208   1453   4516    -95       O1-
ATOM   3164  N   ALA B1029     -19.781 -30.030  -2.479  1.00193.22           N  
ANISOU 3164  N   ALA B1029    36273  16783  20361   1597   5319    -34       N  
ATOM   3165  CA  ALA B1029     -18.936 -29.517  -3.564  1.00192.33           C  
ANISOU 3165  CA  ALA B1029    36355  16644  20078   1657   5207    -27       C  
ATOM   3166  C   ALA B1029     -18.415 -28.111  -3.259  1.00192.80           C  
ANISOU 3166  C   ALA B1029    36474  16772  20009   1772   4969      9       C  
ATOM   3167  O   ALA B1029     -17.240 -27.832  -3.491  1.00192.07           O  
ANISOU 3167  O   ALA B1029    36597  16692  19689   1941   4725     46       O  
ATOM   3168  CB  ALA B1029     -19.708 -29.511  -4.873  1.00193.10           C  
ANISOU 3168  CB  ALA B1029    36251  16749  20368   1422   5397    -95       C  
ATOM   3169  N   LEU B1030     -19.284 -27.239  -2.724  1.00189.52           N  
ANISOU 3169  N   LEU B1030    36362  16127  19521   1746   5253     16       N  
ATOM   3170  CA  LEU B1030     -18.945 -25.866  -2.367  1.00188.83           C  
ANISOU 3170  CA  LEU B1030    36445  16028  19276   1850   5106     48       C  
ATOM   3171  C   LEU B1030     -17.957 -25.820  -1.199  1.00190.86           C  
ANISOU 3171  C   LEU B1030    36602  16474  19442   2027   4715     91       C  
ATOM   3172  O   LEU B1030     -17.054 -24.985  -1.213  1.00190.54           O  
ANISOU 3172  O   LEU B1030    36718  16472  19205   2155   4454    117       O  
ATOM   3173  CB  LEU B1030     -20.213 -25.068  -2.032  1.00188.87           C  
ANISOU 3173  CB  LEU B1030    36316  15987  19460   1712   5352     29       C  
ATOM   3174  CG  LEU B1030     -21.127 -24.736  -3.207  1.00192.13           C  
ANISOU 3174  CG  LEU B1030    36231  16559  20210   1471   5441    -26       C  
ATOM   3175  CD1 LEU B1030     -22.513 -24.383  -2.730  1.00192.55           C  
ANISOU 3175  CD1 LEU B1030    36056  16595  20507   1333   5701    -43       C  
ATOM   3176  CD2 LEU B1030     -20.547 -23.615  -4.054  1.00192.45           C  
ANISOU 3176  CD2 LEU B1030    35991  16836  20294   1465   5109    -29       C  
ATOM   3177  N   THR B1031     -18.105 -26.732  -0.213  1.00188.22           N  
ANISOU 3177  N   THR B1031    36533  15974  19008   2103   4883    117       N  
ATOM   3178  CA  THR B1031     -17.216 -26.821   0.953  1.00187.87           C  
ANISOU 3178  CA  THR B1031    36631  15977  18775   2293   4634    170       C  
ATOM   3179  C   THR B1031     -15.795 -27.197   0.484  1.00190.60           C  
ANISOU 3179  C   THR B1031    36773  16565  19080   2405   4223    193       C  
ATOM   3180  O   THR B1031     -14.831 -26.578   0.939  1.00190.20           O  
ANISOU 3180  O   THR B1031    36869  16572  18826   2560   3938    231       O  
ATOM   3181  CB  THR B1031     -17.773 -27.809   1.999  1.00191.79           C  
ANISOU 3181  CB  THR B1031    36608  16687  19576   2197   4608    158       C  
ATOM   3182  OG1 THR B1031     -19.103 -27.429   2.353  1.00190.22           O  
ANISOU 3182  OG1 THR B1031    36470  16327  19476   2077   4944    132       O  
ATOM   3183  CG2 THR B1031     -16.922 -27.872   3.264  1.00190.43           C  
ANISOU 3183  CG2 THR B1031    36681  16504  19168   2390   4418    219       C  
ATOM   3184  N   LYS B1032     -15.681 -28.184  -0.444  1.00188.45           N  
ANISOU 3184  N   LYS B1032    36715  16141  18747   2418   4395    189       N  
ATOM   3185  CA  LYS B1032     -14.411 -28.643  -1.020  1.00188.28           C  
ANISOU 3185  CA  LYS B1032    36792  16175  18569   2576   4153    223       C  
ATOM   3186  C   LYS B1032     -13.784 -27.530  -1.867  1.00191.14           C  
ANISOU 3186  C   LYS B1032    36903  16755  18967   2559   3837    205       C  
ATOM   3187  O   LYS B1032     -12.580 -27.298  -1.759  1.00190.85           O  
ANISOU 3187  O   LYS B1032    36984  16793  18736   2743   3522    248       O  
ATOM   3188  CB  LYS B1032     -14.605 -29.920  -1.851  1.00189.63           C  
ANISOU 3188  CB  LYS B1032    36739  16382  18929   2472   4288    192       C  
ATOM   3189  N   MET B1033     -14.612 -26.821  -2.670  1.00188.85           N  
ANISOU 3189  N   MET B1033    36806  16283  18665   2437   4094    165       N  
ATOM   3190  CA  MET B1033     -14.200 -25.699  -3.510  1.00186.55           C  
ANISOU 3190  CA  MET B1033    36055  16297  18530   2357   3762    135       C  
ATOM   3191  C   MET B1033     -13.612 -24.559  -2.683  1.00190.17           C  
ANISOU 3191  C   MET B1033    36646  16798  18813   2482   3502    165       C  
ATOM   3192  O   MET B1033     -12.601 -23.977  -3.083  1.00188.32           O  
ANISOU 3192  O   MET B1033    36200  16787  18565   2538   3125    168       O  
ATOM   3193  CB  MET B1033     -15.393 -25.175  -4.315  1.00187.87           C  
ANISOU 3193  CB  MET B1033    35830  16547  19004   2094   3944     73       C  
ATOM   3194  CG  MET B1033     -15.605 -25.916  -5.610  1.00190.91           C  
ANISOU 3194  CG  MET B1033    35881  17047  19609   1937   4000     26       C  
ATOM   3195  SD  MET B1033     -16.508 -25.000  -6.895  1.00193.41           S  
ANISOU 3195  SD  MET B1033    35596  17606  20285   1657   3991    -41       S  
ATOM   3196  CE  MET B1033     -15.659 -23.367  -6.822  1.00188.50           C  
ANISOU 3196  CE  MET B1033    34801  17205  19615   1745   3574    -17       C  
ATOM   3197  N   ARG B1034     -14.258 -24.239  -1.537  1.00188.49           N  
ANISOU 3197  N   ARG B1034    36786  16364  18467   2517   3714    182       N  
ATOM   3198  CA  ARG B1034     -13.857 -23.177  -0.607  1.00188.90           C  
ANISOU 3198  CA  ARG B1034    37037  16408  18330   2622   3524    203       C  
ATOM   3199  C   ARG B1034     -12.458 -23.439  -0.062  1.00191.78           C  
ANISOU 3199  C   ARG B1034    37138  17065  18665   2752   3063    236       C  
ATOM   3200  O   ARG B1034     -11.584 -22.581  -0.175  1.00191.22           O  
ANISOU 3200  O   ARG B1034    37206  17041  18410   2852   2772    242       O  
ATOM   3201  CB  ARG B1034     -14.867 -23.049   0.548  1.00188.95           C  
ANISOU 3201  CB  ARG B1034    36972  16365  18454   2538   3743    198       C  
ATOM   3202  N   ALA B1035     -12.239 -24.646   0.475  1.00190.41           N  
ANISOU 3202  N   ALA B1035    37099  16823  18424   2852   3130    275       N  
ATOM   3203  CA  ALA B1035     -10.959 -25.076   1.025  1.00190.99           C  
ANISOU 3203  CA  ALA B1035    37147  17049  18372   3024   2796    328       C  
ATOM   3204  C   ALA B1035      -9.869 -25.033  -0.039  1.00193.87           C  
ANISOU 3204  C   ALA B1035    37206  17654  18800   3057   2469    327       C  
ATOM   3205  O   ALA B1035      -8.788 -24.514   0.233  1.00193.74           O  
ANISOU 3205  O   ALA B1035    37246  17747  18619   3190   2129    354       O  
ATOM   3206  CB  ALA B1035     -11.085 -26.477   1.593  1.00191.71           C  
ANISOU 3206  CB  ALA B1035    37100  17164  18576   3032   2915    360       C  
ATOM   3207  N   ALA B1036     -10.179 -25.527  -1.258  1.00191.74           N  
ANISOU 3207  N   ALA B1036    37164  17194  18495   3052   2690    309       N  
ATOM   3208  CA  ALA B1036      -9.282 -25.573  -2.412  1.00191.65           C  
ANISOU 3208  CA  ALA B1036    37073  17286  18460   3118   2475    308       C  
ATOM   3209  C   ALA B1036      -8.850 -24.177  -2.857  1.00195.73           C  
ANISOU 3209  C   ALA B1036    37221  18064  19084   3031   2149    270       C  
ATOM   3210  O   ALA B1036      -7.674 -23.988  -3.167  1.00195.09           O  
ANISOU 3210  O   ALA B1036    36975  18179  18971   3128   1798    286       O  
ATOM   3211  CB  ALA B1036      -9.951 -26.298  -3.564  1.00191.08           C  
ANISOU 3211  CB  ALA B1036    36726  17233  18644   2943   2715    265       C  
ATOM   3212  N   ALA B1037      -9.790 -23.203  -2.879  1.00193.06           N  
ANISOU 3212  N   ALA B1037    36757  17724  18875   2854   2274    224       N  
ATOM   3213  CA  ALA B1037      -9.519 -21.812  -3.264  1.00192.13           C  
ANISOU 3213  CA  ALA B1037    36318  17824  18860   2759   2012    188       C  
ATOM   3214  C   ALA B1037      -8.614 -21.132  -2.239  1.00199.25           C  
ANISOU 3214  C   ALA B1037    37394  18769  19541   2899   1707    212       C  
ATOM   3215  O   ALA B1037      -7.687 -20.413  -2.617  1.00198.27           O  
ANISOU 3215  O   ALA B1037    37099  18831  19402   2922   1369    201       O  
ATOM   3216  CB  ALA B1037     -10.825 -21.040  -3.400  1.00191.99           C  
ANISOU 3216  CB  ALA B1037    36170  17758  19020   2560   2263    145       C  
ATOM   3217  N   LEU B1038      -8.874 -21.390  -0.941  1.00198.28           N  
ANISOU 3217  N   LEU B1038    37374  18595  19370   2929   1793    239       N  
ATOM   3218  CA  LEU B1038      -8.124 -20.850   0.193  1.00199.06           C  
ANISOU 3218  CA  LEU B1038    37402  18849  19383   2984   1507    257       C  
ATOM   3219  C   LEU B1038      -6.682 -21.342   0.196  1.00203.54           C  
ANISOU 3219  C   LEU B1038    37418  19818  20100   3021   1114    294       C  
ATOM   3220  O   LEU B1038      -5.796 -20.614   0.638  1.00203.59           O  
ANISOU 3220  O   LEU B1038    37430  19944  19979   3077    809    299       O  
ATOM   3221  CB  LEU B1038      -8.808 -21.239   1.509  1.00199.08           C  
ANISOU 3221  CB  LEU B1038    37381  18818  19443   2942   1698    276       C  
ATOM   3222  N   ASP B1039      -6.454 -22.576  -0.290  1.00202.52           N  
ANISOU 3222  N   ASP B1039    37377  19619  19951   3124   1195    330       N  
ATOM   3223  CA  ASP B1039      -5.134 -23.197  -0.378  1.00203.42           C  
ANISOU 3223  CA  ASP B1039    37352  19909  20028   3267    913    384       C  
ATOM   3224  C   ASP B1039      -4.400 -22.736  -1.630  1.00207.17           C  
ANISOU 3224  C   ASP B1039    37375  20647  20692   3196    671    354       C  
ATOM   3225  O   ASP B1039      -3.171 -22.675  -1.619  1.00207.45           O  
ANISOU 3225  O   ASP B1039    37343  20833  20644   3318    356    388       O  
ATOM   3226  CB  ASP B1039      -5.252 -24.732  -0.365  1.00204.72           C  
ANISOU 3226  CB  ASP B1039    37320  20106  20359   3272   1086    429       C  
ATOM   3227  CG  ASP B1039      -5.175 -25.360   1.014  1.00212.50           C  
ANISOU 3227  CG  ASP B1039    37357  21570  21811   3046   1001    469       C  
ATOM   3228  OD1 ASP B1039      -5.849 -24.845   1.944  1.00212.87           O  
ANISOU 3228  OD1 ASP B1039    37381  21613  21888   2950   1079    449       O  
ATOM   3229  OD2 ASP B1039      -4.477 -26.392   1.157  1.00216.72           O  
ANISOU 3229  OD2 ASP B1039    37353  22393  22597   3006    889    527       O  
ATOM   3230  N   ALA B1040      -5.153 -22.419  -2.706  1.00205.12           N  
ANISOU 3230  N   ALA B1040    37388  20165  20382   3158    864    302       N  
ATOM   3231  CA  ALA B1040      -4.596 -21.961  -3.979  1.00205.11           C  
ANISOU 3231  CA  ALA B1040    37392  20194  20347   3190    694    273       C  
ATOM   3232  C   ALA B1040      -4.089 -20.520  -3.880  1.00207.73           C  
ANISOU 3232  C   ALA B1040    37430  20755  20743   3093    386    235       C  
ATOM   3233  O   ALA B1040      -3.088 -20.194  -4.522  1.00207.76           O  
ANISOU 3233  O   ALA B1040    37405  20854  20680   3180     98    229       O  
ATOM   3234  CB  ALA B1040      -5.630 -22.085  -5.089  1.00204.55           C  
ANISOU 3234  CB  ALA B1040    37198  20055  20465   3019    981    226       C  
ATOM   3235  N   GLN B1041      -4.757 -19.663  -3.070  1.00205.13           N  
ANISOU 3235  N   GLN B1041    37450  20242  20250   3069    473    213       N  
ATOM   3236  CA  GLN B1041      -4.325 -18.271  -2.895  1.00204.98           C  
ANISOU 3236  CA  GLN B1041    37457  20288  20137   3038    212    174       C  
ATOM   3237  C   GLN B1041      -3.042 -18.213  -2.044  1.00207.99           C  
ANISOU 3237  C   GLN B1041    37443  21007  20576   3062   -144    205       C  
ATOM   3238  O   GLN B1041      -2.268 -17.265  -2.189  1.00208.37           O  
ANISOU 3238  O   GLN B1041    37430  21173  20567   3056   -444    174       O  
ATOM   3239  CB  GLN B1041      -5.432 -17.388  -2.293  1.00205.50           C  
ANISOU 3239  CB  GLN B1041    37518  20286  20278   2873    421    140       C  
ATOM   3240  N   LYS B1042      -2.801 -19.248  -1.198  1.00205.04           N  
ANISOU 3240  N   LYS B1042    37392  20507  20005   3247   -108    270       N  
ATOM   3241  CA  LYS B1042      -1.619 -19.381  -0.345  1.00211.22           C  
ANISOU 3241  CA  LYS B1042    37378  21809  21066   3145   -395    322       C  
ATOM   3242  C   LYS B1042      -0.383 -19.687  -1.181  1.00216.25           C  
ANISOU 3242  C   LYS B1042    37342  22841  21982   3099   -640    352       C  
ATOM   3243  O   LYS B1042       0.741 -19.490  -0.722  1.00180.50           O  
ANISOU 3243  O   LYS B1042    34814  17508  16261   3843  -1103    350       O  
ATOM   3244  CB  LYS B1042      -1.833 -20.488   0.694  1.00212.95           C  
ANISOU 3244  CB  LYS B1042    37379  22120  21412   3124   -237    393       C  
ATOM   3245  N   LYS B1059      -2.006  -8.473  -4.074  1.00217.87           N  
ANISOU 3245  N   LYS B1059    37612  22923  22246   2097  -1170   -211       N  
ATOM   3246  CA  LYS B1059      -1.867  -9.237  -5.310  1.00216.75           C  
ANISOU 3246  CA  LYS B1059    37281  22839  22235   2135  -1165   -188       C  
ATOM   3247  C   LYS B1059      -3.212  -9.358  -6.039  1.00218.96           C  
ANISOU 3247  C   LYS B1059    37432  23044  22719   2043   -806   -173       C  
ATOM   3248  O   LYS B1059      -4.247  -9.491  -5.390  1.00219.00           O  
ANISOU 3248  O   LYS B1059    37696  22852  22661   2055   -535   -156       O  
ATOM   3249  CB  LYS B1059      -1.290 -10.633  -5.020  1.00219.50           C  
ANISOU 3249  CB  LYS B1059    37547  23280  22573   2273  -1207   -132       C  
ATOM   3250  N   ASP B1060      -3.184  -9.296  -7.389  1.00213.65           N  
ANISOU 3250  N   ASP B1060    36336  22541  22299   1946   -808   -179       N  
ATOM   3251  CA  ASP B1060      -4.363  -9.399  -8.260  1.00211.72           C  
ANISOU 3251  CA  ASP B1060    35902  22274  22270   1848   -515   -167       C  
ATOM   3252  C   ASP B1060      -4.824 -10.857  -8.414  1.00215.44           C  
ANISOU 3252  C   ASP B1060    36432  22668  22758   1928   -315   -126       C  
ATOM   3253  O   ASP B1060      -5.987 -11.096  -8.745  1.00213.76           O  
ANISOU 3253  O   ASP B1060    36184  22371  22665   1863    -28   -116       O  
ATOM   3254  CB  ASP B1060      -4.074  -8.785  -9.638  1.00211.64           C  
ANISOU 3254  CB  ASP B1060    35440  22476  22496   1719   -618   -189       C  
ATOM   3255  N   PHE B1061      -3.905 -11.820  -8.181  1.00213.46           N  
ANISOU 3255  N   PHE B1061    36266  22448  22393   2068   -466   -104       N  
ATOM   3256  CA  PHE B1061      -4.140 -13.264  -8.221  1.00213.88           C  
ANISOU 3256  CA  PHE B1061    36423  22416  22426   2166   -301    -64       C  
ATOM   3257  C   PHE B1061      -4.766 -13.712  -6.881  1.00219.85           C  
ANISOU 3257  C   PHE B1061    37653  22917  22964   2269   -111    -38       C  
ATOM   3258  O   PHE B1061      -5.783 -14.411  -6.887  1.00219.18           O  
ANISOU 3258  O   PHE B1061    37662  22690  22925   2252    197    -21       O  
ATOM   3259  CB  PHE B1061      -2.834 -14.017  -8.512  1.00216.19           C  
ANISOU 3259  CB  PHE B1061    36613  22845  22683   2290   -547    -43       C  
ATOM   3260  N   ARG B1062      -4.198 -13.239  -5.740  1.00218.03           N  
ANISOU 3260  N   ARG B1062    37633  22665  22541   2338   -286    -39       N  
ATOM   3261  CA  ARG B1062      -4.670 -13.524  -4.376  1.00217.99           C  
ANISOU 3261  CA  ARG B1062    37640  22647  22540   2332   -134    -15       C  
ATOM   3262  C   ARG B1062      -6.032 -12.857  -4.083  1.00220.59           C  
ANISOU 3262  C   ARG B1062    37689  23004  23122   2139    154    -35       C  
ATOM   3263  O   ARG B1062      -6.758 -13.329  -3.205  1.00219.96           O  
ANISOU 3263  O   ARG B1062    37684  22836  23054   2143    367    -15       O  
ATOM   3264  CB  ARG B1062      -3.630 -13.076  -3.338  1.00218.58           C  
ANISOU 3264  CB  ARG B1062    37617  22899  22534   2353   -417    -15       C  
ATOM   3265  N   HIS B1063      -6.369 -11.767  -4.818  1.00218.86           N  
ANISOU 3265  N   HIS B1063    37707  22631  22817   2100    160    -70       N  
ATOM   3266  CA  HIS B1063      -7.634 -11.028  -4.698  1.00218.59           C  
ANISOU 3266  CA  HIS B1063    37726  22465  22863   1999    431    -82       C  
ATOM   3267  C   HIS B1063      -8.792 -11.779  -5.365  1.00220.51           C  
ANISOU 3267  C   HIS B1063    37717  22707  23359   1920    743    -65       C  
ATOM   3268  O   HIS B1063      -9.913 -11.722  -4.861  1.00220.38           O  
ANISOU 3268  O   HIS B1063    37700  22597  23438   1866   1013    -58       O  
ATOM   3269  CB  HIS B1063      -7.524  -9.617  -5.304  1.00219.16           C  
ANISOU 3269  CB  HIS B1063    37753  22566  22953   1911    311   -119       C  
ATOM   3270  N   GLY B1064      -8.511 -12.448  -6.488  1.00216.52           N  
ANISOU 3270  N   GLY B1064    37391  22114  22762   1984    724    -58       N  
ATOM   3271  CA  GLY B1064      -9.483 -13.232  -7.245  1.00214.65           C  
ANISOU 3271  CA  GLY B1064    36986  21854  22715   1910    999    -48       C  
ATOM   3272  C   GLY B1064     -10.104 -14.348  -6.431  1.00217.59           C  
ANISOU 3272  C   GLY B1064    37644  22028  23002   1980   1264    -22       C  
ATOM   3273  O   GLY B1064     -11.311 -14.589  -6.535  1.00217.05           O  
ANISOU 3273  O   GLY B1064    37603  21830  23034   1908   1584    -20       O  
ATOM   3274  N   PHE B1065      -9.282 -15.018  -5.594  1.00214.50           N  
ANISOU 3274  N   PHE B1065    37628  21530  22342   2155   1153      2       N  
ATOM   3275  CA  PHE B1065      -9.720 -16.100  -4.710  1.00213.89           C  
ANISOU 3275  CA  PHE B1065    37590  21390  22289   2189   1349     28       C  
ATOM   3276  C   PHE B1065     -10.569 -15.557  -3.557  1.00215.12           C  
ANISOU 3276  C   PHE B1065    37583  21573  22579   2098   1489     23       C  
ATOM   3277  O   PHE B1065     -11.447 -16.271  -3.076  1.00214.88           O  
ANISOU 3277  O   PHE B1065    37537  21463  22645   2067   1747     33       O  
ATOM   3278  CB  PHE B1065      -8.522 -16.892  -4.176  1.00215.38           C  
ANISOU 3278  CB  PHE B1065    37595  21776  22463   2286   1092     56       C  
ATOM   3279  N   ASP B1066     -10.322 -14.296  -3.128  1.00211.68           N  
ANISOU 3279  N   ASP B1066    37599  20963  21864   2162   1400     12       N  
ATOM   3280  CA  ASP B1066     -11.099 -13.615  -2.084  1.00210.89           C  
ANISOU 3280  CA  ASP B1066    37584  20773  21772   2118   1563      8       C  
ATOM   3281  C   ASP B1066     -12.521 -13.346  -2.600  1.00211.53           C  
ANISOU 3281  C   ASP B1066    37538  20768  22066   1995   1898      1       C  
ATOM   3282  O   ASP B1066     -13.488 -13.489  -1.848  1.00210.99           O  
ANISOU 3282  O   ASP B1066    37482  20605  22080   1962   2154      9       O  
ATOM   3283  CB  ASP B1066     -10.412 -12.305  -1.639  1.00212.33           C  
ANISOU 3283  CB  ASP B1066    37636  21111  21928   2083   1285    -20       C  
ATOM   3284  CG  ASP B1066      -9.135 -12.474  -0.820  1.00219.65           C  
ANISOU 3284  CG  ASP B1066    37685  22616  23158   1993    887    -26       C  
ATOM   3285  OD1 ASP B1066      -9.042 -13.461  -0.051  1.00219.93           O  
ANISOU 3285  OD1 ASP B1066    37667  22694  23203   2038    916      3       O  
ATOM   3286  OD2 ASP B1066      -8.256 -11.587  -0.902  1.00224.06           O  
ANISOU 3286  OD2 ASP B1066    37725  23521  23887   1887    598    -54       O  
ATOM   3287  N   ILE B1067     -12.639 -12.993  -3.900  1.00207.15           N  
ANISOU 3287  N   ILE B1067    37125  20114  21468   1976   1942     -4       N  
ATOM   3288  CA  ILE B1067     -13.923 -12.766  -4.573  1.00205.22           C  
ANISOU 3288  CA  ILE B1067    36612  19871  21491   1837   2223     -7       C  
ATOM   3289  C   ILE B1067     -14.633 -14.118  -4.691  1.00207.66           C  
ANISOU 3289  C   ILE B1067    36965  20070  21866   1826   2505      6       C  
ATOM   3290  O   ILE B1067     -15.819 -14.215  -4.366  1.00207.92           O  
ANISOU 3290  O   ILE B1067    37079  19942  21978   1777   2848     14       O  
ATOM   3291  CB  ILE B1067     -13.760 -12.068  -5.959  1.00206.07           C  
ANISOU 3291  CB  ILE B1067    36207  20248  21844   1714   2039    -27       C  
ATOM   3292  CG1 ILE B1067     -12.916 -10.778  -5.854  1.00206.27           C  
ANISOU 3292  CG1 ILE B1067    36202  20379  21793   1722   1745    -44       C  
ATOM   3293  CG2 ILE B1067     -15.128 -11.768  -6.587  1.00205.76           C  
ANISOU 3293  CG2 ILE B1067    35900  20210  22070   1582   2317    -22       C  
ATOM   3294  CD1 ILE B1067     -12.123 -10.425  -7.110  1.00211.21           C  
ANISOU 3294  CD1 ILE B1067    36406  21280  22564   1653   1454    -63       C  
ATOM   3295  N   LEU B1068     -13.874 -15.162  -5.113  1.00202.43           N  
ANISOU 3295  N   LEU B1068    36265  19485  21165   1874   2367      6       N  
ATOM   3296  CA  LEU B1068     -14.319 -16.544  -5.293  1.00201.93           C  
ANISOU 3296  CA  LEU B1068    36255  19326  21141   1867   2594     13       C  
ATOM   3297  C   LEU B1068     -14.881 -17.134  -3.992  1.00206.38           C  
ANISOU 3297  C   LEU B1068    37282  19601  21532   1954   2883     37       C  
ATOM   3298  O   LEU B1068     -16.036 -17.557  -3.999  1.00206.49           O  
ANISOU 3298  O   LEU B1068    37182  19548  21728   1849   3194     30       O  
ATOM   3299  CB  LEU B1068     -13.170 -17.410  -5.820  1.00201.43           C  
ANISOU 3299  CB  LEU B1068    36126  19389  21018   1942   2350     15       C  
ATOM   3300  N   VAL B1069     -14.102 -17.113  -2.877  1.00202.56           N  
ANISOU 3300  N   VAL B1069    37233  18992  20740   2124   2757     62       N  
ATOM   3301  CA  VAL B1069     -14.526 -17.626  -1.562  1.00202.00           C  
ANISOU 3301  CA  VAL B1069    37262  18836  20652   2158   2908     78       C  
ATOM   3302  C   VAL B1069     -15.808 -16.907  -1.117  1.00203.09           C  
ANISOU 3302  C   VAL B1069    37194  18962  21009   2028   3147     64       C  
ATOM   3303  O   VAL B1069     -16.742 -17.563  -0.650  1.00202.54           O  
ANISOU 3303  O   VAL B1069    37096  18802  21056   1979   3425     66       O  
ATOM   3304  CB  VAL B1069     -13.430 -17.598  -0.453  1.00204.63           C  
ANISOU 3304  CB  VAL B1069    37350  19432  20970   2226   2527     88       C  
ATOM   3305  CG1 VAL B1069     -12.309 -18.584  -0.749  1.00204.61           C  
ANISOU 3305  CG1 VAL B1069    37382  19504  20856   2341   2318    111       C  
ATOM   3306  CG2 VAL B1069     -12.888 -16.204  -0.168  1.00204.57           C  
ANISOU 3306  CG2 VAL B1069    37414  19475  20840   2244   2297     74       C  
ATOM   3307  N   GLY B1070     -15.854 -15.590  -1.340  1.00200.04           N  
ANISOU 3307  N   GLY B1070    37197  18385  20423   2061   3191     65       N  
ATOM   3308  CA  GLY B1070     -17.001 -14.746  -1.026  1.00199.55           C  
ANISOU 3308  CA  GLY B1070    37111  18224  20485   1979   3460     63       C  
ATOM   3309  C   GLY B1070     -18.273 -15.227  -1.694  1.00201.05           C  
ANISOU 3309  C   GLY B1070    36982  18423  20987   1835   3778     57       C  
ATOM   3310  O   GLY B1070     -19.318 -15.343  -1.045  1.00201.01           O  
ANISOU 3310  O   GLY B1070    36868  18366  21143   1777   4031     60       O  
ATOM   3311  N   GLN B1071     -18.171 -15.564  -2.987  1.00195.12           N  
ANISOU 3311  N   GLN B1071    35954  17808  20375   1756   3712     43       N  
ATOM   3312  CA  GLN B1071     -19.287 -16.068  -3.778  1.00193.96           C  
ANISOU 3312  CA  GLN B1071    35501  17686  20509   1606   3979     30       C  
ATOM   3313  C   GLN B1071     -19.648 -17.493  -3.365  1.00197.61           C  
ANISOU 3313  C   GLN B1071    36224  17950  20908   1622   4253     32       C  
ATOM   3314  O   GLN B1071     -20.833 -17.831  -3.381  1.00197.24           O  
ANISOU 3314  O   GLN B1071    36120  17794  21027   1519   4603     26       O  
ATOM   3315  CB  GLN B1071     -18.970 -16.001  -5.271  1.00193.18           C  
ANISOU 3315  CB  GLN B1071    34892  17884  20624   1495   3738      5       C  
ATOM   3316  N   ILE B1072     -18.638 -18.317  -2.976  1.00194.36           N  
ANISOU 3316  N   ILE B1072    36102  17488  20258   1753   4102     43       N  
ATOM   3317  CA  ILE B1072     -18.839 -19.697  -2.500  1.00195.64           C  
ANISOU 3317  CA  ILE B1072    36577  17441  20318   1797   4350     51       C  
ATOM   3318  C   ILE B1072     -19.671 -19.627  -1.205  1.00199.08           C  
ANISOU 3318  C   ILE B1072    36699  17973  20968   1745   4410     49       C  
ATOM   3319  O   ILE B1072     -20.637 -20.376  -1.058  1.00199.14           O  
ANISOU 3319  O   ILE B1072    36565  17940  21160   1647   4666     35       O  
ATOM   3320  CB  ILE B1072     -17.503 -20.493  -2.313  1.00197.80           C  
ANISOU 3320  CB  ILE B1072    36887  17832  20437   1931   4020     64       C  
ATOM   3321  CG1 ILE B1072     -16.758 -20.671  -3.647  1.00196.81           C  
ANISOU 3321  CG1 ILE B1072    36534  17885  20359   1904   3789     47       C  
ATOM   3322  CG2 ILE B1072     -17.769 -21.865  -1.692  1.00198.22           C  
ANISOU 3322  CG2 ILE B1072    36831  17895  20589   1921   4127     65       C  
ATOM   3323  CD1 ILE B1072     -15.236 -20.901  -3.519  1.00201.73           C  
ANISOU 3323  CD1 ILE B1072    37113  18689  20845   2052   3367     67       C  
ATOM   3324  N   ASP B1073     -19.326 -18.680  -0.309  1.00196.65           N  
ANISOU 3324  N   ASP B1073    36743  17545  20428   1863   4354     73       N  
ATOM   3325  CA  ASP B1073     -20.019 -18.435   0.954  1.00196.51           C  
ANISOU 3325  CA  ASP B1073    36682  17499  20484   1855   4472     78       C  
ATOM   3326  C   ASP B1073     -21.494 -18.067   0.721  1.00198.76           C  
ANISOU 3326  C   ASP B1073    36534  17852  21135   1684   4714     59       C  
ATOM   3327  O   ASP B1073     -22.365 -18.501   1.479  1.00198.25           O  
ANISOU 3327  O   ASP B1073    36415  17724  21186   1644   4927     58       O  
ATOM   3328  CB  ASP B1073     -19.297 -17.322   1.734  1.00197.90           C  
ANISOU 3328  CB  ASP B1073    36819  17811  20563   1924   4153     82       C  
ATOM   3329  CG  ASP B1073     -17.982 -17.747   2.371  1.00207.07           C  
ANISOU 3329  CG  ASP B1073    37047  19622  22007   1885   3469     59       C  
ATOM   3330  OD1 ASP B1073     -17.906 -18.889   2.881  1.00208.10           O  
ANISOU 3330  OD1 ASP B1073    37043  19825  22200   1893   3448     65       O  
ATOM   3331  OD2 ASP B1073     -17.049 -16.915   2.418  1.00211.33           O  
ANISOU 3331  OD2 ASP B1073    37184  20485  22627   1864   3064     45       O  
ATOM   3332  N   ASP B1074     -21.769 -17.293  -0.347  1.00196.61           N  
ANISOU 3332  N   ASP B1074    36462  17426  20816   1653   4901     66       N  
ATOM   3333  CA  ASP B1074     -23.121 -16.887  -0.733  1.00196.68           C  
ANISOU 3333  CA  ASP B1074    36264  17385  21080   1525   5228     64       C  
ATOM   3334  C   ASP B1074     -23.877 -18.063  -1.360  1.00198.51           C  
ANISOU 3334  C   ASP B1074    36140  17704  21581   1375   5376     34       C  
ATOM   3335  O   ASP B1074     -25.082 -18.197  -1.154  1.00198.35           O  
ANISOU 3335  O   ASP B1074    35943  17643  21778   1277   5654     29       O  
ATOM   3336  CB  ASP B1074     -23.072 -15.698  -1.697  1.00198.12           C  
ANISOU 3336  CB  ASP B1074    36298  17655  21326   1489   5141     69       C  
ATOM   3337  CG  ASP B1074     -22.457 -14.439  -1.106  1.00205.86           C  
ANISOU 3337  CG  ASP B1074    36552  19139  22526   1482   4526     52       C  
ATOM   3338  OD1 ASP B1074     -22.762 -14.118   0.065  1.00206.11           O  
ANISOU 3338  OD1 ASP B1074    36542  19180  22589   1506   4526     55       O  
ATOM   3339  OD2 ASP B1074     -21.709 -13.748  -1.831  1.00210.78           O  
ANISOU 3339  OD2 ASP B1074    36727  20092  23268   1445   4116     36       O  
ATOM   3340  N   ALA B1075     -23.164 -18.920  -2.104  1.00195.55           N  
ANISOU 3340  N   ALA B1075    36161  17163  20977   1412   5438     30       N  
ATOM   3341  CA  ALA B1075     -23.729 -20.113  -2.736  1.00195.55           C  
ANISOU 3341  CA  ALA B1075    36026  17142  21132   1280   5647     -2       C  
ATOM   3342  C   ALA B1075     -24.029 -21.204  -1.699  1.00197.08           C  
ANISOU 3342  C   ALA B1075    36013  17425  21444   1270   5614    -15       C  
ATOM   3343  O   ALA B1075     -24.961 -21.987  -1.891  1.00196.71           O  
ANISOU 3343  O   ALA B1075    35831  17330  21580   1138   5876    -41       O  
ATOM   3344  CB  ALA B1075     -22.775 -20.645  -3.789  1.00195.13           C  
ANISOU 3344  CB  ALA B1075    35851  17250  21039   1271   5370    -23       C  
ATOM   3345  N   LEU B1076     -23.244 -21.242  -0.602  1.00194.25           N  
ANISOU 3345  N   LEU B1076    36110  16917  20780   1454   5542     19       N  
ATOM   3346  CA  LEU B1076     -23.392 -22.197   0.501  1.00193.90           C  
ANISOU 3346  CA  LEU B1076    36088  16850  20736   1488   5577     22       C  
ATOM   3347  C   LEU B1076     -24.665 -21.937   1.313  1.00197.12           C  
ANISOU 3347  C   LEU B1076    35988  17425  21482   1374   5624      7       C  
ATOM   3348  O   LEU B1076     -25.312 -22.897   1.736  1.00196.67           O  
ANISOU 3348  O   LEU B1076    35874  17324  21528   1317   5793     -7       O  
ATOM   3349  CB  LEU B1076     -22.171 -22.145   1.436  1.00193.38           C  
ANISOU 3349  CB  LEU B1076    36277  16803  20394   1678   5279     55       C  
ATOM   3350  CG  LEU B1076     -20.986 -23.040   1.092  1.00195.99           C  
ANISOU 3350  CG  LEU B1076    36443  17339  20685   1737   4930     53       C  
ATOM   3351  CD1 LEU B1076     -19.700 -22.492   1.682  1.00195.63           C  
ANISOU 3351  CD1 LEU B1076    36613  17343  20375   1912   4600     87       C  
ATOM   3352  CD2 LEU B1076     -21.205 -24.453   1.582  1.00197.93           C  
ANISOU 3352  CD2 LEU B1076    36419  17693  21091   1694   4922     40       C  
ATOM   3353  N   LYS B1077     -25.015 -20.643   1.544  1.00195.41           N  
ANISOU 3353  N   LYS B1077    35932  17096  21219   1404   5746     29       N  
ATOM   3354  CA  LYS B1077     -26.202 -20.243   2.312  1.00195.54           C  
ANISOU 3354  CA  LYS B1077    35777  17095  21424   1345   5942     31       C  
ATOM   3355  C   LYS B1077     -27.494 -20.715   1.613  1.00198.62           C  
ANISOU 3355  C   LYS B1077    35599  17652  22214   1143   6067     -3       C  
ATOM   3356  O   LYS B1077     -28.419 -21.172   2.291  1.00198.84           O  
ANISOU 3356  O   LYS B1077    35468  17683  22399   1084   6207    -10       O  
ATOM   3357  CB  LYS B1077     -26.227 -18.722   2.561  1.00197.04           C  
ANISOU 3357  CB  LYS B1077    35841  17380  21646   1379   5804     47       C  
ATOM   3358  N   LEU B1078     -27.522 -20.662   0.263  1.00196.02           N  
ANISOU 3358  N   LEU B1078    35472  17159  21847   1079   6312     -8       N  
ATOM   3359  CA  LEU B1078     -28.649 -21.106  -0.558  1.00202.74           C  
ANISOU 3359  CA  LEU B1078    35406  18426  23200    848   6147    -55       C  
ATOM   3360  C   LEU B1078     -28.748 -22.634  -0.554  1.00203.32           C  
ANISOU 3360  C   LEU B1078    35386  18535  23331    775   6153    -91       C  
ATOM   3361  O   LEU B1078     -27.735 -23.327  -0.671  1.00165.13           O  
ANISOU 3361  O   LEU B1078    33017  12247  17478    995   7507    -36       O  
ATOM   3362  CB  LEU B1078     -28.510 -20.578  -1.994  1.00202.97           C  
ANISOU 3362  CB  LEU B1078    35378  18475  23266    779   6175    -61       C  
ATOM   3363  N   ALA B1090     -25.903 -18.192  -7.055  1.00216.18           N  
ANISOU 3363  N   ALA B1090    36030  21023  25085    666   5007    -88       N  
ATOM   3364  CA  ALA B1090     -26.060 -18.914  -8.311  1.00216.54           C  
ANISOU 3364  CA  ALA B1090    35962  21101  25212    520   5082   -128       C  
ATOM   3365  C   ALA B1090     -24.755 -19.576  -8.724  1.00219.00           C  
ANISOU 3365  C   ALA B1090    36215  21582  25411    567   4712   -153       C  
ATOM   3366  O   ALA B1090     -23.707 -18.925  -8.728  1.00217.89           O  
ANISOU 3366  O   ALA B1090    36364  21388  25038    698   4561   -127       O  
ATOM   3367  CB  ALA B1090     -26.535 -17.967  -9.402  1.00217.58           C  
ANISOU 3367  CB  ALA B1090    35882  21305  25482    431   5132   -118       C  
ATOM   3368  N   ALA B1091     -24.821 -20.869  -9.086  1.00217.82           N  
ANISOU 3368  N   ALA B1091    36145  21362  25256    482   4842   -195       N  
ATOM   3369  CA  ALA B1091     -23.664 -21.655  -9.527  1.00217.91           C  
ANISOU 3369  CA  ALA B1091    36300  21395  25101    532   4659   -214       C  
ATOM   3370  C   ALA B1091     -23.314 -21.308 -10.994  1.00222.58           C  
ANISOU 3370  C   ALA B1091    36429  22298  25842    434   4352   -239       C  
ATOM   3371  O   ALA B1091     -23.310 -22.172 -11.880  1.00222.45           O  
ANISOU 3371  O   ALA B1091    36391  22282  25848    319   4411   -285       O  
ATOM   3372  CB  ALA B1091     -23.953 -23.142  -9.362  1.00218.44           C  
ANISOU 3372  CB  ALA B1091    36242  21490  25267    457   4714   -255       C  
ATOM   3373  N   GLU B1092     -23.016 -20.015 -11.226  1.00221.62           N  
ANISOU 3373  N   GLU B1092    36475  22124  25608    499   4323   -203       N  
ATOM   3374  CA  GLU B1092     -22.704 -19.409 -12.521  1.00221.09           C  
ANISOU 3374  CA  GLU B1092    36134  22257  25612    430   4112   -212       C  
ATOM   3375  C   GLU B1092     -21.817 -18.175 -12.304  1.00224.61           C  
ANISOU 3375  C   GLU B1092    36600  22795  25948    576   3828   -169       C  
ATOM   3376  O   GLU B1092     -20.935 -17.894 -13.122  1.00222.79           O  
ANISOU 3376  O   GLU B1092    36188  22760  25704    587   3523   -174       O  
ATOM   3377  CB  GLU B1092     -23.999 -19.034 -13.263  1.00222.86           C  
ANISOU 3377  CB  GLU B1092    35950  22601  26125    247   4240   -227       C  
ATOM   3378  N   GLN B1093     -22.032 -17.480 -11.154  1.00222.36           N  
ANISOU 3378  N   GLN B1093    36565  22351  25572    686   3945   -128       N  
ATOM   3379  CA  GLN B1093     -21.294 -16.299 -10.696  1.00221.55           C  
ANISOU 3379  CA  GLN B1093    36557  22280  25341    821   3729    -92       C  
ATOM   3380  C   GLN B1093     -19.878 -16.673 -10.218  1.00224.52           C  
ANISOU 3380  C   GLN B1093    37008  22748  25553    950   3404    -95       C  
ATOM   3381  O   GLN B1093     -19.056 -15.785  -9.988  1.00223.83           O  
ANISOU 3381  O   GLN B1093    37106  22646  25292   1058   3225    -74       O  
ATOM   3382  CB  GLN B1093     -22.067 -15.600  -9.567  1.00223.21           C  
ANISOU 3382  CB  GLN B1093    36746  22433  25630    859   3859    -63       C  
ATOM   3383  N   LEU B1094     -19.611 -17.987 -10.066  1.00222.47           N  
ANISOU 3383  N   LEU B1094    36982  22366  25181    972   3501   -112       N  
ATOM   3384  CA  LEU B1094     -18.330 -18.567  -9.660  1.00222.08           C  
ANISOU 3384  CA  LEU B1094    37099  22337  24944   1107   3275   -108       C  
ATOM   3385  C   LEU B1094     -17.507 -18.973 -10.875  1.00225.13           C  
ANISOU 3385  C   LEU B1094    37200  22946  25395   1065   3021   -132       C  
ATOM   3386  O   LEU B1094     -16.286 -18.840 -10.836  1.00224.61           O  
ANISOU 3386  O   LEU B1094    37300  22899  25141   1192   2789   -117       O  
ATOM   3387  CB  LEU B1094     -18.549 -19.787  -8.750  1.00222.04           C  
ANISOU 3387  CB  LEU B1094    37052  22318  24997   1121   3359   -116       C  
ATOM   3388  N   LYS B1095     -18.171 -19.484 -11.942  1.00223.20           N  
ANISOU 3388  N   LYS B1095    36985  22619  25203    930   3239   -161       N  
ATOM   3389  CA  LYS B1095     -17.542 -19.913 -13.200  1.00221.83           C  
ANISOU 3389  CA  LYS B1095    36545  22641  25099    865   3038   -191       C  
ATOM   3390  C   LYS B1095     -16.953 -18.720 -13.965  1.00224.25           C  
ANISOU 3390  C   LYS B1095    36541  23191  25474    859   2726   -183       C  
ATOM   3391  O   LYS B1095     -15.952 -18.873 -14.669  1.00222.74           O  
ANISOU 3391  O   LYS B1095    36237  23142  25253    887   2488   -192       O  
ATOM   3392  CB  LYS B1095     -18.557 -20.658 -14.085  1.00224.49           C  
ANISOU 3392  CB  LYS B1095    36654  23007  25635    663   3239   -239       C  
ATOM   3393  N   THR B1096     -17.579 -17.541 -13.825  1.00220.87           N  
ANISOU 3393  N   THR B1096    35983  22798  25138    826   2744   -164       N  
ATOM   3394  CA  THR B1096     -17.156 -16.302 -14.478  1.00219.28           C  
ANISOU 3394  CA  THR B1096    35507  22803  25006    816   2485   -153       C  
ATOM   3395  C   THR B1096     -15.980 -15.652 -13.727  1.00222.94           C  
ANISOU 3395  C   THR B1096    36185  23250  25271    979   2260   -128       C  
ATOM   3396  O   THR B1096     -15.091 -15.087 -14.368  1.00221.56           O  
ANISOU 3396  O   THR B1096    35831  23251  25101    991   1986   -130       O  
ATOM   3397  CB  THR B1096     -18.341 -15.320 -14.596  1.00227.64           C  
ANISOU 3397  CB  THR B1096    36359  23891  26245    727   2618   -137       C  
ATOM   3398  OG1 THR B1096     -18.884 -15.055 -13.298  1.00228.85           O  
ANISOU 3398  OG1 THR B1096    36806  23829  26316    802   2830   -111       O  
ATOM   3399  CG2 THR B1096     -19.438 -15.822 -15.534  1.00225.90           C  
ANISOU 3399  CG2 THR B1096    35843  23745  26244    550   2776   -163       C  
ATOM   3400  N   THR B1097     -15.990 -15.730 -12.375  1.00220.20           N  
ANISOU 3400  N   THR B1097    36223  22693  24751   1095   2377   -107       N  
ATOM   3401  CA  THR B1097     -14.992 -15.143 -11.473  1.00219.94           C  
ANISOU 3401  CA  THR B1097    36444  22616  24507   1245   2185    -88       C  
ATOM   3402  C   THR B1097     -13.617 -15.816 -11.636  1.00222.86           C  
ANISOU 3402  C   THR B1097    36879  23058  24740   1344   1938    -92       C  
ATOM   3403  O   THR B1097     -12.609 -15.107 -11.645  1.00221.78           O  
ANISOU 3403  O   THR B1097    36703  23033  24531   1405   1660    -88       O  
ATOM   3404  CB  THR B1097     -15.501 -15.204 -10.024  1.00227.15           C  
ANISOU 3404  CB  THR B1097    37455  23434  25419   1290   2322    -74       C  
ATOM   3405  OG1 THR B1097     -16.716 -14.463  -9.942  1.00226.56           O  
ANISOU 3405  OG1 THR B1097    37375  23264  25444   1219   2559    -64       O  
ATOM   3406  CG2 THR B1097     -14.512 -14.626  -9.018  1.00225.75           C  
ANISOU 3406  CG2 THR B1097    37514  23230  25032   1426   2117    -60       C  
ATOM   3407  N   ARG B1098     -13.572 -17.160 -11.779  1.00219.34           N  
ANISOU 3407  N   ARG B1098    36525  22548  24268   1358   2044    -99       N  
ATOM   3408  CA  ARG B1098     -12.310 -17.895 -11.952  1.00218.91           C  
ANISOU 3408  CA  ARG B1098    36530  22550  24094   1467   1840    -94       C  
ATOM   3409  C   ARG B1098     -11.644 -17.527 -13.279  1.00220.37           C  
ANISOU 3409  C   ARG B1098    36324  22992  24416   1396   1594   -114       C  
ATOM   3410  O   ARG B1098     -10.415 -17.559 -13.373  1.00219.33           O  
ANISOU 3410  O   ARG B1098    36187  22953  24196   1497   1346   -105       O  
ATOM   3411  CB  ARG B1098     -12.517 -19.412 -11.855  1.00220.61           C  
ANISOU 3411  CB  ARG B1098    36936  22622  24263   1492   2047    -96       C  
ATOM   3412  N   ASN B1099     -12.458 -17.143 -14.285  1.00216.03           N  
ANISOU 3412  N   ASN B1099    35448  22555  24079   1228   1664   -137       N  
ATOM   3413  CA  ASN B1099     -11.998 -16.688 -15.595  1.00214.35           C  
ANISOU 3413  CA  ASN B1099    34863  22577  24004   1143   1461   -155       C  
ATOM   3414  C   ASN B1099     -11.418 -15.261 -15.462  1.00217.84           C  
ANISOU 3414  C   ASN B1099    35215  23125  24428   1175   1231   -142       C  
ATOM   3415  O   ASN B1099     -10.421 -14.946 -16.109  1.00216.61           O  
ANISOU 3415  O   ASN B1099    34886  23131  24284   1189    989   -148       O  
ATOM   3416  CB  ASN B1099     -13.139 -16.749 -16.619  1.00214.18           C  
ANISOU 3416  CB  ASN B1099    34556  22627  24194    958   1617   -180       C  
ATOM   3417  N   ALA B1100     -11.983 -14.453 -14.526  1.00214.91           N  
ANISOU 3417  N   ALA B1100    35002  22642  24011   1196   1318   -126       N  
ATOM   3418  CA  ALA B1100     -11.555 -13.084 -14.216  1.00234.98           C  
ANISOU 3418  CA  ALA B1100    37524  25241  26517   1222   1142   -118       C  
ATOM   3419  C   ALA B1100     -10.257 -13.071 -13.401  1.00244.23           C  
ANISOU 3419  C   ALA B1100    37808  26946  28044   1186    788   -127       C  
ATOM   3420  O   ALA B1100     -10.081 -13.868 -12.481  1.00204.00           O  
ANISOU 3420  O   ALA B1100    34146  21145  22219   1478    984   -101       O  
ATOM   3421  CB  ALA B1100     -12.653 -12.349 -13.457  1.00236.08           C  
ANISOU 3421  CB  ALA B1100    37728  25272  26700   1191   1337   -104       C  
ATOM   3422  C   SER B  44      -3.926 -22.279 -24.357  1.00150.59           C  
ANISOU 3422  C   SER B  44    25602  15445  16172   1290    579   -245       C  
ATOM   3423  O   SER B  44      -3.775 -21.827 -25.495  1.00149.98           O  
ANISOU 3423  O   SER B  44    25271  15514  16200   1179    506   -270       O  
ATOM   3424  CB  SER B  44      -6.327 -22.675 -23.687  1.00154.43           C  
ANISOU 3424  CB  SER B  44    26300  15713  16663   1086    940   -289       C  
ATOM   3425  OG  SER B  44      -6.773 -21.725 -24.644  1.00162.51           O  
ANISOU 3425  OG  SER B  44    27027  16900  17820    916    863   -318       O  
ATOM   3426  N   SER B  45      -3.164 -21.911 -23.294  1.00143.70           N  
ANISOU 3426  N   SER B  45    24838  14557  15205   1467    432   -198       N  
ATOM   3427  CA  SER B  45      -2.036 -20.983 -23.330  1.00140.86           C  
ANISOU 3427  CA  SER B  45    24305  14352  14864   1544    171   -175       C  
ATOM   3428  C   SER B  45      -0.892 -21.590 -24.149  1.00140.48           C  
ANISOU 3428  C   SER B  45    24143  14383  14849   1627    109   -164       C  
ATOM   3429  O   SER B  45      -0.203 -20.856 -24.855  1.00139.94           O  
ANISOU 3429  O   SER B  45    23826  14476  14869   1594    -48   -170       O  
ATOM   3430  CB  SER B  45      -1.569 -20.655 -21.917  1.00144.40           C  
ANISOU 3430  CB  SER B  45    24942  14742  15182   1710     47   -133       C  
ATOM   3431  OG  SER B  45      -0.514 -19.709 -21.912  1.00150.93           O  
ANISOU 3431  OG  SER B  45    25594  15721  16031   1763   -212   -120       O  
ATOM   3432  N   LEU B  46      -0.712 -22.929 -24.087  1.00133.75           N  
ANISOU 3432  N   LEU B  46    23477  13410  13933   1730    251   -149       N  
ATOM   3433  CA  LEU B  46       0.323 -23.609 -24.866  1.00131.94           C  
ANISOU 3433  CA  LEU B  46    23162  13233  13736   1820    231   -135       C  
ATOM   3434  C   LEU B  46      -0.152 -23.753 -26.301  1.00130.99           C  
ANISOU 3434  C   LEU B  46    22872  13170  13728   1624    345   -191       C  
ATOM   3435  O   LEU B  46       0.639 -23.570 -27.225  1.00130.13           O  
ANISOU 3435  O   LEU B  46    22560  13186  13698   1620    261   -193       O  
ATOM   3436  CB  LEU B  46       0.702 -24.987 -24.260  1.00133.34           C  
ANISOU 3436  CB  LEU B  46    23621  13247  13797   2018    352    -92       C  
ATOM   3437  CG  LEU B  46       1.749 -25.848 -25.006  1.00137.59           C  
ANISOU 3437  CG  LEU B  46    24107  13809  14363   2139    371    -69       C  
ATOM   3438  CD1 LEU B  46       3.107 -25.172 -25.067  1.00137.66           C  
ANISOU 3438  CD1 LEU B  46    23893  13989  14421   2267    115    -29       C  
ATOM   3439  CD2 LEU B  46       1.900 -27.177 -24.355  1.00140.06           C  
ANISOU 3439  CD2 LEU B  46    24729  13934  14553   2324    523    -24       C  
ATOM   3440  N   ALA B  47      -1.451 -24.051 -26.477  1.00124.33           N  
ANISOU 3440  N   ALA B  47    22110  12237  12891   1457    533   -236       N  
ATOM   3441  CA  ALA B  47      -2.101 -24.208 -27.774  1.00122.32           C  
ANISOU 3441  CA  ALA B  47    21720  12030  12727   1248    642   -295       C  
ATOM   3442  C   ALA B  47      -2.000 -22.930 -28.594  1.00123.21           C  
ANISOU 3442  C   ALA B  47    21530  12337  12949   1128    476   -311       C  
ATOM   3443  O   ALA B  47      -1.777 -22.984 -29.803  1.00122.18           O  
ANISOU 3443  O   ALA B  47    21245  12293  12884   1038    480   -338       O  
ATOM   3444  CB  ALA B  47      -3.559 -24.573 -27.570  1.00123.13           C  
ANISOU 3444  CB  ALA B  47    21950  12014  12820   1093    839   -337       C  
ATOM   3445  N   LEU B  48      -2.143 -21.777 -27.917  1.00118.35           N  
ANISOU 3445  N   LEU B  48    20849  11778  12341   1131    338   -292       N  
ATOM   3446  CA  LEU B  48      -2.077 -20.452 -28.519  1.00116.08           C  
ANISOU 3446  CA  LEU B  48    20301  11657  12147   1030    183   -299       C  
ATOM   3447  C   LEU B  48      -0.639 -20.105 -28.902  1.00118.55           C  
ANISOU 3447  C   LEU B  48    20462  12089  12491   1134     12   -275       C  
ATOM   3448  O   LEU B  48      -0.416 -19.662 -30.031  1.00118.36           O  
ANISOU 3448  O   LEU B  48    20232  12185  12553   1035    -31   -294       O  
ATOM   3449  CB  LEU B  48      -2.662 -19.402 -27.568  1.00115.54           C  
ANISOU 3449  CB  LEU B  48    20253  11582  12066   1015    114   -285       C  
ATOM   3450  CG  LEU B  48      -3.079 -18.092 -28.206  1.00119.33           C  
ANISOU 3450  CG  LEU B  48    20501  12196  12642    871     24   -297       C  
ATOM   3451  CD1 LEU B  48      -4.378 -18.249 -28.991  1.00118.68           C  
ANISOU 3451  CD1 LEU B  48    20357  12114  12622    684    169   -334       C  
ATOM   3452  CD2 LEU B  48      -3.184 -16.983 -27.153  1.00123.18           C  
ANISOU 3452  CD2 LEU B  48    21020  12678  13103    913    -82   -273       C  
ATOM   3453  N   ALA B  49       0.333 -20.328 -27.984  1.00113.45           N  
ANISOU 3453  N   ALA B  49    19915  11411  11778   1332    -82   -232       N  
ATOM   3454  CA  ALA B  49       1.750 -20.064 -28.225  1.00112.69           C  
ANISOU 3454  CA  ALA B  49    19668  11429  11721   1446   -247   -207       C  
ATOM   3455  C   ALA B  49       2.244 -20.813 -29.462  1.00117.92           C  
ANISOU 3455  C   ALA B  49    20239  12123  12442   1432   -157   -219       C  
ATOM   3456  O   ALA B  49       3.027 -20.248 -30.220  1.00117.64           O  
ANISOU 3456  O   ALA B  49    19988  12218  12493   1413   -258   -220       O  
ATOM   3457  CB  ALA B  49       2.578 -20.446 -27.018  1.00114.46           C  
ANISOU 3457  CB  ALA B  49    20042  11597  11850   1669   -340   -157       C  
ATOM   3458  N   ILE B  50       1.746 -22.047 -29.699  1.00115.48           N  
ANISOU 3458  N   ILE B  50    20102  11687  12087   1426     46   -234       N  
ATOM   3459  CA  ILE B  50       2.109 -22.862 -30.869  1.00115.78           C  
ANISOU 3459  CA  ILE B  50    20101  11727  12163   1403    164   -252       C  
ATOM   3460  C   ILE B  50       1.520 -22.219 -32.149  1.00119.37           C  
ANISOU 3460  C   ILE B  50    20368  12285  12702   1175    179   -303       C  
ATOM   3461  O   ILE B  50       2.237 -22.085 -33.144  1.00119.36           O  
ANISOU 3461  O   ILE B  50    20211  12374  12765   1158    153   -308       O  
ATOM   3462  CB  ILE B  50       1.680 -24.355 -30.706  1.00119.51           C  
ANISOU 3462  CB  ILE B  50    20841  12017  12551   1447    389   -259       C  
ATOM   3463  CG1 ILE B  50       2.436 -25.022 -29.534  1.00121.09           C  
ANISOU 3463  CG1 ILE B  50    21227  12119  12662   1705    368   -195       C  
ATOM   3464  CG2 ILE B  50       1.878 -25.145 -32.014  1.00120.00           C  
ANISOU 3464  CG2 ILE B  50    20880  12069  12646   1382    533   -293       C  
ATOM   3465  CD1 ILE B  50       1.753 -26.254 -28.939  1.00129.67           C  
ANISOU 3465  CD1 ILE B  50    22630  12998  13641   1748    581   -196       C  
ATOM   3466  N   ALA B  51       0.233 -21.810 -32.104  1.00114.48           N  
ANISOU 3466  N   ALA B  51    19764  11652  12081   1009    221   -337       N  
ATOM   3467  CA  ALA B  51      -0.479 -21.191 -33.221  1.00112.87           C  
ANISOU 3467  CA  ALA B  51    19398  11544  11944    798    226   -378       C  
ATOM   3468  C   ALA B  51       0.207 -19.898 -33.672  1.00115.81           C  
ANISOU 3468  C   ALA B  51    19532  12077  12395    785     45   -361       C  
ATOM   3469  O   ALA B  51       0.313 -19.641 -34.869  1.00114.04           O  
ANISOU 3469  O   ALA B  51    19168  11940  12222    680     46   -382       O  
ATOM   3470  CB  ALA B  51      -1.920 -20.914 -32.822  1.00113.13           C  
ANISOU 3470  CB  ALA B  51    19482  11535  11967    665    283   -401       C  
ATOM   3471  N   ILE B  52       0.706 -19.108 -32.709  1.00113.63           N  
ANISOU 3471  N   ILE B  52    19222  11832  12119    889   -104   -325       N  
ATOM   3472  CA  ILE B  52       1.405 -17.855 -32.975  1.00113.26           C  
ANISOU 3472  CA  ILE B  52    18966  11923  12144    878   -274   -311       C  
ATOM   3473  C   ILE B  52       2.776 -18.170 -33.600  1.00117.37           C  
ANISOU 3473  C   ILE B  52    19383  12503  12710    972   -306   -298       C  
ATOM   3474  O   ILE B  52       3.094 -17.604 -34.652  1.00116.75           O  
ANISOU 3474  O   ILE B  52    19133  12525  12704    885   -333   -310       O  
ATOM   3475  CB  ILE B  52       1.477 -17.004 -31.686  1.00116.61           C  
ANISOU 3475  CB  ILE B  52    19419  12345  12543    950   -412   -285       C  
ATOM   3476  CG1 ILE B  52       0.134 -16.267 -31.495  1.00116.97           C  
ANISOU 3476  CG1 ILE B  52    19480  12376  12589    814   -383   -298       C  
ATOM   3477  CG2 ILE B  52       2.648 -16.016 -31.711  1.00117.04           C  
ANISOU 3477  CG2 ILE B  52    19293  12518  12657    997   -595   -269       C  
ATOM   3478  CD1 ILE B  52      -0.225 -15.850 -30.078  1.00131.74           C  
ANISOU 3478  CD1 ILE B  52    21486  14173  14396    879   -431   -280       C  
ATOM   3479  N   THR B  53       3.544 -19.117 -32.991  1.00113.65           N  
ANISOU 3479  N   THR B  53    19024  11962  12196   1153   -286   -270       N  
ATOM   3480  CA  THR B  53       4.860 -19.577 -33.467  1.00113.44           C  
ANISOU 3480  CA  THR B  53    18911  11977  12216   1275   -296   -249       C  
ATOM   3481  C   THR B  53       4.730 -20.104 -34.894  1.00116.01           C  
ANISOU 3481  C   THR B  53    19202  12303  12573   1169   -144   -281       C  
ATOM   3482  O   THR B  53       5.616 -19.884 -35.715  1.00114.49           O  
ANISOU 3482  O   THR B  53    18851  12192  12456   1178   -163   -277       O  
ATOM   3483  CB  THR B  53       5.441 -20.636 -32.513  1.00116.28           C  
ANISOU 3483  CB  THR B  53    19437  12237  12506   1494   -274   -208       C  
ATOM   3484  OG1 THR B  53       5.547 -20.064 -31.216  1.00107.68           O  
ANISOU 3484  OG1 THR B  53    18387  11154  11373   1580   -432   -181       O  
ATOM   3485  CG2 THR B  53       6.819 -21.142 -32.946  1.00117.61           C  
ANISOU 3485  CG2 THR B  53    19504  12448  12733   1646   -280   -175       C  
ATOM   3486  N   ALA B  54       3.599 -20.757 -35.187  1.00113.30           N  
ANISOU 3486  N   ALA B  54    19008  11870  12172   1056      9   -318       N  
ATOM   3487  CA  ALA B  54       3.292 -21.293 -36.503  1.00113.47           C  
ANISOU 3487  CA  ALA B  54    19035  11882  12198    929    153   -359       C  
ATOM   3488  C   ALA B  54       3.050 -20.168 -37.499  1.00115.43           C  
ANISOU 3488  C   ALA B  54    19091  12260  12509    761     81   -381       C  
ATOM   3489  O   ALA B  54       3.580 -20.226 -38.607  1.00115.48           O  
ANISOU 3489  O   ALA B  54    19016  12312  12551    723    125   -393       O  
ATOM   3490  CB  ALA B  54       2.075 -22.196 -36.429  1.00114.52           C  
ANISOU 3490  CB  ALA B  54    19372  11890  12252    834    313   -399       C  
ATOM   3491  N   LEU B  55       2.271 -19.139 -37.101  1.00109.54           N  
ANISOU 3491  N   LEU B  55    18283  11565  11773    669    -21   -381       N  
ATOM   3492  CA  LEU B  55       1.958 -18.016 -37.974  1.00107.46           C  
ANISOU 3492  CA  LEU B  55    17852  11416  11561    520    -91   -393       C  
ATOM   3493  C   LEU B  55       3.230 -17.267 -38.334  1.00111.90           C  
ANISOU 3493  C   LEU B  55    18238  12077  12201    581   -192   -368       C  
ATOM   3494  O   LEU B  55       3.510 -17.117 -39.520  1.00111.50           O  
ANISOU 3494  O   LEU B  55    18101  12082  12182    505   -154   -381       O  
ATOM   3495  CB  LEU B  55       0.914 -17.085 -37.335  1.00106.15           C  
ANISOU 3495  CB  LEU B  55    17667  11270  11393    443   -169   -388       C  
ATOM   3496  CG  LEU B  55       0.392 -15.907 -38.173  1.00109.36           C  
ANISOU 3496  CG  LEU B  55    17922  11786  11845    295   -233   -391       C  
ATOM   3497  CD1 LEU B  55      -0.029 -16.339 -39.573  1.00108.85           C  
ANISOU 3497  CD1 LEU B  55    17846  11746  11764    159   -141   -425       C  
ATOM   3498  CD2 LEU B  55      -0.776 -15.226 -37.476  1.00112.35           C  
ANISOU 3498  CD2 LEU B  55    18313  12157  12218    235   -270   -383       C  
ATOM   3499  N   TYR B  56       4.031 -16.883 -37.319  1.00109.36           N  
ANISOU 3499  N   TYR B  56    17874  11771  11907    718   -311   -335       N  
ATOM   3500  CA  TYR B  56       5.281 -16.144 -37.485  1.00109.68           C  
ANISOU 3500  CA  TYR B  56    17733  11908  12033    775   -419   -315       C  
ATOM   3501  C   TYR B  56       6.359 -16.934 -38.231  1.00111.89           C  
ANISOU 3501  C   TYR B  56    17971  12189  12354    858   -332   -309       C  
ATOM   3502  O   TYR B  56       7.135 -16.329 -38.964  1.00111.65           O  
ANISOU 3502  O   TYR B  56    17775  12243  12405    832   -360   -306       O  
ATOM   3503  CB  TYR B  56       5.830 -15.678 -36.131  1.00112.71           C  
ANISOU 3503  CB  TYR B  56    18099  12303  12422    897   -574   -287       C  
ATOM   3504  CG  TYR B  56       5.087 -14.507 -35.518  1.00115.83           C  
ANISOU 3504  CG  TYR B  56    18484  12721  12805    811   -680   -290       C  
ATOM   3505  CD1 TYR B  56       4.566 -13.492 -36.318  1.00117.64           C  
ANISOU 3505  CD1 TYR B  56    18609  13014  13073    656   -689   -303       C  
ATOM   3506  CD2 TYR B  56       4.957 -14.381 -34.140  1.00117.00           C  
ANISOU 3506  CD2 TYR B  56    18733  12822  12899    895   -768   -276       C  
ATOM   3507  CE1 TYR B  56       3.911 -12.394 -35.757  1.00117.95           C  
ANISOU 3507  CE1 TYR B  56    18643  13067  13107    591   -773   -300       C  
ATOM   3508  CE2 TYR B  56       4.298 -13.293 -33.572  1.00117.42           C  
ANISOU 3508  CE2 TYR B  56    18790  12885  12940    821   -849   -279       C  
ATOM   3509  CZ  TYR B  56       3.784 -12.297 -34.384  1.00126.21           C  
ANISOU 3509  CZ  TYR B  56    19793  14059  14103    671   -847   -290       C  
ATOM   3510  OH  TYR B  56       3.131 -11.225 -33.827  1.00130.28           O  
ANISOU 3510  OH  TYR B  56    20320  14572  14608    610   -911   -287       O  
ATOM   3511  N   SER B  57       6.418 -18.257 -38.060  1.00107.46           N  
ANISOU 3511  N   SER B  57    17563  11528  11739    959   -213   -306       N  
ATOM   3512  CA  SER B  57       7.415 -19.051 -38.773  1.00108.01           C  
ANISOU 3512  CA  SER B  57    17607  11584  11847   1050   -106   -296       C  
ATOM   3513  C   SER B  57       7.046 -19.172 -40.276  1.00112.33           C  
ANISOU 3513  C   SER B  57    18156  12136  12390    892     31   -335       C  
ATOM   3514  O   SER B  57       7.925 -19.049 -41.140  1.00112.09           O  
ANISOU 3514  O   SER B  57    18008  12153  12427    903     71   -330       O  
ATOM   3515  CB  SER B  57       7.569 -20.423 -38.132  1.00110.81           C  
ANISOU 3515  CB  SER B  57    18148  11817  12138   1213     -7   -277       C  
ATOM   3516  OG  SER B  57       6.329 -21.102 -38.035  1.00115.41           O  
ANISOU 3516  OG  SER B  57    18940  12291  12619   1127    106   -309       O  
ATOM   3517  N   ALA B  58       5.741 -19.375 -40.577  1.00108.01           N  
ANISOU 3517  N   ALA B  58    17736  11542  11762    742     97   -374       N  
ATOM   3518  CA  ALA B  58       5.227 -19.475 -41.942  1.00106.90           C  
ANISOU 3518  CA  ALA B  58    17617  11408  11591    577    202   -416       C  
ATOM   3519  C   ALA B  58       5.332 -18.133 -42.630  1.00110.75           C  
ANISOU 3519  C   ALA B  58    17923  12019  12139    470    102   -412       C  
ATOM   3520  O   ALA B  58       5.667 -18.093 -43.810  1.00111.02           O  
ANISOU 3520  O   ALA B  58    17920  12080  12183    405    175   -425       O  
ATOM   3521  CB  ALA B  58       3.783 -19.944 -41.938  1.00106.97           C  
ANISOU 3521  CB  ALA B  58    17782  11354  11508    442    264   -457       C  
ATOM   3522  N   VAL B  59       5.072 -17.021 -41.895  1.00106.31           N  
ANISOU 3522  N   VAL B  59    17261  11521  11609    455    -54   -391       N  
ATOM   3523  CA  VAL B  59       5.186 -15.672 -42.459  1.00105.02           C  
ANISOU 3523  CA  VAL B  59    16936  11464  11503    363   -145   -383       C  
ATOM   3524  C   VAL B  59       6.672 -15.373 -42.695  1.00110.69           C  
ANISOU 3524  C   VAL B  59    17506  12231  12319    455   -161   -361       C  
ATOM   3525  O   VAL B  59       6.995 -14.777 -43.716  1.00111.07           O  
ANISOU 3525  O   VAL B  59    17463  12335  12405    376   -138   -364       O  
ATOM   3526  CB  VAL B  59       4.462 -14.584 -41.616  1.00107.26           C  
ANISOU 3526  CB  VAL B  59    17176  11786  11792    320   -286   -368       C  
ATOM   3527  CG1 VAL B  59       4.930 -13.171 -41.922  1.00106.74           C  
ANISOU 3527  CG1 VAL B  59    16942  11814  11800    273   -386   -350       C  
ATOM   3528  CG2 VAL B  59       2.958 -14.703 -41.753  1.00106.22           C  
ANISOU 3528  CG2 VAL B  59    17144  11629  11587    196   -254   -389       C  
ATOM   3529  N   CYS B  60       7.569 -15.864 -41.820  1.00108.12           N  
ANISOU 3529  N   CYS B  60    17163  11884  12033    623   -189   -338       N  
ATOM   3530  CA  CYS B  60       9.007 -15.657 -41.980  1.00108.80           C  
ANISOU 3530  CA  CYS B  60    17086  12025  12230    720   -206   -316       C  
ATOM   3531  C   CYS B  60       9.545 -16.440 -43.202  1.00112.76           C  
ANISOU 3531  C   CYS B  60    17607  12493  12743    726    -25   -325       C  
ATOM   3532  O   CYS B  60      10.088 -15.837 -44.118  1.00111.11           O  
ANISOU 3532  O   CYS B  60    17279  12340  12599    664      8   -326       O  
ATOM   3533  CB  CYS B  60       9.759 -16.018 -40.701  1.00109.92           C  
ANISOU 3533  CB  CYS B  60    17203  12158  12402    905   -299   -286       C  
ATOM   3534  SG  CYS B  60      11.508 -15.552 -40.712  1.00115.24           S  
ANISOU 3534  SG  CYS B  60    17620  12930  13235   1015   -369   -258       S  
ATOM   3535  N   ALA B  61       9.357 -17.754 -43.233  1.00111.48           N  
ANISOU 3535  N   ALA B  61    17612  12231  12513    793    107   -332       N  
ATOM   3536  CA  ALA B  61       9.864 -18.577 -44.329  1.00113.12           C  
ANISOU 3536  CA  ALA B  61    17872  12389  12721    808    297   -342       C  
ATOM   3537  C   ALA B  61       9.249 -18.220 -45.697  1.00118.57           C  
ANISOU 3537  C   ALA B  61    18601  13092  13359    614    378   -380       C  
ATOM   3538  O   ALA B  61       9.963 -18.265 -46.699  1.00118.78           O  
ANISOU 3538  O   ALA B  61    18584  13121  13424    608    491   -381       O  
ATOM   3539  CB  ALA B  61       9.637 -20.036 -44.024  1.00114.53           C  
ANISOU 3539  CB  ALA B  61    18257  12440  12819    904    427   -346       C  
ATOM   3540  N   VAL B  62       7.954 -17.853 -45.751  1.00115.53           N  
ANISOU 3540  N   VAL B  62    18295  12715  12887    462    321   -407       N  
ATOM   3541  CA  VAL B  62       7.340 -17.472 -47.031  1.00115.60           C  
ANISOU 3541  CA  VAL B  62    18338  12749  12836    284    370   -437       C  
ATOM   3542  C   VAL B  62       7.908 -16.087 -47.436  1.00119.56           C  
ANISOU 3542  C   VAL B  62    18649  13353  13425    242    286   -413       C  
ATOM   3543  O   VAL B  62       8.395 -15.931 -48.549  1.00119.12           O  
ANISOU 3543  O   VAL B  62    18573  13308  13380    195    380   -417       O  
ATOM   3544  CB  VAL B  62       5.786 -17.534 -47.010  1.00118.77           C  
ANISOU 3544  CB  VAL B  62    18862  13138  13126    139    333   -470       C  
ATOM   3545  CG1 VAL B  62       5.153 -16.748 -48.159  1.00118.14           C  
ANISOU 3545  CG1 VAL B  62    18765  13125  12999    -35    312   -485       C  
ATOM   3546  CG2 VAL B  62       5.307 -18.983 -47.026  1.00119.14           C  
ANISOU 3546  CG2 VAL B  62    19116  13070  13081    139    471   -509       C  
ATOM   3547  N   GLY B  63       7.917 -15.146 -46.502  1.00116.01           N  
ANISOU 3547  N   GLY B  63    18075  12965  13037    267    125   -388       N  
ATOM   3548  CA  GLY B  63       8.442 -13.806 -46.716  1.00115.79           C  
ANISOU 3548  CA  GLY B  63    17875  13023  13096    227     43   -368       C  
ATOM   3549  C   GLY B  63       9.910 -13.781 -47.089  1.00121.33           C  
ANISOU 3549  C   GLY B  63    18443  13744  13913    310    111   -353       C  
ATOM   3550  O   GLY B  63      10.238 -13.534 -48.246  1.00121.45           O  
ANISOU 3550  O   GLY B  63    18441  13767  13936    241    213   -357       O  
ATOM   3551  N   LEU B  64      10.784 -14.145 -46.133  1.00119.36           N  
ANISOU 3551  N   LEU B  64    18109  13495  13747    464     68   -334       N  
ATOM   3552  CA  LEU B  64      12.250 -14.181 -46.227  1.00120.80           C  
ANISOU 3552  CA  LEU B  64    18126  13708  14066    573    110   -314       C  
ATOM   3553  C   LEU B  64      12.755 -14.922 -47.469  1.00124.76           C  
ANISOU 3553  C   LEU B  64    18678  14157  14569    581    326   -320       C  
ATOM   3554  O   LEU B  64      13.506 -14.346 -48.248  1.00124.72           O  
ANISOU 3554  O   LEU B  64    18552  14188  14649    544    392   -315       O  
ATOM   3555  CB  LEU B  64      12.850 -14.813 -44.958  1.00121.88           C  
ANISOU 3555  CB  LEU B  64    18218  13839  14251    757     31   -290       C  
ATOM   3556  CG  LEU B  64      14.320 -14.562 -44.697  1.00128.57           C  
ANISOU 3556  CG  LEU B  64    18835  14754  15260    871     -6   -264       C  
ATOM   3557  CD1 LEU B  64      14.533 -13.227 -44.017  1.00128.43           C  
ANISOU 3557  CD1 LEU B  64    18651  14830  15315    812   -200   -266       C  
ATOM   3558  CD2 LEU B  64      14.895 -15.645 -43.832  1.00133.55           C  
ANISOU 3558  CD2 LEU B  64    19478  15355  15911   1079    -14   -234       C  
ATOM   3559  N   LEU B  65      12.335 -16.167 -47.666  1.00121.61           N  
ANISOU 3559  N   LEU B  65    18468  13665  14072    620    449   -333       N  
ATOM   3560  CA  LEU B  65      12.763 -16.950 -48.828  1.00122.74           C  
ANISOU 3560  CA  LEU B  65    18699  13740  14199    628    670   -343       C  
ATOM   3561  C   LEU B  65      12.148 -16.419 -50.139  1.00124.17           C  
ANISOU 3561  C   LEU B  65    18964  13923  14294    438    739   -373       C  
ATOM   3562  O   LEU B  65      12.858 -16.347 -51.141  1.00124.91           O  
ANISOU 3562  O   LEU B  65    19028  14004  14427    424    881   -372       O  
ATOM   3563  CB  LEU B  65      12.458 -18.458 -48.659  1.00123.59           C  
ANISOU 3563  CB  LEU B  65    19014  13731  14215    715    792   -354       C  
ATOM   3564  N   GLY B  66      10.868 -16.041 -50.107  1.00117.42           N  
ANISOU 3564  N   GLY B  66    18206  13083  13326    303    639   -395       N  
ATOM   3565  CA  GLY B  66      10.145 -15.509 -51.262  1.00115.92           C  
ANISOU 3565  CA  GLY B  66    18101  12907  13037    129    668   -416       C  
ATOM   3566  C   GLY B  66      10.743 -14.233 -51.833  1.00117.54           C  
ANISOU 3566  C   GLY B  66    18155  13182  13324     75    649   -394       C  
ATOM   3567  O   GLY B  66      10.919 -14.139 -53.049  1.00117.29           O  
ANISOU 3567  O   GLY B  66    18186  13130  13251      1    775   -403       O  
ATOM   3568  N   ASN B  67      11.095 -13.261 -50.956  1.00111.55           N  
ANISOU 3568  N   ASN B  67    17210  12495  12677    109    500   -368       N  
ATOM   3569  CA  ASN B  67      11.707 -11.985 -51.328  1.00110.44           C  
ANISOU 3569  CA  ASN B  67    16916  12416  12631     55    477   -349       C  
ATOM   3570  C   ASN B  67      13.133 -12.164 -51.841  1.00114.89           C  
ANISOU 3570  C   ASN B  67    17365  12966  13321    129    628   -340       C  
ATOM   3571  O   ASN B  67      13.511 -11.475 -52.790  1.00115.91           O  
ANISOU 3571  O   ASN B  67    17464  13104  13475     51    715   -335       O  
ATOM   3572  CB  ASN B  67      11.711 -11.007 -50.167  1.00109.83           C  
ANISOU 3572  CB  ASN B  67    16689  12405  12634     69    284   -333       C  
ATOM   3573  CG  ASN B  67      10.359 -10.501 -49.778  1.00134.31           C  
ANISOU 3573  CG  ASN B  67    19876  15524  15633    -16    150   -334       C  
ATOM   3574  OD1 ASN B  67       9.736  -9.666 -50.435  1.00134.69           O  
ANISOU 3574  OD1 ASN B  67    19960  15593  15623   -131    133   -327       O  
ATOM   3575  ND2 ASN B  67       9.963 -10.839 -48.582  1.00123.35           N  
ANISOU 3575  ND2 ASN B  67    18498  14132  14237     51     40   -335       N  
ATOM   3576  N   VAL B  68      13.929 -13.071 -51.222  1.00110.46           N  
ANISOU 3576  N   VAL B  68    16741  12385  12844    284    667   -332       N  
ATOM   3577  CA  VAL B  68      15.311 -13.361 -51.643  1.00110.95           C  
ANISOU 3577  CA  VAL B  68    16675  12436  13046    379    820   -317       C  
ATOM   3578  C   VAL B  68      15.287 -13.936 -53.085  1.00114.08           C  
ANISOU 3578  C   VAL B  68    17244  12747  13352    326   1056   -333       C  
ATOM   3579  O   VAL B  68      16.060 -13.496 -53.946  1.00114.45           O  
ANISOU 3579  O   VAL B  68    17220  12793  13474    296   1189   -326       O  
ATOM   3580  CB  VAL B  68      16.054 -14.279 -50.635  1.00115.10           C  
ANISOU 3580  CB  VAL B  68    17109  12957  13665    576    800   -297       C  
ATOM   3581  CG1 VAL B  68      17.349 -14.830 -51.229  1.00116.79           C  
ANISOU 3581  CG1 VAL B  68    17224  13143  14006    687   1000   -278       C  
ATOM   3582  CG2 VAL B  68      16.343 -13.530 -49.335  1.00114.36           C  
ANISOU 3582  CG2 VAL B  68    16819  12959  13675    620    573   -282       C  
ATOM   3583  N   LEU B  69      14.342 -14.860 -53.342  1.00109.46           N  
ANISOU 3583  N   LEU B  69    16899  12090  12601    298   1102   -358       N  
ATOM   3584  CA  LEU B  69      14.090 -15.485 -54.637  1.00109.64           C  
ANISOU 3584  CA  LEU B  69    17137  12025  12495    227   1300   -384       C  
ATOM   3585  C   LEU B  69      13.727 -14.427 -55.668  1.00114.26           C  
ANISOU 3585  C   LEU B  69    17760  12640  13014     63   1304   -389       C  
ATOM   3586  O   LEU B  69      14.221 -14.514 -56.788  1.00115.03           O  
ANISOU 3586  O   LEU B  69    17928  12684  13093     33   1493   -394       O  
ATOM   3587  CB  LEU B  69      12.959 -16.523 -54.506  1.00108.91           C  
ANISOU 3587  CB  LEU B  69    17282  11868  12233    197   1293   -419       C  
ATOM   3588  CG  LEU B  69      12.461 -17.219 -55.775  1.00114.04           C  
ANISOU 3588  CG  LEU B  69    18192  12425  12711     94   1464   -461       C  
ATOM   3589  CD1 LEU B  69      13.564 -18.027 -56.431  1.00116.26           C  
ANISOU 3589  CD1 LEU B  69    18518  12614  13044    196   1719   -457       C  
ATOM   3590  CD2 LEU B  69      11.258 -18.096 -55.476  1.00114.92           C  
ANISOU 3590  CD2 LEU B  69    18504  12491  12671     39   1417   -502       C  
ATOM   3591  N   VAL B  70      12.875 -13.429 -55.287  1.00109.86           N  
ANISOU 3591  N   VAL B  70    17166  12158  12418    -34   1107   -384       N  
ATOM   3592  CA  VAL B  70      12.443 -12.319 -56.149  1.00109.23           C  
ANISOU 3592  CA  VAL B  70    17121  12111  12272   -177   1084   -377       C  
ATOM   3593  C   VAL B  70      13.666 -11.483 -56.509  1.00116.64           C  
ANISOU 3593  C   VAL B  70    17889  13066  13362   -161   1175   -352       C  
ATOM   3594  O   VAL B  70      13.870 -11.199 -57.688  1.00117.16           O  
ANISOU 3594  O   VAL B  70    18042  13095  13377   -233   1318   -351       O  
ATOM   3595  CB  VAL B  70      11.316 -11.460 -55.514  1.00110.96           C  
ANISOU 3595  CB  VAL B  70    17320  12402  12437   -253    858   -368       C  
ATOM   3596  CG1 VAL B  70      11.121 -10.153 -56.267  1.00110.39           C  
ANISOU 3596  CG1 VAL B  70    17242  12367  12336   -365    835   -345       C  
ATOM   3597  CG2 VAL B  70      10.006 -12.219 -55.472  1.00110.11           C  
ANISOU 3597  CG2 VAL B  70    17396  12276  12166   -306    799   -396       C  
ATOM   3598  N   MET B  71      14.495 -11.134 -55.501  1.00115.78           N  
ANISOU 3598  N   MET B  71    17545  13010  13438    -70   1098   -335       N  
ATOM   3599  CA  MET B  71      15.724 -10.354 -55.672  1.00117.88           C  
ANISOU 3599  CA  MET B  71    17607  13301  13881    -57   1171   -318       C  
ATOM   3600  C   MET B  71      16.722 -11.071 -56.584  1.00126.04           C  
ANISOU 3600  C   MET B  71    18658  14264  14969      1   1431   -318       C  
ATOM   3601  O   MET B  71      17.317 -10.425 -57.449  1.00126.14           O  
ANISOU 3601  O   MET B  71    18637  14261  15031    -59   1568   -310       O  
ATOM   3602  CB  MET B  71      16.373 -10.051 -54.319  1.00120.24           C  
ANISOU 3602  CB  MET B  71    17656  13675  14355     33   1018   -307       C  
ATOM   3603  CG  MET B  71      15.733  -8.887 -53.593  1.00122.59           C  
ANISOU 3603  CG  MET B  71    17897  14038  14643    -49    803   -304       C  
ATOM   3604  SD  MET B  71      16.562  -8.511 -52.027  1.00127.14           S  
ANISOU 3604  SD  MET B  71    18199  14698  15411     43    619   -301       S  
ATOM   3605  CE  MET B  71      15.859  -9.726 -50.991  1.00122.92           C  
ANISOU 3605  CE  MET B  71    17771  14149  14783    164    507   -304       C  
ATOM   3606  N   PHE B  72      16.877 -12.402 -56.416  1.00125.69           N  
ANISOU 3606  N   PHE B  72    18684  14166  14908    118   1516   -325       N  
ATOM   3607  CA  PHE B  72      17.779 -13.225 -57.234  1.00128.51           C  
ANISOU 3607  CA  PHE B  72    19080  14440  15309    194   1782   -323       C  
ATOM   3608  C   PHE B  72      17.373 -13.223 -58.735  1.00132.59           C  
ANISOU 3608  C   PHE B  72    19848  14872  15657     70   1962   -342       C  
ATOM   3609  O   PHE B  72      18.241 -13.040 -59.584  1.00133.59           O  
ANISOU 3609  O   PHE B  72    19946  14956  15855     68   2168   -332       O  
ATOM   3610  CB  PHE B  72      17.850 -14.665 -56.696  1.00131.45           C  
ANISOU 3610  CB  PHE B  72    19518  14758  15670    346   1827   -326       C  
ATOM   3611  CG  PHE B  72      18.544 -15.645 -57.616  1.00135.83           C  
ANISOU 3611  CG  PHE B  72    20184  15201  16226    420   2120   -326       C  
ATOM   3612  CD1 PHE B  72      19.930 -15.633 -57.759  1.00141.71           C  
ANISOU 3612  CD1 PHE B  72    20722  15946  17177    531   2278   -296       C  
ATOM   3613  CD2 PHE B  72      17.813 -16.586 -58.334  1.00139.27           C  
ANISOU 3613  CD2 PHE B  72    20928  15528  16459    376   2243   -360       C  
ATOM   3614  CE1 PHE B  72      20.571 -16.545 -58.608  1.00145.08           C  
ANISOU 3614  CE1 PHE B  72    21257  16258  17608    610   2570   -293       C  
ATOM   3615  CE2 PHE B  72      18.454 -17.502 -59.177  1.00144.56           C  
ANISOU 3615  CE2 PHE B  72    21726  16080  17122    445   2528   -363       C  
ATOM   3616  CZ  PHE B  72      19.830 -17.480 -59.302  1.00144.61           C  
ANISOU 3616  CZ  PHE B  72    21530  16080  17335    570   2697   -326       C  
ATOM   3617  N   VAL B  73      16.069 -13.447 -59.049  1.00127.57           N  
ANISOU 3617  N   VAL B  73    19456  14216  14800    -33   1885   -368       N  
ATOM   3618  CA  VAL B  73      15.491 -13.472 -60.408  1.00127.12           C  
ANISOU 3618  CA  VAL B  73    19665  14092  14544   -162   2006   -389       C  
ATOM   3619  C   VAL B  73      15.739 -12.131 -61.089  1.00132.09           C  
ANISOU 3619  C   VAL B  73    20239  14752  15199   -260   2025   -366       C  
ATOM   3620  O   VAL B  73      16.115 -12.097 -62.255  1.00132.81           O  
ANISOU 3620  O   VAL B  73    20457  14771  15233   -305   2228   -367       O  
ATOM   3621  CB  VAL B  73      13.976 -13.820 -60.359  1.00128.89           C  
ANISOU 3621  CB  VAL B  73    20097  14325  14552   -258   1851   -420       C  
ATOM   3622  CG1 VAL B  73      13.248 -13.441 -61.647  1.00128.34           C  
ANISOU 3622  CG1 VAL B  73    20256  14231  14278   -413   1888   -434       C  
ATOM   3623  CG2 VAL B  73      13.769 -15.294 -60.040  1.00129.15           C  
ANISOU 3623  CG2 VAL B  73    20260  14285  14527   -185   1913   -453       C  
ATOM   3624  N   ILE B  74      15.549 -11.037 -60.341  1.00128.66           N  
ANISOU 3624  N   ILE B  74    19627  14412  14845   -289   1826   -344       N  
ATOM   3625  CA  ILE B  74      15.741  -9.660 -60.785  1.00128.90           C  
ANISOU 3625  CA  ILE B  74    19591  14472  14912   -380   1821   -319       C  
ATOM   3626  C   ILE B  74      17.221  -9.427 -61.182  1.00137.37           C  
ANISOU 3626  C   ILE B  74    20509  15510  16175   -334   2040   -305       C  
ATOM   3627  O   ILE B  74      17.481  -8.654 -62.104  1.00137.67           O  
ANISOU 3627  O   ILE B  74    20601  15514  16194   -416   2163   -292       O  
ATOM   3628  CB  ILE B  74      15.220  -8.706 -59.662  1.00129.64           C  
ANISOU 3628  CB  ILE B  74    19527  14666  15064   -401   1557   -303       C  
ATOM   3629  CG1 ILE B  74      13.843  -8.146 -60.033  1.00128.49           C  
ANISOU 3629  CG1 ILE B  74    19559  14542  14718   -515   1421   -296       C  
ATOM   3630  CG2 ILE B  74      16.194  -7.595 -59.280  1.00129.86           C  
ANISOU 3630  CG2 ILE B  74    19309  14736  15298   -403   1554   -284       C  
ATOM   3631  CD1 ILE B  74      12.885  -8.010 -58.909  1.00133.10           C  
ANISOU 3631  CD1 ILE B  74    20094  15196  15281   -508   1175   -295       C  
ATOM   3632  N   VAL B  75      18.161 -10.139 -60.534  1.00136.76           N  
ANISOU 3632  N   VAL B  75    20253  15436  16274   -200   2099   -307       N  
ATOM   3633  CA  VAL B  75      19.595 -10.011 -60.781  1.00139.36           C  
ANISOU 3633  CA  VAL B  75    20389  15746  16815   -140   2298   -293       C  
ATOM   3634  C   VAL B  75      20.032 -10.983 -61.901  1.00148.32           C  
ANISOU 3634  C   VAL B  75    21706  16760  17889   -100   2596   -300       C  
ATOM   3635  O   VAL B  75      20.555 -10.532 -62.922  1.00149.23           O  
ANISOU 3635  O   VAL B  75    21870  16816  18015   -158   2804   -293       O  
ATOM   3636  CB  VAL B  75      20.398 -10.200 -59.459  1.00143.04           C  
ANISOU 3636  CB  VAL B  75    20543  16294  17512     -8   2184   -284       C  
ATOM   3637  CG1 VAL B  75      21.892 -10.398 -59.718  1.00145.02           C  
ANISOU 3637  CG1 VAL B  75    20586  16525  17989     83   2406   -269       C  
ATOM   3638  CG2 VAL B  75      20.161  -9.023 -58.497  1.00141.52           C  
ANISOU 3638  CG2 VAL B  75    20172  16207  17392    -72   1928   -282       C  
ATOM   3639  N   ARG B  76      19.792 -12.290 -61.717  1.00147.87           N  
ANISOU 3639  N   ARG B  76    21770  16656  17759     -5   2629   -315       N  
ATOM   3640  CA  ARG B  76      20.189 -13.376 -62.624  1.00150.74           C  
ANISOU 3640  CA  ARG B  76    22320  16893  18062     52   2912   -325       C  
ATOM   3641  C   ARG B  76      19.392 -13.433 -63.944  1.00158.12           C  
ANISOU 3641  C   ARG B  76    23613  17735  18729    -86   3022   -351       C  
ATOM   3642  O   ARG B  76      19.963 -13.869 -64.943  1.00159.84           O  
ANISOU 3642  O   ARG B  76    23969  17843  18921    -73   3301   -355       O  
ATOM   3643  CB  ARG B  76      20.071 -14.740 -61.908  1.00150.39           C  
ANISOU 3643  CB  ARG B  76    22313  16821  18009    193   2892   -334       C  
ATOM   3644  CG  ARG B  76      20.938 -15.864 -62.484  1.00162.35           C  
ANISOU 3644  CG  ARG B  76    23903  18213  19569    319   3202   -330       C  
ATOM   3645  CD  ARG B  76      20.127 -17.119 -62.760  1.00177.84           C  
ANISOU 3645  CD  ARG B  76    26190  20070  21310    322   3261   -367       C  
ATOM   3646  NE  ARG B  76      20.951 -18.334 -62.762  1.00195.17           N  
ANISOU 3646  NE  ARG B  76    28402  22164  23589    499   3495   -354       N  
ATOM   3647  CZ  ARG B  76      20.530 -19.543 -62.387  1.00211.57           C  
ANISOU 3647  CZ  ARG B  76    30644  24172  25572    578   3508   -372       C  
ATOM   3648  NH1 ARG B  76      19.287 -19.718 -61.956  1.00198.63           N  
ANISOU 3648  NH1 ARG B  76    29154  22558  23758    486   3296   -408       N  
ATOM   3649  NH2 ARG B  76      21.353 -20.582 -62.428  1.00198.96           N1+
ANISOU 3649  NH2 ARG B  76    29060  22474  24061    753   3742   -351       N1+
ATOM   3650  N   TYR B  77      18.098 -13.047 -63.964  1.00155.19           N  
ANISOU 3650  N   TYR B  77    23398  17407  18160   -210   2813   -367       N  
ATOM   3651  CA  TYR B  77      17.301 -13.178 -65.188  1.00156.29           C  
ANISOU 3651  CA  TYR B  77    23878  17472  18032   -337   2889   -392       C  
ATOM   3652  C   TYR B  77      16.782 -11.835 -65.795  1.00160.53           C  
ANISOU 3652  C   TYR B  77    24472  18052  18470   -479   2798   -372       C  
ATOM   3653  O   TYR B  77      17.286 -11.456 -66.854  1.00161.78           O  
ANISOU 3653  O   TYR B  77    24736  18138  18595   -524   3003   -362       O  
ATOM   3654  CB  TYR B  77      16.124 -14.149 -64.965  1.00157.27           C  
ANISOU 3654  CB  TYR B  77    24208  17587  17960   -367   2761   -434       C  
ATOM   3655  CG  TYR B  77      16.509 -15.600 -64.733  1.00161.20           C  
ANISOU 3655  CG  TYR B  77    24771  17996  18482   -249   2910   -459       C  
ATOM   3656  CD1 TYR B  77      17.134 -16.346 -65.731  1.00165.62           C  
ANISOU 3656  CD1 TYR B  77    25519  18419  18991   -222   3214   -475       C  
ATOM   3657  CD2 TYR B  77      16.141 -16.260 -63.563  1.00161.30           C  
ANISOU 3657  CD2 TYR B  77    24701  18048  18540   -168   2756   -468       C  
ATOM   3658  CE1 TYR B  77      17.446 -17.695 -65.542  1.00168.17           C  
ANISOU 3658  CE1 TYR B  77    25928  18646  19324   -108   3366   -495       C  
ATOM   3659  CE2 TYR B  77      16.436 -17.611 -63.367  1.00163.45           C  
ANISOU 3659  CE2 TYR B  77    25062  18224  18816    -56   2901   -487       C  
ATOM   3660  CZ  TYR B  77      17.088 -18.327 -64.360  1.00174.08           C  
ANISOU 3660  CZ  TYR B  77    26587  19434  20121    -24   3207   -500       C  
ATOM   3661  OH  TYR B  77      17.384 -19.660 -64.169  1.00175.92           O  
ANISOU 3661  OH  TYR B  77    26923  19561  20358     97   3366   -515       O  
ATOM   3662  N   THR B  78      15.766 -11.152 -65.176  1.00155.46           N  
ANISOU 3662  N   THR B  78    23784  17514  17771   -544   2512   -364       N  
ATOM   3663  CA  THR B  78      15.137  -9.904 -65.689  1.00154.61           C  
ANISOU 3663  CA  THR B  78    23744  17448  17554   -663   2407   -337       C  
ATOM   3664  C   THR B  78      16.147  -8.731 -65.839  1.00159.78           C  
ANISOU 3664  C   THR B  78    24223  18103  18385   -665   2513   -298       C  
ATOM   3665  O   THR B  78      15.929  -7.847 -66.671  1.00159.41           O  
ANISOU 3665  O   THR B  78    24301  18036  18233   -755   2548   -274       O  
ATOM   3666  CB  THR B  78      13.908  -9.482 -64.854  1.00157.01           C  
ANISOU 3666  CB  THR B  78    24002  17860  17794   -703   2093   -331       C  
ATOM   3667  OG1 THR B  78      13.948 -10.095 -63.571  1.00154.91           O  
ANISOU 3667  OG1 THR B  78    23560  17640  17659   -610   1978   -346       O  
ATOM   3668  CG2 THR B  78      12.598  -9.852 -65.524  1.00153.94           C  
ANISOU 3668  CG2 THR B  78    23888  17471  17132   -801   2000   -351       C  
ATOM   3669  N   LYS B  79      17.235  -8.745 -65.037  1.00157.58           N  
ANISOU 3669  N   LYS B  79    23660  17846  18368   -569   2563   -293       N  
ATOM   3670  CA  LYS B  79      18.403  -7.847 -65.021  1.00158.86           C  
ANISOU 3670  CA  LYS B  79    23599  18009  18751   -563   2685   -270       C  
ATOM   3671  C   LYS B  79      18.103  -6.333 -64.732  1.00162.39           C  
ANISOU 3671  C   LYS B  79    23949  18521  19229   -652   2526   -242       C  
ATOM   3672  O   LYS B  79      19.032  -5.529 -64.851  1.00163.66           O  
ANISOU 3672  O   LYS B  79    23957  18669  19556   -674   2646   -228       O  
ATOM   3673  CB  LYS B  79      19.217  -7.978 -66.328  1.00163.87           C  
ANISOU 3673  CB  LYS B  79    24371  18523  19370   -579   3018   -266       C  
ATOM   3674  CG  LYS B  79      19.909  -9.332 -66.512  1.00183.77           C  
ANISOU 3674  CG  LYS B  79    26917  20968  21941   -468   3230   -287       C  
ATOM   3675  CD  LYS B  79      21.343  -9.349 -65.976  1.00197.54           C  
ANISOU 3675  CD  LYS B  79    28329  22726  24000   -361   3364   -275       C  
ATOM   3676  CE  LYS B  79      22.023 -10.691 -66.158  1.00211.25           C  
ANISOU 3676  CE  LYS B  79    30091  24383  25792   -229   3584   -285       C  
ATOM   3677  NZ  LYS B  79      22.537 -10.889 -67.543  1.00220.97           N1+
ANISOU 3677  NZ  LYS B  79    31533  25472  26953   -256   3928   -285       N1+
ATOM   3678  N   MET B  80      16.870  -5.962 -64.282  1.00156.61           N  
ANISOU 3678  N   MET B  80    23286  17856  18362   -698   2269   -235       N  
ATOM   3679  CA  MET B  80      16.453  -4.590 -63.880  1.00155.14           C  
ANISOU 3679  CA  MET B  80    23022  17729  18196   -767   2103   -206       C  
ATOM   3680  C   MET B  80      16.643  -3.489 -64.956  1.00157.72           C  
ANISOU 3680  C   MET B  80    23469  17993  18465   -859   2248   -172       C  
ATOM   3681  O   MET B  80      16.996  -2.349 -64.621  1.00156.73           O  
ANISOU 3681  O   MET B  80    23203  17885  18463   -900   2223   -153       O  
ATOM   3682  CB  MET B  80      17.178  -4.141 -62.593  1.00157.40           C  
ANISOU 3682  CB  MET B  80    22982  18084  18738   -723   2001   -212       C  
ATOM   3683  CG  MET B  80      16.468  -4.535 -61.320  1.00159.65           C  
ANISOU 3683  CG  MET B  80    23181  18452  19025   -668   1743   -225       C  
ATOM   3684  SD  MET B  80      17.199  -3.796 -59.834  1.00163.65           S  
ANISOU 3684  SD  MET B  80    23346  19043  19791   -639   1591   -232       S  
ATOM   3685  CE  MET B  80      18.737  -4.720 -59.704  1.00162.14           C  
ANISOU 3685  CE  MET B  80    22945  18841  19821   -531   1771   -254       C  
ATOM   3686  N   LYS B  81      16.355  -3.813 -66.223  1.00154.08           N  
ANISOU 3686  N   LYS B  81    23287  17455  17803   -896   2393   -165       N  
ATOM   3687  CA  LYS B  81      16.454  -2.865 -67.341  1.00154.42           C  
ANISOU 3687  CA  LYS B  81    23499  17425  17750   -976   2540   -129       C  
ATOM   3688  C   LYS B  81      15.299  -1.856 -67.274  1.00155.81           C  
ANISOU 3688  C   LYS B  81    23769  17651  17780  -1031   2324    -86       C  
ATOM   3689  O   LYS B  81      15.448  -0.719 -67.723  1.00156.18           O  
ANISOU 3689  O   LYS B  81    23861  17659  17820  -1085   2390    -46       O  
ATOM   3690  CB  LYS B  81      16.436  -3.613 -68.693  1.00158.13           C  
ANISOU 3690  CB  LYS B  81    24268  17794  18019   -993   2747   -137       C  
ATOM   3691  CG  LYS B  81      17.599  -4.591 -68.911  1.00171.29           C  
ANISOU 3691  CG  LYS B  81    25875  19387  19819   -930   3007   -171       C  
ATOM   3692  CD  LYS B  81      17.118  -6.014 -69.253  1.00176.10           C  
ANISOU 3692  CD  LYS B  81    26686  19966  20259   -897   3026   -209       C  
ATOM   3693  CE  LYS B  81      18.239  -6.914 -69.724  1.00178.03           C  
ANISOU 3693  CE  LYS B  81    26937  20107  20598   -833   3333   -234       C  
ATOM   3694  NZ  LYS B  81      17.869  -8.350 -69.639  1.00181.87           N1+
ANISOU 3694  NZ  LYS B  81    27543  20574  20985   -780   3324   -276       N1+
ATOM   3695  N   THR B  82      14.139  -2.301 -66.732  1.00149.00           N  
ANISOU 3695  N   THR B  82    22941  16869  16802  -1015   2079    -92       N  
ATOM   3696  CA  THR B  82      12.920  -1.508 -66.558  1.00146.50           C  
ANISOU 3696  CA  THR B  82    22694  16615  16353  -1047   1853    -49       C  
ATOM   3697  C   THR B  82      12.895  -0.812 -65.214  1.00146.58           C  
ANISOU 3697  C   THR B  82    22454  16697  16544  -1024   1682    -43       C  
ATOM   3698  O   THR B  82      13.552  -1.253 -64.263  1.00145.39           O  
ANISOU 3698  O   THR B  82    22085  16573  16584   -976   1669    -82       O  
ATOM   3699  CB  THR B  82      11.644  -2.374 -66.668  1.00150.93           C  
ANISOU 3699  CB  THR B  82    23411  17229  16705  -1048   1682    -62       C  
ATOM   3700  OG1 THR B  82      11.960  -3.768 -66.702  1.00148.68           O  
ANISOU 3700  OG1 THR B  82    23150  16919  16421  -1018   1769   -120       O  
ATOM   3701  CG2 THR B  82      10.760  -1.972 -67.834  1.00149.53           C  
ANISOU 3701  CG2 THR B  82    23510  17040  16266  -1106   1656    -19       C  
ATOM   3702  N   ALA B  83      12.077   0.249 -65.133  1.00140.55           N  
ANISOU 3702  N   ALA B  83    21737  15961  15703  -1052   1543      8       N  
ATOM   3703  CA  ALA B  83      11.837   1.017 -63.927  1.00138.01           C  
ANISOU 3703  CA  ALA B  83    21232  15697  15509  -1038   1372     19       C  
ATOM   3704  C   ALA B  83      11.075   0.161 -62.881  1.00138.03           C  
ANISOU 3704  C   ALA B  83    21146  15785  15513   -986   1162    -11       C  
ATOM   3705  O   ALA B  83      11.433   0.194 -61.704  1.00137.52           O  
ANISOU 3705  O   ALA B  83    20878  15756  15619   -954   1083    -37       O  
ATOM   3706  CB  ALA B  83      11.052   2.277 -64.272  1.00138.56           C  
ANISOU 3706  CB  ALA B  83    21423  15761  15463  -1069   1300     90       C  
ATOM   3707  N   THR B  84      10.033  -0.595 -63.309  1.00131.40           N  
ANISOU 3707  N   THR B  84    20466  14977  14484   -986   1076    -10       N  
ATOM   3708  CA  THR B  84       9.212  -1.429 -62.419  1.00128.77           C  
ANISOU 3708  CA  THR B  84    20077  14714  14136   -950    896    -39       C  
ATOM   3709  C   THR B  84      10.027  -2.534 -61.730  1.00130.68           C  
ANISOU 3709  C   THR B  84    20186  14948  14519   -896    953   -101       C  
ATOM   3710  O   THR B  84       9.766  -2.828 -60.561  1.00129.35           O  
ANISOU 3710  O   THR B  84    19888  14827  14433   -851    816   -120       O  
ATOM   3711  CB  THR B  84       8.007  -2.026 -63.148  1.00135.15           C  
ANISOU 3711  CB  THR B  84    21084  15553  14715   -981    813    -33       C  
ATOM   3712  OG1 THR B  84       8.292  -2.166 -64.540  1.00136.52           O  
ANISOU 3712  OG1 THR B  84    21458  15665  14748  -1025    972    -28       O  
ATOM   3713  CG2 THR B  84       6.745  -1.202 -62.947  1.00132.66           C  
ANISOU 3713  CG2 THR B  84    20790  15303  14311   -989    618     24       C  
ATOM   3714  N   ASN B  85      11.025  -3.113 -62.426  1.00126.56           N  
ANISOU 3714  N   ASN B  85    19700  14361  14027   -891   1161   -127       N  
ATOM   3715  CA  ASN B  85      11.894  -4.158 -61.877  1.00125.60           C  
ANISOU 3715  CA  ASN B  85    19455  14224  14042   -822   1241   -175       C  
ATOM   3716  C   ASN B  85      12.760  -3.621 -60.722  1.00125.74           C  
ANISOU 3716  C   ASN B  85    19204  14272  14299   -777   1199   -179       C  
ATOM   3717  O   ASN B  85      12.992  -4.351 -59.762  1.00124.39           O  
ANISOU 3717  O   ASN B  85    18907  14130  14226   -703   1135   -208       O  
ATOM   3718  CB  ASN B  85      12.772  -4.757 -62.977  1.00130.33           C  
ANISOU 3718  CB  ASN B  85    20160  14739  14622   -825   1496   -192       C  
ATOM   3719  CG  ASN B  85      12.041  -5.585 -64.021  1.00156.09           C  
ANISOU 3719  CG  ASN B  85    23695  17965  17649   -866   1544   -207       C  
ATOM   3720  OD1 ASN B  85      10.813  -5.755 -63.998  1.00149.40           O  
ANISOU 3720  OD1 ASN B  85    22958  17164  16644   -902   1378   -206       O  
ATOM   3721  ND2 ASN B  85      12.798  -6.132 -64.964  1.00149.12           N  
ANISOU 3721  ND2 ASN B  85    22926  16994  16739   -866   1780   -224       N  
ATOM   3722  N   ILE B  86      13.214  -2.345 -60.815  1.00120.90           N  
ANISOU 3722  N   ILE B  86    18519  13651  13769   -824   1232   -151       N  
ATOM   3723  CA  ILE B  86      13.996  -1.627 -59.794  1.00119.74           C  
ANISOU 3723  CA  ILE B  86    18129  13532  13834   -812   1182   -159       C  
ATOM   3724  C   ILE B  86      13.095  -1.406 -58.552  1.00119.33           C  
ANISOU 3724  C   ILE B  86    18016  13547  13775   -789    933   -156       C  
ATOM   3725  O   ILE B  86      13.546  -1.641 -57.424  1.00117.90           O  
ANISOU 3725  O   ILE B  86    17657  13404  13733   -736    846   -183       O  
ATOM   3726  CB  ILE B  86      14.584  -0.305 -60.397  1.00124.05           C  
ANISOU 3726  CB  ILE B  86    18664  14031  14437   -893   1304   -132       C  
ATOM   3727  CG1 ILE B  86      15.874  -0.611 -61.187  1.00126.42           C  
ANISOU 3727  CG1 ILE B  86    18921  14270  14842   -896   1563   -149       C  
ATOM   3728  CG2 ILE B  86      14.855   0.774 -59.342  1.00124.46           C  
ANISOU 3728  CG2 ILE B  86    18532  14116  14641   -920   1189   -135       C  
ATOM   3729  CD1 ILE B  86      16.060   0.144 -62.463  1.00134.94           C  
ANISOU 3729  CD1 ILE B  86    20159  15268  15844   -974   1753   -117       C  
ATOM   3730  N   TYR B  87      11.814  -1.020 -58.778  1.00113.85           N  
ANISOU 3730  N   TYR B  87    17477  12867  12914   -822    822   -122       N  
ATOM   3731  CA  TYR B  87      10.813  -0.815 -57.725  1.00111.58           C  
ANISOU 3731  CA  TYR B  87    17161  12634  12602   -800    609   -113       C  
ATOM   3732  C   TYR B  87      10.501  -2.123 -57.010  1.00112.42           C  
ANISOU 3732  C   TYR B  87    17244  12771  12700   -731    528   -150       C  
ATOM   3733  O   TYR B  87      10.340  -2.115 -55.789  1.00111.40           O  
ANISOU 3733  O   TYR B  87    17008  12676  12643   -689    392   -162       O  
ATOM   3734  CB  TYR B  87       9.523  -0.208 -58.294  1.00112.80           C  
ANISOU 3734  CB  TYR B  87    17482  12798  12580   -841    532    -62       C  
ATOM   3735  CG  TYR B  87       9.515   1.304 -58.374  1.00115.40           C  
ANISOU 3735  CG  TYR B  87    17810  13105  12931   -884    530    -15       C  
ATOM   3736  CD1 TYR B  87       9.111   2.078 -57.290  1.00116.37           C  
ANISOU 3736  CD1 TYR B  87    17849  13250  13116   -873    391     -2       C  
ATOM   3737  CD2 TYR B  87       9.862   1.964 -59.552  1.00117.39           C  
ANISOU 3737  CD2 TYR B  87    18172  13301  13129   -936    678     18       C  
ATOM   3738  CE1 TYR B  87       9.090   3.469 -57.363  1.00117.38           C  
ANISOU 3738  CE1 TYR B  87    17996  13342  13259   -912    404     40       C  
ATOM   3739  CE2 TYR B  87       9.861   3.355 -59.631  1.00118.56           C  
ANISOU 3739  CE2 TYR B  87    18338  13415  13294   -973    693     63       C  
ATOM   3740  CZ  TYR B  87       9.463   4.103 -58.537  1.00126.90           C  
ANISOU 3740  CZ  TYR B  87    19308  14492  14417   -962    556     74       C  
ATOM   3741  OH  TYR B  87       9.439   5.472 -58.627  1.00131.99           O  
ANISOU 3741  OH  TYR B  87    19991  15087  15071   -998    584    119       O  
ATOM   3742  N   ILE B  88      10.429  -3.249 -57.761  1.00107.69           N  
ANISOU 3742  N   ILE B  88    16762  12149  12005   -721    623   -170       N  
ATOM   3743  CA  ILE B  88      10.178  -4.571 -57.179  1.00106.30           C  
ANISOU 3743  CA  ILE B  88    16592  11983  11815   -659    580   -207       C  
ATOM   3744  C   ILE B  88      11.412  -5.003 -56.364  1.00108.14           C  
ANISOU 3744  C   ILE B  88    16642  12213  12234   -574    622   -234       C  
ATOM   3745  O   ILE B  88      11.230  -5.553 -55.277  1.00107.44           O  
ANISOU 3745  O   ILE B  88    16489  12149  12186   -508    512   -251       O  
ATOM   3746  CB  ILE B  88       9.728  -5.641 -58.214  1.00110.06           C  
ANISOU 3746  CB  ILE B  88    17265  12426  12127   -683    674   -226       C  
ATOM   3747  CG1 ILE B  88       8.430  -5.180 -58.915  1.00110.03           C  
ANISOU 3747  CG1 ILE B  88    17420  12448  11938   -765    588   -197       C  
ATOM   3748  CG2 ILE B  88       9.488  -7.012 -57.530  1.00110.76           C  
ANISOU 3748  CG2 ILE B  88    17366  12510  12208   -620    643   -267       C  
ATOM   3749  CD1 ILE B  88       8.168  -5.768 -60.250  1.00121.62           C  
ANISOU 3749  CD1 ILE B  88    19096  13881  13235   -823    694   -208       C  
ATOM   3750  N   PHE B  89      12.652  -4.709 -56.844  1.00103.67           N  
ANISOU 3750  N   PHE B  89    15985  11619  11786   -575    775   -235       N  
ATOM   3751  CA  PHE B  89      13.865  -5.054 -56.091  1.00103.51           C  
ANISOU 3751  CA  PHE B  89    15760  11611  11958   -492    804   -255       C  
ATOM   3752  C   PHE B  89      13.871  -4.351 -54.732  1.00108.21           C  
ANISOU 3752  C   PHE B  89    16193  12264  12658   -476    613   -256       C  
ATOM   3753  O   PHE B  89      14.182  -4.974 -53.707  1.00107.44           O  
ANISOU 3753  O   PHE B  89    15988  12194  12639   -386    530   -273       O  
ATOM   3754  CB  PHE B  89      15.159  -4.720 -56.853  1.00106.37           C  
ANISOU 3754  CB  PHE B  89    16029  11941  12446   -509   1003   -254       C  
ATOM   3755  CG  PHE B  89      16.402  -5.110 -56.068  1.00108.67           C  
ANISOU 3755  CG  PHE B  89    16081  12260  12947   -417   1019   -272       C  
ATOM   3756  CD1 PHE B  89      16.929  -6.393 -56.158  1.00112.32           C  
ANISOU 3756  CD1 PHE B  89    16538  12698  13441   -310   1129   -283       C  
ATOM   3757  CD2 PHE B  89      17.011  -4.209 -55.199  1.00111.15           C  
ANISOU 3757  CD2 PHE B  89    16181  12629  13423   -432    914   -277       C  
ATOM   3758  CE1 PHE B  89      18.062  -6.756 -55.426  1.00114.20           C  
ANISOU 3758  CE1 PHE B  89    16544  12972  13874   -207   1132   -289       C  
ATOM   3759  CE2 PHE B  89      18.132  -4.581 -54.446  1.00114.86           C  
ANISOU 3759  CE2 PHE B  89    16417  13141  14083   -345    901   -292       C  
ATOM   3760  CZ  PHE B  89      18.657  -5.846 -54.575  1.00113.64           C  
ANISOU 3760  CZ  PHE B  89    16245  12969  13963   -225   1008   -293       C  
ATOM   3761  N   SER B  90      13.544  -3.045 -54.744  1.00105.42           N  
ANISOU 3761  N   SER B  90    15837  11919  12297   -562    552   -236       N  
ATOM   3762  CA  SER B  90      13.470  -2.183 -53.570  1.00104.74           C  
ANISOU 3762  CA  SER B  90    15636  11873  12289   -571    385   -238       C  
ATOM   3763  C   SER B  90      12.453  -2.738 -52.576  1.00108.44           C  
ANISOU 3763  C   SER B  90    16160  12367  12676   -514    215   -242       C  
ATOM   3764  O   SER B  90      12.777  -2.902 -51.395  1.00107.94           O  
ANISOU 3764  O   SER B  90    15981  12333  12698   -454    102   -260       O  
ATOM   3765  CB  SER B  90      13.094  -0.772 -53.998  1.00107.79           C  
ANISOU 3765  CB  SER B  90    16077  12240  12639   -673    385   -210       C  
ATOM   3766  OG  SER B  90      13.433   0.182 -53.008  1.00118.18           O  
ANISOU 3766  OG  SER B  90    17260  13575  14066   -700    278   -221       O  
ATOM   3767  N   LEU B  91      11.250  -3.093 -53.080  1.00105.20           N  
ANISOU 3767  N   LEU B  91    15928  11944  12100   -532    204   -224       N  
ATOM   3768  CA  LEU B  91      10.163  -3.658 -52.287  1.00104.63           C  
ANISOU 3768  CA  LEU B  91    15925  11888  11943   -492     71   -227       C  
ATOM   3769  C   LEU B  91      10.591  -4.972 -51.624  1.00109.18           C  
ANISOU 3769  C   LEU B  91    16461  12461  12560   -390     72   -258       C  
ATOM   3770  O   LEU B  91      10.424  -5.126 -50.410  1.00108.29           O  
ANISOU 3770  O   LEU B  91    16301  12365  12479   -332    -53   -266       O  
ATOM   3771  CB  LEU B  91       8.914  -3.881 -53.161  1.00104.51           C  
ANISOU 3771  CB  LEU B  91    16090  11866  11752   -543     82   -208       C  
ATOM   3772  CG  LEU B  91       7.602  -3.219 -52.731  1.00109.16           C  
ANISOU 3772  CG  LEU B  91    16733  12479  12263   -572    -56   -178       C  
ATOM   3773  CD1 LEU B  91       6.458  -3.730 -53.563  1.00109.47           C  
ANISOU 3773  CD1 LEU B  91    16924  12527  12142   -614    -53   -167       C  
ATOM   3774  CD2 LEU B  91       7.266  -3.499 -51.258  1.00112.24           C  
ANISOU 3774  CD2 LEU B  91    17068  12882  12698   -509   -185   -193       C  
ATOM   3775  N   ALA B  92      11.181  -5.891 -52.419  1.00107.16           N  
ANISOU 3775  N   ALA B  92    16238  12176  12302   -362    222   -271       N  
ATOM   3776  CA  ALA B  92      11.662  -7.205 -51.986  1.00107.38           C  
ANISOU 3776  CA  ALA B  92    16250  12186  12365   -254    262   -293       C  
ATOM   3777  C   ALA B  92      12.836  -7.090 -51.011  1.00112.24           C  
ANISOU 3777  C   ALA B  92    16661  12833  13154   -167    211   -298       C  
ATOM   3778  O   ALA B  92      12.970  -7.947 -50.127  1.00112.75           O  
ANISOU 3778  O   ALA B  92    16702  12897  13239    -60    157   -306       O  
ATOM   3779  CB  ALA B  92      12.064  -8.035 -53.191  1.00108.93           C  
ANISOU 3779  CB  ALA B  92    16538  12331  12518   -253    459   -302       C  
ATOM   3780  N   LEU B  93      13.676  -6.038 -51.153  1.00108.12           N  
ANISOU 3780  N   LEU B  93    15991  12337  12751   -215    225   -293       N  
ATOM   3781  CA  LEU B  93      14.787  -5.829 -50.224  1.00108.43           C  
ANISOU 3781  CA  LEU B  93    15816  12422  12960   -152    155   -303       C  
ATOM   3782  C   LEU B  93      14.216  -5.446 -48.847  1.00111.24           C  
ANISOU 3782  C   LEU B  93    16158  12810  13298   -136    -59   -308       C  
ATOM   3783  O   LEU B  93      14.616  -6.032 -47.830  1.00110.95           O  
ANISOU 3783  O   LEU B  93    16047  12797  13313    -30   -151   -315       O  
ATOM   3784  CB  LEU B  93      15.772  -4.767 -50.756  1.00109.28           C  
ANISOU 3784  CB  LEU B  93    15774  12547  13202   -233    231   -305       C  
ATOM   3785  CG  LEU B  93      17.023  -4.462 -49.914  1.00114.32           C  
ANISOU 3785  CG  LEU B  93    16157  13244  14034   -194    160   -322       C  
ATOM   3786  CD1 LEU B  93      17.824  -5.714 -49.636  1.00115.12           C  
ANISOU 3786  CD1 LEU B  93    16164  13361  14215    -44    201   -321       C  
ATOM   3787  CD2 LEU B  93      17.895  -3.461 -50.604  1.00117.02           C  
ANISOU 3787  CD2 LEU B  93    16371  13589  14501   -297    270   -329       C  
ATOM   3788  N   ALA B  94      13.224  -4.514 -48.847  1.00106.25           N  
ANISOU 3788  N   ALA B  94    15620  12170  12578   -232   -129   -298       N  
ATOM   3789  CA  ALA B  94      12.510  -4.026 -47.660  1.00104.86           C  
ANISOU 3789  CA  ALA B  94    15469  12006  12366   -231   -306   -300       C  
ATOM   3790  C   ALA B  94      11.716  -5.142 -46.989  1.00107.51           C  
ANISOU 3790  C   ALA B  94    15918  12324  12605   -142   -363   -300       C  
ATOM   3791  O   ALA B  94      11.689  -5.212 -45.763  1.00108.21           O  
ANISOU 3791  O   ALA B  94    15983  12424  12708    -82   -493   -308       O  
ATOM   3792  CB  ALA B  94      11.584  -2.884 -48.038  1.00104.72           C  
ANISOU 3792  CB  ALA B  94    15543  11973  12273   -341   -323   -279       C  
ATOM   3793  N   GLY B  95      11.107  -6.007 -47.793  1.00102.01           N  
ANISOU 3793  N   GLY B  95    15354  11595  11809   -140   -260   -295       N  
ATOM   3794  CA  GLY B  95      10.333  -7.151 -47.322  1.00100.67           C  
ANISOU 3794  CA  GLY B  95    15309  11396  11547    -73   -279   -300       C  
ATOM   3795  C   GLY B  95      11.167  -8.206 -46.622  1.00104.58           C  
ANISOU 3795  C   GLY B  95    15750  11883  12102     64   -277   -310       C  
ATOM   3796  O   GLY B  95      10.737  -8.751 -45.596  1.00103.95           O  
ANISOU 3796  O   GLY B  95    15729  11787  11982    138   -361   -312       O  
ATOM   3797  N   ALA B  96      12.374  -8.496 -47.176  1.00101.77           N  
ANISOU 3797  N   ALA B  96    15285  11536  11847    108   -173   -311       N  
ATOM   3798  CA  ALA B  96      13.318  -9.490 -46.646  1.00102.35           C  
ANISOU 3798  CA  ALA B  96    15285  11609  11996    257   -155   -309       C  
ATOM   3799  C   ALA B  96      13.926  -9.027 -45.303  1.00106.41           C  
ANISOU 3799  C   ALA B  96    15651  12178  12602    324   -334   -308       C  
ATOM   3800  O   ALA B  96      14.165  -9.855 -44.421  1.00106.53           O  
ANISOU 3800  O   ALA B  96    15671  12187  12619    458   -391   -300       O  
ATOM   3801  CB  ALA B  96      14.413  -9.776 -47.667  1.00104.16           C  
ANISOU 3801  CB  ALA B  96    15422  11836  12320    279     16   -306       C  
ATOM   3802  N   LEU B  97      14.153  -7.707 -45.151  1.00102.09           N  
ANISOU 3802  N   LEU B  97    14992  11679  12120    228   -421   -316       N  
ATOM   3803  CA  LEU B  97      14.669  -7.124 -43.908  1.00101.61           C  
ANISOU 3803  CA  LEU B  97    14806  11669  12131    259   -603   -325       C  
ATOM   3804  C   LEU B  97      13.601  -7.167 -42.834  1.00106.17           C  
ANISOU 3804  C   LEU B  97    15534  12218  12589    279   -735   -324       C  
ATOM   3805  O   LEU B  97      13.905  -7.418 -41.667  1.00106.96           O  
ANISOU 3805  O   LEU B  97    15608  12336  12698    373   -867   -326       O  
ATOM   3806  CB  LEU B  97      15.140  -5.680 -44.123  1.00101.15           C  
ANISOU 3806  CB  LEU B  97    14613  11653  12166    128   -638   -341       C  
ATOM   3807  CG  LEU B  97      16.479  -5.543 -44.813  1.00106.36           C  
ANISOU 3807  CG  LEU B  97    15069  12355  12986    120   -541   -346       C  
ATOM   3808  CD1 LEU B  97      16.575  -4.245 -45.541  1.00106.22           C  
ANISOU 3808  CD1 LEU B  97    15006  12339  13016    -40   -485   -357       C  
ATOM   3809  CD2 LEU B  97      17.605  -5.666 -43.822  1.00109.29           C  
ANISOU 3809  CD2 LEU B  97    15241  12799  13486    210   -672   -356       C  
ATOM   3810  N   ALA B  98      12.342  -6.929 -43.235  1.00102.18           N  
ANISOU 3810  N   ALA B  98    15187  11668  11969    193   -696   -320       N  
ATOM   3811  CA  ALA B  98      11.178  -6.931 -42.359  1.00101.71           C  
ANISOU 3811  CA  ALA B  98    15275  11571  11797    197   -786   -318       C  
ATOM   3812  C   ALA B  98      11.012  -8.276 -41.679  1.00107.58           C  
ANISOU 3812  C   ALA B  98    16118  12277  12483    331   -787   -313       C  
ATOM   3813  O   ALA B  98      10.956  -8.325 -40.450  1.00107.27           O  
ANISOU 3813  O   ALA B  98    16109  12230  12420    401   -911   -313       O  
ATOM   3814  CB  ALA B  98       9.932  -6.589 -43.152  1.00101.36           C  
ANISOU 3814  CB  ALA B  98    15356  11498  11660     89   -716   -309       C  
ATOM   3815  N   THR B  99      11.010  -9.367 -42.471  1.00106.26           N  
ANISOU 3815  N   THR B  99    16010  12076  12289    371   -644   -309       N  
ATOM   3816  CA  THR B  99      10.855 -10.745 -41.976  1.00107.25           C  
ANISOU 3816  CA  THR B  99    16252  12145  12355    498   -608   -303       C  
ATOM   3817  C   THR B  99      12.097 -11.244 -41.210  1.00113.78           C  
ANISOU 3817  C   THR B  99    16969  12999  13265    658   -670   -290       C  
ATOM   3818  O   THR B  99      11.956 -12.131 -40.367  1.00113.87           O  
ANISOU 3818  O   THR B  99    17082  12965  13219    779   -697   -278       O  
ATOM   3819  CB  THR B  99      10.493 -11.716 -43.116  1.00112.13           C  
ANISOU 3819  CB  THR B  99    16979  12710  12915    477   -425   -309       C  
ATOM   3820  OG1 THR B  99      11.325 -11.464 -44.250  1.00110.48           O  
ANISOU 3820  OG1 THR B  99    16658  12533  12786    439   -324   -309       O  
ATOM   3821  CG2 THR B  99       9.030 -11.611 -43.512  1.00108.67           C  
ANISOU 3821  CG2 THR B  99    16690  12238  12361    355   -395   -321       C  
ATOM   3822  N   SER B 100      13.289 -10.658 -41.464  1.00111.58           N  
ANISOU 3822  N   SER B 100    16482  12792  13119    659   -696   -289       N  
ATOM   3823  CA  SER B 100      14.528 -11.056 -40.791  1.00112.96           C  
ANISOU 3823  CA  SER B 100    16512  13014  13392    808   -770   -273       C  
ATOM   3824  C   SER B 100      14.520 -10.699 -39.277  1.00116.87           C  
ANISOU 3824  C   SER B 100    17011  13535  13859    864   -986   -274       C  
ATOM   3825  O   SER B 100      15.393 -11.153 -38.527  1.00117.77           O  
ANISOU 3825  O   SER B 100    17040  13686  14022   1008  -1078   -256       O  
ATOM   3826  CB  SER B 100      15.735 -10.438 -41.486  1.00117.76           C  
ANISOU 3826  CB  SER B 100    16881  13699  14162    771   -738   -278       C  
ATOM   3827  OG  SER B 100      15.894  -9.070 -41.153  1.00128.28           O  
ANISOU 3827  OG  SER B 100    18099  15092  15548    652   -871   -301       O  
ATOM   3828  N   THR B 101      13.525  -9.907 -38.835  1.00112.44           N  
ANISOU 3828  N   THR B 101    16557  12952  13214    756  -1063   -291       N  
ATOM   3829  CA  THR B 101      13.356  -9.518 -37.427  1.00112.58           C  
ANISOU 3829  CA  THR B 101    16624  12974  13178    791  -1250   -296       C  
ATOM   3830  C   THR B 101      12.469 -10.539 -36.689  1.00116.24           C  
ANISOU 3830  C   THR B 101    17317  13347  13503    894  -1233   -278       C  
ATOM   3831  O   THR B 101      12.635 -10.720 -35.476  1.00116.37           O  
ANISOU 3831  O   THR B 101    17385  13357  13472    996  -1367   -270       O  
ATOM   3832  CB  THR B 101      12.776  -8.090 -37.285  1.00118.19           C  
ANISOU 3832  CB  THR B 101    17340  13693  13874    629  -1324   -322       C  
ATOM   3833  OG1 THR B 101      11.403  -8.073 -37.685  1.00113.72           O  
ANISOU 3833  OG1 THR B 101    16945  13056  13208    550  -1226   -319       O  
ATOM   3834  CG2 THR B 101      13.573  -7.042 -38.048  1.00117.56           C  
ANISOU 3834  CG2 THR B 101    17059  13684  13923    512  -1318   -341       C  
ATOM   3835  N   LEU B 102      11.534 -11.200 -37.431  1.00111.73           N  
ANISOU 3835  N   LEU B 102    16888  12703  12863    858  -1067   -276       N  
ATOM   3836  CA  LEU B 102      10.576 -12.184 -36.905  1.00110.96           C  
ANISOU 3836  CA  LEU B 102    17014  12508  12640    923  -1012   -267       C  
ATOM   3837  C   LEU B 102      11.224 -13.209 -35.976  1.00116.28           C  
ANISOU 3837  C   LEU B 102    17736  13154  13289   1122  -1058   -239       C  
ATOM   3838  O   LEU B 102      10.753 -13.272 -34.847  1.00115.62           O  
ANISOU 3838  O   LEU B 102    17788  13025  13118   1174  -1144   -233       O  
ATOM   3839  CB  LEU B 102       9.772 -12.896 -37.998  1.00110.06           C  
ANISOU 3839  CB  LEU B 102    17006  12334  12479    858   -820   -274       C  
ATOM   3840  CG  LEU B 102       8.600 -12.090 -38.529  1.00113.20           C  
ANISOU 3840  CG  LEU B 102    17446  12728  12836    683   -793   -293       C  
ATOM   3841  CD1 LEU B 102       8.182 -12.569 -39.898  1.00112.62           C  
ANISOU 3841  CD1 LEU B 102    17407  12636  12746    599   -630   -304       C  
ATOM   3842  CD2 LEU B 102       7.435 -12.103 -37.552  1.00114.94           C  
ANISOU 3842  CD2 LEU B 102    17831  12883  12958    676   -832   -293       C  
ATOM   3843  N   PRO B 103      12.330 -13.929 -36.329  1.00114.05           N  
ANISOU 3843  N   PRO B 103    17349  12901  13085   1246  -1014   -217       N  
ATOM   3844  CA  PRO B 103      12.930 -14.876 -35.361  1.00115.27           C  
ANISOU 3844  CA  PRO B 103    17557  13030  13210   1458  -1072   -180       C  
ATOM   3845  C   PRO B 103      13.185 -14.314 -33.946  1.00120.82           C  
ANISOU 3845  C   PRO B 103    18256  13772  13879   1519  -1300   -173       C  
ATOM   3846  O   PRO B 103      12.974 -15.039 -32.971  1.00119.70           O  
ANISOU 3846  O   PRO B 103    18284  13563  13634   1654  -1337   -148       O  
ATOM   3847  CB  PRO B 103      14.259 -15.275 -36.025  1.00118.22           C  
ANISOU 3847  CB  PRO B 103    17732  13468  13717   1558  -1023   -156       C  
ATOM   3848  CG  PRO B 103      14.398 -14.425 -37.245  1.00121.68           C  
ANISOU 3848  CG  PRO B 103    18013  13965  14255   1387   -952   -187       C  
ATOM   3849  CD  PRO B 103      13.029 -14.004 -37.629  1.00115.43           C  
ANISOU 3849  CD  PRO B 103    17374  13117  13369   1214   -889   -219       C  
ATOM   3850  N   PHE B 104      13.607 -13.028 -33.831  1.00119.75           N  
ANISOU 3850  N   PHE B 104    17949  13734  13817   1413  -1447   -199       N  
ATOM   3851  CA  PHE B 104      13.899 -12.368 -32.545  1.00121.02           C  
ANISOU 3851  CA  PHE B 104    18102  13936  13943   1442  -1674   -205       C  
ATOM   3852  C   PHE B 104      12.625 -11.973 -31.825  1.00125.99           C  
ANISOU 3852  C   PHE B 104    18958  14479  14433   1365  -1694   -223       C  
ATOM   3853  O   PHE B 104      12.539 -12.160 -30.609  1.00126.62           O  
ANISOU 3853  O   PHE B 104    19174  14522  14411   1462  -1811   -210       O  
ATOM   3854  CB  PHE B 104      14.792 -11.137 -32.731  1.00123.07           C  
ANISOU 3854  CB  PHE B 104    18107  14319  14332   1335  -1805   -236       C  
ATOM   3855  CG  PHE B 104      16.021 -11.413 -33.551  1.00125.85           C  
ANISOU 3855  CG  PHE B 104    18211  14760  14846   1388  -1761   -221       C  
ATOM   3856  CD1 PHE B 104      17.173 -11.914 -32.955  1.00131.60           C  
ANISOU 3856  CD1 PHE B 104    18808  15561  15632   1561  -1887   -191       C  
ATOM   3857  CD2 PHE B 104      16.018 -11.210 -34.929  1.00127.15           C  
ANISOU 3857  CD2 PHE B 104    18278  14932  15103   1275  -1587   -234       C  
ATOM   3858  CE1 PHE B 104      18.302 -12.197 -33.722  1.00134.15           C  
ANISOU 3858  CE1 PHE B 104    18888  15964  16119   1620  -1827   -172       C  
ATOM   3859  CE2 PHE B 104      17.147 -11.482 -35.693  1.00131.69           C  
ANISOU 3859  CE2 PHE B 104    18633  15576  15829   1327  -1521   -219       C  
ATOM   3860  CZ  PHE B 104      18.284 -11.972 -35.085  1.00132.26           C  
ANISOU 3860  CZ  PHE B 104    18559  15720  15973   1500  -1636   -189       C  
ATOM   3861  N   GLN B 105      11.635 -11.441 -32.570  1.00122.30           N  
ANISOU 3861  N   GLN B 105    18534  13976  13960   1200  -1575   -247       N  
ATOM   3862  CA  GLN B 105      10.347 -11.029 -32.022  1.00121.96           C  
ANISOU 3862  CA  GLN B 105    18683  13850  13805   1120  -1565   -260       C  
ATOM   3863  C   GLN B 105       9.496 -12.266 -31.614  1.00127.25           C  
ANISOU 3863  C   GLN B 105    19593  14401  14357   1217  -1449   -237       C  
ATOM   3864  O   GLN B 105       8.680 -12.166 -30.693  1.00127.19           O  
ANISOU 3864  O   GLN B 105    19767  14316  14244   1220  -1472   -238       O  
ATOM   3865  CB  GLN B 105       9.609 -10.120 -33.023  1.00122.10           C  
ANISOU 3865  CB  GLN B 105    18649  13879  13866    930  -1475   -283       C  
ATOM   3866  CG  GLN B 105       8.421 -10.749 -33.736  1.00141.14           C  
ANISOU 3866  CG  GLN B 105    21186  16214  16225    878  -1290   -279       C  
ATOM   3867  CD  GLN B 105       7.122 -10.373 -33.060  1.00162.99           C  
ANISOU 3867  CD  GLN B 105    24124  18905  18898    821  -1282   -283       C  
ATOM   3868  OE1 GLN B 105       6.664  -9.230 -33.138  1.00160.28           O  
ANISOU 3868  OE1 GLN B 105    23748  18580  18570    706  -1314   -294       O  
ATOM   3869  NE2 GLN B 105       6.484 -11.327 -32.409  1.00152.19           N  
ANISOU 3869  NE2 GLN B 105    22946  17443  17436    903  -1221   -271       N  
ATOM   3870  N   SER B 106       9.701 -13.418 -32.300  1.00124.22           N  
ANISOU 3870  N   SER B 106    19216  13990  13990   1293  -1311   -219       N  
ATOM   3871  CA  SER B 106       9.032 -14.697 -32.031  1.00123.64           C  
ANISOU 3871  CA  SER B 106    19365  13797  13816   1384  -1179   -201       C  
ATOM   3872  C   SER B 106       9.613 -15.332 -30.787  1.00127.19           C  
ANISOU 3872  C   SER B 106    19919  14214  14195   1583  -1282   -166       C  
ATOM   3873  O   SER B 106       8.899 -16.034 -30.076  1.00126.38           O  
ANISOU 3873  O   SER B 106    20047  13995  13975   1648  -1220   -153       O  
ATOM   3874  CB  SER B 106       9.173 -15.644 -33.219  1.00127.75           C  
ANISOU 3874  CB  SER B 106    19860  14299  14380   1392   -998   -198       C  
ATOM   3875  OG  SER B 106       8.712 -15.039 -34.416  1.00137.58           O  
ANISOU 3875  OG  SER B 106    21010  15583  15681   1212   -917   -229       O  
ATOM   3876  N   ALA B 107      10.915 -15.087 -30.531  1.00124.87           N  
ANISOU 3876  N   ALA B 107    19452  14021  13972   1680  -1439   -149       N  
ATOM   3877  CA  ALA B 107      11.631 -15.570 -29.356  1.00126.70           C  
ANISOU 3877  CA  ALA B 107    19748  14251  14142   1879  -1581   -111       C  
ATOM   3878  C   ALA B 107      11.177 -14.812 -28.127  1.00132.22           C  
ANISOU 3878  C   ALA B 107    20575  14927  14734   1850  -1735   -125       C  
ATOM   3879  O   ALA B 107      10.859 -15.434 -27.113  1.00132.54           O  
ANISOU 3879  O   ALA B 107    20844  14874  14642   1973  -1750    -98       O  
ATOM   3880  CB  ALA B 107      13.127 -15.409 -29.548  1.00128.89           C  
ANISOU 3880  CB  ALA B 107    19761  14666  14546   1965  -1714    -93       C  
ATOM   3881  N   ASP B 108      11.090 -13.467 -28.242  1.00129.72           N  
ANISOU 3881  N   ASP B 108    20138  14680  14469   1682  -1829   -167       N  
ATOM   3882  CA  ASP B 108      10.657 -12.572 -27.165  1.00130.43           C  
ANISOU 3882  CA  ASP B 108    20346  14746  14465   1627  -1964   -190       C  
ATOM   3883  C   ASP B 108       9.229 -12.907 -26.712  1.00133.28           C  
ANISOU 3883  C   ASP B 108    20988  14956  14697   1604  -1824   -188       C  
ATOM   3884  O   ASP B 108       8.956 -12.820 -25.518  1.00134.02           O  
ANISOU 3884  O   ASP B 108    21272  14983  14665   1661  -1906   -183       O  
ATOM   3885  CB  ASP B 108      10.768 -11.091 -27.587  1.00132.03           C  
ANISOU 3885  CB  ASP B 108    20370  15035  14760   1437  -2042   -236       C  
ATOM   3886  CG  ASP B 108      10.484 -10.082 -26.478  1.00146.04           C  
ANISOU 3886  CG  ASP B 108    22258  16786  16443   1378  -2189   -264       C  
ATOM   3887  OD1 ASP B 108      11.317  -9.957 -25.555  1.00149.05           O1-
ANISOU 3887  OD1 ASP B 108    22634  17216  16784   1461  -2389   -265       O1-
ATOM   3888  OD2 ASP B 108       9.434  -9.416 -26.542  1.00151.12           O1-
ANISOU 3888  OD2 ASP B 108    22998  17365  17055   1250  -2105   -284       O1-
ATOM   3889  N   TYR B 109       8.340 -13.320 -27.638  1.00127.28           N  
ANISOU 3889  N   TYR B 109    20258  14141  13964   1522  -1613   -192       N  
ATOM   3890  CA  TYR B 109       6.976 -13.696 -27.274  1.00125.86           C  
ANISOU 3890  CA  TYR B 109    20316  13823  13682   1491  -1466   -192       C  
ATOM   3891  C   TYR B 109       6.981 -14.957 -26.395  1.00129.82           C  
ANISOU 3891  C   TYR B 109    21047  14215  14063   1676  -1425   -155       C  
ATOM   3892  O   TYR B 109       6.272 -15.012 -25.384  1.00128.65           O  
ANISOU 3892  O   TYR B 109    21125  13960  13795   1705  -1411   -150       O  
ATOM   3893  CB  TYR B 109       6.101 -13.914 -28.529  1.00125.77           C  
ANISOU 3893  CB  TYR B 109    20260  13795  13733   1357  -1267   -209       C  
ATOM   3894  CG  TYR B 109       4.794 -14.611 -28.229  1.00127.53           C  
ANISOU 3894  CG  TYR B 109    20710  13879  13867   1341  -1096   -208       C  
ATOM   3895  CD1 TYR B 109       3.766 -13.947 -27.562  1.00128.98           C  
ANISOU 3895  CD1 TYR B 109    21012  14001  13996   1266  -1084   -218       C  
ATOM   3896  CD2 TYR B 109       4.598 -15.943 -28.560  1.00128.90           C  
ANISOU 3896  CD2 TYR B 109    20988  13975  14013   1403   -938   -197       C  
ATOM   3897  CE1 TYR B 109       2.574 -14.592 -27.246  1.00129.68           C  
ANISOU 3897  CE1 TYR B 109    21297  13961  14016   1249   -918   -218       C  
ATOM   3898  CE2 TYR B 109       3.416 -16.603 -28.234  1.00129.72           C  
ANISOU 3898  CE2 TYR B 109    21301  13946  14039   1378   -776   -202       C  
ATOM   3899  CZ  TYR B 109       2.401 -15.917 -27.587  1.00137.09           C  
ANISOU 3899  CZ  TYR B 109    22328  14828  14932   1298   -767   -213       C  
ATOM   3900  OH  TYR B 109       1.235 -16.551 -27.253  1.00139.14           O  
ANISOU 3900  OH  TYR B 109    22778  14958  15130   1267   -597   -218       O  
ATOM   3901  N   LEU B 110       7.776 -15.965 -26.798  1.00127.46           N  
ANISOU 3901  N   LEU B 110    20700  13934  13796   1805  -1391   -127       N  
ATOM   3902  CA  LEU B 110       7.868 -17.259 -26.135  1.00128.34           C  
ANISOU 3902  CA  LEU B 110    21023  13937  13802   1996  -1329    -83       C  
ATOM   3903  C   LEU B 110       8.509 -17.169 -24.760  1.00136.80           C  
ANISOU 3903  C   LEU B 110    22199  15009  14770   2156  -1529    -52       C  
ATOM   3904  O   LEU B 110       7.948 -17.733 -23.821  1.00137.34           O  
ANISOU 3904  O   LEU B 110    22541  14946  14696   2244  -1479    -30       O  
ATOM   3905  CB  LEU B 110       8.623 -18.280 -27.004  1.00128.38           C  
ANISOU 3905  CB  LEU B 110    20935  13964  13881   2097  -1235    -57       C  
ATOM   3906  CG  LEU B 110       7.955 -18.703 -28.313  1.00130.41           C  
ANISOU 3906  CG  LEU B 110    21161  14187  14202   1963  -1011    -86       C  
ATOM   3907  CD1 LEU B 110       8.948 -19.374 -29.223  1.00130.99           C  
ANISOU 3907  CD1 LEU B 110    21091  14312  14368   2049   -956    -66       C  
ATOM   3908  CD2 LEU B 110       6.757 -19.602 -28.072  1.00130.92           C  
ANISOU 3908  CD2 LEU B 110    21499  14083  14161   1947   -811    -91       C  
ATOM   3909  N   MET B 111       9.656 -16.474 -24.623  1.00136.64           N  
ANISOU 3909  N   MET B 111    21972  15133  14813   2189  -1753    -51       N  
ATOM   3910  CA  MET B 111      10.338 -16.382 -23.326  1.00139.82           C  
ANISOU 3910  CA  MET B 111    22462  15553  15109   2339  -1974    -24       C  
ATOM   3911  C   MET B 111       9.970 -15.105 -22.512  1.00144.21           C  
ANISOU 3911  C   MET B 111    23075  16119  15599   2218  -2122    -66       C  
ATOM   3912  O   MET B 111      10.448 -14.958 -21.382  1.00144.84           O  
ANISOU 3912  O   MET B 111    23259  16207  15569   2322  -2314    -52       O  
ATOM   3913  CB  MET B 111      11.863 -16.514 -23.484  1.00144.45           C  
ANISOU 3913  CB  MET B 111    22805  16289  15790   2471  -2149      6       C  
ATOM   3914  CG  MET B 111      12.497 -15.471 -24.381  1.00148.39           C  
ANISOU 3914  CG  MET B 111    22966  16947  16467   2316  -2232    -37       C  
ATOM   3915  SD  MET B 111      13.950 -16.088 -25.258  1.00155.05           S  
ANISOU 3915  SD  MET B 111    23507  17923  17483   2449  -2250      2       S  
ATOM   3916  CE  MET B 111      13.257 -17.548 -26.098  1.00151.30           C  
ANISOU 3916  CE  MET B 111    23194  17301  16992   2518  -1922     35       C  
ATOM   3917  N   GLU B 112       9.116 -14.207 -23.079  1.00140.05           N  
ANISOU 3917  N   GLU B 112    22497  15586  15131   2005  -2031   -115       N  
ATOM   3918  CA  GLU B 112       8.597 -12.950 -22.485  1.00139.99           C  
ANISOU 3918  CA  GLU B 112    22550  15566  15075   1869  -2115   -156       C  
ATOM   3919  C   GLU B 112       9.699 -11.891 -22.180  1.00144.69           C  
ANISOU 3919  C   GLU B 112    22962  16302  15713   1833  -2379   -185       C  
ATOM   3920  O   GLU B 112       9.371 -10.713 -21.971  1.00143.91           O  
ANISOU 3920  O   GLU B 112    22863  16207  15610   1687  -2435   -229       O  
ATOM   3921  CB  GLU B 112       7.750 -13.220 -21.221  1.00142.17           C  
ANISOU 3921  CB  GLU B 112    23174  15682  15161   1936  -2076   -143       C  
ATOM   3922  CG  GLU B 112       6.387 -13.844 -21.500  1.00156.02           C  
ANISOU 3922  CG  GLU B 112    25100  17292  16890   1892  -1802   -136       C  
ATOM   3923  CD  GLU B 112       6.279 -15.354 -21.369  1.00191.54           C  
ANISOU 3923  CD  GLU B 112    29769  21688  21320   2051  -1664    -91       C  
ATOM   3924  OE1 GLU B 112       6.685 -15.898 -20.315  1.00191.28           O  
ANISOU 3924  OE1 GLU B 112    29930  21597  21149   2225  -1751    -54       O  
ATOM   3925  OE2 GLU B 112       5.719 -15.984 -22.296  1.00194.47           O1-
ANISOU 3925  OE2 GLU B 112    30104  22024  21763   1997  -1462    -93       O1-
ATOM   3926  N   THR B 113      10.990 -12.311 -22.199  1.00141.77           N  
ANISOU 3926  N   THR B 113    22427  16044  15393   1960  -2530   -161       N  
ATOM   3927  CA  THR B 113      12.199 -11.524 -21.904  1.00142.10           C  
ANISOU 3927  CA  THR B 113    22267  16236  15489   1946  -2794   -185       C  
ATOM   3928  C   THR B 113      13.046 -11.335 -23.194  1.00143.91           C  
ANISOU 3928  C   THR B 113    22137  16607  15934   1882  -2780   -196       C  
ATOM   3929  O   THR B 113      12.929 -12.142 -24.124  1.00142.76           O  
ANISOU 3929  O   THR B 113    21932  16445  15864   1922  -2597   -167       O  
ATOM   3930  CB  THR B 113      12.974 -12.269 -20.785  1.00148.24           C  
ANISOU 3930  CB  THR B 113    23155  17025  16143   2172  -2981   -139       C  
ATOM   3931  OG1 THR B 113      12.101 -12.463 -19.672  1.00145.85           O  
ANISOU 3931  OG1 THR B 113    23212  16570  15635   2224  -2956   -129       O  
ATOM   3932  CG2 THR B 113      14.226 -11.548 -20.318  1.00147.81           C  
ANISOU 3932  CG2 THR B 113    22905  17131  16126   2170  -3284   -164       C  
ATOM   3933  N   TRP B 114      13.873 -10.257 -23.247  1.00139.19           N  
ANISOU 3933  N   TRP B 114    21317  16140  15430   1770  -2960   -241       N  
ATOM   3934  CA  TRP B 114      14.763  -9.954 -24.370  1.00138.10           C  
ANISOU 3934  CA  TRP B 114    20836  16137  15497   1700  -2957   -255       C  
ATOM   3935  C   TRP B 114      16.209 -10.382 -24.019  1.00141.92           C  
ANISOU 3935  C   TRP B 114    21124  16757  16041   1856  -3163   -228       C  
ATOM   3936  O   TRP B 114      16.937  -9.635 -23.357  1.00142.52           O  
ANISOU 3936  O   TRP B 114    21105  16929  16118   1815  -3402   -263       O  
ATOM   3937  CB  TRP B 114      14.688  -8.471 -24.780  1.00136.03           C  
ANISOU 3937  CB  TRP B 114    20446  15921  15319   1459  -2985   -323       C  
ATOM   3938  CG  TRP B 114      15.592  -8.127 -25.933  1.00137.41           C  
ANISOU 3938  CG  TRP B 114    20283  16222  15703   1378  -2964   -339       C  
ATOM   3939  CD1 TRP B 114      16.863  -7.646 -25.854  1.00142.29           C  
ANISOU 3939  CD1 TRP B 114    20644  16984  16434   1357  -3152   -364       C  
ATOM   3940  CD2 TRP B 114      15.327  -8.324 -27.334  1.00135.74           C  
ANISOU 3940  CD2 TRP B 114    19960  16003  15611   1316  -2736   -328       C  
ATOM   3941  NE1 TRP B 114      17.391  -7.481 -27.113  1.00141.48           N  
ANISOU 3941  NE1 TRP B 114    20277  16956  16521   1281  -3039   -370       N  
ATOM   3942  CE2 TRP B 114      16.473  -7.897 -28.042  1.00140.63           C  
ANISOU 3942  CE2 TRP B 114    20265  16756  16413   1259  -2785   -347       C  
ATOM   3943  CE3 TRP B 114      14.226  -8.807 -28.060  1.00134.92           C  
ANISOU 3943  CE3 TRP B 114    19994  15795  15476   1295  -2498   -308       C  
ATOM   3944  CZ2 TRP B 114      16.553  -7.933 -29.440  1.00138.97           C  
ANISOU 3944  CZ2 TRP B 114    19895  16565  16341   1190  -2594   -343       C  
ATOM   3945  CZ3 TRP B 114      14.301  -8.832 -29.446  1.00135.57           C  
ANISOU 3945  CZ3 TRP B 114    19915  15906  15688   1221  -2330   -307       C  
ATOM   3946  CH2 TRP B 114      15.454  -8.399 -30.121  1.00137.21           C  
ANISOU 3946  CH2 TRP B 114    19833  16237  16066   1173  -2374   -323       C  
ATOM   3947  N   PRO B 115      16.645 -11.575 -24.490  1.00138.16           N  
ANISOU 3947  N   PRO B 115    20580  16293  15621   2033  -3069   -167       N  
ATOM   3948  CA  PRO B 115      17.996 -12.052 -24.147  1.00140.76           C  
ANISOU 3948  CA  PRO B 115    20717  16752  16013   2210  -3257   -128       C  
ATOM   3949  C   PRO B 115      19.144 -11.540 -25.031  1.00146.19           C  
ANISOU 3949  C   PRO B 115    21006  17606  16934   2133  -3305   -150       C  
ATOM   3950  O   PRO B 115      20.304 -11.597 -24.618  1.00149.13           O  
ANISOU 3950  O   PRO B 115    21177  18112  17372   2236  -3512   -134       O  
ATOM   3951  CB  PRO B 115      17.870 -13.565 -24.321  1.00142.61           C  
ANISOU 3951  CB  PRO B 115    21075  16903  16207   2435  -3093    -48       C  
ATOM   3952  CG  PRO B 115      16.849 -13.735 -25.387  1.00144.29           C  
ANISOU 3952  CG  PRO B 115    21370  17006  16449   2317  -2796    -62       C  
ATOM   3953  CD  PRO B 115      15.894 -12.589 -25.263  1.00137.99           C  
ANISOU 3953  CD  PRO B 115    20678  16159  15594   2089  -2792   -128       C  
ATOM   3954  N   PHE B 116      18.829 -11.076 -26.243  1.00139.96           N  
ANISOU 3954  N   PHE B 116    20103  16807  16270   1962  -3110   -183       N  
ATOM   3955  CA  PHE B 116      19.772 -10.663 -27.279  1.00139.76           C  
ANISOU 3955  CA  PHE B 116    19728  16905  16468   1879  -3080   -201       C  
ATOM   3956  C   PHE B 116      20.572  -9.381 -26.946  1.00143.77           C  
ANISOU 3956  C   PHE B 116    20013  17547  17065   1723  -3308   -267       C  
ATOM   3957  O   PHE B 116      21.598  -9.139 -27.588  1.00144.97           O  
ANISOU 3957  O   PHE B 116    19847  17824  17413   1690  -3325   -276       O  
ATOM   3958  CB  PHE B 116      19.019 -10.518 -28.612  1.00139.11           C  
ANISOU 3958  CB  PHE B 116    19657  16747  16449   1734  -2799   -218       C  
ATOM   3959  CG  PHE B 116      18.035 -11.641 -28.864  1.00139.06           C  
ANISOU 3959  CG  PHE B 116    19909  16597  16332   1838  -2583   -173       C  
ATOM   3960  CD1 PHE B 116      18.475 -12.913 -29.205  1.00142.63           C  
ANISOU 3960  CD1 PHE B 116    20338  17036  16818   2035  -2475   -111       C  
ATOM   3961  CD2 PHE B 116      16.673 -11.439 -28.702  1.00139.12           C  
ANISOU 3961  CD2 PHE B 116    20184  16476  16199   1740  -2488   -193       C  
ATOM   3962  CE1 PHE B 116      17.570 -13.955 -29.401  1.00142.10           C  
ANISOU 3962  CE1 PHE B 116    20523  16826  16642   2116  -2274    -77       C  
ATOM   3963  CE2 PHE B 116      15.770 -12.480 -28.911  1.00140.57           C  
ANISOU 3963  CE2 PHE B 116    20593  16529  16286   1818  -2292   -159       C  
ATOM   3964  CZ  PHE B 116      16.225 -13.731 -29.257  1.00139.14           C  
ANISOU 3964  CZ  PHE B 116    20399  16333  16136   1999  -2187   -105       C  
ATOM   3965  N   GLY B 117      20.136  -8.615 -25.947  1.00139.18           N  
ANISOU 3965  N   GLY B 117    19600  16936  16344   1632  -3471   -312       N  
ATOM   3966  CA  GLY B 117      20.828  -7.405 -25.506  1.00140.40           C  
ANISOU 3966  CA  GLY B 117    19590  17201  16555   1472  -3696   -383       C  
ATOM   3967  C   GLY B 117      20.513  -6.143 -26.284  1.00142.83           C  
ANISOU 3967  C   GLY B 117    19822  17493  16953   1203  -3590   -453       C  
ATOM   3968  O   GLY B 117      19.870  -6.212 -27.334  1.00141.06           O  
ANISOU 3968  O   GLY B 117    19625  17196  16775   1145  -3340   -441       O  
ATOM   3969  N   GLU B 118      21.005  -4.980 -25.780  1.00139.74           N  
ANISOU 3969  N   GLU B 118    19337  17174  16585   1037  -3784   -527       N  
ATOM   3970  CA  GLU B 118      20.796  -3.631 -26.328  1.00138.11           C  
ANISOU 3970  CA  GLU B 118    19076  16948  16450    773  -3715   -600       C  
ATOM   3971  C   GLU B 118      21.289  -3.462 -27.764  1.00140.56           C  
ANISOU 3971  C   GLU B 118    19110  17313  16983    688  -3530   -600       C  
ATOM   3972  O   GLU B 118      20.601  -2.821 -28.556  1.00138.27           O  
ANISOU 3972  O   GLU B 118    18882  16943  16712    539  -3342   -619       O  
ATOM   3973  CB  GLU B 118      21.465  -2.573 -25.445  1.00141.65           C  
ANISOU 3973  CB  GLU B 118    19453  17476  16890    631  -3981   -681       C  
ATOM   3974  CG  GLU B 118      20.729  -1.248 -25.481  1.00151.89           C  
ANISOU 3974  CG  GLU B 118    20902  18675  18136    393  -3917   -750       C  
ATOM   3975  CD  GLU B 118      21.259  -0.198 -24.529  1.00174.71           C  
ANISOU 3975  CD  GLU B 118    23785  21613  20985    238  -4167   -839       C  
ATOM   3976  OE1 GLU B 118      22.285   0.439 -24.861  1.00170.83           O  
ANISOU 3976  OE1 GLU B 118    23005  21239  20663    101  -4249   -894       O  
ATOM   3977  OE2 GLU B 118      20.639   0.001 -23.458  1.00168.19           O1-
ANISOU 3977  OE2 GLU B 118    23250  20700  19954    245  -4271   -857       O1-
ATOM   3978  N   LEU B 119      22.472  -4.008 -28.092  1.00138.41           N  
ANISOU 3978  N   LEU B 119    18539  17174  16876    785  -3578   -576       N  
ATOM   3979  CA  LEU B 119      23.068  -3.923 -29.431  1.00137.94           C  
ANISOU 3979  CA  LEU B 119    18208  17168  17035    721  -3395   -573       C  
ATOM   3980  C   LEU B 119      22.157  -4.575 -30.481  1.00137.82           C  
ANISOU 3980  C   LEU B 119    18338  17034  16992    772  -3096   -520       C  
ATOM   3981  O   LEU B 119      21.971  -3.999 -31.552  1.00136.32           O  
ANISOU 3981  O   LEU B 119    18092  16813  16892    625  -2910   -539       O  
ATOM   3982  CB  LEU B 119      24.475  -4.555 -29.452  1.00140.99           C  
ANISOU 3982  CB  LEU B 119    18261  17714  17595    858  -3502   -545       C  
ATOM   3983  CG  LEU B 119      25.389  -4.211 -28.253  1.00148.97           C  
ANISOU 3983  CG  LEU B 119    19133  18860  18608    862  -3844   -583       C  
ATOM   3984  CD1 LEU B 119      26.298  -5.373 -27.911  1.00151.92           C  
ANISOU 3984  CD1 LEU B 119    19332  19348  19042   1124  -3962   -512       C  
ATOM   3985  CD2 LEU B 119      26.169  -2.922 -28.485  1.00152.06           C  
ANISOU 3985  CD2 LEU B 119    19264  19346  19166    609  -3921   -674       C  
ATOM   3986  N   LEU B 120      21.544  -5.735 -30.147  1.00132.39           N  
ANISOU 3986  N   LEU B 120    17860  16274  16169    970  -3053   -457       N  
ATOM   3987  CA  LEU B 120      20.595  -6.438 -31.028  1.00129.36           C  
ANISOU 3987  CA  LEU B 120    17644  15772  15735   1016  -2786   -413       C  
ATOM   3988  C   LEU B 120      19.158  -5.908 -30.859  1.00130.56           C  
ANISOU 3988  C   LEU B 120    18094  15790  15721    902  -2716   -433       C  
ATOM   3989  O   LEU B 120      18.284  -6.266 -31.642  1.00127.80           O  
ANISOU 3989  O   LEU B 120    17873  15351  15334    892  -2506   -409       O  
ATOM   3990  CB  LEU B 120      20.596  -7.957 -30.795  1.00129.47           C  
ANISOU 3990  CB  LEU B 120    17748  15758  15686   1272  -2748   -339       C  
ATOM   3991  CG  LEU B 120      21.198  -8.822 -31.881  1.00134.06           C  
ANISOU 3991  CG  LEU B 120    18162  16365  16409   1376  -2562   -293       C  
ATOM   3992  CD1 LEU B 120      21.301 -10.296 -31.489  1.00134.81           C  
ANISOU 3992  CD1 LEU B 120    18355  16429  16439   1642  -2544   -219       C  
ATOM   3993  CD2 LEU B 120      20.715  -8.451 -33.312  1.00134.64           C  
ANISOU 3993  CD2 LEU B 120    18226  16382  16550   1218  -2304   -311       C  
ATOM   3994  N   CYS B 121      18.921  -5.089 -29.819  1.00127.70           N  
ANISOU 3994  N   CYS B 121    17843  15417  15260    821  -2894   -477       N  
ATOM   3995  CA  CYS B 121      17.650  -4.432 -29.523  1.00125.68           C  
ANISOU 3995  CA  CYS B 121    17851  15040  14860    711  -2845   -498       C  
ATOM   3996  C   CYS B 121      17.546  -3.228 -30.435  1.00124.99           C  
ANISOU 3996  C   CYS B 121    17668  14951  14872    493  -2740   -541       C  
ATOM   3997  O   CYS B 121      16.513  -3.023 -31.070  1.00121.69           O  
ANISOU 3997  O   CYS B 121    17386  14441  14410    426  -2565   -529       O  
ATOM   3998  CB  CYS B 121      17.581  -4.042 -28.046  1.00127.88           C  
ANISOU 3998  CB  CYS B 121    18285  15305  14998    719  -3071   -528       C  
ATOM   3999  SG  CYS B 121      16.154  -3.023 -27.589  1.00130.58           S  
ANISOU 3999  SG  CYS B 121    18932  15500  15183    572  -3017   -562       S  
ATOM   4000  N   LYS B 122      18.657  -2.471 -30.534  1.00121.89           N  
ANISOU 4000  N   LYS B 122    17030  14663  14620    388  -2846   -587       N  
ATOM   4001  CA  LYS B 122      18.802  -1.297 -31.383  1.00121.23           C  
ANISOU 4001  CA  LYS B 122    16828  14583  14649    180  -2753   -630       C  
ATOM   4002  C   LYS B 122      18.789  -1.720 -32.849  1.00124.89           C  
ANISOU 4002  C   LYS B 122    17188  15042  15220    187  -2513   -592       C  
ATOM   4003  O   LYS B 122      18.178  -1.038 -33.675  1.00123.83           O  
ANISOU 4003  O   LYS B 122    17112  14845  15093     58  -2356   -597       O  
ATOM   4004  CB  LYS B 122      20.091  -0.514 -31.046  1.00125.39           C  
ANISOU 4004  CB  LYS B 122    17107  15227  15307     70  -2930   -694       C  
ATOM   4005  CG  LYS B 122      20.009   0.282 -29.746  1.00130.03           C  
ANISOU 4005  CG  LYS B 122    17824  15801  15779    -12  -3150   -753       C  
ATOM   4006  CD  LYS B 122      21.240   1.138 -29.485  1.00133.74           C  
ANISOU 4006  CD  LYS B 122    18048  16386  16382   -157  -3321   -828       C  
ATOM   4007  CE  LYS B 122      21.201   1.800 -28.129  1.00140.56           C  
ANISOU 4007  CE  LYS B 122    19058  17237  17110   -228  -3557   -890       C  
ATOM   4008  NZ  LYS B 122      20.299   2.981 -28.117  1.00150.01           N1+
ANISOU 4008  NZ  LYS B 122    20477  18301  18219   -408  -3466   -932       N1+
ATOM   4009  N   ALA B 123      19.435  -2.859 -33.164  1.00121.06           N  
ANISOU 4009  N   ALA B 123    16570  14618  14809    345  -2480   -549       N  
ATOM   4010  CA  ALA B 123      19.494  -3.386 -34.518  1.00119.31           C  
ANISOU 4010  CA  ALA B 123    16266  14387  14679    367  -2250   -514       C  
ATOM   4011  C   ALA B 123      18.114  -3.876 -34.984  1.00119.93           C  
ANISOU 4011  C   ALA B 123    16605  14345  14617    396  -2079   -476       C  
ATOM   4012  O   ALA B 123      17.718  -3.541 -36.093  1.00119.03           O  
ANISOU 4012  O   ALA B 123    16502  14191  14532    298  -1902   -473       O  
ATOM   4013  CB  ALA B 123      20.517  -4.501 -34.599  1.00121.56           C  
ANISOU 4013  CB  ALA B 123    16365  14754  15067    545  -2261   -476       C  
ATOM   4014  N   VAL B 124      17.353  -4.588 -34.122  1.00114.62           N  
ANISOU 4014  N   VAL B 124    16148  13613  13791    517  -2137   -452       N  
ATOM   4015  CA  VAL B 124      16.018  -5.124 -34.466  1.00111.81           C  
ANISOU 4015  CA  VAL B 124    16030  13146  13305    542  -1984   -420       C  
ATOM   4016  C   VAL B 124      14.953  -4.017 -34.520  1.00111.68           C  
ANISOU 4016  C   VAL B 124    16158  13061  13215    383  -1952   -442       C  
ATOM   4017  O   VAL B 124      14.225  -3.941 -35.516  1.00108.34           O  
ANISOU 4017  O   VAL B 124    15792  12592  12782    318  -1785   -427       O  
ATOM   4018  CB  VAL B 124      15.605  -6.285 -33.513  1.00115.96           C  
ANISOU 4018  CB  VAL B 124    16735  13624  13701    723  -2038   -387       C  
ATOM   4019  CG1 VAL B 124      14.091  -6.462 -33.432  1.00114.16           C  
ANISOU 4019  CG1 VAL B 124    16774  13279  13324    704  -1938   -374       C  
ATOM   4020  CG2 VAL B 124      16.269  -7.595 -33.922  1.00116.53           C  
ANISOU 4020  CG2 VAL B 124    16724  13723  13829    890  -1963   -345       C  
ATOM   4021  N   LEU B 125      14.853  -3.177 -33.466  1.00108.93           N  
ANISOU 4021  N   LEU B 125    15876  12703  12811    326  -2109   -475       N  
ATOM   4022  CA  LEU B 125      13.852  -2.111 -33.426  1.00108.15           C  
ANISOU 4022  CA  LEU B 125    15923  12528  12641    193  -2073   -491       C  
ATOM   4023  C   LEU B 125      13.993  -1.140 -34.606  1.00112.38           C  
ANISOU 4023  C   LEU B 125    16342  13077  13281     37  -1956   -503       C  
ATOM   4024  O   LEU B 125      12.965  -0.757 -35.168  1.00111.18           O  
ANISOU 4024  O   LEU B 125    16309  12858  13077    -26  -1833   -484       O  
ATOM   4025  CB  LEU B 125      13.846  -1.325 -32.098  1.00109.01           C  
ANISOU 4025  CB  LEU B 125    16128  12617  12675    153  -2252   -530       C  
ATOM   4026  CG  LEU B 125      13.187  -1.988 -30.875  1.00113.50           C  
ANISOU 4026  CG  LEU B 125    16919  13120  13085    278  -2332   -514       C  
ATOM   4027  CD1 LEU B 125      13.103  -1.023 -29.710  1.00114.32           C  
ANISOU 4027  CD1 LEU B 125    17143  13188  13106    208  -2482   -558       C  
ATOM   4028  CD2 LEU B 125      11.769  -2.468 -31.165  1.00114.26           C  
ANISOU 4028  CD2 LEU B 125    17211  13115  13086    313  -2167   -472       C  
ATOM   4029  N   SER B 126      15.238  -0.780 -35.009  1.00109.82           N  
ANISOU 4029  N   SER B 126    15786  12837  13103    -21  -1985   -531       N  
ATOM   4030  CA  SER B 126      15.479   0.135 -36.129  1.00109.40           C  
ANISOU 4030  CA  SER B 126    15626  12790  13152   -169  -1861   -543       C  
ATOM   4031  C   SER B 126      15.065  -0.482 -37.483  1.00110.56           C  
ANISOU 4031  C   SER B 126    15782  12916  13310   -142  -1654   -498       C  
ATOM   4032  O   SER B 126      14.301   0.151 -38.215  1.00108.02           O  
ANISOU 4032  O   SER B 126    15551  12539  12954   -233  -1537   -484       O  
ATOM   4033  CB  SER B 126      16.936   0.585 -36.168  1.00114.95           C  
ANISOU 4033  CB  SER B 126    16073  13587  14018   -236  -1935   -587       C  
ATOM   4034  OG  SER B 126      17.831  -0.502 -36.326  1.00123.90           O  
ANISOU 4034  OG  SER B 126    17037  14800  15238   -107  -1944   -569       O  
ATOM   4035  N   ILE B 127      15.530  -1.716 -37.787  1.00107.24           N  
ANISOU 4035  N   ILE B 127    15287  12534  12926    -13  -1610   -473       N  
ATOM   4036  CA  ILE B 127      15.219  -2.446 -39.025  1.00106.56           C  
ANISOU 4036  CA  ILE B 127    15224  12425  12840     18  -1417   -437       C  
ATOM   4037  C   ILE B 127      13.692  -2.618 -39.161  1.00110.47           C  
ANISOU 4037  C   ILE B 127    15955  12837  13183     16  -1349   -409       C  
ATOM   4038  O   ILE B 127      13.166  -2.395 -40.248  1.00109.96           O  
ANISOU 4038  O   ILE B 127    15934  12743  13102    -54  -1210   -392       O  
ATOM   4039  CB  ILE B 127      15.972  -3.816 -39.115  1.00110.27           C  
ANISOU 4039  CB  ILE B 127    15601  12936  13361    176  -1390   -417       C  
ATOM   4040  CG1 ILE B 127      17.516  -3.615 -39.118  1.00112.47           C  
ANISOU 4040  CG1 ILE B 127    15606  13309  13817    177  -1442   -438       C  
ATOM   4041  CG2 ILE B 127      15.508  -4.637 -40.352  1.00109.92           C  
ANISOU 4041  CG2 ILE B 127    15632  12846  13284    204  -1182   -384       C  
ATOM   4042  CD1 ILE B 127      18.376  -4.912 -38.821  1.00118.25           C  
ANISOU 4042  CD1 ILE B 127    16228  14094  14607    368  -1468   -412       C  
ATOM   4043  N   ASP B 128      12.983  -2.964 -38.062  1.00106.75           N  
ANISOU 4043  N   ASP B 128    15632  12327  12601     88  -1448   -405       N  
ATOM   4044  CA  ASP B 128      11.525  -3.136 -38.037  1.00104.96           C  
ANISOU 4044  CA  ASP B 128    15612  12025  12244     88  -1391   -382       C  
ATOM   4045  C   ASP B 128      10.777  -1.874 -38.540  1.00106.71           C  
ANISOU 4045  C   ASP B 128    15884  12213  12447    -51  -1342   -378       C  
ATOM   4046  O   ASP B 128       9.920  -1.982 -39.416  1.00103.89           O  
ANISOU 4046  O   ASP B 128    15600  11829  12044    -81  -1226   -350       O  
ATOM   4047  CB  ASP B 128      11.060  -3.502 -36.607  1.00106.98           C  
ANISOU 4047  CB  ASP B 128    16005  12240  12401    176  -1512   -384       C  
ATOM   4048  CG  ASP B 128       9.558  -3.486 -36.372  1.00115.27           C  
ANISOU 4048  CG  ASP B 128    17256  13211  13332    164  -1464   -364       C  
ATOM   4049  OD1 ASP B 128       8.817  -3.908 -37.265  1.00113.15           O1-
ANISOU 4049  OD1 ASP B 128    17034  12922  13036    147  -1336   -341       O1-
ATOM   4050  OD2 ASP B 128       9.135  -3.080 -35.274  1.00125.34           O  
ANISOU 4050  OD2 ASP B 128    18640  14444  14541    172  -1555   -372       O  
ATOM   4051  N   TYR B 129      11.120  -0.703 -37.988  1.00104.77           N  
ANISOU 4051  N   TYR B 129    15604  11969  12234   -131  -1432   -405       N  
ATOM   4052  CA  TYR B 129      10.529   0.577 -38.348  1.00104.85           C  
ANISOU 4052  CA  TYR B 129    15668  11938  12232   -251  -1388   -399       C  
ATOM   4053  C   TYR B 129      11.003   1.095 -39.707  1.00108.02           C  
ANISOU 4053  C   TYR B 129    15961  12363  12717   -343  -1267   -392       C  
ATOM   4054  O   TYR B 129      10.181   1.577 -40.484  1.00107.16           O  
ANISOU 4054  O   TYR B 129    15932  12218  12565   -395  -1170   -359       O  
ATOM   4055  CB  TYR B 129      10.848   1.630 -37.280  1.00107.98           C  
ANISOU 4055  CB  TYR B 129    16078  12317  12635   -312  -1515   -438       C  
ATOM   4056  CG  TYR B 129       9.842   1.683 -36.164  1.00110.59           C  
ANISOU 4056  CG  TYR B 129    16596  12578  12846   -268  -1579   -431       C  
ATOM   4057  CD1 TYR B 129       9.964   0.866 -35.046  1.00113.17           C  
ANISOU 4057  CD1 TYR B 129    16975  12906  13117   -162  -1690   -444       C  
ATOM   4058  CD2 TYR B 129       8.773   2.576 -36.195  1.00110.99           C  
ANISOU 4058  CD2 TYR B 129    16779  12555  12838   -324  -1521   -408       C  
ATOM   4059  CE1 TYR B 129       9.054   0.921 -34.000  1.00113.96           C  
ANISOU 4059  CE1 TYR B 129    17263  12931  13104   -122  -1732   -439       C  
ATOM   4060  CE2 TYR B 129       7.849   2.642 -35.156  1.00111.87           C  
ANISOU 4060  CE2 TYR B 129    17062  12594  12848   -281  -1559   -401       C  
ATOM   4061  CZ  TYR B 129       8.003   1.817 -34.054  1.00122.14           C  
ANISOU 4061  CZ  TYR B 129    18422  13893  14094   -185  -1661   -419       C  
ATOM   4062  OH  TYR B 129       7.117   1.887 -33.015  1.00127.46           O  
ANISOU 4062  OH  TYR B 129    19280  14486  14665   -143  -1684   -413       O  
ATOM   4063  N   TYR B 130      12.324   1.045 -39.971  1.00104.19           N  
ANISOU 4063  N   TYR B 130    15296  11938  12353   -361  -1273   -420       N  
ATOM   4064  CA  TYR B 130      12.946   1.513 -41.208  1.00103.86           C  
ANISOU 4064  CA  TYR B 130    15144  11913  12403   -448  -1145   -419       C  
ATOM   4065  C   TYR B 130      12.412   0.754 -42.422  1.00106.32           C  
ANISOU 4065  C   TYR B 130    15514  12215  12669   -412   -994   -377       C  
ATOM   4066  O   TYR B 130      12.016   1.393 -43.402  1.00105.26           O  
ANISOU 4066  O   TYR B 130    15427  12051  12514   -490   -885   -353       O  
ATOM   4067  CB  TYR B 130      14.469   1.369 -41.110  1.00106.61           C  
ANISOU 4067  CB  TYR B 130    15273  12334  12899   -450  -1184   -457       C  
ATOM   4068  CG  TYR B 130      15.228   1.730 -42.368  1.00108.98           C  
ANISOU 4068  CG  TYR B 130    15448  12649  13311   -532  -1031   -457       C  
ATOM   4069  CD1 TYR B 130      15.429   3.059 -42.728  1.00111.51           C  
ANISOU 4069  CD1 TYR B 130    15749  12939  13680   -679   -984   -474       C  
ATOM   4070  CD2 TYR B 130      15.814   0.745 -43.158  1.00109.90           C  
ANISOU 4070  CD2 TYR B 130    15471  12800  13488   -462   -923   -443       C  
ATOM   4071  CE1 TYR B 130      16.162   3.399 -43.859  1.00112.60           C  
ANISOU 4071  CE1 TYR B 130    15781  13081  13921   -756   -830   -475       C  
ATOM   4072  CE2 TYR B 130      16.556   1.072 -44.286  1.00111.66           C  
ANISOU 4072  CE2 TYR B 130    15585  13028  13814   -535   -769   -443       C  
ATOM   4073  CZ  TYR B 130      16.719   2.400 -44.637  1.00120.79           C  
ANISOU 4073  CZ  TYR B 130    16726  14153  15015   -684   -721   -459       C  
ATOM   4074  OH  TYR B 130      17.454   2.714 -45.742  1.00126.31           O  
ANISOU 4074  OH  TYR B 130    17330  14847  15814   -757   -553   -459       O  
ATOM   4075  N   SER B 131      12.360  -0.603 -42.330  1.00102.87           N  
ANISOU 4075  N   SER B 131    15091  11796  12201   -294   -990   -368       N  
ATOM   4076  CA  SER B 131      11.834  -1.491 -43.375  1.00102.24           C  
ANISOU 4076  CA  SER B 131    15085  11700  12060   -260   -856   -338       C  
ATOM   4077  C   SER B 131      10.310  -1.344 -43.483  1.00104.63           C  
ANISOU 4077  C   SER B 131    15567  11957  12230   -282   -845   -308       C  
ATOM   4078  O   SER B 131       9.740  -1.791 -44.478  1.00104.87           O  
ANISOU 4078  O   SER B 131    15668  11977  12199   -292   -742   -285       O  
ATOM   4079  CB  SER B 131      12.213  -2.950 -43.125  1.00105.90           C  
ANISOU 4079  CB  SER B 131    15529  12181  12527   -131   -852   -341       C  
ATOM   4080  OG  SER B 131      11.459  -3.499 -42.057  1.00112.57           O  
ANISOU 4080  OG  SER B 131    16490  13001  13282    -53   -949   -338       O  
ATOM   4081  N   MET B 132       9.648  -0.725 -42.471  1.00 97.88           N  
ANISOU 4081  N   MET B 132    14785  11076  11330   -289   -950   -308       N  
ATOM   4082  CA  MET B 132       8.211  -0.478 -42.547  1.00 95.14           C  
ANISOU 4082  CA  MET B 132    14582  10689  10876   -307   -935   -274       C  
ATOM   4083  C   MET B 132       7.994   0.697 -43.456  1.00 98.35           C  
ANISOU 4083  C   MET B 132    14996  11085  11289   -406   -868   -248       C  
ATOM   4084  O   MET B 132       7.174   0.613 -44.360  1.00 97.08           O  
ANISOU 4084  O   MET B 132    14906  10920  11061   -424   -796   -213       O  
ATOM   4085  CB  MET B 132       7.582  -0.246 -41.170  1.00 96.60           C  
ANISOU 4085  CB  MET B 132    14852  10837  11014   -271  -1045   -279       C  
ATOM   4086  CG  MET B 132       6.078  -0.144 -41.216  1.00 98.50           C  
ANISOU 4086  CG  MET B 132    15224  11042  11161   -274  -1017   -241       C  
ATOM   4087  SD  MET B 132       5.419   0.648 -39.737  1.00101.54           S  
ANISOU 4087  SD  MET B 132    15708  11364  11507   -260  -1110   -242       S  
ATOM   4088  CE  MET B 132       3.788   1.084 -40.284  1.00 97.15           C  
ANISOU 4088  CE  MET B 132    15249  10782  10883   -283  -1038   -182       C  
ATOM   4089  N   PHE B 133       8.776   1.768 -43.260  1.00 96.36           N  
ANISOU 4089  N   PHE B 133    14672  10827  11114   -472   -891   -268       N  
ATOM   4090  CA  PHE B 133       8.670   2.982 -44.052  1.00 96.87           C  
ANISOU 4090  CA  PHE B 133    14754  10864  11186   -565   -818   -243       C  
ATOM   4091  C   PHE B 133       9.175   2.781 -45.468  1.00101.74           C  
ANISOU 4091  C   PHE B 133    15326  11503  11830   -600   -688   -230       C  
ATOM   4092  O   PHE B 133       8.434   3.138 -46.387  1.00101.15           O  
ANISOU 4092  O   PHE B 133    15338  11409  11684   -628   -614   -184       O  
ATOM   4093  CB  PHE B 133       9.368   4.156 -43.366  1.00 99.87           C  
ANISOU 4093  CB  PHE B 133    15086  11220  11640   -638   -871   -276       C  
ATOM   4094  CG  PHE B 133       8.464   4.770 -42.314  1.00101.41           C  
ANISOU 4094  CG  PHE B 133    15400  11362  11769   -627   -952   -267       C  
ATOM   4095  CD1 PHE B 133       7.540   5.760 -42.653  1.00104.20           C  
ANISOU 4095  CD1 PHE B 133    15865  11660  12068   -662   -897   -219       C  
ATOM   4096  CD2 PHE B 133       8.479   4.309 -41.005  1.00103.71           C  
ANISOU 4096  CD2 PHE B 133    15706  11654  12045   -568  -1073   -300       C  
ATOM   4097  CE1 PHE B 133       6.674   6.303 -41.691  1.00104.30           C  
ANISOU 4097  CE1 PHE B 133    15991  11614  12023   -640   -951   -207       C  
ATOM   4098  CE2 PHE B 133       7.608   4.849 -40.047  1.00106.07           C  
ANISOU 4098  CE2 PHE B 133    16134  11892  12275   -555  -1127   -291       C  
ATOM   4099  CZ  PHE B 133       6.712   5.843 -40.399  1.00103.61           C  
ANISOU 4099  CZ  PHE B 133    15923  11523  11922   -591  -1059   -245       C  
ATOM   4100  N   THR B 134      10.376   2.159 -45.665  1.00 99.41           N  
ANISOU 4100  N   THR B 134    14901  11244  11627   -588   -656   -265       N  
ATOM   4101  CA  THR B 134      10.915   1.917 -47.022  1.00 99.58           C  
ANISOU 4101  CA  THR B 134    14888  11273  11674   -617   -508   -254       C  
ATOM   4102  C   THR B 134       9.975   1.017 -47.840  1.00103.01           C  
ANISOU 4102  C   THR B 134    15444  11707  11987   -576   -448   -221       C  
ATOM   4103  O   THR B 134       9.832   1.247 -49.038  1.00101.26           O  
ANISOU 4103  O   THR B 134    15280  11471  11722   -623   -337   -194       O  
ATOM   4104  CB  THR B 134      12.350   1.346 -47.036  1.00100.62           C  
ANISOU 4104  CB  THR B 134    14849  11444  11938   -596   -474   -294       C  
ATOM   4105  OG1 THR B 134      12.386   0.058 -46.433  1.00 97.07           O  
ANISOU 4105  OG1 THR B 134    14382  11023  11477   -484   -533   -307       O  
ATOM   4106  CG2 THR B 134      13.359   2.266 -46.397  1.00 96.82           C  
ANISOU 4106  CG2 THR B 134    14225  10974  11587   -662   -529   -333       C  
ATOM   4107  N   SER B 135       9.303   0.037 -47.185  1.00100.50           N  
ANISOU 4107  N   SER B 135    15180  11400  11607   -497   -520   -225       N  
ATOM   4108  CA  SER B 135       8.384  -0.877 -47.870  1.00100.27           C  
ANISOU 4108  CA  SER B 135    15264  11371  11464   -473   -472   -205       C  
ATOM   4109  C   SER B 135       7.112  -0.179 -48.288  1.00103.31           C  
ANISOU 4109  C   SER B 135    15760  11745  11748   -518   -484   -160       C  
ATOM   4110  O   SER B 135       6.623  -0.442 -49.390  1.00103.80           O  
ANISOU 4110  O   SER B 135    15899  11814  11728   -546   -415   -137       O  
ATOM   4111  CB  SER B 135       8.036  -2.089 -47.010  1.00103.47           C  
ANISOU 4111  CB  SER B 135    15697  11780  11838   -385   -534   -225       C  
ATOM   4112  OG  SER B 135       7.588  -3.161 -47.826  1.00110.93           O  
ANISOU 4112  OG  SER B 135    16725  12721  12702   -374   -454   -224       O  
ATOM   4113  N   ILE B 136       6.570   0.697 -47.421  1.00 97.61           N  
ANISOU 4113  N   ILE B 136    15053  11007  11028   -522   -572   -145       N  
ATOM   4114  CA  ILE B 136       5.328   1.408 -47.705  1.00 95.99           C  
ANISOU 4114  CA  ILE B 136    14941  10793  10740   -544   -587    -92       C  
ATOM   4115  C   ILE B 136       5.586   2.460 -48.792  1.00102.14           C  
ANISOU 4115  C   ILE B 136    15737  11556  11515   -611   -505    -56       C  
ATOM   4116  O   ILE B 136       4.867   2.471 -49.789  1.00101.45           O  
ANISOU 4116  O   ILE B 136    15727  11483  11337   -626   -467    -14       O  
ATOM   4117  CB  ILE B 136       4.683   1.998 -46.415  1.00 97.36           C  
ANISOU 4117  CB  ILE B 136    15137  10939  10918   -516   -683    -84       C  
ATOM   4118  CG1 ILE B 136       4.119   0.877 -45.515  1.00 96.52           C  
ANISOU 4118  CG1 ILE B 136    15054  10837  10781   -449   -744   -106       C  
ATOM   4119  CG2 ILE B 136       3.571   2.959 -46.763  1.00 97.05           C  
ANISOU 4119  CG2 ILE B 136    15173  10884  10818   -533   -680    -20       C  
ATOM   4120  CD1 ILE B 136       3.979   1.226 -44.021  1.00 94.61           C  
ANISOU 4120  CD1 ILE B 136    14825  10558  10563   -411   -831   -121       C  
ATOM   4121  N   PHE B 137       6.639   3.278 -48.638  1.00101.29           N  
ANISOU 4121  N   PHE B 137    15560  11422  11502   -653   -476    -76       N  
ATOM   4122  CA  PHE B 137       6.934   4.347 -49.586  1.00102.86           C  
ANISOU 4122  CA  PHE B 137    15788  11589  11703   -720   -382    -44       C  
ATOM   4123  C   PHE B 137       7.390   3.846 -50.940  1.00106.90           C  
ANISOU 4123  C   PHE B 137    16316  12113  12187   -744   -262    -39       C  
ATOM   4124  O   PHE B 137       7.103   4.524 -51.926  1.00107.53           O  
ANISOU 4124  O   PHE B 137    16483  12171  12204   -780   -190     10       O  
ATOM   4125  CB  PHE B 137       7.923   5.365 -49.019  1.00106.31           C  
ANISOU 4125  CB  PHE B 137    16150  11988  12256   -777   -375    -74       C  
ATOM   4126  CG  PHE B 137       7.201   6.320 -48.091  1.00108.70           C  
ANISOU 4126  CG  PHE B 137    16512  12249  12541   -774   -453    -55       C  
ATOM   4127  CD1 PHE B 137       6.390   7.339 -48.602  1.00113.05           C  
ANISOU 4127  CD1 PHE B 137    17175  12757  13023   -787   -411     13       C  
ATOM   4128  CD2 PHE B 137       7.263   6.154 -46.711  1.00110.87           C  
ANISOU 4128  CD2 PHE B 137    16747  12525  12855   -746   -565    -97       C  
ATOM   4129  CE1 PHE B 137       5.655   8.169 -47.743  1.00114.35           C  
ANISOU 4129  CE1 PHE B 137    17404  12874  13169   -770   -468     37       C  
ATOM   4130  CE2 PHE B 137       6.546   6.995 -45.855  1.00113.74           C  
ANISOU 4130  CE2 PHE B 137    17187  12838  13190   -740   -621    -79       C  
ATOM   4131  CZ  PHE B 137       5.745   7.992 -46.374  1.00112.67           C  
ANISOU 4131  CZ  PHE B 137    17157  12656  12998   -750   -566    -12       C  
ATOM   4132  N   THR B 138       8.043   2.662 -51.005  1.00102.17           N  
ANISOU 4132  N   THR B 138    15654  11543  11624   -717   -234    -83       N  
ATOM   4133  CA  THR B 138       8.460   2.062 -52.278  1.00101.76           C  
ANISOU 4133  CA  THR B 138    15636  11491  11535   -734   -105    -82       C  
ATOM   4134  C   THR B 138       7.208   1.643 -53.028  1.00103.99           C  
ANISOU 4134  C   THR B 138    16062  11791  11657   -726   -119    -43       C  
ATOM   4135  O   THR B 138       7.093   1.903 -54.224  1.00105.21           O  
ANISOU 4135  O   THR B 138    16310  11933  11732   -764    -33    -10       O  
ATOM   4136  CB  THR B 138       9.420   0.889 -52.042  1.00108.69           C  
ANISOU 4136  CB  THR B 138    16415  12387  12495   -690    -70   -135       C  
ATOM   4137  OG1 THR B 138      10.680   1.390 -51.585  1.00109.23           O  
ANISOU 4137  OG1 THR B 138    16333  12450  12719   -711    -47   -167       O  
ATOM   4138  CG2 THR B 138       9.610   0.020 -53.276  1.00107.00           C  
ANISOU 4138  CG2 THR B 138    16273  12166  12217   -692     64   -136       C  
ATOM   4139  N   LEU B 139       6.259   1.034 -52.294  1.00 97.82           N  
ANISOU 4139  N   LEU B 139    15298  11039  10829   -680   -230    -46       N  
ATOM   4140  CA  LEU B 139       4.972   0.539 -52.752  1.00 96.04           C  
ANISOU 4140  CA  LEU B 139    15177  10845  10469   -677   -274    -19       C  
ATOM   4141  C   LEU B 139       4.116   1.700 -53.250  1.00 98.76           C  
ANISOU 4141  C   LEU B 139    15593  11191  10741   -700   -300     52       C  
ATOM   4142  O   LEU B 139       3.591   1.600 -54.357  1.00 99.55           O  
ANISOU 4142  O   LEU B 139    15789  11310  10725   -725   -274     84       O  
ATOM   4143  CB  LEU B 139       4.304  -0.211 -51.591  1.00 94.76           C  
ANISOU 4143  CB  LEU B 139    14990  10702  10314   -625   -378    -43       C  
ATOM   4144  CG  LEU B 139       2.859  -0.624 -51.659  1.00 98.30           C  
ANISOU 4144  CG  LEU B 139    15507  11184  10656   -624   -448    -21       C  
ATOM   4145  CD1 LEU B 139       2.660  -1.768 -52.624  1.00 98.72           C  
ANISOU 4145  CD1 LEU B 139    15636  11258  10614   -655   -397    -45       C  
ATOM   4146  CD2 LEU B 139       2.402  -0.966 -50.293  1.00 99.97           C  
ANISOU 4146  CD2 LEU B 139    15681  11392  10911   -574   -531    -40       C  
ATOM   4147  N   THR B 140       4.035   2.819 -52.477  1.00 93.03           N  
ANISOU 4147  N   THR B 140    14832  10439  10077   -689   -345     77       N  
ATOM   4148  CA  THR B 140       3.263   4.025 -52.828  1.00 92.22           C  
ANISOU 4148  CA  THR B 140    14798  10324   9917   -692   -360    153       C  
ATOM   4149  C   THR B 140       3.814   4.670 -54.109  1.00 97.93           C  
ANISOU 4149  C   THR B 140    15591  11016  10600   -738   -246    185       C  
ATOM   4150  O   THR B 140       3.024   5.016 -54.994  1.00 97.28           O  
ANISOU 4150  O   THR B 140    15609  10951  10403   -734   -250    250       O  
ATOM   4151  CB  THR B 140       3.235   5.044 -51.674  1.00 93.51           C  
ANISOU 4151  CB  THR B 140    14923  10444  10163   -674   -406    162       C  
ATOM   4152  OG1 THR B 140       3.089   4.380 -50.426  1.00 93.19           O  
ANISOU 4152  OG1 THR B 140    14820  10416  10174   -636   -488    116       O  
ATOM   4153  CG2 THR B 140       2.108   6.039 -51.810  1.00 89.99           C  
ANISOU 4153  CG2 THR B 140    14551   9989   9653   -645   -438    246       C  
ATOM   4154  N   MET B 141       5.163   4.813 -54.208  1.00 96.80           N  
ANISOU 4154  N   MET B 141    15396  10832  10553   -779   -143    143       N  
ATOM   4155  CA  MET B 141       5.862   5.401 -55.357  1.00 98.66           C  
ANISOU 4155  CA  MET B 141    15695  11022  10770   -830     -3    165       C  
ATOM   4156  C   MET B 141       5.660   4.554 -56.602  1.00106.59           C  
ANISOU 4156  C   MET B 141    16798  12053  11648   -837     51    173       C  
ATOM   4157  O   MET B 141       5.525   5.107 -57.696  1.00105.83           O  
ANISOU 4157  O   MET B 141    16825  11932  11455   -859    123    225       O  
ATOM   4158  CB  MET B 141       7.353   5.585 -55.077  1.00101.41           C  
ANISOU 4158  CB  MET B 141    15932  11328  11271   -876     94    107       C  
ATOM   4159  N   MET B 142       5.615   3.208 -56.431  1.00107.03           N  
ANISOU 4159  N   MET B 142    16821  12152  11695   -819     19    122       N  
ATOM   4160  CA  MET B 142       5.371   2.256 -57.512  1.00109.18           C  
ANISOU 4160  CA  MET B 142    17199  12445  11838   -835     64    115       C  
ATOM   4161  C   MET B 142       3.989   2.497 -58.114  1.00116.48           C  
ANISOU 4161  C   MET B 142    18243  13414  12600   -831    -30    179       C  
ATOM   4162  O   MET B 142       3.832   2.391 -59.333  1.00117.84           O  
ANISOU 4162  O   MET B 142    18548  13587  12640   -861     22    203       O  
ATOM   4163  CB  MET B 142       5.504   0.810 -57.038  1.00111.50           C  
ANISOU 4163  CB  MET B 142    17441  12765  12158   -813     44     47       C  
ATOM   4164  CG  MET B 142       5.834  -0.132 -58.179  1.00117.35           C  
ANISOU 4164  CG  MET B 142    18287  13493  12808   -842    158     21       C  
ATOM   4165  SD  MET B 142       5.533  -1.900 -57.904  1.00122.40           S  
ANISOU 4165  SD  MET B 142    18942  14156  13408   -823    133    -46       S  
ATOM   4166  CE  MET B 142       6.926  -2.333 -56.870  1.00119.05           C  
ANISOU 4166  CE  MET B 142    18347  13699  13186   -764    197    -98       C  
ATOM   4167  N   CYS B 143       3.007   2.874 -57.265  1.00113.67           N  
ANISOU 4167  N   CYS B 143    17839  13094  12255   -793   -165    210       N  
ATOM   4168  CA  CYS B 143       1.637   3.191 -57.678  1.00113.95           C  
ANISOU 4168  CA  CYS B 143    17948  13185  12164   -776   -270    279       C  
ATOM   4169  C   CYS B 143       1.596   4.526 -58.407  1.00117.87           C  
ANISOU 4169  C   CYS B 143    18534  13645  12606   -769   -227    363       C  
ATOM   4170  O   CYS B 143       0.808   4.691 -59.340  1.00118.39           O  
ANISOU 4170  O   CYS B 143    18706  13750  12527   -764   -269    423       O  
ATOM   4171  CB  CYS B 143       0.693   3.178 -56.483  1.00113.60           C  
ANISOU 4171  CB  CYS B 143    17812  13178  12171   -729   -401    286       C  
ATOM   4172  SG  CYS B 143       0.330   1.515 -55.858  1.00116.93           S  
ANISOU 4172  SG  CYS B 143    18178  13648  12601   -737   -461    204       S  
ATOM   4173  N   VAL B 144       2.471   5.456 -58.006  1.00114.16           N  
ANISOU 4173  N   VAL B 144    18029  13100  12248   -772   -142    365       N  
ATOM   4174  CA  VAL B 144       2.616   6.769 -58.631  1.00115.24           C  
ANISOU 4174  CA  VAL B 144    18261  13176  12350   -771    -65    438       C  
ATOM   4175  C   VAL B 144       3.247   6.572 -60.017  1.00123.37           C  
ANISOU 4175  C   VAL B 144    19416  14175  13283   -818     64    440       C  
ATOM   4176  O   VAL B 144       2.808   7.208 -60.980  1.00124.15           O  
ANISOU 4176  O   VAL B 144    19658  14263  13251   -804     82    517       O  
ATOM   4177  CB  VAL B 144       3.435   7.712 -57.725  1.00117.98           C  
ANISOU 4177  CB  VAL B 144    18530  13443  12853   -784     -4    420       C  
ATOM   4178  CG1 VAL B 144       3.877   8.970 -58.448  1.00118.54           C  
ANISOU 4178  CG1 VAL B 144    18710  13426  12902   -806    123    478       C  
ATOM   4179  CG2 VAL B 144       2.642   8.070 -56.487  1.00116.75           C  
ANISOU 4179  CG2 VAL B 144    18302  13304  12753   -731   -125    436       C  
ATOM   4180  N   ASP B 145       4.235   5.649 -60.114  1.00121.31           N  
ANISOU 4180  N   ASP B 145    19110  13901  13080   -862    155    358       N  
ATOM   4181  CA  ASP B 145       4.935   5.283 -61.347  1.00122.65           C  
ANISOU 4181  CA  ASP B 145    19395  14033  13173   -907    303    346       C  
ATOM   4182  C   ASP B 145       3.954   4.705 -62.358  1.00125.55           C  
ANISOU 4182  C   ASP B 145    19915  14459  13331   -904    233    378       C  
ATOM   4183  O   ASP B 145       3.991   5.094 -63.529  1.00126.35           O  
ANISOU 4183  O   ASP B 145    20183  14525  13299   -920    312    425       O  
ATOM   4184  CB  ASP B 145       6.049   4.268 -61.042  1.00124.93           C  
ANISOU 4184  CB  ASP B 145    19578  14307  13582   -934    396    252       C  
ATOM   4185  CG  ASP B 145       7.054   4.084 -62.157  1.00139.29           C  
ANISOU 4185  CG  ASP B 145    21490  16060  15375   -978    597    236       C  
ATOM   4186  OD1 ASP B 145       7.824   5.039 -62.429  1.00141.94           O1-
ANISOU 4186  OD1 ASP B 145    21836  16321  15775  -1007    730    257       O1-
ATOM   4187  OD2 ASP B 145       7.125   2.966 -62.709  1.00144.03           O1-
ANISOU 4187  OD2 ASP B 145    22151  16672  15901   -988    637    197       O1-
ATOM   4188  N   ARG B 146       3.051   3.813 -61.883  1.00120.15           N  
ANISOU 4188  N   ARG B 146    19176  13859  12614   -889     82    352       N  
ATOM   4189  CA  ARG B 146       2.017   3.175 -62.691  1.00120.32           C  
ANISOU 4189  CA  ARG B 146    19314  13954  12449   -902    -17    369       C  
ATOM   4190  C   ARG B 146       0.928   4.187 -63.088  1.00124.99           C  
ANISOU 4190  C   ARG B 146    19977  14588  12927   -858   -129    476       C  
ATOM   4191  O   ARG B 146       0.277   3.997 -64.112  1.00125.90           O  
ANISOU 4191  O   ARG B 146    20228  14749  12859   -873   -184    510       O  
ATOM   4192  CB  ARG B 146       1.421   1.954 -61.978  1.00119.44           C  
ANISOU 4192  CB  ARG B 146    19109  13913  12360   -909   -130    304       C  
ATOM   4193  CG  ARG B 146       2.331   0.722 -62.049  1.00132.29           C  
ANISOU 4193  CG  ARG B 146    20738  15503  14022   -949    -15    210       C  
ATOM   4194  CD  ARG B 146       1.706  -0.519 -61.423  1.00145.46           C  
ANISOU 4194  CD  ARG B 146    22349  17227  15694   -959   -111    148       C  
ATOM   4195  NE  ARG B 146       2.097  -0.695 -60.017  1.00155.79           N  
ANISOU 4195  NE  ARG B 146    23488  18520  17184   -914   -124    110       N  
ATOM   4196  CZ  ARG B 146       1.287  -1.158 -59.066  1.00166.56           C  
ANISOU 4196  CZ  ARG B 146    24767  19933  18585   -895   -245     92       C  
ATOM   4197  NH1 ARG B 146       0.037  -1.492 -59.343  1.00155.29           N1+
ANISOU 4197  NH1 ARG B 146    23383  18578  17044   -923   -363    105       N1+
ATOM   4198  NH2 ARG B 146       1.734  -1.279 -57.817  1.00145.94           N  
ANISOU 4198  NH2 ARG B 146    22027  17298  16126   -850   -248     60       N  
ATOM   4199  N   TYR B 147       0.773   5.284 -62.328  1.00120.93           N  
ANISOU 4199  N   TYR B 147    19384  14051  12512   -803   -155    530       N  
ATOM   4200  CA  TYR B 147      -0.172   6.345 -62.668  1.00121.67           C  
ANISOU 4200  CA  TYR B 147    19547  14169  12514   -741   -238    642       C  
ATOM   4201  C   TYR B 147       0.363   7.161 -63.841  1.00127.64           C  
ANISOU 4201  C   TYR B 147    20486  14848  13163   -746   -108    702       C  
ATOM   4202  O   TYR B 147      -0.400   7.484 -64.751  1.00128.39           O  
ANISOU 4202  O   TYR B 147    20714  14982  13087   -713   -175    784       O  
ATOM   4203  CB  TYR B 147      -0.459   7.250 -61.464  1.00122.24           C  
ANISOU 4203  CB  TYR B 147    19498  14221  12726   -678   -280    678       C  
ATOM   4204  CG  TYR B 147      -0.957   8.624 -61.854  1.00126.10           C  
ANISOU 4204  CG  TYR B 147    20082  14678  13151   -607   -282    799       C  
ATOM   4205  CD1 TYR B 147      -2.309   8.850 -62.102  1.00129.05           C  
ANISOU 4205  CD1 TYR B 147    20472  15140  13420   -534   -433    888       C  
ATOM   4206  CD2 TYR B 147      -0.072   9.688 -62.019  1.00127.78           C  
ANISOU 4206  CD2 TYR B 147    20371  14771  13407   -612   -125    826       C  
ATOM   4207  CE1 TYR B 147      -2.772  10.112 -62.474  1.00132.03           C  
ANISOU 4207  CE1 TYR B 147    20944  15486  13736   -448   -430   1010       C  
ATOM   4208  CE2 TYR B 147      -0.521  10.948 -62.407  1.00129.91           C  
ANISOU 4208  CE2 TYR B 147    20754  14996  13609   -540   -110    941       C  
ATOM   4209  CZ  TYR B 147      -1.875  11.159 -62.625  1.00138.93           C  
ANISOU 4209  CZ  TYR B 147    21916  16226  14645   -449   -263   1038       C  
ATOM   4210  OH  TYR B 147      -2.334  12.401 -63.001  1.00141.35           O  
ANISOU 4210  OH  TYR B 147    22337  16486  14882   -357   -246   1162       O  
ATOM   4211  N   ILE B 148       1.668   7.526 -63.787  1.00124.42           N  
ANISOU 4211  N   ILE B 148    20082  14331  12862   -785     78    666       N  
ATOM   4212  CA  ILE B 148       2.388   8.297 -64.810  1.00125.21           C  
ANISOU 4212  CA  ILE B 148    20351  14331  12892   -803    249    710       C  
ATOM   4213  C   ILE B 148       2.416   7.465 -66.094  1.00130.77           C  
ANISOU 4213  C   ILE B 148    21221  15054  13413   -844    284    695       C  
ATOM   4214  O   ILE B 148       2.124   7.995 -67.165  1.00131.84           O  
ANISOU 4214  O   ILE B 148    21552  15169  13375   -824    306    773       O  
ATOM   4215  CB  ILE B 148       3.808   8.697 -64.302  1.00127.47           C  
ANISOU 4215  CB  ILE B 148    20555  14508  13370   -855    435    651       C  
ATOM   4216  CG1 ILE B 148       3.688   9.706 -63.145  1.00126.86           C  
ANISOU 4216  CG1 ILE B 148    20363  14401  13437   -821    396    675       C  
ATOM   4217  CG2 ILE B 148       4.697   9.253 -65.418  1.00128.85           C  
ANISOU 4217  CG2 ILE B 148    20899  14572  13486   -896    649    676       C  
ATOM   4218  CD1 ILE B 148       4.755   9.615 -62.096  1.00130.23           C  
ANISOU 4218  CD1 ILE B 148    20614  14788  14081   -873    464    584       C  
ATOM   4219  N   ALA B 149       2.692   6.151 -65.965  1.00126.78           N  
ANISOU 4219  N   ALA B 149    20652  14586  12932   -895    281    598       N  
ATOM   4220  CA  ALA B 149       2.713   5.209 -67.080  1.00127.48           C  
ANISOU 4220  CA  ALA B 149    20900  14687  12850   -943    316    567       C  
ATOM   4221  C   ALA B 149       1.381   5.221 -67.847  1.00132.21           C  
ANISOU 4221  C   ALA B 149    21634  15379  13221   -919    137    637       C  
ATOM   4222  O   ALA B 149       1.379   5.408 -69.073  1.00134.09           O  
ANISOU 4222  O   ALA B 149    22091  15588  13268   -931    189    681       O  
ATOM   4223  CB  ALA B 149       3.008   3.807 -66.565  1.00127.14           C  
ANISOU 4223  CB  ALA B 149    20747  14676  12886   -986    312    457       C  
ATOM   4224  N   VAL B 150       0.254   5.089 -67.106  1.00126.32           N  
ANISOU 4224  N   VAL B 150    20754  14744  12499   -882    -72    654       N  
ATOM   4225  CA  VAL B 150      -1.101   5.029 -67.653  1.00126.00           C  
ANISOU 4225  CA  VAL B 150    20780  14819  12277   -859   -275    715       C  
ATOM   4226  C   VAL B 150      -1.585   6.422 -68.125  1.00130.06           C  
ANISOU 4226  C   VAL B 150    21393  15323  12702   -771   -309    852       C  
ATOM   4227  O   VAL B 150      -1.827   6.598 -69.317  1.00130.66           O  
ANISOU 4227  O   VAL B 150    21671  15405  12568   -768   -322    908       O  
ATOM   4228  CB  VAL B 150      -2.096   4.364 -66.643  1.00127.98           C  
ANISOU 4228  CB  VAL B 150    20831  15186  12610   -855   -464    680       C  
ATOM   4229  CG1 VAL B 150      -3.543   4.470 -67.122  1.00128.62           C  
ANISOU 4229  CG1 VAL B 150    20937  15399  12535   -824   -683    755       C  
ATOM   4230  CG2 VAL B 150      -1.737   2.902 -66.393  1.00126.97           C  
ANISOU 4230  CG2 VAL B 150    20659  15066  12519   -941   -433    553       C  
ATOM   4231  N   CYS B 151      -1.731   7.382 -67.197  1.00126.65           N  
ANISOU 4231  N   CYS B 151    20834  14868  12417   -695   -321    906       N  
ATOM   4232  CA  CYS B 151      -2.301   8.707 -67.438  1.00127.92           C  
ANISOU 4232  CA  CYS B 151    21068  15018  12519   -592   -358   1041       C  
ATOM   4233  C   CYS B 151      -1.446   9.627 -68.278  1.00134.42           C  
ANISOU 4233  C   CYS B 151    22095  15706  13272   -584   -166   1095       C  
ATOM   4234  O   CYS B 151      -2.016  10.359 -69.083  1.00135.59           O  
ANISOU 4234  O   CYS B 151    22401  15862  13257   -511   -211   1208       O  
ATOM   4235  CB  CYS B 151      -2.668   9.380 -66.127  1.00126.98           C  
ANISOU 4235  CB  CYS B 151    20763  14897  12585   -521   -404   1070       C  
ATOM   4236  SG  CYS B 151      -4.010   8.556 -65.251  1.00129.89           S  
ANISOU 4236  SG  CYS B 151    20917  15428  13005   -501   -643   1048       S  
ATOM   4237  N   HIS B 152      -0.121   9.641 -68.096  1.00131.78           N  
ANISOU 4237  N   HIS B 152    21758  15251  13062   -651     47   1023       N  
ATOM   4238  CA  HIS B 152       0.727  10.545 -68.878  1.00133.80           C  
ANISOU 4238  CA  HIS B 152    22206  15367  13267   -654    255   1071       C  
ATOM   4239  C   HIS B 152       1.760   9.732 -69.667  1.00140.15           C  
ANISOU 4239  C   HIS B 152    23117  16111  14024   -753    425    987       C  
ATOM   4240  O   HIS B 152       2.938   9.768 -69.318  1.00138.98           O  
ANISOU 4240  O   HIS B 152    22903  15866  14037   -811    613    920       O  
ATOM   4241  CB  HIS B 152       1.394  11.583 -67.954  1.00134.08           C  
ANISOU 4241  CB  HIS B 152    22143  15293  13508   -644    384   1076       C  
ATOM   4242  CG  HIS B 152       0.435  12.245 -67.021  1.00136.86           C  
ANISOU 4242  CG  HIS B 152    22378  15694  13930   -552    235   1141       C  
ATOM   4243  ND1 HIS B 152      -0.485  13.176 -67.470  1.00139.84           N  
ANISOU 4243  ND1 HIS B 152    22878  16080  14175   -441    161   1277       N  
ATOM   4244  CD2 HIS B 152       0.259  12.060 -65.695  1.00136.79           C  
ANISOU 4244  CD2 HIS B 152    22149  15724  14100   -549    154   1089       C  
ATOM   4245  CE1 HIS B 152      -1.182  13.531 -66.404  1.00138.12           C  
ANISOU 4245  CE1 HIS B 152    22505  15903  14071   -374     49   1304       C  
ATOM   4246  NE2 HIS B 152      -0.769  12.888 -65.313  1.00136.61           N  
ANISOU 4246  NE2 HIS B 152    22113  15729  14063   -441     43   1191       N  
ATOM   4247  N   PRO B 153       1.352   8.977 -70.722  1.00140.11           N  
ANISOU 4247  N   PRO B 153    23274  16162  13800   -775    363    986       N  
ATOM   4248  CA  PRO B 153       2.327   8.133 -71.429  1.00141.39           C  
ANISOU 4248  CA  PRO B 153    23546  16258  13920   -866    540    901       C  
ATOM   4249  C   PRO B 153       3.351   8.912 -72.252  1.00147.65           C  
ANISOU 4249  C   PRO B 153    24533  16890  14676   -882    804    935       C  
ATOM   4250  O   PRO B 153       4.450   8.407 -72.467  1.00147.17           O  
ANISOU 4250  O   PRO B 153    24485  16746  14686   -954   1007    856       O  
ATOM   4251  CB  PRO B 153       1.452   7.259 -72.325  1.00144.38           C  
ANISOU 4251  CB  PRO B 153    24070  16736  14050   -884    383    900       C  
ATOM   4252  CG  PRO B 153       0.221   8.054 -72.546  1.00149.43           C  
ANISOU 4252  CG  PRO B 153    24765  17460  14553   -791    180   1023       C  
ATOM   4253  CD  PRO B 153      -0.008   8.795 -71.277  1.00143.03           C  
ANISOU 4253  CD  PRO B 153    23725  16662  13958   -725    126   1054       C  
ATOM   4254  N   VAL B 154       3.004  10.127 -72.690  1.00146.78           N  
ANISOU 4254  N   VAL B 154    24572  16732  14467   -812    813   1054       N  
ATOM   4255  CA  VAL B 154       3.882  10.997 -73.479  1.00148.90           C  
ANISOU 4255  CA  VAL B 154    25048  16836  14690   -823   1070   1100       C  
ATOM   4256  C   VAL B 154       5.013  11.540 -72.571  1.00153.39           C  
ANISOU 4256  C   VAL B 154    25436  17299  15546   -870   1265   1047       C  
ATOM   4257  O   VAL B 154       6.176  11.590 -72.989  1.00154.01           O  
ANISOU 4257  O   VAL B 154    25580  17254  15684   -940   1523   1005       O  
ATOM   4258  CB  VAL B 154       3.076  12.132 -74.166  1.00154.04           C  
ANISOU 4258  CB  VAL B 154    25919  17468  15141   -719   1007   1252       C  
ATOM   4259  CG1 VAL B 154       3.933  12.875 -75.180  1.00155.69           C  
ANISOU 4259  CG1 VAL B 154    26402  17501  15254   -736   1284   1299       C  
ATOM   4260  CG2 VAL B 154       1.814  11.585 -74.832  1.00154.56           C  
ANISOU 4260  CG2 VAL B 154    26095  17680  14951   -668    748   1302       C  
ATOM   4261  N   LYS B 155       4.660  11.904 -71.321  1.00148.86           N  
ANISOU 4261  N   LYS B 155    24632  16777  15150   -837   1139   1044       N  
ATOM   4262  CA  LYS B 155       5.580  12.415 -70.301  1.00147.73           C  
ANISOU 4262  CA  LYS B 155    24297  16558  15276   -885   1268    989       C  
ATOM   4263  C   LYS B 155       6.362  11.255 -69.647  1.00151.08           C  
ANISOU 4263  C   LYS B 155    24499  17023  15881   -963   1295    853       C  
ATOM   4264  O   LYS B 155       7.543  11.427 -69.335  1.00150.55           O  
ANISOU 4264  O   LYS B 155    24334  16870  15999  -1032   1483    791       O  
ATOM   4265  CB  LYS B 155       4.813  13.239 -69.236  1.00148.35           C  
ANISOU 4265  CB  LYS B 155    24248  16673  15445   -814   1114   1041       C  
ATOM   4266  CG  LYS B 155       4.165  14.538 -69.753  1.00153.16           C  
ANISOU 4266  CG  LYS B 155    25063  17219  15912   -722   1119   1183       C  
ATOM   4267  CD  LYS B 155       2.751  14.771 -69.197  1.00152.57           C  
ANISOU 4267  CD  LYS B 155    24921  17258  15789   -605    863   1262       C  
ATOM   4268  CE  LYS B 155       1.948  15.770 -70.004  1.00150.39           C  
ANISOU 4268  CE  LYS B 155    24878  16950  15312   -488    836   1417       C  
ATOM   4269  NZ  LYS B 155       0.498  15.426 -70.053  1.00149.02           N1+
ANISOU 4269  NZ  LYS B 155    24675  16940  15005   -381    559   1488       N1+
ATOM   4270  N   ALA B 156       5.710  10.073 -69.480  1.00147.44           N  
ANISOU 4270  N   ALA B 156    23966  16691  15365   -950   1113    809       N  
ATOM   4271  CA  ALA B 156       6.268   8.851 -68.876  1.00146.69           C  
ANISOU 4271  CA  ALA B 156    23682  16643  15410  -1001   1113    691       C  
ATOM   4272  C   ALA B 156       7.500   8.340 -69.602  1.00154.22           C  
ANISOU 4272  C   ALA B 156    24704  17506  16388  -1071   1361    630       C  
ATOM   4273  O   ALA B 156       8.336   7.673 -68.987  1.00153.64           O  
ANISOU 4273  O   ALA B 156    24446  17432  16498  -1109   1430    540       O  
ATOM   4274  CB  ALA B 156       5.227   7.750 -68.844  1.00146.56           C  
ANISOU 4274  CB  ALA B 156    23651  16761  15276   -979    896    671       C  
ATOM   4275  N   LEU B 157       7.617   8.665 -70.904  1.00154.12           N  
ANISOU 4275  N   LEU B 157    24958  17412  16189  -1080   1500    684       N  
ATOM   4276  CA  LEU B 157       8.727   8.287 -71.777  1.00155.96           C  
ANISOU 4276  CA  LEU B 157    25305  17538  16414  -1140   1767    642       C  
ATOM   4277  C   LEU B 157      10.074   8.841 -71.303  1.00161.06           C  
ANISOU 4277  C   LEU B 157    25794  18082  17318  -1194   1994    600       C  
ATOM   4278  O   LEU B 157      11.123   8.290 -71.651  1.00161.81           O  
ANISOU 4278  O   LEU B 157    25872  18114  17496  -1244   2205    539       O  
ATOM   4279  CB  LEU B 157       8.442   8.785 -73.197  1.00158.00           C  
ANISOU 4279  CB  LEU B 157    25907  17721  16403  -1128   1856    728       C  
ATOM   4280  CG  LEU B 157       8.291   7.703 -74.253  1.00163.95           C  
ANISOU 4280  CG  LEU B 157    26868  18485  16939  -1149   1879    701       C  
ATOM   4281  CD1 LEU B 157       6.957   6.959 -74.113  1.00163.33           C  
ANISOU 4281  CD1 LEU B 157    26786  18564  16708  -1116   1571    702       C  
ATOM   4282  CD2 LEU B 157       8.445   8.287 -75.648  1.00168.95           C  
ANISOU 4282  CD2 LEU B 157    27847  19000  17346  -1151   2053    774       C  
ATOM   4283  N   ASP B 158      10.044   9.913 -70.503  1.00157.34           N  
ANISOU 4283  N   ASP B 158    25207  17597  16980  -1187   1954    630       N  
ATOM   4284  CA  ASP B 158      11.240  10.570 -69.989  1.00157.69           C  
ANISOU 4284  CA  ASP B 158    25094  17550  17269  -1254   2143    589       C  
ATOM   4285  C   ASP B 158      11.370  10.399 -68.470  1.00159.38           C  
ANISOU 4285  C   ASP B 158    24990  17848  17718  -1259   1994    522       C  
ATOM   4286  O   ASP B 158      12.485  10.488 -67.951  1.00159.85           O  
ANISOU 4286  O   ASP B 158    24862  17871  18005  -1323   2123    455       O  
ATOM   4287  CB  ASP B 158      11.222  12.055 -70.370  1.00160.86           C  
ANISOU 4287  CB  ASP B 158    25660  17836  17624  -1262   2256    674       C  
ATOM   4288  CG  ASP B 158      10.801  12.261 -71.809  1.00175.00           C  
ANISOU 4288  CG  ASP B 158    27797  19561  19136  -1229   2342    761       C  
ATOM   4289  OD1 ASP B 158      11.672  12.159 -72.703  1.00177.79           O  
ANISOU 4289  OD1 ASP B 158    28278  19807  19468  -1282   2598    745       O  
ATOM   4290  OD2 ASP B 158       9.582  12.418 -72.052  1.00181.04           O1-
ANISOU 4290  OD2 ASP B 158    28702  20389  19696  -1146   2145    842       O1-
ATOM   4291  N   PHE B 159      10.251  10.146 -67.762  1.00152.73           N  
ANISOU 4291  N   PHE B 159    24086  17120  16824  -1193   1727    538       N  
ATOM   4292  CA  PHE B 159      10.295   9.958 -66.318  1.00150.28           C  
ANISOU 4292  CA  PHE B 159    23506  16884  16710  -1191   1581    478       C  
ATOM   4293  C   PHE B 159      10.625   8.510 -65.941  1.00150.50           C  
ANISOU 4293  C   PHE B 159    23378  16991  16812  -1188   1534    390       C  
ATOM   4294  O   PHE B 159      11.458   8.301 -65.066  1.00150.03           O  
ANISOU 4294  O   PHE B 159    23096  16943  16966  -1216   1556    320       O  
ATOM   4295  CB  PHE B 159       8.973  10.393 -65.641  1.00151.28           C  
ANISOU 4295  CB  PHE B 159    23632  17083  16765  -1119   1339    536       C  
ATOM   4296  CG  PHE B 159       8.824   9.913 -64.213  1.00151.74           C  
ANISOU 4296  CG  PHE B 159    23448  17229  16978  -1103   1166    473       C  
ATOM   4297  CD1 PHE B 159       9.459  10.578 -63.172  1.00154.84           C  
ANISOU 4297  CD1 PHE B 159    23674  17587  17570  -1143   1184    434       C  
ATOM   4298  CD2 PHE B 159       8.098   8.761 -63.919  1.00153.05           C  
ANISOU 4298  CD2 PHE B 159    23560  17506  17086  -1057    995    447       C  
ATOM   4299  CE1 PHE B 159       9.351  10.116 -61.862  1.00154.33           C  
ANISOU 4299  CE1 PHE B 159    23408  17599  17632  -1126   1026    376       C  
ATOM   4300  CE2 PHE B 159       8.016   8.285 -62.609  1.00154.37           C  
ANISOU 4300  CE2 PHE B 159    23522  17741  17390  -1040    856    389       C  
ATOM   4301  CZ  PHE B 159       8.622   8.977 -61.587  1.00152.15           C  
ANISOU 4301  CZ  PHE B 159    23091  17426  17293  -1069    867    358       C  
ATOM   4302  N   ARG B 160       9.938   7.522 -66.541  1.00143.99           N  
ANISOU 4302  N   ARG B 160    22672  16226  15813  -1152   1458    395       N  
ATOM   4303  CA  ARG B 160      10.080   6.107 -66.179  1.00141.53           C  
ANISOU 4303  CA  ARG B 160    22245  15984  15547  -1140   1405    318       C  
ATOM   4304  C   ARG B 160      11.409   5.458 -66.677  1.00144.90           C  
ANISOU 4304  C   ARG B 160    22642  16344  16071  -1179   1645    257       C  
ATOM   4305  O   ARG B 160      11.437   4.281 -67.049  1.00144.24           O  
ANISOU 4305  O   ARG B 160    22602  16280  15923  -1167   1669    218       O  
ATOM   4306  CB  ARG B 160       8.858   5.310 -66.659  1.00139.26           C  
ANISOU 4306  CB  ARG B 160    22104  15773  15035  -1105   1246    339       C  
ATOM   4307  CG  ARG B 160       7.554   5.779 -66.035  1.00142.30           C  
ANISOU 4307  CG  ARG B 160    22467  16241  15361  -1057   1004    392       C  
ATOM   4308  CD  ARG B 160       6.446   4.784 -66.259  1.00148.13           C  
ANISOU 4308  CD  ARG B 160    23273  17074  15934  -1037    835    387       C  
ATOM   4309  NE  ARG B 160       6.690   3.517 -65.559  1.00157.58           N  
ANISOU 4309  NE  ARG B 160    24328  18316  17230  -1040    801    297       N  
ATOM   4310  CZ  ARG B 160       6.466   2.312 -66.076  1.00178.49           C  
ANISOU 4310  CZ  ARG B 160    27063  20990  19763  -1059    796    253       C  
ATOM   4311  NH1 ARG B 160       5.984   2.187 -67.305  1.00172.01           N1+
ANISOU 4311  NH1 ARG B 160    26472  20165  18719  -1085    809    284       N1+
ATOM   4312  NH2 ARG B 160       6.726   1.220 -65.368  1.00167.00           N  
ANISOU 4312  NH2 ARG B 160    25481  19561  18409  -1053    780    177       N  
ATOM   4313  N   THR B 161      12.511   6.219 -66.601  1.00141.82           N  
ANISOU 4313  N   THR B 161    22159  15875  15850  -1227   1823    247       N  
ATOM   4314  CA  THR B 161      13.876   5.823 -66.950  1.00142.88           C  
ANISOU 4314  CA  THR B 161    22215  15944  16128  -1265   2068    194       C  
ATOM   4315  C   THR B 161      14.452   4.945 -65.818  1.00144.82           C  
ANISOU 4315  C   THR B 161    22176  16264  16584  -1237   1996    117       C  
ATOM   4316  O   THR B 161      14.281   5.309 -64.651  1.00143.38           O  
ANISOU 4316  O   THR B 161    21818  16141  16519  -1229   1829    104       O  
ATOM   4317  CB  THR B 161      14.714   7.103 -67.173  1.00157.60           C  
ANISOU 4317  CB  THR B 161    24068  17706  18108  -1336   2259    214       C  
ATOM   4318  OG1 THR B 161      14.109   7.883 -68.205  1.00161.18           O  
ANISOU 4318  OG1 THR B 161    24809  18087  18347  -1344   2317    295       O  
ATOM   4319  CG2 THR B 161      16.188   6.819 -67.511  1.00158.26           C  
ANISOU 4319  CG2 THR B 161    24037  17721  18373  -1383   2531    162       C  
ATOM   4320  N   PRO B 162      15.164   3.824 -66.116  1.00141.46           N  
ANISOU 4320  N   PRO B 162    21709  15830  16210  -1217   2126     69       N  
ATOM   4321  CA  PRO B 162      15.737   2.998 -65.029  1.00140.34           C  
ANISOU 4321  CA  PRO B 162    21300  15758  16267  -1172   2058      6       C  
ATOM   4322  C   PRO B 162      16.738   3.769 -64.165  1.00143.53           C  
ANISOU 4322  C   PRO B 162    21436  16166  16935  -1211   2084    -21       C  
ATOM   4323  O   PRO B 162      16.894   3.449 -62.988  1.00142.43           O  
ANISOU 4323  O   PRO B 162    21078  16104  16935  -1175   1933    -59       O  
ATOM   4324  CB  PRO B 162      16.413   1.842 -65.770  1.00143.42           C  
ANISOU 4324  CB  PRO B 162    21736  16104  16653  -1143   2256    -24       C  
ATOM   4325  CG  PRO B 162      16.633   2.352 -67.147  1.00149.96           C  
ANISOU 4325  CG  PRO B 162    22794  16822  17360  -1198   2486     12       C  
ATOM   4326  CD  PRO B 162      15.470   3.244 -67.436  1.00144.79           C  
ANISOU 4326  CD  PRO B 162    22338  16172  16504  -1224   2345     74       C  
ATOM   4327  N   ALA B 163      17.382   4.802 -64.740  1.00140.69           N  
ANISOU 4327  N   ALA B 163    21104  15721  16633  -1291   2270     -3       N  
ATOM   4328  CA  ALA B 163      18.308   5.680 -64.028  1.00140.71           C  
ANISOU 4328  CA  ALA B 163    20871  15717  16874  -1358   2307    -33       C  
ATOM   4329  C   ALA B 163      17.529   6.581 -63.064  1.00141.86           C  
ANISOU 4329  C   ALA B 163    20991  15904  17005  -1376   2076    -18       C  
ATOM   4330  O   ALA B 163      17.987   6.817 -61.942  1.00141.80           O  
ANISOU 4330  O   ALA B 163    20749  15948  17180  -1396   1971    -63       O  
ATOM   4331  CB  ALA B 163      19.105   6.514 -65.016  1.00143.47           C  
ANISOU 4331  CB  ALA B 163    21298  15947  17267  -1448   2591    -17       C  
ATOM   4332  N   LYS B 164      16.331   7.047 -63.489  1.00135.72           N  
ANISOU 4332  N   LYS B 164    20458  15107  16005  -1362   1992     45       N  
ATOM   4333  CA  LYS B 164      15.451   7.885 -62.671  1.00133.43           C  
ANISOU 4333  CA  LYS B 164    20178  14844  15676  -1361   1790     72       C  
ATOM   4334  C   LYS B 164      14.818   7.054 -61.537  1.00132.80           C  
ANISOU 4334  C   LYS B 164    19976  14878  15604  -1284   1537     44       C  
ATOM   4335  O   LYS B 164      14.783   7.519 -60.398  1.00130.55           O  
ANISOU 4335  O   LYS B 164    19552  14627  15423  -1295   1397     21       O  
ATOM   4336  CB  LYS B 164      14.376   8.577 -63.517  1.00135.78           C  
ANISOU 4336  CB  LYS B 164    20762  15091  15739  -1349   1785    159       C  
ATOM   4337  CG  LYS B 164      14.898   9.770 -64.328  1.00151.58           C  
ANISOU 4337  CG  LYS B 164    22888  16965  17740  -1429   2006    196       C  
ATOM   4338  CD  LYS B 164      13.754  10.685 -64.783  1.00161.65           C  
ANISOU 4338  CD  LYS B 164    24413  18199  18808  -1400   1945    290       C  
ATOM   4339  CE  LYS B 164      14.210  11.998 -65.390  1.00169.36           C  
ANISOU 4339  CE  LYS B 164    25520  19039  19791  -1473   2151    331       C  
ATOM   4340  NZ  LYS B 164      13.082  12.968 -65.521  1.00172.76           N1+
ANISOU 4340  NZ  LYS B 164    26153  19438  20050  -1426   2058    425       N1+
ATOM   4341  N   ALA B 165      14.377   5.810 -61.840  1.00127.81           N  
ANISOU 4341  N   ALA B 165    19404  14293  14863  -1214   1494     39       N  
ATOM   4342  CA  ALA B 165      13.799   4.870 -60.866  1.00125.38           C  
ANISOU 4342  CA  ALA B 165    19003  14081  14554  -1140   1286     11       C  
ATOM   4343  C   ALA B 165      14.812   4.528 -59.768  1.00127.68           C  
ANISOU 4343  C   ALA B 165    19022  14415  15076  -1131   1254    -55       C  
ATOM   4344  O   ALA B 165      14.416   4.397 -58.610  1.00126.36           O  
ANISOU 4344  O   ALA B 165    18755  14310  14947  -1094   1062    -74       O  
ATOM   4345  CB  ALA B 165      13.333   3.601 -61.558  1.00125.79           C  
ANISOU 4345  CB  ALA B 165    19184  14152  14457  -1087   1299     10       C  
ATOM   4346  N   LYS B 166      16.120   4.429 -60.125  1.00124.08           N  
ANISOU 4346  N   LYS B 166    18446  13925  14774  -1164   1444    -88       N  
ATOM   4347  CA  LYS B 166      17.211   4.168 -59.180  1.00123.65           C  
ANISOU 4347  CA  LYS B 166    18110  13918  14953  -1157   1423   -147       C  
ATOM   4348  C   LYS B 166      17.322   5.325 -58.185  1.00125.09           C  
ANISOU 4348  C   LYS B 166    18171  14112  15243  -1225   1304   -163       C  
ATOM   4349  O   LYS B 166      17.381   5.076 -56.977  1.00123.67           O  
ANISOU 4349  O   LYS B 166    17835  14004  15151  -1190   1127   -199       O  
ATOM   4350  CB  LYS B 166      18.547   3.940 -59.907  1.00128.51           C  
ANISOU 4350  CB  LYS B 166    18623  14492  15715  -1184   1672   -169       C  
ATOM   4351  CG  LYS B 166      18.853   2.466 -60.155  1.00154.77           C  
ANISOU 4351  CG  LYS B 166    21924  17841  19042  -1085   1736   -185       C  
ATOM   4352  CD  LYS B 166      19.696   2.245 -61.424  1.00171.74           C  
ANISOU 4352  CD  LYS B 166    24126  19907  21219  -1106   2037   -179       C  
ATOM   4353  CE  LYS B 166      19.768   0.790 -61.845  1.00182.04           C  
ANISOU 4353  CE  LYS B 166    25488  21209  22468  -1006   2118   -187       C  
ATOM   4354  NZ  LYS B 166      20.295   0.635 -63.229  1.00190.43           N1+
ANISOU 4354  NZ  LYS B 166    26693  22171  23490  -1030   2415   -173       N1+
ATOM   4355  N   LEU B 167      17.276   6.588 -58.687  1.00120.23           N  
ANISOU 4355  N   LEU B 167    17659  13419  14603  -1319   1399   -135       N  
ATOM   4356  CA  LEU B 167      17.349   7.795 -57.855  1.00119.02           C  
ANISOU 4356  CA  LEU B 167    17434  13252  14535  -1400   1315   -151       C  
ATOM   4357  C   LEU B 167      16.236   7.793 -56.785  1.00117.33           C  
ANISOU 4357  C   LEU B 167    17257  13092  14231  -1341   1060   -141       C  
ATOM   4358  O   LEU B 167      16.562   7.830 -55.600  1.00116.18           O  
ANISOU 4358  O   LEU B 167    16942  12997  14204  -1348    921   -190       O  
ATOM   4359  CB  LEU B 167      17.293   9.080 -58.719  1.00120.15           C  
ANISOU 4359  CB  LEU B 167    17746  13283  14623  -1495   1480   -109       C  
ATOM   4360  CG  LEU B 167      17.067  10.421 -57.980  1.00124.81           C  
ANISOU 4360  CG  LEU B 167    18347  13832  15245  -1574   1403   -111       C  
ATOM   4361  CD1 LEU B 167      18.349  10.946 -57.366  1.00126.45           C  
ANISOU 4361  CD1 LEU B 167    18318  14036  15690  -1690   1452   -187       C  
ATOM   4362  CD2 LEU B 167      16.490  11.465 -58.904  1.00127.66           C  
ANISOU 4362  CD2 LEU B 167    18963  14082  15462  -1609   1528    -38       C  
ATOM   4363  N   ILE B 168      14.948   7.696 -57.210  1.00110.33           N  
ANISOU 4363  N   ILE B 168    16586  12198  13137  -1282   1001    -79       N  
ATOM   4364  CA  ILE B 168      13.737   7.673 -56.368  1.00107.36           C  
ANISOU 4364  CA  ILE B 168    16269  11863  12658  -1219    788    -57       C  
ATOM   4365  C   ILE B 168      13.877   6.630 -55.252  1.00111.19           C  
ANISOU 4365  C   ILE B 168    16591  12435  13219  -1152    633   -110       C  
ATOM   4366  O   ILE B 168      13.667   6.972 -54.088  1.00109.50           O  
ANISOU 4366  O   ILE B 168    16312  12245  13050  -1150    482   -131       O  
ATOM   4367  CB  ILE B 168      12.450   7.423 -57.212  1.00108.66           C  
ANISOU 4367  CB  ILE B 168    16659  12026  12601  -1160    769     15       C  
ATOM   4368  CG1 ILE B 168      12.282   8.473 -58.321  1.00109.18           C  
ANISOU 4368  CG1 ILE B 168    16906  12004  12572  -1209    913     78       C  
ATOM   4369  CG2 ILE B 168      11.185   7.332 -56.332  1.00107.10           C  
ANISOU 4369  CG2 ILE B 168    16499  11878  12317  -1093    560     37       C  
ATOM   4370  CD1 ILE B 168      11.588   7.960 -59.567  1.00112.30           C  
ANISOU 4370  CD1 ILE B 168    17497  12397  12772  -1168    965    133       C  
ATOM   4371  N   ASN B 169      14.266   5.385 -55.600  1.00109.21           N  
ANISOU 4371  N   ASN B 169    16292  12224  12981  -1096    681   -130       N  
ATOM   4372  CA  ASN B 169      14.427   4.310 -54.621  1.00109.06           C  
ANISOU 4372  CA  ASN B 169    16138  12277  13024  -1016    552   -172       C  
ATOM   4373  C   ASN B 169      15.595   4.571 -53.646  1.00115.14           C  
ANISOU 4373  C   ASN B 169    16670  13077  13999  -1046    509   -230       C  
ATOM   4374  O   ASN B 169      15.463   4.233 -52.472  1.00114.17           O  
ANISOU 4374  O   ASN B 169    16466  13007  13907   -996    337   -257       O  
ATOM   4375  CB  ASN B 169      14.560   2.954 -55.303  1.00107.70           C  
ANISOU 4375  CB  ASN B 169    15994  12120  12807   -946    638   -175       C  
ATOM   4376  CG  ASN B 169      13.259   2.510 -55.923  1.00119.14           C  
ANISOU 4376  CG  ASN B 169    17659  13564  14046   -913    609   -133       C  
ATOM   4377  OD1 ASN B 169      13.153   2.328 -57.130  1.00115.56           O  
ANISOU 4377  OD1 ASN B 169    17343  13074  13493   -931    743   -108       O  
ATOM   4378  ND2 ASN B 169      12.215   2.378 -55.124  1.00106.61           N  
ANISOU 4378  ND2 ASN B 169    16113  12013  12382   -872    433   -123       N  
ATOM   4379  N   ILE B 170      16.691   5.218 -54.104  1.00113.76           N  
ANISOU 4379  N   ILE B 170    16393  12871  13961  -1135    656   -251       N  
ATOM   4380  CA  ILE B 170      17.831   5.580 -53.250  1.00114.93           C  
ANISOU 4380  CA  ILE B 170    16300  13055  14313  -1188    612   -310       C  
ATOM   4381  C   ILE B 170      17.373   6.648 -52.252  1.00118.02           C  
ANISOU 4381  C   ILE B 170    16715  13435  14693  -1250    458   -323       C  
ATOM   4382  O   ILE B 170      17.709   6.558 -51.078  1.00117.80           O  
ANISOU 4382  O   ILE B 170    16546  13464  14750  -1240    298   -369       O  
ATOM   4383  CB  ILE B 170      19.052   6.028 -54.096  1.00120.37           C  
ANISOU 4383  CB  ILE B 170    16877  13705  15151  -1281    833   -328       C  
ATOM   4384  CG1 ILE B 170      19.793   4.788 -54.652  1.00121.95           C  
ANISOU 4384  CG1 ILE B 170    16976  13938  15422  -1197    955   -332       C  
ATOM   4385  CG2 ILE B 170      20.009   6.941 -53.296  1.00122.38           C  
ANISOU 4385  CG2 ILE B 170    16924  13978  15598  -1395    786   -387       C  
ATOM   4386  CD1 ILE B 170      20.618   5.017 -55.913  1.00132.90           C  
ANISOU 4386  CD1 ILE B 170    18356  15258  16882  -1263   1233   -325       C  
ATOM   4387  N   CYS B 171      16.558   7.607 -52.711  1.00114.32           N  
ANISOU 4387  N   CYS B 171    16440  12890  14105  -1302    502   -279       N  
ATOM   4388  CA  CYS B 171      15.988   8.680 -51.895  1.00114.05           C  
ANISOU 4388  CA  CYS B 171    16476  12822  14038  -1354    388   -281       C  
ATOM   4389  C   CYS B 171      15.046   8.133 -50.840  1.00116.03           C  
ANISOU 4389  C   CYS B 171    16767  13120  14198  -1256    180   -276       C  
ATOM   4390  O   CYS B 171      15.000   8.695 -49.754  1.00114.58           O  
ANISOU 4390  O   CYS B 171    16554  12935  14046  -1288     53   -308       O  
ATOM   4391  CB  CYS B 171      15.280   9.696 -52.776  1.00114.69           C  
ANISOU 4391  CB  CYS B 171    16771  12805  14000  -1401    506   -218       C  
ATOM   4392  SG  CYS B 171      16.357  10.452 -54.007  1.00120.95           S  
ANISOU 4392  SG  CYS B 171    17553  13517  14888  -1525    775   -220       S  
ATOM   4393  N   ILE B 172      14.283   7.055 -51.166  1.00111.74           N  
ANISOU 4393  N   ILE B 172    16306  12612  13539  -1144    155   -239       N  
ATOM   4394  CA  ILE B 172      13.355   6.369 -50.249  1.00109.41           C  
ANISOU 4394  CA  ILE B 172    16054  12359  13157  -1046    -17   -234       C  
ATOM   4395  C   ILE B 172      14.163   5.749 -49.094  1.00113.58           C  
ANISOU 4395  C   ILE B 172    16400  12952  13804  -1012   -141   -296       C  
ATOM   4396  O   ILE B 172      13.820   5.974 -47.934  1.00113.26           O  
ANISOU 4396  O   ILE B 172    16364  12919  13751   -998   -292   -315       O  
ATOM   4397  CB  ILE B 172      12.471   5.313 -50.989  1.00110.68           C  
ANISOU 4397  CB  ILE B 172    16335  12539  13180   -957      8   -189       C  
ATOM   4398  CG1 ILE B 172      11.432   6.007 -51.892  1.00109.67           C  
ANISOU 4398  CG1 ILE B 172    16399  12362  12910   -978     69   -120       C  
ATOM   4399  CG2 ILE B 172      11.774   4.353 -49.994  1.00109.99           C  
ANISOU 4399  CG2 ILE B 172    16253  12499  13039   -859   -149   -199       C  
ATOM   4400  CD1 ILE B 172      11.015   5.227 -53.068  1.00110.62           C  
ANISOU 4400  CD1 ILE B 172    16621  12491  12919   -943    155    -86       C  
ATOM   4401  N   TRP B 173      15.247   5.016 -49.416  1.00110.59           N  
ANISOU 4401  N   TRP B 173    15866  12615  13538   -995    -72   -325       N  
ATOM   4402  CA  TRP B 173      16.114   4.363 -48.444  1.00111.34           C  
ANISOU 4402  CA  TRP B 173    15771  12781  13751   -945   -184   -375       C  
ATOM   4403  C   TRP B 173      16.977   5.381 -47.690  1.00116.04           C  
ANISOU 4403  C   TRP B 173    16223  13385  14481  -1052   -252   -429       C  
ATOM   4404  O   TRP B 173      17.292   5.160 -46.526  1.00115.95           O  
ANISOU 4404  O   TRP B 173    16112  13427  14517  -1020   -419   -467       O  
ATOM   4405  CB  TRP B 173      16.960   3.283 -49.121  1.00111.60           C  
ANISOU 4405  CB  TRP B 173    15688  12850  13864   -881    -68   -377       C  
ATOM   4406  CG  TRP B 173      16.134   2.084 -49.510  1.00112.07           C  
ANISOU 4406  CG  TRP B 173    15886  12908  13788   -768    -47   -341       C  
ATOM   4407  CD1 TRP B 173      15.267   1.989 -50.560  1.00114.39           C  
ANISOU 4407  CD1 TRP B 173    16366  13155  13942   -775     59   -298       C  
ATOM   4408  CD2 TRP B 173      16.031   0.850 -48.792  1.00111.64           C  
ANISOU 4408  CD2 TRP B 173    15808  12898  13714   -639   -146   -348       C  
ATOM   4409  NE1 TRP B 173      14.638   0.768 -50.548  1.00113.11           N  
ANISOU 4409  NE1 TRP B 173    16290  13006  13681   -673     33   -286       N  
ATOM   4410  CE2 TRP B 173      15.095   0.043 -49.483  1.00114.79           C  
ANISOU 4410  CE2 TRP B 173    16383  13267  13965   -587    -80   -314       C  
ATOM   4411  CE3 TRP B 173      16.658   0.332 -47.651  1.00113.61           C  
ANISOU 4411  CE3 TRP B 173    15910  13205  14050   -562   -283   -378       C  
ATOM   4412  CZ2 TRP B 173      14.782  -1.253 -49.073  1.00113.91           C  
ANISOU 4412  CZ2 TRP B 173    16309  13171  13799   -469   -127   -313       C  
ATOM   4413  CZ3 TRP B 173      16.333  -0.944 -47.235  1.00114.93           C  
ANISOU 4413  CZ3 TRP B 173    16124  13389  14155   -428   -333   -368       C  
ATOM   4414  CH2 TRP B 173      15.413  -1.727 -47.947  1.00114.67           C  
ANISOU 4414  CH2 TRP B 173    16272  13315  13983   -386   -246   -338       C  
ATOM   4415  N   VAL B 174      17.285   6.526 -48.304  1.00113.32           N  
ANISOU 4415  N   VAL B 174    15889  12983  14184  -1184   -132   -433       N  
ATOM   4416  CA  VAL B 174      18.039   7.572 -47.613  1.00114.19           C  
ANISOU 4416  CA  VAL B 174    15883  13091  14415  -1311   -189   -492       C  
ATOM   4417  C   VAL B 174      17.085   8.312 -46.661  1.00117.28           C  
ANISOU 4417  C   VAL B 174    16431  13438  14694  -1331   -330   -492       C  
ATOM   4418  O   VAL B 174      17.393   8.440 -45.484  1.00116.80           O  
ANISOU 4418  O   VAL B 174    16292  13412  14674  -1348   -495   -544       O  
ATOM   4419  CB  VAL B 174      18.770   8.524 -48.596  1.00119.24           C  
ANISOU 4419  CB  VAL B 174    16482  13672  15154  -1454     12   -501       C  
ATOM   4420  CG1 VAL B 174      19.200   9.817 -47.913  1.00120.07           C  
ANISOU 4420  CG1 VAL B 174    16542  13740  15337  -1611    -39   -559       C  
ATOM   4421  CG2 VAL B 174      19.977   7.834 -49.222  1.00120.61           C  
ANISOU 4421  CG2 VAL B 174    16442  13899  15486  -1445    133   -519       C  
ATOM   4422  N   LEU B 175      15.920   8.744 -47.164  1.00113.87           N  
ANISOU 4422  N   LEU B 175    16220  12930  14115  -1318   -268   -432       N  
ATOM   4423  CA  LEU B 175      14.905   9.483 -46.419  1.00113.74           C  
ANISOU 4423  CA  LEU B 175    16370  12855  13988  -1323   -361   -417       C  
ATOM   4424  C   LEU B 175      14.415   8.743 -45.176  1.00117.24           C  
ANISOU 4424  C   LEU B 175    16822  13347  14375  -1221   -555   -432       C  
ATOM   4425  O   LEU B 175      14.431   9.333 -44.099  1.00117.05           O  
ANISOU 4425  O   LEU B 175    16814  13304  14354  -1265   -672   -472       O  
ATOM   4426  CB  LEU B 175      13.713   9.804 -47.323  1.00113.34           C  
ANISOU 4426  CB  LEU B 175    16530  12738  13795  -1288   -256   -333       C  
ATOM   4427  CG  LEU B 175      12.626  10.671 -46.719  1.00118.62           C  
ANISOU 4427  CG  LEU B 175    17376  13335  14359  -1285   -314   -303       C  
ATOM   4428  CD1 LEU B 175      12.872  12.142 -47.019  1.00120.38           C  
ANISOU 4428  CD1 LEU B 175    17669  13457  14611  -1413   -203   -304       C  
ATOM   4429  CD2 LEU B 175      11.256  10.216 -47.192  1.00120.71           C  
ANISOU 4429  CD2 LEU B 175    17790  13598  14474  -1171   -307   -220       C  
ATOM   4430  N   ALA B 176      13.994   7.471 -45.307  1.00113.78           N  
ANISOU 4430  N   ALA B 176    16390  12963  13880  -1090   -581   -402       N  
ATOM   4431  CA  ALA B 176      13.484   6.682 -44.179  1.00113.46           C  
ANISOU 4431  CA  ALA B 176    16377  12957  13775   -985   -743   -410       C  
ATOM   4432  C   ALA B 176      14.522   6.490 -43.035  1.00119.52           C  
ANISOU 4432  C   ALA B 176    16985  13783  14643   -992   -893   -480       C  
ATOM   4433  O   ALA B 176      14.136   5.998 -41.970  1.00118.98           O  
ANISOU 4433  O   ALA B 176    16963  13731  14513   -913  -1035   -490       O  
ATOM   4434  CB  ALA B 176      12.976   5.335 -44.652  1.00113.28           C  
ANISOU 4434  CB  ALA B 176    16384  12971  13685   -861   -715   -371       C  
ATOM   4435  N   SER B 177      15.801   6.936 -43.215  1.00117.42           N  
ANISOU 4435  N   SER B 177    16539  13548  14527  -1092   -865   -529       N  
ATOM   4436  CA  SER B 177      16.812   6.871 -42.153  1.00118.21           C  
ANISOU 4436  CA  SER B 177    16471  13716  14727  -1113  -1025   -598       C  
ATOM   4437  C   SER B 177      16.555   8.015 -41.126  1.00122.14           C  
ANISOU 4437  C   SER B 177    17067  14158  15181  -1214  -1138   -641       C  
ATOM   4438  O   SER B 177      17.254   8.127 -40.114  1.00122.81           O  
ANISOU 4438  O   SER B 177    17052  14290  15319  -1251  -1297   -704       O  
ATOM   4439  CB  SER B 177      18.228   6.901 -42.720  1.00122.87           C  
ANISOU 4439  CB  SER B 177    16815  14367  15504  -1185   -954   -635       C  
ATOM   4440  OG  SER B 177      18.615   8.194 -43.150  1.00131.94           O  
ANISOU 4440  OG  SER B 177    17949  15459  16723  -1360   -856   -664       O  
ATOM   4441  N   GLY B 178      15.503   8.803 -41.391  1.00117.10           N  
ANISOU 4441  N   GLY B 178    16637  13419  14437  -1248  -1057   -602       N  
ATOM   4442  CA  GLY B 178      14.986   9.852 -40.521  1.00116.89           C  
ANISOU 4442  CA  GLY B 178    16763  13311  14339  -1320  -1125   -626       C  
ATOM   4443  C   GLY B 178      14.007   9.260 -39.524  1.00119.97           C  
ANISOU 4443  C   GLY B 178    17296  13692  14594  -1194  -1249   -605       C  
ATOM   4444  O   GLY B 178      13.475   9.967 -38.669  1.00120.29           O  
ANISOU 4444  O   GLY B 178    17484  13661  14558  -1226  -1310   -621       O  
ATOM   4445  N   VAL B 179      13.747   7.949 -39.661  1.00115.31           N  
ANISOU 4445  N   VAL B 179    16676  13164  13974  -1050  -1267   -568       N  
ATOM   4446  CA  VAL B 179      12.918   7.103 -38.803  1.00114.26           C  
ANISOU 4446  CA  VAL B 179    16656  13032  13727   -916  -1367   -547       C  
ATOM   4447  C   VAL B 179      13.848   6.031 -38.209  1.00120.33           C  
ANISOU 4447  C   VAL B 179    17269  13898  14552   -838  -1497   -582       C  
ATOM   4448  O   VAL B 179      13.738   5.695 -37.030  1.00120.40           O  
ANISOU 4448  O   VAL B 179    17336  13912  14498   -777  -1644   -603       O  
ATOM   4449  CB  VAL B 179      11.697   6.468 -39.534  1.00116.19           C  
ANISOU 4449  CB  VAL B 179    17018  13252  13878   -817  -1259   -469       C  
ATOM   4450  CG1 VAL B 179      10.711   5.869 -38.532  1.00115.00           C  
ANISOU 4450  CG1 VAL B 179    17010  13075  13609   -708  -1345   -452       C  
ATOM   4451  CG2 VAL B 179      10.991   7.474 -40.435  1.00115.46           C  
ANISOU 4451  CG2 VAL B 179    17028  13087  13754   -886  -1119   -423       C  
ATOM   4452  N   GLY B 180      14.758   5.527 -39.046  1.00117.96           N  
ANISOU 4452  N   GLY B 180    16783  13668  14367   -835  -1432   -583       N  
ATOM   4453  CA  GLY B 180      15.758   4.523 -38.696  1.00118.75           C  
ANISOU 4453  CA  GLY B 180    16705  13868  14548   -751  -1526   -605       C  
ATOM   4454  C   GLY B 180      16.725   4.988 -37.625  1.00123.07           C  
ANISOU 4454  C   GLY B 180    17135  14464  15160   -814  -1708   -676       C  
ATOM   4455  O   GLY B 180      16.817   4.349 -36.576  1.00122.66           O  
ANISOU 4455  O   GLY B 180    17095  14450  15059   -717  -1870   -687       O  
ATOM   4456  N   VAL B 181      17.430   6.121 -37.867  1.00120.06           N  
ANISOU 4456  N   VAL B 181    16654  14080  14882   -984  -1684   -725       N  
ATOM   4457  CA  VAL B 181      18.383   6.697 -36.904  1.00121.26           C  
ANISOU 4457  CA  VAL B 181    16686  14283  15104  -1081  -1861   -805       C  
ATOM   4458  C   VAL B 181      17.649   7.056 -35.574  1.00124.41           C  
ANISOU 4458  C   VAL B 181    17302  14622  15347  -1076  -2017   -828       C  
ATOM   4459  O   VAL B 181      18.054   6.504 -34.549  1.00124.27           O  
ANISOU 4459  O   VAL B 181    17245  14669  15305  -1003  -2208   -854       O  
ATOM   4460  CB  VAL B 181      19.204   7.896 -37.453  1.00125.79           C  
ANISOU 4460  CB  VAL B 181    17129  14849  15817  -1288  -1782   -859       C  
ATOM   4461  CG1 VAL B 181      20.135   8.456 -36.379  1.00127.68           C  
ANISOU 4461  CG1 VAL B 181    17249  15145  16117  -1402  -1987   -951       C  
ATOM   4462  CG2 VAL B 181      19.995   7.509 -38.699  1.00125.91           C  
ANISOU 4462  CG2 VAL B 181    16930  14919  15989  -1289  -1621   -838       C  
ATOM   4463  N   PRO B 182      16.558   7.882 -35.558  1.00119.90           N  
ANISOU 4463  N   PRO B 182    16968  13927  14662  -1130  -1936   -811       N  
ATOM   4464  CA  PRO B 182      15.888   8.198 -34.279  1.00120.06           C  
ANISOU 4464  CA  PRO B 182    17201  13881  14537  -1118  -2065   -832       C  
ATOM   4465  C   PRO B 182      15.462   6.986 -33.437  1.00126.16           C  
ANISOU 4465  C   PRO B 182    18052  14681  15202   -934  -2183   -803       C  
ATOM   4466  O   PRO B 182      15.617   7.046 -32.217  1.00127.40           O  
ANISOU 4466  O   PRO B 182    18280  14839  15286   -929  -2359   -847       O  
ATOM   4467  CB  PRO B 182      14.657   8.994 -34.712  1.00119.90           C  
ANISOU 4467  CB  PRO B 182    17402  13728  14429  -1153  -1902   -788       C  
ATOM   4468  CG  PRO B 182      15.042   9.599 -35.975  1.00123.96           C  
ANISOU 4468  CG  PRO B 182    17808  14236  15055  -1258  -1738   -779       C  
ATOM   4469  CD  PRO B 182      15.921   8.618 -36.671  1.00119.86           C  
ANISOU 4469  CD  PRO B 182    17051  13833  14655  -1200  -1723   -770       C  
ATOM   4470  N   ILE B 183      14.925   5.908 -34.067  1.00122.54           N  
ANISOU 4470  N   ILE B 183    17599  14237  14723   -790  -2084   -732       N  
ATOM   4471  CA  ILE B 183      14.482   4.690 -33.368  1.00122.42           C  
ANISOU 4471  CA  ILE B 183    17670  14235  14608   -614  -2163   -699       C  
ATOM   4472  C   ILE B 183      15.718   3.962 -32.824  1.00130.05           C  
ANISOU 4472  C   ILE B 183    18450  15319  15645   -549  -2332   -731       C  
ATOM   4473  O   ILE B 183      15.714   3.543 -31.669  1.00130.15           O  
ANISOU 4473  O   ILE B 183    18549  15338  15565   -466  -2492   -743       O  
ATOM   4474  CB  ILE B 183      13.584   3.781 -34.274  1.00123.48           C  
ANISOU 4474  CB  ILE B 183    17862  14347  14709   -503  -1997   -623       C  
ATOM   4475  CG1 ILE B 183      12.201   4.429 -34.561  1.00122.15           C  
ANISOU 4475  CG1 ILE B 183    17895  14068  14447   -539  -1869   -585       C  
ATOM   4476  CG2 ILE B 183      13.435   2.344 -33.748  1.00123.70           C  
ANISOU 4476  CG2 ILE B 183    17927  14403  14673   -324  -2056   -594       C  
ATOM   4477  CD1 ILE B 183      11.250   4.796 -33.335  1.00127.97           C  
ANISOU 4477  CD1 ILE B 183    18870  14711  15044   -518  -1935   -589       C  
ATOM   4478  N   MET B 184      16.787   3.883 -33.632  1.00129.32           N  
ANISOU 4478  N   MET B 184    18104  15317  15715   -588  -2296   -742       N  
ATOM   4479  CA  MET B 184      18.052   3.250 -33.273  1.00131.94           C  
ANISOU 4479  CA  MET B 184    18209  15774  16148   -527  -2441   -765       C  
ATOM   4480  C   MET B 184      18.721   3.997 -32.135  1.00138.43           C  
ANISOU 4480  C   MET B 184    18997  16635  16967   -624  -2664   -842       C  
ATOM   4481  O   MET B 184      19.475   3.406 -31.362  1.00139.59           O  
ANISOU 4481  O   MET B 184    19038  16874  17125   -538  -2852   -856       O  
ATOM   4482  CB  MET B 184      18.968   3.226 -34.490  1.00135.44           C  
ANISOU 4482  CB  MET B 184    18393  16288  16780   -576  -2314   -763       C  
ATOM   4483  CG  MET B 184      20.027   2.175 -34.421  1.00141.25           C  
ANISOU 4483  CG  MET B 184    18901  17144  17622   -445  -2393   -750       C  
ATOM   4484  SD  MET B 184      21.537   2.801 -35.172  1.00148.37           S  
ANISOU 4484  SD  MET B 184    19448  18151  18777   -589  -2357   -799       S  
ATOM   4485  CE  MET B 184      22.188   3.855 -33.808  1.00147.22           C  
ANISOU 4485  CE  MET B 184    19247  18057  18633   -740  -2638   -896       C  
ATOM   4486  N   VAL B 185      18.437   5.301 -32.043  1.00135.73           N  
ANISOU 4486  N   VAL B 185    18754  16216  16601   -803  -2642   -889       N  
ATOM   4487  CA  VAL B 185      18.952   6.201 -31.017  1.00137.47           C  
ANISOU 4487  CA  VAL B 185    18986  16446  16800   -937  -2832   -974       C  
ATOM   4488  C   VAL B 185      18.278   5.886 -29.665  1.00141.73           C  
ANISOU 4488  C   VAL B 185    19777  16934  17140   -837  -2986   -974       C  
ATOM   4489  O   VAL B 185      18.987   5.712 -28.671  1.00143.91           O  
ANISOU 4489  O   VAL B 185    20001  17286  17392   -819  -3215  -1018       O  
ATOM   4490  CB  VAL B 185      18.764   7.685 -31.453  1.00140.86           C  
ANISOU 4490  CB  VAL B 185    19479  16783  17260  -1157  -2714  -1020       C  
ATOM   4491  CG1 VAL B 185      18.709   8.640 -30.263  1.00141.64           C  
ANISOU 4491  CG1 VAL B 185    19742  16823  17254  -1282  -2869  -1098       C  
ATOM   4492  CG2 VAL B 185      19.843   8.111 -32.444  1.00141.97           C  
ANISOU 4492  CG2 VAL B 185    19336  16995  17609  -1290  -2630  -1051       C  
ATOM   4493  N   MET B 186      16.930   5.793 -29.635  1.00135.55           N  
ANISOU 4493  N   MET B 186    19260  16025  16217   -768  -2862   -922       N  
ATOM   4494  CA  MET B 186      16.196   5.585 -28.388  1.00135.16           C  
ANISOU 4494  CA  MET B 186    19476  15903  15977   -685  -2969   -920       C  
ATOM   4495  C   MET B 186      15.826   4.119 -28.093  1.00139.63           C  
ANISOU 4495  C   MET B 186    20100  16488  16465   -458  -2988   -853       C  
ATOM   4496  O   MET B 186      15.199   3.866 -27.062  1.00139.43           O  
ANISOU 4496  O   MET B 186    20306  16393  16277   -378  -3060   -846       O  
ATOM   4497  CB  MET B 186      14.948   6.476 -28.317  1.00135.91           C  
ANISOU 4497  CB  MET B 186    19840  15838  15963   -755  -2831   -912       C  
ATOM   4498  CG  MET B 186      13.983   6.322 -29.450  1.00137.28           C  
ANISOU 4498  CG  MET B 186    20048  15953  16159   -714  -2591   -836       C  
ATOM   4499  SD  MET B 186      12.858   7.731 -29.455  1.00140.61           S  
ANISOU 4499  SD  MET B 186    20713  16209  16503   -836  -2446   -837       S  
ATOM   4500  CE  MET B 186      12.345   7.713 -31.151  1.00135.67           C  
ANISOU 4500  CE  MET B 186    19991  15582  15976   -834  -2203   -763       C  
ATOM   4501  N   ALA B 187      16.258   3.159 -28.922  1.00136.82           N  
ANISOU 4501  N   ALA B 187    19552  16217  16218   -356  -2923   -807       N  
ATOM   4502  CA  ALA B 187      15.979   1.747 -28.637  1.00136.83           C  
ANISOU 4502  CA  ALA B 187    19615  16227  16146   -144  -2933   -746       C  
ATOM   4503  C   ALA B 187      16.843   1.286 -27.464  1.00144.71           C  
ANISOU 4503  C   ALA B 187    20577  17307  17100    -54  -3188   -770       C  
ATOM   4504  O   ALA B 187      18.062   1.392 -27.549  1.00146.48           O  
ANISOU 4504  O   ALA B 187    20549  17655  17451    -92  -3310   -804       O  
ATOM   4505  CB  ALA B 187      16.246   0.897 -29.865  1.00136.97           C  
ANISOU 4505  CB  ALA B 187    19450  16303  16290    -68  -2784   -695       C  
ATOM   4506  N   VAL B 188      16.228   0.864 -26.341  1.00142.46           N  
ANISOU 4506  N   VAL B 188    20545  16952  16633     53  -3273   -757       N  
ATOM   4507  CA  VAL B 188      16.992   0.444 -25.154  1.00144.94           C  
ANISOU 4507  CA  VAL B 188    20862  17336  16873    148  -3531   -775       C  
ATOM   4508  C   VAL B 188      16.413  -0.808 -24.489  1.00149.11           C  
ANISOU 4508  C   VAL B 188    21596  17807  17250    369  -3533   -710       C  
ATOM   4509  O   VAL B 188      15.204  -1.050 -24.548  1.00146.42           O  
ANISOU 4509  O   VAL B 188    21480  17340  16813    407  -3364   -674       O  
ATOM   4510  CB  VAL B 188      17.157   1.560 -24.078  1.00150.36           C  
ANISOU 4510  CB  VAL B 188    21671  17998  17461      6  -3719   -857       C  
ATOM   4511  CG1 VAL B 188      18.055   2.700 -24.557  1.00151.40           C  
ANISOU 4511  CG1 VAL B 188    21566  18210  17750   -210  -3769   -932       C  
ATOM   4512  CG2 VAL B 188      15.813   2.075 -23.571  1.00148.67           C  
ANISOU 4512  CG2 VAL B 188    21803  17608  17076    -33  -3611   -857       C  
ATOM   4513  N   THR B 189      17.298  -1.566 -23.807  1.00148.56           N  
ANISOU 4513  N   THR B 189    21451  17834  17160    513  -3733   -697       N  
ATOM   4514  CA  THR B 189      16.951  -2.737 -23.003  1.00148.64           C  
ANISOU 4514  CA  THR B 189    21666  17796  17016    732  -3773   -638       C  
ATOM   4515  C   THR B 189      16.974  -2.336 -21.546  1.00153.99           C  
ANISOU 4515  C   THR B 189    22558  18441  17508    730  -3997   -678       C  
ATOM   4516  O   THR B 189      18.009  -1.873 -21.046  1.00155.59           O  
ANISOU 4516  O   THR B 189    22620  18760  17739    676  -4239   -729       O  
ATOM   4517  CB  THR B 189      17.865  -3.941 -23.257  1.00158.32           C  
ANISOU 4517  CB  THR B 189    22690  19134  18330    926  -3824   -581       C  
ATOM   4518  OG1 THR B 189      19.230  -3.531 -23.247  1.00163.41           O  
ANISOU 4518  OG1 THR B 189    23032  19945  19110    874  -4027   -621       O  
ATOM   4519  CG2 THR B 189      17.542  -4.653 -24.526  1.00153.89           C  
ANISOU 4519  CG2 THR B 189    22036  18553  17884    977  -3566   -528       C  
ATOM   4520  N   ARG B 190      15.843  -2.496 -20.858  1.00149.88           N  
ANISOU 4520  N   ARG B 190    22382  17766  16799    780  -3918   -659       N  
ATOM   4521  CA  ARG B 190      15.820  -2.153 -19.450  1.00151.84           C  
ANISOU 4521  CA  ARG B 190    22875  17967  16850    785  -4115   -695       C  
ATOM   4522  C   ARG B 190      14.990  -3.139 -18.654  1.00157.22           C  
ANISOU 4522  C   ARG B 190    23880  18521  17335    976  -4056   -634       C  
ATOM   4523  O   ARG B 190      14.085  -3.761 -19.210  1.00154.30           O  
ANISOU 4523  O   ARG B 190    23591  18059  16976   1039  -3814   -581       O  
ATOM   4524  CB  ARG B 190      15.385  -0.706 -19.204  1.00151.32           C  
ANISOU 4524  CB  ARG B 190    22930  17823  16741    562  -4108   -774       C  
ATOM   4525  CG  ARG B 190      13.923  -0.335 -19.381  1.00157.04           C  
ANISOU 4525  CG  ARG B 190    23900  18369  17399    507  -3850   -759       C  
ATOM   4526  CD  ARG B 190      13.756   1.160 -19.125  1.00166.15           C  
ANISOU 4526  CD  ARG B 190    25140  19464  18527    290  -3871   -839       C  
ATOM   4527  NE  ARG B 190      14.681   1.955 -19.942  1.00177.34           N  
ANISOU 4527  NE  ARG B 190    26243  21003  20133    124  -3925   -892       N  
ATOM   4528  CZ  ARG B 190      15.807   2.510 -19.498  1.00196.56           C  
ANISOU 4528  CZ  ARG B 190    28548  23546  22591     24  -4169   -965       C  
ATOM   4529  NH1 ARG B 190      16.147   2.402 -18.216  1.00187.96           N1+
ANISOU 4529  NH1 ARG B 190    27625  22461  21329     74  -4403   -995       N1+
ATOM   4530  NH2 ARG B 190      16.595   3.182 -20.324  1.00184.72           N  
ANISOU 4530  NH2 ARG B 190    26756  22149  21281   -130  -4181  -1010       N  
ATOM   4531  N   PRO B 191      15.318  -3.339 -17.359  1.00158.01           N  
ANISOU 4531  N   PRO B 191    24168  18616  17254   1070  -4278   -641       N  
ATOM   4532  CA  PRO B 191      14.559  -4.312 -16.580  1.00158.64           C  
ANISOU 4532  CA  PRO B 191    24573  18564  17140   1259  -4209   -579       C  
ATOM   4533  C   PRO B 191      13.214  -3.737 -16.162  1.00163.81           C  
ANISOU 4533  C   PRO B 191    25555  19025  17661   1171  -4033   -598       C  
ATOM   4534  O   PRO B 191      13.147  -2.733 -15.452  1.00164.37           O  
ANISOU 4534  O   PRO B 191    25772  19050  17630   1046  -4135   -662       O  
ATOM   4535  CB  PRO B 191      15.480  -4.637 -15.398  1.00163.32           C  
ANISOU 4535  CB  PRO B 191    25236  19231  17588   1386  -4524   -579       C  
ATOM   4536  CG  PRO B 191      16.475  -3.558 -15.339  1.00169.11           C  
ANISOU 4536  CG  PRO B 191    25750  20105  18399   1213  -4761   -663       C  
ATOM   4537  CD  PRO B 191      16.371  -2.698 -16.545  1.00162.54           C  
ANISOU 4537  CD  PRO B 191    24678  19301  17780   1006  -4598   -706       C  
ATOM   4538  N   ARG B 192      12.138  -4.344 -16.690  1.00160.09           N  
ANISOU 4538  N   ARG B 192    25179  18440  17206   1225  -3754   -544       N  
ATOM   4539  CA  ARG B 192      10.751  -3.971 -16.423  1.00159.16           C  
ANISOU 4539  CA  ARG B 192    25342  18138  16992   1165  -3541   -545       C  
ATOM   4540  C   ARG B 192       9.939  -5.231 -16.139  1.00165.02           C  
ANISOU 4540  C   ARG B 192    26307  18759  17633   1344  -3373   -473       C  
ATOM   4541  O   ARG B 192       9.882  -6.134 -16.983  1.00164.14           O  
ANISOU 4541  O   ARG B 192    26056  18681  17630   1421  -3243   -425       O  
ATOM   4542  CB  ARG B 192      10.149  -3.170 -17.594  1.00156.24           C  
ANISOU 4542  CB  ARG B 192    24811  17763  16792    992  -3341   -563       C  
ATOM   4543  CG  ARG B 192      10.626  -1.720 -17.670  1.00165.69           C  
ANISOU 4543  CG  ARG B 192    25899  19011  18045    791  -3455   -641       C  
ATOM   4544  CD  ARG B 192       9.762  -0.779 -16.848  1.00175.91           C  
ANISOU 4544  CD  ARG B 192    27494  20148  19195    700  -3400   -677       C  
ATOM   4545  NE  ARG B 192       8.509  -0.454 -17.531  1.00183.34           N  
ANISOU 4545  NE  ARG B 192    28478  20983  20200    638  -3118   -650       N  
ATOM   4546  CZ  ARG B 192       8.309   0.651 -18.244  1.00198.56           C  
ANISOU 4546  CZ  ARG B 192    30292  22913  22240    474  -3034   -680       C  
ATOM   4547  NH1 ARG B 192       9.268   1.558 -18.366  1.00186.51           N  
ANISOU 4547  NH1 ARG B 192    28611  21477  20776    340  -3195   -744       N  
ATOM   4548  NH2 ARG B 192       7.138   0.859 -18.836  1.00185.47           N1+
ANISOU 4548  NH2 ARG B 192    28673  21164  20633    444  -2788   -644       N1+
ATOM   4549  N   ASP B 193       9.360  -5.302 -14.916  1.00163.46           N  
ANISOU 4549  N   ASP B 193    26471  18418  17220   1408  -3376   -470       N  
ATOM   4550  CA  ASP B 193       8.529  -6.391 -14.358  1.00163.33           C  
ANISOU 4550  CA  ASP B 193    26742  18250  17065   1569  -3216   -409       C  
ATOM   4551  C   ASP B 193       9.394  -7.653 -14.048  1.00167.43           C  
ANISOU 4551  C   ASP B 193    27252  18835  17529   1785  -3353   -354       C  
ATOM   4552  O   ASP B 193       8.969  -8.779 -14.321  1.00166.79           O  
ANISOU 4552  O   ASP B 193    27227  18693  17454   1910  -3182   -295       O  
ATOM   4553  CB  ASP B 193       7.329  -6.742 -15.287  1.00163.20           C  
ANISOU 4553  CB  ASP B 193    26698  18149  17163   1530  -2890   -377       C  
ATOM   4554  CG  ASP B 193       6.455  -5.566 -15.687  1.00176.11           C  
ANISOU 4554  CG  ASP B 193    28317  19729  18868   1342  -2746   -415       C  
ATOM   4555  OD1 ASP B 193       5.678  -5.093 -14.834  1.00178.33           O1-
ANISOU 4555  OD1 ASP B 193    28877  19865  19016   1317  -2676   -428       O1-
ATOM   4556  OD2 ASP B 193       6.517  -5.149 -16.875  1.00179.87           O1-
ANISOU 4556  OD2 ASP B 193    28512  20298  19532   1230  -2688   -426       O1-
ATOM   4557  N   GLY B 194      10.602  -7.443 -13.504  1.00164.01           N  
ANISOU 4557  N   GLY B 194    26742  18528  17048   1825  -3659   -375       N  
ATOM   4558  CA  GLY B 194      11.563  -8.503 -13.183  1.00164.46           C  
ANISOU 4558  CA  GLY B 194    26759  18671  17059   2038  -3830   -320       C  
ATOM   4559  C   GLY B 194      12.306  -9.115 -14.369  1.00165.04           C  
ANISOU 4559  C   GLY B 194    26461  18894  17352   2089  -3813   -286       C  
ATOM   4560  O   GLY B 194      13.357  -9.735 -14.190  1.00166.41           O  
ANISOU 4560  O   GLY B 194    26516  19183  17529   2243  -4002   -249       O  
ATOM   4561  N   ALA B 195      11.757  -8.968 -15.588  1.00156.76           N  
ANISOU 4561  N   ALA B 195    25235  17843  16486   1968  -3582   -294       N  
ATOM   4562  CA  ALA B 195      12.293  -9.472 -16.858  1.00154.34           C  
ANISOU 4562  CA  ALA B 195    24597  17654  16393   1986  -3510   -269       C  
ATOM   4563  C   ALA B 195      13.104  -8.370 -17.581  1.00154.76           C  
ANISOU 4563  C   ALA B 195    24303  17871  16628   1808  -3637   -330       C  
ATOM   4564  O   ALA B 195      13.322  -7.309 -16.998  1.00154.80           O  
ANISOU 4564  O   ALA B 195    24336  17901  16582   1686  -3802   -391       O  
ATOM   4565  CB  ALA B 195      11.123  -9.932 -17.711  1.00152.55           C  
ANISOU 4565  CB  ALA B 195    24423  17312  16228   1947  -3182   -247       C  
ATOM   4566  N   VAL B 196      13.543  -8.613 -18.839  1.00147.94           N  
ANISOU 4566  N   VAL B 196    23132  17108  15972   1786  -3548   -318       N  
ATOM   4567  CA  VAL B 196      14.273  -7.644 -19.686  1.00146.07           C  
ANISOU 4567  CA  VAL B 196    22559  17014  15928   1615  -3617   -370       C  
ATOM   4568  C   VAL B 196      13.357  -7.233 -20.861  1.00144.02           C  
ANISOU 4568  C   VAL B 196    22241  16697  15783   1457  -3351   -384       C  
ATOM   4569  O   VAL B 196      12.734  -8.100 -21.484  1.00141.88           O  
ANISOU 4569  O   VAL B 196    22013  16360  15535   1524  -3139   -339       O  
ATOM   4570  CB  VAL B 196      15.650  -8.177 -20.178  1.00151.15           C  
ANISOU 4570  CB  VAL B 196    22878  17830  16723   1718  -3743   -344       C  
ATOM   4571  CG1 VAL B 196      16.437  -7.106 -20.928  1.00151.11           C  
ANISOU 4571  CG1 VAL B 196    22539  17965  16909   1530  -3820   -405       C  
ATOM   4572  CG2 VAL B 196      16.473  -8.731 -19.020  1.00153.62           C  
ANISOU 4572  CG2 VAL B 196    23258  18200  16912   1909  -4003   -314       C  
ATOM   4573  N   VAL B 197      13.247  -5.913 -21.132  1.00137.87           N  
ANISOU 4573  N   VAL B 197    21383  15936  15065   1248  -3365   -447       N  
ATOM   4574  CA  VAL B 197      12.405  -5.394 -22.221  1.00134.42           C  
ANISOU 4574  CA  VAL B 197    20891  15453  14729   1100  -3136   -457       C  
ATOM   4575  C   VAL B 197      13.245  -4.600 -23.224  1.00133.97           C  
ANISOU 4575  C   VAL B 197    20510  15527  14867    956  -3169   -494       C  
ATOM   4576  O   VAL B 197      14.226  -3.960 -22.850  1.00134.91           O  
ANISOU 4576  O   VAL B 197    20496  15743  15020    899  -3374   -539       O  
ATOM   4577  CB  VAL B 197      11.167  -4.561 -21.753  1.00138.04           C  
ANISOU 4577  CB  VAL B 197    21603  15769  15078    989  -3039   -481       C  
ATOM   4578  CG1 VAL B 197      10.219  -5.392 -20.889  1.00137.92           C  
ANISOU 4578  CG1 VAL B 197    21906  15608  14887   1122  -2952   -441       C  
ATOM   4579  CG2 VAL B 197      11.566  -3.262 -21.046  1.00139.26           C  
ANISOU 4579  CG2 VAL B 197    21785  15939  15189    855  -3217   -549       C  
ATOM   4580  N   CYS B 198      12.845  -4.667 -24.497  1.00126.28           N  
ANISOU 4580  N   CYS B 198    19415  14552  14015    896  -2964   -477       N  
ATOM   4581  CA  CYS B 198      13.445  -3.943 -25.614  1.00124.89           C  
ANISOU 4581  CA  CYS B 198    18962  14471  14018    756  -2933   -505       C  
ATOM   4582  C   CYS B 198      12.399  -2.944 -26.089  1.00124.71           C  
ANISOU 4582  C   CYS B 198    19027  14363  13994    593  -2782   -524       C  
ATOM   4583  O   CYS B 198      11.406  -3.317 -26.720  1.00122.81           O  
ANISOU 4583  O   CYS B 198    18864  14051  13746    601  -2587   -488       O  
ATOM   4584  CB  CYS B 198      13.892  -4.899 -26.718  1.00124.67           C  
ANISOU 4584  CB  CYS B 198    18741  14508  14118    839  -2817   -463       C  
ATOM   4585  SG  CYS B 198      14.525  -4.076 -28.202  1.00127.87           S  
ANISOU 4585  SG  CYS B 198    18837  15009  14738    670  -2729   -491       S  
ATOM   4586  N   MET B 199      12.592  -1.685 -25.710  1.00119.62           N  
ANISOU 4586  N   MET B 199    18384  13719  13347    449  -2880   -579       N  
ATOM   4587  CA  MET B 199      11.632  -0.608 -25.918  1.00117.16           C  
ANISOU 4587  CA  MET B 199    18189  13314  13014    307  -2760   -596       C  
ATOM   4588  C   MET B 199      12.272   0.674 -26.431  1.00120.57           C  
ANISOU 4588  C   MET B 199    18452  13800  13561    125  -2796   -649       C  
ATOM   4589  O   MET B 199      13.471   0.707 -26.692  1.00121.04           O  
ANISOU 4589  O   MET B 199    18282  13977  13732     97  -2905   -676       O  
ATOM   4590  CB  MET B 199      10.948  -0.329 -24.573  1.00119.66           C  
ANISOU 4590  CB  MET B 199    18801  13516  13150    328  -2822   -610       C  
ATOM   4591  CG  MET B 199      11.900  -0.487 -23.399  1.00125.08           C  
ANISOU 4591  CG  MET B 199    19518  14253  13755    387  -3072   -644       C  
ATOM   4592  SD  MET B 199      11.499   0.510 -21.969  1.00129.71           S  
ANISOU 4592  SD  MET B 199    20401  14724  14158    314  -3183   -698       S  
ATOM   4593  CE  MET B 199      12.216   2.076 -22.461  1.00127.18           C  
ANISOU 4593  CE  MET B 199    19898  14462  13962     76  -3244   -776       C  
ATOM   4594  N   LEU B 200      11.455   1.736 -26.559  1.00116.65           N  
ANISOU 4594  N   LEU B 200    18073  13210  13039      2  -2693   -661       N  
ATOM   4595  CA  LEU B 200      11.876   3.055 -27.024  1.00117.36           C  
ANISOU 4595  CA  LEU B 200    18057  13315  13219   -180  -2691   -709       C  
ATOM   4596  C   LEU B 200      11.840   4.059 -25.867  1.00124.89           C  
ANISOU 4596  C   LEU B 200    19193  14195  14063   -270  -2808   -769       C  
ATOM   4597  O   LEU B 200      10.786   4.290 -25.265  1.00123.56           O  
ANISOU 4597  O   LEU B 200    19277  13901  13770   -249  -2740   -754       O  
ATOM   4598  CB  LEU B 200      11.001   3.542 -28.207  1.00115.33           C  
ANISOU 4598  CB  LEU B 200    17793  13006  13023   -247  -2465   -670       C  
ATOM   4599  CG  LEU B 200      11.044   2.712 -29.498  1.00118.41           C  
ANISOU 4599  CG  LEU B 200    18011  13463  13517   -192  -2338   -620       C  
ATOM   4600  CD1 LEU B 200       9.817   2.961 -30.344  1.00116.37           C  
ANISOU 4600  CD1 LEU B 200    17834  13132  13251   -214  -2137   -569       C  
ATOM   4601  CD2 LEU B 200      12.303   2.978 -30.288  1.00121.59           C  
ANISOU 4601  CD2 LEU B 200    18147  13975  14075   -274  -2370   -650       C  
ATOM   4602  N   GLN B 201      13.004   4.626 -25.541  1.00125.80           N  
ANISOU 4602  N   GLN B 201    19182  14388  14229   -372  -2983   -839       N  
ATOM   4603  CA  GLN B 201      13.118   5.616 -24.484  1.00128.25           C  
ANISOU 4603  CA  GLN B 201    19657  14636  14437   -483  -3110   -911       C  
ATOM   4604  C   GLN B 201      12.917   7.003 -25.087  1.00134.54           C  
ANISOU 4604  C   GLN B 201    20455  15365  15299   -672  -2985   -943       C  
ATOM   4605  O   GLN B 201      13.876   7.656 -25.519  1.00135.50           O  
ANISOU 4605  O   GLN B 201    20383  15559  15542   -815  -3038   -997       O  
ATOM   4606  CB  GLN B 201      14.458   5.496 -23.728  1.00132.11           C  
ANISOU 4606  CB  GLN B 201    20019  15245  14931   -503  -3385   -976       C  
ATOM   4607  CG  GLN B 201      14.527   6.297 -22.418  1.00146.42           C  
ANISOU 4607  CG  GLN B 201    22054  16989  16589   -595  -3549  -1053       C  
ATOM   4608  CD  GLN B 201      13.665   5.734 -21.308  1.00163.81           C  
ANISOU 4608  CD  GLN B 201    24576  19083  18581   -451  -3570  -1021       C  
ATOM   4609  OE1 GLN B 201      12.429   5.790 -21.341  1.00157.44           O  
ANISOU 4609  OE1 GLN B 201    23981  18138  17701   -408  -3376   -975       O  
ATOM   4610  NE2 GLN B 201      14.301   5.234 -20.270  1.00157.14           N  
ANISOU 4610  NE2 GLN B 201    23778  18296  17631   -378  -3806  -1047       N  
ATOM   4611  N   PHE B 202      11.649   7.439 -25.127  1.00131.18           N  
ANISOU 4611  N   PHE B 202    20248  14797  14797   -666  -2808   -904       N  
ATOM   4612  CA  PHE B 202      11.280   8.749 -25.643  1.00131.59           C  
ANISOU 4612  CA  PHE B 202    20350  14760  14889   -816  -2667   -919       C  
ATOM   4613  C   PHE B 202      11.760   9.865 -24.687  1.00140.47           C  
ANISOU 4613  C   PHE B 202    21606  15824  15942   -971  -2793  -1014       C  
ATOM   4614  O   PHE B 202      11.793   9.649 -23.465  1.00140.77           O  
ANISOU 4614  O   PHE B 202    21813  15832  15839   -931  -2940  -1049       O  
ATOM   4615  CB  PHE B 202       9.765   8.832 -25.877  1.00131.18           C  
ANISOU 4615  CB  PHE B 202    20490  14579  14774   -742  -2453   -842       C  
ATOM   4616  CG  PHE B 202       9.292   7.999 -27.042  1.00130.36           C  
ANISOU 4616  CG  PHE B 202    20244  14531  14755   -642  -2313   -759       C  
ATOM   4617  CD1 PHE B 202       9.499   8.421 -28.349  1.00132.31           C  
ANISOU 4617  CD1 PHE B 202    20315  14820  15135   -719  -2200   -740       C  
ATOM   4618  CD2 PHE B 202       8.639   6.792 -26.834  1.00131.37           C  
ANISOU 4618  CD2 PHE B 202    20429  14662  14823   -479  -2288   -704       C  
ATOM   4619  CE1 PHE B 202       9.070   7.644 -29.427  1.00131.57           C  
ANISOU 4619  CE1 PHE B 202    20110  14779  15104   -634  -2078   -669       C  
ATOM   4620  CE2 PHE B 202       8.205   6.017 -27.915  1.00132.73           C  
ANISOU 4620  CE2 PHE B 202    20480  14884  15066   -405  -2162   -637       C  
ATOM   4621  CZ  PHE B 202       8.423   6.450 -29.204  1.00130.09           C  
ANISOU 4621  CZ  PHE B 202    19977  14597  14855   -483  -2064   -621       C  
ATOM   4622  N   PRO B 203      12.162  11.048 -25.223  1.00140.27           N  
ANISOU 4622  N   PRO B 203    21516  15776  16006  -1154  -2736  -1061       N  
ATOM   4623  CA  PRO B 203      12.632  12.136 -24.344  1.00143.20           C  
ANISOU 4623  CA  PRO B 203    22021  16081  16309  -1324  -2848  -1162       C  
ATOM   4624  C   PRO B 203      11.524  12.672 -23.444  1.00149.67           C  
ANISOU 4624  C   PRO B 203    23202  16714  16951  -1302  -2770  -1156       C  
ATOM   4625  O   PRO B 203      10.351  12.447 -23.734  1.00148.14           O  
ANISOU 4625  O   PRO B 203    23123  16438  16725  -1182  -2587  -1069       O  
ATOM   4626  CB  PRO B 203      13.106  13.215 -25.329  1.00145.18           C  
ANISOU 4626  CB  PRO B 203    22134  16325  16705  -1508  -2737  -1194       C  
ATOM   4627  CG  PRO B 203      13.237  12.526 -26.641  1.00147.85           C  
ANISOU 4627  CG  PRO B 203    22212  16769  17194  -1433  -2632  -1122       C  
ATOM   4628  CD  PRO B 203      12.196  11.466 -26.638  1.00141.19           C  
ANISOU 4628  CD  PRO B 203    21459  15911  16275  -1219  -2561  -1026       C  
ATOM   4629  N   SER B 204      11.887  13.363 -22.355  1.00149.44           N  
ANISOU 4629  N   SER B 204    23352  16621  16808  -1418  -2904  -1249       N  
ATOM   4630  CA  SER B 204      10.897  13.923 -21.439  1.00150.14           C  
ANISOU 4630  CA  SER B 204    23806  16519  16721  -1404  -2822  -1251       C  
ATOM   4631  C   SER B 204      10.090  15.031 -22.164  1.00154.19           C  
ANISOU 4631  C   SER B 204    24418  16887  17281  -1472  -2556  -1214       C  
ATOM   4632  O   SER B 204      10.712  15.911 -22.775  1.00155.18           O  
ANISOU 4632  O   SER B 204    24432  17020  17511  -1640  -2527  -1261       O  
ATOM   4633  CB  SER B 204      11.578  14.462 -20.184  1.00157.16           C  
ANISOU 4633  CB  SER B 204    24864  17374  17476  -1535  -3032  -1369       C  
ATOM   4634  OG  SER B 204      10.689  14.535 -19.082  1.00168.14           O  
ANISOU 4634  OG  SER B 204    26616  18604  18664  -1463  -2996  -1364       O  
ATOM   4635  N   PRO B 205       8.728  14.980 -22.191  1.00148.87           N  
ANISOU 4635  N   PRO B 205    23929  16087  16547  -1338  -2353  -1123       N  
ATOM   4636  CA  PRO B 205       7.831  14.000 -21.553  1.00147.25           C  
ANISOU 4636  CA  PRO B 205    23867  15849  16231  -1144  -2335  -1060       C  
ATOM   4637  C   PRO B 205       7.545  12.819 -22.476  1.00148.04           C  
ANISOU 4637  C   PRO B 205    23738  16074  16436   -993  -2283   -967       C  
ATOM   4638  O   PRO B 205       6.969  12.976 -23.554  1.00146.05           O  
ANISOU 4638  O   PRO B 205    23385  15820  16287   -968  -2105   -894       O  
ATOM   4639  CB  PRO B 205       6.584  14.832 -21.235  1.00148.78           C  
ANISOU 4639  CB  PRO B 205    24355  15835  16340  -1122  -2115  -1020       C  
ATOM   4640  CG  PRO B 205       6.596  15.995 -22.220  1.00153.61           C  
ANISOU 4640  CG  PRO B 205    24898  16400  17065  -1244  -1963  -1012       C  
ATOM   4641  CD  PRO B 205       7.953  16.021 -22.895  1.00149.92           C  
ANISOU 4641  CD  PRO B 205    24146  16090  16727  -1380  -2107  -1075       C  
ATOM   4642  N   SER B 206       7.990  11.630 -22.041  1.00143.86           N  
ANISOU 4642  N   SER B 206    23135  15654  15873   -894  -2446   -971       N  
ATOM   4643  CA  SER B 206       7.893  10.359 -22.755  1.00141.57           C  
ANISOU 4643  CA  SER B 206    22642  15483  15663   -753  -2428   -899       C  
ATOM   4644  C   SER B 206       6.514  10.148 -23.379  1.00141.17           C  
ANISOU 4644  C   SER B 206    22641  15363  15635   -647  -2191   -798       C  
ATOM   4645  O   SER B 206       6.438   9.971 -24.595  1.00139.86           O  
ANISOU 4645  O   SER B 206    22273  15270  15597   -639  -2097   -748       O  
ATOM   4646  CB  SER B 206       8.241   9.203 -21.822  1.00146.54           C  
ANISOU 4646  CB  SER B 206    23316  16170  16193   -634  -2603   -910       C  
ATOM   4647  OG  SER B 206       9.489   9.424 -21.180  1.00159.33           O  
ANISOU 4647  OG  SER B 206    24891  17863  17784   -728  -2844  -1002       O  
ATOM   4648  N   TRP B 207       5.434  10.271 -22.571  1.00135.41           N  
ANISOU 4648  N   TRP B 207    22181  14485  14782   -577  -2089   -771       N  
ATOM   4649  CA  TRP B 207       4.028  10.085 -22.964  1.00132.41           C  
ANISOU 4649  CA  TRP B 207    21865  14030  14415   -472  -1869   -677       C  
ATOM   4650  C   TRP B 207       3.608  10.967 -24.131  1.00131.28           C  
ANISOU 4650  C   TRP B 207    21619  13873  14388   -532  -1706   -630       C  
ATOM   4651  O   TRP B 207       2.648  10.628 -24.815  1.00128.81           O  
ANISOU 4651  O   TRP B 207    21253  13563  14127   -446  -1559   -547       O  
ATOM   4652  CB  TRP B 207       3.088  10.355 -21.772  1.00131.96           C  
ANISOU 4652  CB  TRP B 207    22130  13797  14210   -417  -1785   -671       C  
ATOM   4653  CG  TRP B 207       3.134  11.771 -21.272  1.00134.39           C  
ANISOU 4653  CG  TRP B 207    22630  13971  14459   -536  -1752   -722       C  
ATOM   4654  CD1 TRP B 207       3.970  12.269 -20.320  1.00139.25           C  
ANISOU 4654  CD1 TRP B 207    23390  14549  14970   -637  -1911   -819       C  
ATOM   4655  CD2 TRP B 207       2.346  12.883 -21.739  1.00134.07           C  
ANISOU 4655  CD2 TRP B 207    22660  13817  14463   -571  -1550   -679       C  
ATOM   4656  NE1 TRP B 207       3.738  13.613 -20.142  1.00139.72           N  
ANISOU 4656  NE1 TRP B 207    23621  14466  15000   -742  -1809   -846       N  
ATOM   4657  CE2 TRP B 207       2.762  14.021 -21.017  1.00139.88           C  
ANISOU 4657  CE2 TRP B 207    23598  14437  15115   -697  -1582   -758       C  
ATOM   4658  CE3 TRP B 207       1.340  13.032 -22.716  1.00133.94           C  
ANISOU 4658  CE3 TRP B 207    22555  13790  14548   -506  -1349   -580       C  
ATOM   4659  CZ2 TRP B 207       2.196  15.291 -21.225  1.00139.56           C  
ANISOU 4659  CZ2 TRP B 207    23686  14254  15087   -752  -1401   -737       C  
ATOM   4660  CZ3 TRP B 207       0.790  14.293 -22.932  1.00135.67           C  
ANISOU 4660  CZ3 TRP B 207    22884  13882  14783   -550  -1185   -553       C  
ATOM   4661  CH2 TRP B 207       1.209  15.401 -22.185  1.00138.03           C  
ANISOU 4661  CH2 TRP B 207    23397  14051  14996   -666  -1202   -629       C  
ATOM   4662  N   TYR B 208       4.263  12.133 -24.288  1.00127.05           N  
ANISOU 4662  N   TYR B 208    21082  13310  13882   -679  -1729   -684       N  
ATOM   4663  CA  TYR B 208       4.016  13.124 -25.338  1.00125.61           C  
ANISOU 4663  CA  TYR B 208    20832  13098  13796   -748  -1581   -647       C  
ATOM   4664  C   TYR B 208       4.607  12.620 -26.644  1.00127.37           C  
ANISOU 4664  C   TYR B 208    20758  13481  14157   -762  -1603   -624       C  
ATOM   4665  O   TYR B 208       3.885  12.360 -27.613  1.00124.89           O  
ANISOU 4665  O   TYR B 208    20350  13196  13907   -691  -1476   -540       O  
ATOM   4666  CB  TYR B 208       4.649  14.472 -24.934  1.00127.90           C  
ANISOU 4666  CB  TYR B 208    21245  13294  14058   -914  -1605   -728       C  
ATOM   4667  CG  TYR B 208       4.444  15.610 -25.906  1.00129.97           C  
ANISOU 4667  CG  TYR B 208    21481  13498  14403   -991  -1443   -693       C  
ATOM   4668  CD1 TYR B 208       5.350  15.844 -26.939  1.00132.00           C  
ANISOU 4668  CD1 TYR B 208    21518  13855  14781  -1095  -1470   -713       C  
ATOM   4669  CD2 TYR B 208       3.408  16.520 -25.734  1.00131.31           C  
ANISOU 4669  CD2 TYR B 208    21866  13500  14526   -961  -1258   -643       C  
ATOM   4670  CE1 TYR B 208       5.188  16.922 -27.814  1.00132.78           C  
ANISOU 4670  CE1 TYR B 208    21620  13886  14944  -1165  -1313   -679       C  
ATOM   4671  CE2 TYR B 208       3.236  17.600 -26.600  1.00132.39           C  
ANISOU 4671  CE2 TYR B 208    22000  13573  14730  -1020  -1106   -605       C  
ATOM   4672  CZ  TYR B 208       4.129  17.799 -27.637  1.00139.77           C  
ANISOU 4672  CZ  TYR B 208    22726  14605  15775  -1123  -1136   -623       C  
ATOM   4673  OH  TYR B 208       3.955  18.879 -28.469  1.00141.81           O  
ANISOU 4673  OH  TYR B 208    23008  14786  16087  -1177   -976   -582       O  
ATOM   4674  N   TRP B 209       5.935  12.443 -26.641  1.00123.95           N  
ANISOU 4674  N   TRP B 209    20178  13153  13767   -852  -1770   -700       N  
ATOM   4675  CA  TRP B 209       6.707  12.000 -27.787  1.00122.59           C  
ANISOU 4675  CA  TRP B 209    19727  13126  13727   -878  -1797   -693       C  
ATOM   4676  C   TRP B 209       6.287  10.611 -28.228  1.00125.52           C  
ANISOU 4676  C   TRP B 209    19986  13590  14117   -730  -1784   -629       C  
ATOM   4677  O   TRP B 209       6.467  10.285 -29.398  1.00125.61           O  
ANISOU 4677  O   TRP B 209    19808  13689  14228   -726  -1731   -592       O  
ATOM   4678  CB  TRP B 209       8.205  12.085 -27.488  1.00122.43           C  
ANISOU 4678  CB  TRP B 209    19577  13193  13747   -998  -1985   -792       C  
ATOM   4679  CG  TRP B 209       8.615  13.492 -27.198  1.00124.68           C  
ANISOU 4679  CG  TRP B 209    19963  13385  14025  -1171  -1980   -862       C  
ATOM   4680  CD1 TRP B 209       8.906  14.020 -25.977  1.00129.19           C  
ANISOU 4680  CD1 TRP B 209    20715  13881  14491  -1249  -2094   -944       C  
ATOM   4681  CD2 TRP B 209       8.580  14.595 -28.111  1.00124.49           C  
ANISOU 4681  CD2 TRP B 209    19919  13303  14079  -1280  -1828   -849       C  
ATOM   4682  NE1 TRP B 209       9.157  15.364 -26.090  1.00129.62           N  
ANISOU 4682  NE1 TRP B 209    20844  13842  14565  -1416  -2029   -993       N  
ATOM   4683  CE2 TRP B 209       8.958  15.746 -27.391  1.00130.13           C  
ANISOU 4683  CE2 TRP B 209    20790  13910  14743  -1434  -1859   -933       C  
ATOM   4684  CE3 TRP B 209       8.303  14.716 -29.486  1.00124.68           C  
ANISOU 4684  CE3 TRP B 209    19817  13352  14204  -1266  -1670   -775       C  
ATOM   4685  CZ2 TRP B 209       9.074  17.001 -27.997  1.00130.23           C  
ANISOU 4685  CZ2 TRP B 209    20835  13835  14811  -1572  -1724   -945       C  
ATOM   4686  CZ3 TRP B 209       8.420  15.958 -30.086  1.00126.65           C  
ANISOU 4686  CZ3 TRP B 209    20100  13519  14502  -1392  -1544   -781       C  
ATOM   4687  CH2 TRP B 209       8.803  17.083 -29.347  1.00129.10           C  
ANISOU 4687  CH2 TRP B 209    20567  13717  14769  -1543  -1565   -864       C  
ATOM   4688  N   ASP B 210       5.663   9.825 -27.325  1.00120.53           N  
ANISOU 4688  N   ASP B 210    19491  12922  13383   -611  -1813   -613       N  
ATOM   4689  CA  ASP B 210       5.112   8.517 -27.656  1.00118.52           C  
ANISOU 4689  CA  ASP B 210    19171  12729  13134   -474  -1776   -553       C  
ATOM   4690  C   ASP B 210       3.902   8.743 -28.564  1.00118.05           C  
ANISOU 4690  C   ASP B 210    19111  12630  13111   -438  -1583   -467       C  
ATOM   4691  O   ASP B 210       3.870   8.227 -29.681  1.00115.83           O  
ANISOU 4691  O   ASP B 210    18663  12438  12910   -417  -1534   -426       O  
ATOM   4692  CB  ASP B 210       4.731   7.742 -26.381  1.00121.05           C  
ANISOU 4692  CB  ASP B 210    19670  12996  13328   -368  -1838   -560       C  
ATOM   4693  CG  ASP B 210       4.460   6.269 -26.618  1.00135.58           C  
ANISOU 4693  CG  ASP B 210    21435  14906  15173   -240  -1829   -517       C  
ATOM   4694  OD1 ASP B 210       3.438   5.947 -27.273  1.00136.41           O1-
ANISOU 4694  OD1 ASP B 210    21525  14999  15307   -187  -1681   -451       O1-
ATOM   4695  OD2 ASP B 210       5.253   5.435 -26.128  1.00142.89           O  
ANISOU 4695  OD2 ASP B 210    22325  15896  16071   -192  -1970   -550       O  
ATOM   4696  N   THR B 211       2.966   9.601 -28.101  1.00113.20           N  
ANISOU 4696  N   THR B 211    18687  11884  12441   -436  -1476   -442       N  
ATOM   4697  CA  THR B 211       1.744  10.022 -28.784  1.00111.48           C  
ANISOU 4697  CA  THR B 211    18492  11615  12252   -395  -1298   -356       C  
ATOM   4698  C   THR B 211       2.083  10.666 -30.148  1.00114.65           C  
ANISOU 4698  C   THR B 211    18735  12073  12754   -471  -1244   -331       C  
ATOM   4699  O   THR B 211       1.473  10.282 -31.150  1.00113.67           O  
ANISOU 4699  O   THR B 211    18505  12007  12678   -421  -1163   -262       O  
ATOM   4700  CB  THR B 211       0.959  10.965 -27.868  1.00115.85           C  
ANISOU 4700  CB  THR B 211    19286  12004  12727   -387  -1209   -347       C  
ATOM   4701  OG1 THR B 211       0.687  10.266 -26.659  1.00120.05           O  
ANISOU 4701  OG1 THR B 211    19968  12485  13160   -313  -1253   -370       O  
ATOM   4702  CG2 THR B 211      -0.356  11.383 -28.454  1.00111.44           C  
ANISOU 4702  CG2 THR B 211    18748  11392  12200   -322  -1028   -251       C  
ATOM   4703  N   VAL B 212       3.072  11.603 -30.188  1.00110.25           N  
ANISOU 4703  N   VAL B 212    18166  11500  12223   -597  -1291   -390       N  
ATOM   4704  CA  VAL B 212       3.545  12.279 -31.414  1.00108.70           C  
ANISOU 4704  CA  VAL B 212    17840  11343  12119   -683  -1234   -375       C  
ATOM   4705  C   VAL B 212       3.885  11.218 -32.479  1.00109.58           C  
ANISOU 4705  C   VAL B 212    17733  11600  12302   -649  -1256   -352       C  
ATOM   4706  O   VAL B 212       3.248  11.187 -33.527  1.00107.47           O  
ANISOU 4706  O   VAL B 212    17407  11359  12066   -612  -1152   -278       O  
ATOM   4707  CB  VAL B 212       4.758  13.223 -31.134  1.00113.38           C  
ANISOU 4707  CB  VAL B 212    18437  11907  12734   -840  -1304   -465       C  
ATOM   4708  CG1 VAL B 212       5.443  13.661 -32.425  1.00113.01           C  
ANISOU 4708  CG1 VAL B 212    18227  11919  12794   -931  -1251   -459       C  
ATOM   4709  CG2 VAL B 212       4.339  14.440 -30.328  1.00114.03           C  
ANISOU 4709  CG2 VAL B 212    18755  11826  12746   -889  -1241   -482       C  
ATOM   4710  N   THR B 213       4.836  10.317 -32.156  1.00105.79           N  
ANISOU 4710  N   THR B 213    17147  11212  11838   -652  -1392   -411       N  
ATOM   4711  CA  THR B 213       5.308   9.219 -32.989  1.00104.83           C  
ANISOU 4711  CA  THR B 213    16835  11218  11778   -615  -1419   -401       C  
ATOM   4712  C   THR B 213       4.130   8.391 -33.498  1.00108.25           C  
ANISOU 4712  C   THR B 213    17276  11669  12187   -503  -1331   -323       C  
ATOM   4713  O   THR B 213       4.070   8.111 -34.700  1.00107.93           O  
ANISOU 4713  O   THR B 213    17119  11694  12196   -502  -1266   -284       O  
ATOM   4714  CB  THR B 213       6.303   8.374 -32.184  1.00111.41           C  
ANISOU 4714  CB  THR B 213    17606  12117  12605   -598  -1582   -469       C  
ATOM   4715  OG1 THR B 213       7.395   9.213 -31.828  1.00110.99           O  
ANISOU 4715  OG1 THR B 213    17520  12062  12588   -722  -1669   -543       O  
ATOM   4716  CG2 THR B 213       6.830   7.160 -32.957  1.00110.21           C  
ANISOU 4716  CG2 THR B 213    17270  12087  12517   -544  -1601   -458       C  
ATOM   4717  N   LYS B 214       3.186   8.037 -32.592  1.00104.02           N  
ANISOU 4717  N   LYS B 214    16882  11069  11570   -418  -1322   -304       N  
ATOM   4718  CA  LYS B 214       1.991   7.248 -32.906  1.00102.21           C  
ANISOU 4718  CA  LYS B 214    16665  10850  11319   -322  -1240   -239       C  
ATOM   4719  C   LYS B 214       1.103   7.989 -33.935  1.00104.13           C  
ANISOU 4719  C   LYS B 214    16894  11080  11592   -331  -1112   -163       C  
ATOM   4720  O   LYS B 214       0.728   7.378 -34.943  1.00103.79           O  
ANISOU 4720  O   LYS B 214    16749  11111  11575   -306  -1070   -120       O  
ATOM   4721  CB  LYS B 214       1.182   6.901 -31.623  1.00104.52           C  
ANISOU 4721  CB  LYS B 214    17129  11057  11526   -242  -1238   -237       C  
ATOM   4722  CG  LYS B 214       1.905   6.104 -30.525  1.00115.23           C  
ANISOU 4722  CG  LYS B 214    18536  12417  12827   -208  -1365   -300       C  
ATOM   4723  CD  LYS B 214       2.348   4.690 -30.949  1.00125.47           C  
ANISOU 4723  CD  LYS B 214    19707  13818  14148   -155  -1411   -305       C  
ATOM   4724  CE  LYS B 214       2.987   3.897 -29.835  1.00132.71           C  
ANISOU 4724  CE  LYS B 214    20690  14733  15003    -96  -1532   -353       C  
ATOM   4725  NZ  LYS B 214       2.001   3.526 -28.784  1.00137.60           N1+
ANISOU 4725  NZ  LYS B 214    21506  15252  15525    -15  -1488   -336       N1+
ATOM   4726  N   ILE B 215       0.824   9.313 -33.710  1.00 98.13           N  
ANISOU 4726  N   ILE B 215    16240  10223  10823   -368  -1054   -147       N  
ATOM   4727  CA  ILE B 215       0.007  10.145 -34.610  1.00 96.30           C  
ANISOU 4727  CA  ILE B 215    16011   9966  10612   -361   -935    -66       C  
ATOM   4728  C   ILE B 215       0.752  10.376 -35.937  1.00100.43           C  
ANISOU 4728  C   ILE B 215    16399  10564  11194   -431   -925    -60       C  
ATOM   4729  O   ILE B 215       0.122  10.660 -36.950  1.00 99.61           O  
ANISOU 4729  O   ILE B 215    16263  10482  11103   -410   -845     14       O  
ATOM   4730  CB  ILE B 215      -0.432  11.490 -33.965  1.00 99.16           C  
ANISOU 4730  CB  ILE B 215    16543  10188  10946   -371   -861    -49       C  
ATOM   4731  CG1 ILE B 215      -1.119  11.280 -32.610  1.00 98.63           C  
ANISOU 4731  CG1 ILE B 215    16629  10031  10813   -304   -856    -59       C  
ATOM   4732  CG2 ILE B 215      -1.383  12.257 -34.900  1.00 99.83           C  
ANISOU 4732  CG2 ILE B 215    16628  10251  11051   -332   -735     52       C  
ATOM   4733  CD1 ILE B 215      -1.118  12.448 -31.755  1.00101.19           C  
ANISOU 4733  CD1 ILE B 215    17137  10214  11097   -337   -814    -79       C  
ATOM   4734  N   CYS B 216       2.076  10.225 -35.934  1.00 98.12           N  
ANISOU 4734  N   CYS B 216    16028  10316  10938   -510  -1005   -134       N  
ATOM   4735  CA  CYS B 216       2.880  10.412 -37.127  1.00 98.47           C  
ANISOU 4735  CA  CYS B 216    15948  10422  11045   -581   -981   -135       C  
ATOM   4736  C   CYS B 216       2.949   9.167 -37.971  1.00101.90           C  
ANISOU 4736  C   CYS B 216    16250  10970  11497   -541   -993   -122       C  
ATOM   4737  O   CYS B 216       2.748   9.271 -39.183  1.00102.37           O  
ANISOU 4737  O   CYS B 216    16260  11067  11571   -549   -921    -72       O  
ATOM   4738  CB  CYS B 216       4.269  10.898 -36.759  1.00100.15           C  
ANISOU 4738  CB  CYS B 216    16120  10626  11304   -693  -1046   -221       C  
ATOM   4739  SG  CYS B 216       4.297  12.608 -36.197  1.00105.34           S  
ANISOU 4739  SG  CYS B 216    16937  11139  11947   -783   -994   -238       S  
ATOM   4740  N   VAL B 217       3.241   7.995 -37.363  1.00 97.19           N  
ANISOU 4740  N   VAL B 217    15613  10422  10891   -496  -1078   -165       N  
ATOM   4741  CA  VAL B 217       3.318   6.736 -38.116  1.00 96.49           C  
ANISOU 4741  CA  VAL B 217    15419  10428  10815   -456  -1078   -157       C  
ATOM   4742  C   VAL B 217       1.909   6.349 -38.629  1.00 99.95           C  
ANISOU 4742  C   VAL B 217    15895  10875  11206   -392  -1010    -85       C  
ATOM   4743  O   VAL B 217       1.810   5.642 -39.627  1.00 99.71           O  
ANISOU 4743  O   VAL B 217    15794  10915  11178   -385   -980    -65       O  
ATOM   4744  CB  VAL B 217       3.990   5.572 -37.357  1.00100.24           C  
ANISOU 4744  CB  VAL B 217    15853  10944  11289   -412  -1174   -214       C  
ATOM   4745  CG1 VAL B 217       5.437   5.900 -36.992  1.00100.72           C  
ANISOU 4745  CG1 VAL B 217    15835  11023  11410   -477  -1256   -282       C  
ATOM   4746  CG2 VAL B 217       3.190   5.192 -36.124  1.00100.24           C  
ANISOU 4746  CG2 VAL B 217    15980  10887  11219   -337  -1209   -214       C  
ATOM   4747  N   PHE B 218       0.829   6.839 -37.964  1.00 95.66           N  
ANISOU 4747  N   PHE B 218    15464  10262  10623   -349   -983    -47       N  
ATOM   4748  CA  PHE B 218      -0.541   6.573 -38.397  1.00 94.64           C  
ANISOU 4748  CA  PHE B 218    15348  10145  10464   -292   -923     23       C  
ATOM   4749  C   PHE B 218      -0.879   7.383 -39.643  1.00 96.98           C  
ANISOU 4749  C   PHE B 218    15615  10462  10770   -316   -857     90       C  
ATOM   4750  O   PHE B 218      -1.478   6.873 -40.593  1.00 95.69           O  
ANISOU 4750  O   PHE B 218    15397  10368  10592   -300   -835    132       O  
ATOM   4751  CB  PHE B 218      -1.559   6.882 -37.288  1.00 96.61           C  
ANISOU 4751  CB  PHE B 218    15715  10310  10682   -232   -898     46       C  
ATOM   4752  CG  PHE B 218      -2.976   6.658 -37.763  1.00 98.19           C  
ANISOU 4752  CG  PHE B 218    15899  10535  10873   -177   -835    121       C  
ATOM   4753  CD1 PHE B 218      -3.416   5.385 -38.124  1.00101.45           C  
ANISOU 4753  CD1 PHE B 218    16246  11022  11276   -157   -844    119       C  
ATOM   4754  CD2 PHE B 218      -3.852   7.723 -37.910  1.00100.49           C  
ANISOU 4754  CD2 PHE B 218    16233  10779  11168   -147   -767    195       C  
ATOM   4755  CE1 PHE B 218      -4.715   5.182 -38.598  1.00102.17           C  
ANISOU 4755  CE1 PHE B 218    16303  11150  11367   -123   -799    182       C  
ATOM   4756  CE2 PHE B 218      -5.154   7.516 -38.376  1.00103.42           C  
ANISOU 4756  CE2 PHE B 218    16562  11191  11542    -93   -722    268       C  
ATOM   4757  CZ  PHE B 218      -5.574   6.251 -38.726  1.00101.21           C  
ANISOU 4757  CZ  PHE B 218    16203  10995  11257    -89   -745    258       C  
ATOM   4758  N   LEU B 219      -0.527   8.661 -39.602  1.00 93.19           N  
ANISOU 4758  N   LEU B 219    15187   9915  10305   -356   -826     99       N  
ATOM   4759  CA  LEU B 219      -0.771   9.594 -40.677  1.00 93.08           C  
ANISOU 4759  CA  LEU B 219    15177   9897  10293   -372   -755    166       C  
ATOM   4760  C   LEU B 219       0.147   9.276 -41.860  1.00100.47           C  
ANISOU 4760  C   LEU B 219    16020  10906  11248   -434   -751    148       C  
ATOM   4761  O   LEU B 219      -0.334   8.784 -42.885  1.00100.22           O  
ANISOU 4761  O   LEU B 219    15944  10945  11190   -414   -734    193       O  
ATOM   4762  CB  LEU B 219      -0.563  11.033 -40.148  1.00 93.00           C  
ANISOU 4762  CB  LEU B 219    15275   9770  10291   -402   -709    170       C  
ATOM   4763  CG  LEU B 219      -0.692  12.206 -41.103  1.00 96.56           C  
ANISOU 4763  CG  LEU B 219    15766  10183  10741   -418   -619    240       C  
ATOM   4764  CD1 LEU B 219      -2.100  12.345 -41.628  1.00 95.94           C  
ANISOU 4764  CD1 LEU B 219    15704  10122  10629   -318   -574    349       C  
ATOM   4765  CD2 LEU B 219      -0.299  13.470 -40.413  1.00 98.70           C  
ANISOU 4765  CD2 LEU B 219    16154  10326  11022   -466   -574    219       C  
ATOM   4766  N   PHE B 220       1.464   9.490 -41.688  1.00 99.06           N  
ANISOU 4766  N   PHE B 220    15810  10713  11117   -511   -769     79       N  
ATOM   4767  CA  PHE B 220       2.470   9.345 -42.736  1.00 99.87           C  
ANISOU 4767  CA  PHE B 220    15827  10866  11255   -577   -741     58       C  
ATOM   4768  C   PHE B 220       2.732   7.906 -43.215  1.00103.80           C  
ANISOU 4768  C   PHE B 220    16229  11460  11752   -557   -772     32       C  
ATOM   4769  O   PHE B 220       3.197   7.752 -44.352  1.00103.21           O  
ANISOU 4769  O   PHE B 220    16106  11425  11684   -592   -720     41       O  
ATOM   4770  CB  PHE B 220       3.776   9.992 -42.299  1.00102.65           C  
ANISOU 4770  CB  PHE B 220    16153  11176  11674   -670   -751    -13       C  
ATOM   4771  CG  PHE B 220       3.590  11.472 -42.094  1.00105.42           C  
ANISOU 4771  CG  PHE B 220    16614  11420  12021   -709   -691     13       C  
ATOM   4772  CD1 PHE B 220       3.388  12.323 -43.177  1.00109.21           C  
ANISOU 4772  CD1 PHE B 220    17139  11868  12488   -728   -585     78       C  
ATOM   4773  CD2 PHE B 220       3.582  12.017 -40.814  1.00108.28           C  
ANISOU 4773  CD2 PHE B 220    17056  11704  12380   -722   -733    -26       C  
ATOM   4774  CE1 PHE B 220       3.208  13.696 -42.984  1.00110.87           C  
ANISOU 4774  CE1 PHE B 220    17469  11965  12691   -757   -514    106       C  
ATOM   4775  CE2 PHE B 220       3.410  13.393 -40.622  1.00111.61           C  
ANISOU 4775  CE2 PHE B 220    17602  12012  12794   -762   -662     -6       C  
ATOM   4776  CZ  PHE B 220       3.224  14.221 -41.707  1.00110.08           C  
ANISOU 4776  CZ  PHE B 220    17447  11783  12595   -776   -548     62       C  
ATOM   4777  N   ALA B 221       2.427   6.867 -42.405  1.00 99.43           N  
ANISOU 4777  N   ALA B 221    15667  10931  11183   -501   -839      3       N  
ATOM   4778  CA  ALA B 221       2.650   5.507 -42.887  1.00 98.96           C  
ANISOU 4778  CA  ALA B 221    15537  10947  11117   -481   -850    -20       C  
ATOM   4779  C   ALA B 221       1.335   4.743 -43.184  1.00103.07           C  
ANISOU 4779  C   ALA B 221    16090  11502  11571   -426   -844     25       C  
ATOM   4780  O   ALA B 221       1.395   3.584 -43.604  1.00102.48           O  
ANISOU 4780  O   ALA B 221    15980  11479  11479   -415   -843      5       O  
ATOM   4781  CB  ALA B 221       3.514   4.731 -41.917  1.00 99.82           C  
ANISOU 4781  CB  ALA B 221    15601  11064  11263   -463   -922    -91       C  
ATOM   4782  N   PHE B 222       0.159   5.391 -43.019  1.00100.25           N  
ANISOU 4782  N   PHE B 222    15795  11115  11181   -395   -831     84       N  
ATOM   4783  CA  PHE B 222      -1.127   4.749 -43.328  1.00 99.58           C  
ANISOU 4783  CA  PHE B 222    15716  11073  11047   -354   -829    127       C  
ATOM   4784  C   PHE B 222      -2.059   5.682 -44.092  1.00103.43           C  
ANISOU 4784  C   PHE B 222    16225  11566  11506   -343   -795    215       C  
ATOM   4785  O   PHE B 222      -2.387   5.391 -45.240  1.00103.59           O  
ANISOU 4785  O   PHE B 222    16221  11653  11485   -358   -786    247       O  
ATOM   4786  CB  PHE B 222      -1.820   4.228 -42.064  1.00100.70           C  
ANISOU 4786  CB  PHE B 222    15895  11181  11186   -300   -857    111       C  
ATOM   4787  CG  PHE B 222      -3.147   3.533 -42.275  1.00101.30           C  
ANISOU 4787  CG  PHE B 222    15962  11299  11229   -270   -848    147       C  
ATOM   4788  CD1 PHE B 222      -3.199   2.187 -42.623  1.00103.50           C  
ANISOU 4788  CD1 PHE B 222    16210  11631  11483   -284   -855    111       C  
ATOM   4789  CD2 PHE B 222      -4.344   4.201 -42.045  1.00102.46           C  
ANISOU 4789  CD2 PHE B 222    16131  11426  11375   -229   -827    213       C  
ATOM   4790  CE1 PHE B 222      -4.422   1.530 -42.755  1.00103.77           C  
ANISOU 4790  CE1 PHE B 222    16232  11703  11494   -276   -847    132       C  
ATOM   4791  CE2 PHE B 222      -5.568   3.541 -42.181  1.00104.58           C  
ANISOU 4791  CE2 PHE B 222    16367  11741  11629   -209   -822    241       C  
ATOM   4792  CZ  PHE B 222      -5.599   2.213 -42.531  1.00102.43           C  
ANISOU 4792  CZ  PHE B 222    16061  11525  11334   -241   -835    197       C  
ATOM   4793  N   VAL B 223      -2.483   6.789 -43.470  1.00 99.30           N  
ANISOU 4793  N   VAL B 223    15759  10973  10997   -311   -776    255       N  
ATOM   4794  CA  VAL B 223      -3.412   7.730 -44.095  1.00 99.39           C  
ANISOU 4794  CA  VAL B 223    15797  10983  10986   -276   -740    350       C  
ATOM   4795  C   VAL B 223      -2.819   8.303 -45.398  1.00101.80           C  
ANISOU 4795  C   VAL B 223    16104  11307  11268   -320   -705    380       C  
ATOM   4796  O   VAL B 223      -3.458   8.157 -46.445  1.00101.58           O  
ANISOU 4796  O   VAL B 223    16059  11348  11189   -306   -709    437       O  
ATOM   4797  CB  VAL B 223      -3.866   8.842 -43.111  1.00104.09           C  
ANISOU 4797  CB  VAL B 223    16472  11476  11603   -228   -704    385       C  
ATOM   4798  CG1 VAL B 223      -4.758   9.878 -43.804  1.00104.57           C  
ANISOU 4798  CG1 VAL B 223    16560  11528  11643   -173   -657    495       C  
ATOM   4799  CG2 VAL B 223      -4.584   8.236 -41.901  1.00103.49           C  
ANISOU 4799  CG2 VAL B 223    16407  11377  11539   -178   -722    365       C  
ATOM   4800  N   VAL B 224      -1.587   8.877 -45.344  1.00 97.27           N  
ANISOU 4800  N   VAL B 224    15551  10678  10729   -380   -673    336       N  
ATOM   4801  CA  VAL B 224      -0.919   9.490 -46.506  1.00 97.23           C  
ANISOU 4801  CA  VAL B 224    15562  10671  10711   -429   -614    359       C  
ATOM   4802  C   VAL B 224      -0.709   8.426 -47.631  1.00100.59           C  
ANISOU 4802  C   VAL B 224    15934  11189  11094   -457   -623    345       C  
ATOM   4803  O   VAL B 224      -1.228   8.666 -48.726  1.00 99.85           O  
ANISOU 4803  O   VAL B 224    15872  11131  10936   -443   -603    414       O  
ATOM   4804  CB  VAL B 224       0.400  10.249 -46.158  1.00101.04           C  
ANISOU 4804  CB  VAL B 224    16060  11075  11257   -506   -571    302       C  
ATOM   4805  CG1 VAL B 224       1.026  10.879 -47.404  1.00101.15           C  
ANISOU 4805  CG1 VAL B 224    16099  11076  11258   -559   -486    330       C  
ATOM   4806  CG2 VAL B 224       0.175  11.306 -45.073  1.00101.08           C  
ANISOU 4806  CG2 VAL B 224    16144  10976  11286   -491   -558    309       C  
ATOM   4807  N   PRO B 225      -0.045   7.247 -47.403  1.00 96.64           N  
ANISOU 4807  N   PRO B 225    15370  10729  10620   -485   -653    265       N  
ATOM   4808  CA  PRO B 225       0.121   6.283 -48.496  1.00 96.43           C  
ANISOU 4808  CA  PRO B 225    15319  10774  10546   -511   -642    253       C  
ATOM   4809  C   PRO B 225      -1.197   5.844 -49.124  1.00103.07           C  
ANISOU 4809  C   PRO B 225    16176  11684  11301   -477   -679    310       C  
ATOM   4810  O   PRO B 225      -1.210   5.668 -50.342  1.00104.67           O  
ANISOU 4810  O   PRO B 225    16405  11930  11436   -503   -657    334       O  
ATOM   4811  CB  PRO B 225       0.832   5.112 -47.827  1.00 97.22           C  
ANISOU 4811  CB  PRO B 225    15357  10890  10692   -520   -669    166       C  
ATOM   4812  CG  PRO B 225       1.561   5.714 -46.719  1.00101.66           C  
ANISOU 4812  CG  PRO B 225    15903  11390  11334   -526   -682    127       C  
ATOM   4813  CD  PRO B 225       0.654   6.767 -46.192  1.00 97.65           C  
ANISOU 4813  CD  PRO B 225    15457  10833  10814   -492   -692    184       C  
ATOM   4814  N   ILE B 226      -2.304   5.711 -48.331  1.00 99.23           N  
ANISOU 4814  N   ILE B 226    15679  11208  10818   -424   -733    332       N  
ATOM   4815  CA  ILE B 226      -3.618   5.299 -48.868  1.00 99.09           C  
ANISOU 4815  CA  ILE B 226    15649  11266  10734   -398   -779    384       C  
ATOM   4816  C   ILE B 226      -4.178   6.383 -49.784  1.00104.46           C  
ANISOU 4816  C   ILE B 226    16370  11960  11362   -370   -770    484       C  
ATOM   4817  O   ILE B 226      -4.571   6.065 -50.905  1.00105.02           O  
ANISOU 4817  O   ILE B 226    16449  12103  11350   -387   -795    515       O  
ATOM   4818  CB  ILE B 226      -4.640   4.895 -47.774  1.00101.14           C  
ANISOU 4818  CB  ILE B 226    15873  11529  11026   -351   -820    383       C  
ATOM   4819  CG1 ILE B 226      -4.308   3.502 -47.260  1.00100.75           C  
ANISOU 4819  CG1 ILE B 226    15798  11491  10990   -380   -833    294       C  
ATOM   4820  CG2 ILE B 226      -6.093   4.919 -48.303  1.00101.67           C  
ANISOU 4820  CG2 ILE B 226    15908  11673  11050   -319   -864    459       C  
ATOM   4821  CD1 ILE B 226      -4.644   3.271 -45.853  1.00105.98           C  
ANISOU 4821  CD1 ILE B 226    16459  12104  11704   -339   -841    268       C  
ATOM   4822  N   LEU B 227      -4.183   7.646 -49.332  1.00100.52           N  
ANISOU 4822  N   LEU B 227    15909  11384  10899   -327   -733    534       N  
ATOM   4823  CA  LEU B 227      -4.707   8.749 -50.124  1.00101.19           C  
ANISOU 4823  CA  LEU B 227    16049  11465  10935   -281   -713    639       C  
ATOM   4824  C   LEU B 227      -4.007   8.871 -51.476  1.00104.58           C  
ANISOU 4824  C   LEU B 227    16535  11909  11292   -330   -675    650       C  
ATOM   4825  O   LEU B 227      -4.698   9.009 -52.483  1.00105.71           O  
ANISOU 4825  O   LEU B 227    16705  12114  11346   -302   -706    725       O  
ATOM   4826  CB  LEU B 227      -4.626  10.077 -49.364  1.00101.68           C  
ANISOU 4826  CB  LEU B 227    16168  11415  11049   -236   -653    678       C  
ATOM   4827  CG  LEU B 227      -5.374  10.134 -48.041  1.00106.62           C  
ANISOU 4827  CG  LEU B 227    16769  12006  11736   -176   -669    679       C  
ATOM   4828  CD1 LEU B 227      -5.198  11.479 -47.384  1.00108.24           C  
ANISOU 4828  CD1 LEU B 227    17061  12085  11978   -143   -594    712       C  
ATOM   4829  CD2 LEU B 227      -6.849   9.805 -48.208  1.00108.66           C  
ANISOU 4829  CD2 LEU B 227    16965  12350  11971   -103   -727    751       C  
ATOM   4830  N   ILE B 228      -2.662   8.755 -51.506  1.00 98.36           N  
ANISOU 4830  N   ILE B 228    15761  11073  10541   -403   -611    576       N  
ATOM   4831  CA  ILE B 228      -1.868   8.836 -52.733  1.00 97.79           C  
ANISOU 4831  CA  ILE B 228    15746  10998  10412   -457   -546    577       C  
ATOM   4832  C   ILE B 228      -2.285   7.722 -53.726  1.00101.84           C  
ANISOU 4832  C   ILE B 228    16257  11612  10826   -477   -596    571       C  
ATOM   4833  O   ILE B 228      -2.614   8.022 -54.873  1.00101.48           O  
ANISOU 4833  O   ILE B 228    16287  11596  10676   -469   -593    636       O  
ATOM   4834  CB  ILE B 228      -0.349   8.779 -52.405  1.00 99.86           C  
ANISOU 4834  CB  ILE B 228    15985  11196  10761   -532   -467    487       C  
ATOM   4835  CG1 ILE B 228       0.099  10.017 -51.621  1.00 99.65           C  
ANISOU 4835  CG1 ILE B 228    15982  11065  10814   -535   -415    492       C  
ATOM   4836  CG2 ILE B 228       0.490   8.598 -53.678  1.00100.87           C  
ANISOU 4836  CG2 ILE B 228    16160  11325  10839   -591   -383    477       C  
ATOM   4837  CD1 ILE B 228       1.473   9.900 -51.000  1.00104.29           C  
ANISOU 4837  CD1 ILE B 228    16511  11607  11507   -610   -375    395       C  
ATOM   4838  N   ILE B 229      -2.285   6.455 -53.268  1.00 98.44           N  
ANISOU 4838  N   ILE B 229    15756  11228  10419   -504   -642    493       N  
ATOM   4839  CA  ILE B 229      -2.624   5.270 -54.063  1.00 98.61           C  
ANISOU 4839  CA  ILE B 229    15782  11333  10352   -542   -682    466       C  
ATOM   4840  C   ILE B 229      -4.112   5.327 -54.529  1.00105.31           C  
ANISOU 4840  C   ILE B 229    16631  12269  11113   -503   -782    543       C  
ATOM   4841  O   ILE B 229      -4.389   4.983 -55.686  1.00105.97           O  
ANISOU 4841  O   ILE B 229    16771  12414  11080   -534   -809    562       O  
ATOM   4842  CB  ILE B 229      -2.272   3.971 -53.266  1.00100.24           C  
ANISOU 4842  CB  ILE B 229    15922  11546  10618   -570   -692    366       C  
ATOM   4843  CG1 ILE B 229      -0.739   3.846 -53.077  1.00 99.36           C  
ANISOU 4843  CG1 ILE B 229    15800  11369  10582   -604   -601    297       C  
ATOM   4844  CG2 ILE B 229      -2.814   2.728 -53.962  1.00101.69           C  
ANISOU 4844  CG2 ILE B 229    16121  11807  10711   -613   -733    335       C  
ATOM   4845  CD1 ILE B 229      -0.307   2.906 -52.055  1.00 97.26           C  
ANISOU 4845  CD1 ILE B 229    15469  11093  10394   -601   -612    218       C  
ATOM   4846  N   THR B 230      -5.043   5.781 -53.646  1.00102.85           N  
ANISOU 4846  N   THR B 230    16259  11963  10857   -436   -835    589       N  
ATOM   4847  CA  THR B 230      -6.478   5.922 -53.948  1.00103.62           C  
ANISOU 4847  CA  THR B 230    16321  12148  10902   -386   -931    669       C  
ATOM   4848  C   THR B 230      -6.657   6.971 -55.037  1.00110.73           C  
ANISOU 4848  C   THR B 230    17305  13057  11711   -343   -929    773       C  
ATOM   4849  O   THR B 230      -7.377   6.716 -56.009  1.00112.67           O  
ANISOU 4849  O   THR B 230    17564  13399  11848   -347  -1011    817       O  
ATOM   4850  CB  THR B 230      -7.277   6.283 -52.682  1.00107.85           C  
ANISOU 4850  CB  THR B 230    16777  12664  11538   -314   -951    697       C  
ATOM   4851  OG1 THR B 230      -7.051   5.288 -51.693  1.00108.66           O  
ANISOU 4851  OG1 THR B 230    16827  12749  11710   -352   -945    601       O  
ATOM   4852  CG2 THR B 230      -8.768   6.401 -52.941  1.00104.40           C  
ANISOU 4852  CG2 THR B 230    16272  12324  11071   -257  -1044    782       C  
ATOM   4853  N   VAL B 231      -5.978   8.136 -54.884  1.00107.00           N  
ANISOU 4853  N   VAL B 231    16900  12480  11275   -308   -837    811       N  
ATOM   4854  CA  VAL B 231      -6.013   9.240 -55.850  1.00108.05           C  
ANISOU 4854  CA  VAL B 231    17140  12590  11324   -260   -806    913       C  
ATOM   4855  C   VAL B 231      -5.482   8.717 -57.211  1.00113.91           C  
ANISOU 4855  C   VAL B 231    17973  13368  11938   -331   -794    892       C  
ATOM   4856  O   VAL B 231      -6.153   8.902 -58.227  1.00114.26           O  
ANISOU 4856  O   VAL B 231    18077  13480  11858   -299   -858    970       O  
ATOM   4857  CB  VAL B 231      -5.263  10.509 -55.327  1.00110.79           C  
ANISOU 4857  CB  VAL B 231    17553  12797  11745   -233   -685    936       C  
ATOM   4858  CG1 VAL B 231      -4.950  11.498 -56.443  1.00111.30           C  
ANISOU 4858  CG1 VAL B 231    17760  12812  11716   -211   -614   1018       C  
ATOM   4859  CG2 VAL B 231      -6.060  11.195 -54.228  1.00110.19           C  
ANISOU 4859  CG2 VAL B 231    17427  12687  11752   -142   -700    987       C  
ATOM   4860  N   CYS B 232      -4.335   8.001 -57.204  1.00111.00           N  
ANISOU 4860  N   CYS B 232    17615  12960  11600   -423   -719    787       N  
ATOM   4861  CA  CYS B 232      -3.742   7.422 -58.404  1.00112.13           C  
ANISOU 4861  CA  CYS B 232    17852  13119  11633   -493   -679    756       C  
ATOM   4862  C   CYS B 232      -4.780   6.573 -59.122  1.00119.26           C  
ANISOU 4862  C   CYS B 232    18755  14147  12411   -507   -809    767       C  
ATOM   4863  O   CYS B 232      -5.016   6.816 -60.302  1.00120.50           O  
ANISOU 4863  O   CYS B 232    19024  14337  12423   -504   -831    826       O  
ATOM   4864  CB  CYS B 232      -2.495   6.610 -58.064  1.00111.65           C  
ANISOU 4864  CB  CYS B 232    17762  13007  11652   -573   -587    638       C  
ATOM   4865  SG  CYS B 232      -1.032   7.604 -57.665  1.00115.40           S  
ANISOU 4865  SG  CYS B 232    18254  13344  12247   -591   -425    618       S  
ATOM   4866  N   TYR B 233      -5.447   5.641 -58.387  1.00116.63           N  
ANISOU 4866  N   TYR B 233    18303  13882  12129   -524   -898    715       N  
ATOM   4867  CA  TYR B 233      -6.487   4.738 -58.888  1.00117.85           C  
ANISOU 4867  CA  TYR B 233    18430  14159  12188   -559  -1027    708       C  
ATOM   4868  C   TYR B 233      -7.650   5.509 -59.508  1.00124.84           C  
ANISOU 4868  C   TYR B 233    19321  15129  12983   -485  -1142    830       C  
ATOM   4869  O   TYR B 233      -8.059   5.180 -60.630  1.00125.62           O  
ANISOU 4869  O   TYR B 233    19491  15308  12929   -521  -1220    849       O  
ATOM   4870  CB  TYR B 233      -7.009   3.822 -57.765  1.00118.21           C  
ANISOU 4870  CB  TYR B 233    18338  14239  12337   -579  -1076    639       C  
ATOM   4871  CG  TYR B 233      -8.212   2.970 -58.146  1.00121.68           C  
ANISOU 4871  CG  TYR B 233    18725  14806  12702   -624  -1211    631       C  
ATOM   4872  CD1 TYR B 233      -8.087   1.902 -59.039  1.00124.12           C  
ANISOU 4872  CD1 TYR B 233    19110  15159  12891   -729  -1230    562       C  
ATOM   4873  CD2 TYR B 233      -9.461   3.196 -57.572  1.00123.29           C  
ANISOU 4873  CD2 TYR B 233    18800  15083  12962   -570  -1310    686       C  
ATOM   4874  CE1 TYR B 233      -9.179   1.097 -59.370  1.00125.63           C  
ANISOU 4874  CE1 TYR B 233    19252  15466  13014   -793  -1357    542       C  
ATOM   4875  CE2 TYR B 233     -10.564   2.396 -57.899  1.00125.58           C  
ANISOU 4875  CE2 TYR B 233    19019  15498  13199   -626  -1435    671       C  
ATOM   4876  CZ  TYR B 233     -10.414   1.339 -58.789  1.00133.83           C  
ANISOU 4876  CZ  TYR B 233    20143  16587  14121   -746  -1464    595       C  
ATOM   4877  OH  TYR B 233     -11.491   0.542 -59.123  1.00134.93           O  
ANISOU 4877  OH  TYR B 233    20215  16848  14204   -823  -1591    570       O  
ATOM   4878  N   GLY B 234      -8.159   6.503 -58.766  1.00122.06           N  
ANISOU 4878  N   GLY B 234    18900  14756  12722   -381  -1150    910       N  
ATOM   4879  CA  GLY B 234      -9.277   7.352 -59.170  1.00123.63           C  
ANISOU 4879  CA  GLY B 234    19083  15025  12865   -279  -1249   1042       C  
ATOM   4880  C   GLY B 234      -9.029   8.090 -60.469  1.00129.69           C  
ANISOU 4880  C   GLY B 234    20014  15784  13480   -248  -1237   1125       C  
ATOM   4881  O   GLY B 234      -9.907   8.152 -61.339  1.00130.62           O  
ANISOU 4881  O   GLY B 234    20149  16010  13472   -215  -1364   1201       O  
ATOM   4882  N   LEU B 235      -7.811   8.639 -60.606  1.00126.10           N  
ANISOU 4882  N   LEU B 235    19682  15197  13033   -263  -1082   1110       N  
ATOM   4883  CA  LEU B 235      -7.380   9.372 -61.791  1.00126.73           C  
ANISOU 4883  CA  LEU B 235    19946  15233  12973   -241  -1026   1181       C  
ATOM   4884  C   LEU B 235      -7.102   8.404 -62.936  1.00132.85           C  
ANISOU 4884  C   LEU B 235    20823  16062  13592   -343  -1053   1123       C  
ATOM   4885  O   LEU B 235      -7.429   8.722 -64.076  1.00134.01           O  
ANISOU 4885  O   LEU B 235    21100  16249  13569   -314  -1105   1200       O  
ATOM   4886  CB  LEU B 235      -6.138  10.235 -61.502  1.00125.65           C  
ANISOU 4886  CB  LEU B 235    19896  14930  12915   -243   -833   1171       C  
ATOM   4887  CG  LEU B 235      -6.270  11.346 -60.470  1.00128.81           C  
ANISOU 4887  CG  LEU B 235    20248  15247  13448   -153   -780   1227       C  
ATOM   4888  CD1 LEU B 235      -4.924  11.902 -60.119  1.00127.92           C  
ANISOU 4888  CD1 LEU B 235    20199  14982  13424   -204   -599   1175       C  
ATOM   4889  CD2 LEU B 235      -7.185  12.453 -60.945  1.00132.50           C  
ANISOU 4889  CD2 LEU B 235    20781  15728  13834    -16   -826   1384       C  
ATOM   4890  N   MET B 236      -6.518   7.221 -62.644  1.00129.96           N  
ANISOU 4890  N   MET B 236    20414  15693  13274   -454  -1017    991       N  
ATOM   4891  CA  MET B 236      -6.238   6.187 -63.648  1.00131.37           C  
ANISOU 4891  CA  MET B 236    20698  15909  13310   -558  -1025    922       C  
ATOM   4892  C   MET B 236      -7.546   5.650 -64.233  1.00139.48           C  
ANISOU 4892  C   MET B 236    21700  17092  14204   -570  -1227    951       C  
ATOM   4893  O   MET B 236      -7.626   5.383 -65.435  1.00140.32           O  
ANISOU 4893  O   MET B 236    21952  17240  14122   -613  -1270    960       O  
ATOM   4894  CB  MET B 236      -5.409   5.046 -63.044  1.00132.15           C  
ANISOU 4894  CB  MET B 236    20739  15964  13508   -655   -938    781       C  
ATOM   4895  CG  MET B 236      -3.915   5.290 -63.106  1.00135.00           C  
ANISOU 4895  CG  MET B 236    21179  16189  13926   -682   -739    739       C  
ATOM   4896  SD  MET B 236      -2.980   4.246 -61.959  1.00136.96           S  
ANISOU 4896  SD  MET B 236    21300  16385  14355   -742   -648    601       S  
ATOM   4897  CE  MET B 236      -3.034   2.685 -62.797  1.00134.13           C  
ANISOU 4897  CE  MET B 236    21023  16078  13860   -846   -667    511       C  
ATOM   4898  N   LEU B 237      -8.575   5.539 -63.367  1.00137.84           N  
ANISOU 4898  N   LEU B 237    21307  16969  14096   -531  -1347    966       N  
ATOM   4899  CA  LEU B 237      -9.933   5.095 -63.673  1.00139.44           C  
ANISOU 4899  CA  LEU B 237    21423  17333  14224   -539  -1548    994       C  
ATOM   4900  C   LEU B 237     -10.591   6.015 -64.715  1.00146.91           C  
ANISOU 4900  C   LEU B 237    22457  18348  15013   -449  -1657   1133       C  
ATOM   4901  O   LEU B 237     -11.327   5.524 -65.571  1.00148.22           O  
ANISOU 4901  O   LEU B 237    22647  18641  15028   -494  -1814   1141       O  
ATOM   4902  CB  LEU B 237     -10.748   5.088 -62.372  1.00138.48           C  
ANISOU 4902  CB  LEU B 237    21080  17253  14284   -490  -1602   1000       C  
ATOM   4903  CG  LEU B 237     -12.027   4.288 -62.371  1.00143.85           C  
ANISOU 4903  CG  LEU B 237    21617  18090  14948   -538  -1780    983       C  
ATOM   4904  CD1 LEU B 237     -12.071   3.377 -61.183  1.00142.18           C  
ANISOU 4904  CD1 LEU B 237    21268  17860  14894   -602  -1739    877       C  
ATOM   4905  CD2 LEU B 237     -13.243   5.206 -62.392  1.00148.15           C  
ANISOU 4905  CD2 LEU B 237    22049  18737  15503   -408  -1913   1124       C  
ATOM   4906  N   LEU B 238     -10.321   7.338 -64.637  1.00144.73           N  
ANISOU 4906  N   LEU B 238    22238  17986  14766   -322  -1574   1241       N  
ATOM   4907  CA  LEU B 238     -10.854   8.349 -65.557  1.00147.34           C  
ANISOU 4907  CA  LEU B 238    22674  18356  14954   -207  -1650   1390       C  
ATOM   4908  C   LEU B 238     -10.208   8.242 -66.933  1.00154.99           C  
ANISOU 4908  C   LEU B 238    23890  19294  15705   -264  -1613   1385       C  
ATOM   4909  O   LEU B 238     -10.917   8.270 -67.945  1.00155.99           O  
ANISOU 4909  O   LEU B 238    24095  19529  15645   -242  -1767   1454       O  
ATOM   4910  CB  LEU B 238     -10.634   9.765 -65.000  1.00147.12           C  
ANISOU 4910  CB  LEU B 238    22661  18211  15028    -63  -1533   1495       C  
ATOM   4911  CG  LEU B 238     -11.565  10.217 -63.891  1.00151.53           C  
ANISOU 4911  CG  LEU B 238    23015  18808  15751     45  -1590   1556       C  
ATOM   4912  CD1 LEU B 238     -10.833  11.099 -62.905  1.00150.56           C  
ANISOU 4912  CD1 LEU B 238    22903  18517  15785     99  -1403   1562       C  
ATOM   4913  CD2 LEU B 238     -12.773  10.939 -64.452  1.00155.97           C  
ANISOU 4913  CD2 LEU B 238    23553  19484  16225    191  -1746   1716       C  
ATOM   4914  N   ARG B 239      -8.854   8.133 -66.963  1.00153.25           N  
ANISOU 4914  N   ARG B 239    23793  18925  15509   -336  -1408   1306       N  
ATOM   4915  CA  ARG B 239      -8.041   8.008 -68.181  1.00155.26           C  
ANISOU 4915  CA  ARG B 239    24295  19115  15581   -398  -1316   1288       C  
ATOM   4916  C   ARG B 239      -8.449   6.744 -68.930  1.00162.47           C  
ANISOU 4916  C   ARG B 239    25250  20143  16337   -518  -1447   1209       C  
ATOM   4917  O   ARG B 239      -8.465   6.742 -70.160  1.00164.79           O  
ANISOU 4917  O   ARG B 239    25748  20456  16409   -536  -1483   1242       O  
ATOM   4918  CB  ARG B 239      -6.531   8.007 -67.844  1.00154.11           C  
ANISOU 4918  CB  ARG B 239    24209  18798  15548   -459  -1063   1203       C  
ATOM   4919  CG  ARG B 239      -5.575   7.790 -69.027  1.00164.10           C  
ANISOU 4919  CG  ARG B 239    25720  19979  16652   -532   -925   1171       C  
ATOM   4920  CD  ARG B 239      -5.368   9.020 -69.894  1.00174.08           C  
ANISOU 4920  CD  ARG B 239    27194  21162  17787   -444   -847   1296       C  
ATOM   4921  NE  ARG B 239      -4.928   8.652 -71.241  1.00184.29           N  
ANISOU 4921  NE  ARG B 239    28740  22424  18856   -508   -789   1282       N  
ATOM   4922  CZ  ARG B 239      -5.558   8.999 -72.360  1.00202.33           C  
ANISOU 4922  CZ  ARG B 239    31211  24764  20901   -457   -899   1380       C  
ATOM   4923  NH1 ARG B 239      -6.655   9.744 -72.310  1.00189.69           N1+
ANISOU 4923  NH1 ARG B 239    29555  23257  19260   -330  -1075   1507       N1+
ATOM   4924  NH2 ARG B 239      -5.090   8.612 -73.538  1.00193.11           N  
ANISOU 4924  NH2 ARG B 239    30293  23555  19527   -525   -830   1355       N  
ATOM   4925  N   LEU B 240      -8.829   5.697 -68.186  1.00158.48           N  
ANISOU 4925  N   LEU B 240    24566  19710  15939   -600  -1520   1108       N  
ATOM   4926  CA  LEU B 240      -9.310   4.442 -68.740  1.00159.30           C  
ANISOU 4926  CA  LEU B 240    24690  19923  15916   -728  -1647   1020       C  
ATOM   4927  C   LEU B 240     -10.669   4.610 -69.403  1.00166.98           C  
ANISOU 4927  C   LEU B 240    25638  21069  16739   -693  -1900   1109       C  
ATOM   4928  O   LEU B 240     -10.941   3.930 -70.390  1.00167.94           O  
ANISOU 4928  O   LEU B 240    25884  21264  16661   -788  -2004   1071       O  
ATOM   4929  CB  LEU B 240      -9.404   3.424 -67.627  1.00157.50           C  
ANISOU 4929  CB  LEU B 240    24267  19712  15865   -808  -1643    902       C  
ATOM   4930  CG  LEU B 240      -8.698   2.128 -67.882  1.00161.82           C  
ANISOU 4930  CG  LEU B 240    24909  20210  16365   -956  -1551    757       C  
ATOM   4931  CD1 LEU B 240      -7.170   2.315 -67.906  1.00160.92           C  
ANISOU 4931  CD1 LEU B 240    24921  19922  16299   -954  -1300    721       C  
ATOM   4932  CD2 LEU B 240      -9.108   1.124 -66.840  1.00163.73           C  
ANISOU 4932  CD2 LEU B 240    24960  20495  16756  -1024  -1590    660       C  
ATOM   4933  N   ARG B 241     -11.513   5.525 -68.871  1.00165.47           N  
ANISOU 4933  N   ARG B 241    25287  20941  16642   -553  -1999   1228       N  
ATOM   4934  CA  ARG B 241     -12.835   5.824 -69.417  1.00168.25           C  
ANISOU 4934  CA  ARG B 241    25577  21469  16880   -487  -2246   1333       C  
ATOM   4935  C   ARG B 241     -12.706   6.740 -70.653  1.00177.26           C  
ANISOU 4935  C   ARG B 241    26961  22591  17797   -395  -2265   1458       C  
ATOM   4936  O   ARG B 241     -13.593   6.743 -71.509  1.00179.39           O  
ANISOU 4936  O   ARG B 241    27264  23007  17890   -377  -2478   1524       O  
ATOM   4937  CB  ARG B 241     -13.757   6.431 -68.343  1.00166.95           C  
ANISOU 4937  CB  ARG B 241    25149  21369  16917   -360  -2319   1417       C  
ATOM   4938  CG  ARG B 241     -15.264   6.273 -68.610  1.00179.10           C  
ANISOU 4938  CG  ARG B 241    26518  23126  18406   -336  -2593   1480       C  
ATOM   4939  CD  ARG B 241     -15.746   4.832 -68.822  1.00191.45           C  
ANISOU 4939  CD  ARG B 241    28012  24815  19916   -529  -2730   1344       C  
ATOM   4940  NE  ARG B 241     -15.949   4.520 -70.244  1.00201.78           N  
ANISOU 4940  NE  ARG B 241    29504  26216  20946   -601  -2882   1348       N  
ATOM   4941  CZ  ARG B 241     -16.498   3.400 -70.709  1.00212.68           C  
ANISOU 4941  CZ  ARG B 241    30863  27724  22223   -769  -3041   1248       C  
ATOM   4942  NH1 ARG B 241     -16.916   2.459 -69.869  1.00197.38           N  
ANISOU 4942  NH1 ARG B 241    28719  25834  20441   -884  -3059   1137       N  
ATOM   4943  NH2 ARG B 241     -16.638   3.213 -72.014  1.00198.60           N1+
ANISOU 4943  NH2 ARG B 241    29275  26014  20169   -829  -3177   1256       N1+
ATOM   4944  N   SER B 242     -11.583   7.472 -70.764  1.00175.15           N  
ANISOU 4944  N   SER B 242    26871  22145  17535   -345  -2041   1485       N  
ATOM   4945  CA  SER B 242     -11.262   8.333 -71.907  1.00177.67           C  
ANISOU 4945  CA  SER B 242    27459  22404  17645   -266  -2002   1593       C  
ATOM   4946  C   SER B 242     -10.771   7.467 -73.095  1.00184.98           C  
ANISOU 4946  C   SER B 242    28629  23322  18335   -409  -1993   1507       C  
ATOM   4947  O   SER B 242     -11.243   7.639 -74.219  1.00186.26           O  
ANISOU 4947  O   SER B 242    28960  23558  18252   -383  -2132   1581       O  
ATOM   4948  CB  SER B 242     -10.213   9.369 -71.501  1.00179.99           C  
ANISOU 4948  CB  SER B 242    27838  22497  18054   -185  -1743   1636       C  
ATOM   4949  OG  SER B 242      -9.440   9.847 -72.590  1.00189.73           O  
ANISOU 4949  OG  SER B 242    29372  23616  19100   -176  -1613   1678       O  
ATOM   4950  N   VAL B 243      -9.840   6.523 -72.812  1.00182.58           N  
ANISOU 4950  N   VAL B 243    28343  22925  18104   -554  -1831   1353       N  
ATOM   4951  CA  VAL B 243      -9.193   5.562 -73.724  1.00184.03           C  
ANISOU 4951  CA  VAL B 243    28746  23065  18111   -703  -1762   1244       C  
ATOM   4952  C   VAL B 243     -10.238   4.592 -74.343  1.00191.70           C  
ANISOU 4952  C   VAL B 243    29715  24218  18905   -806  -2021   1198       C  
ATOM   4953  O   VAL B 243     -10.113   4.228 -75.518  1.00193.04           O  
ANISOU 4953  O   VAL B 243    30136  24389  18821   -879  -2048   1178       O  
ATOM   4954  CB  VAL B 243      -8.065   4.811 -72.942  1.00185.52           C  
ANISOU 4954  CB  VAL B 243    28875  23124  18492   -803  -1532   1099       C  
ATOM   4955  CG1 VAL B 243      -7.799   3.405 -73.470  1.00185.55           C  
ANISOU 4955  CG1 VAL B 243    28989  23133  18378   -973  -1518    956       C  
ATOM   4956  CG2 VAL B 243      -6.778   5.629 -72.912  1.00184.65           C  
ANISOU 4956  CG2 VAL B 243    28882  22822  18454   -749  -1259   1127       C  
ATOM   4957  N   ARG B 244     -11.269   4.204 -73.557  1.00189.20           N  
ANISOU 4957  N   ARG B 244    29119  24049  18719   -818  -2205   1180       N  
ATOM   4958  CA  ARG B 244     -12.348   3.294 -73.959  1.00191.03           C  
ANISOU 4958  CA  ARG B 244    29289  24465  18828   -929  -2461   1129       C  
ATOM   4959  C   ARG B 244     -13.213   3.848 -75.110  1.00199.53           C  
ANISOU 4959  C   ARG B 244    30486  25678  19648   -864  -2696   1252       C  
ATOM   4960  O   ARG B 244     -13.915   3.066 -75.755  1.00201.27           O  
ANISOU 4960  O   ARG B 244    30735  26037  19701   -984  -2900   1198       O  
ATOM   4961  CB  ARG B 244     -13.245   2.967 -72.757  1.00189.78           C  
ANISOU 4961  CB  ARG B 244    28784  24421  18903   -932  -2577   1104       C  
ATOM   4962  N   LEU B 245     -13.160   5.174 -75.374  1.00197.56           N  
ANISOU 4962  N   LEU B 245    30316  25386  19360   -679  -2672   1414       N  
ATOM   4963  CA  LEU B 245     -13.952   5.803 -76.437  1.00200.56           C  
ANISOU 4963  CA  LEU B 245    30820  25889  19496   -584  -2892   1552       C  
ATOM   4964  C   LEU B 245     -13.081   6.535 -77.482  1.00205.26           C  
ANISOU 4964  C   LEU B 245    31781  26333  19874   -517  -2738   1627       C  
ATOM   4965  O   LEU B 245     -13.303   6.345 -78.681  1.00206.82           O  
ANISOU 4965  O   LEU B 245    32213  26589  19780   -557  -2867   1644       O  
ATOM   4966  CB  LEU B 245     -14.989   6.770 -75.837  1.00201.13           C  
ANISOU 4966  CB  LEU B 245    30637  26078  19704   -393  -3047   1707       C  
ATOM   4967  CG  LEU B 245     -16.187   6.109 -75.148  1.00205.84           C  
ANISOU 4967  CG  LEU B 245    30891  26876  20443   -448  -3273   1665       C  
ATOM   4968  CD1 LEU B 245     -16.114   6.273 -73.643  1.00203.15           C  
ANISOU 4968  CD1 LEU B 245    30278  26473  20438   -398  -3133   1645       C  
ATOM   4969  CD2 LEU B 245     -17.496   6.657 -75.684  1.00211.22           C  
ANISOU 4969  CD2 LEU B 245    31474  27768  21010   -324  -3580   1814       C  
ATOM   4970  N   LEU B 246     -12.105   7.361 -77.032  1.00200.40           N  
ANISOU 4970  N   LEU B 246    31222  25525  19397   -423  -2465   1668       N  
ATOM   4971  CA  LEU B 246     -11.218   8.137 -77.908  1.00201.28           C  
ANISOU 4971  CA  LEU B 246    31667  25470  19340   -358  -2276   1741       C  
ATOM   4972  C   LEU B 246     -10.260   7.256 -78.721  1.00206.27           C  
ANISOU 4972  C   LEU B 246    32574  25994  19806   -526  -2121   1611       C  
ATOM   4973  O   LEU B 246     -10.145   7.474 -79.926  1.00208.30           O  
ANISOU 4973  O   LEU B 246    33141  26223  19782   -515  -2132   1664       O  
ATOM   4974  CB  LEU B 246     -10.407   9.177 -77.115  1.00199.44           C  
ANISOU 4974  CB  LEU B 246    31395  25057  19328   -244  -2013   1797       C  
ATOM   4975  CG  LEU B 246     -11.141  10.451 -76.684  1.00204.41           C  
ANISOU 4975  CG  LEU B 246    31902  25725  20040    -32  -2095   1973       C  
ATOM   4976  CD1 LEU B 246     -10.463  11.092 -75.493  1.00201.93           C  
ANISOU 4976  CD1 LEU B 246    31449  25261  20016     20  -1863   1967       C  
ATOM   4977  CD2 LEU B 246     -11.214  11.461 -77.817  1.00209.80           C  
ANISOU 4977  CD2 LEU B 246    32880  26365  20468    108  -2107   2134       C  
ATOM   4978  N   SER B 247      -9.555   6.301 -78.076  1.00201.34           N  
ANISOU 4978  N   SER B 247    31854  25298  19349   -670  -1964   1449       N  
ATOM   4979  CA  SER B 247      -8.607   5.410 -78.759  1.00201.67           C  
ANISOU 4979  CA  SER B 247    32139  25225  19261   -822  -1789   1322       C  
ATOM   4980  C   SER B 247      -9.344   4.381 -79.623  1.00208.11           C  
ANISOU 4980  C   SER B 247    33069  26181  19822   -956  -2017   1253       C  
ATOM   4981  O   SER B 247      -8.928   4.117 -80.754  1.00209.20           O  
ANISOU 4981  O   SER B 247    33533  26254  19701  -1021  -1956   1230       O  
ATOM   4982  CB  SER B 247      -7.694   4.710 -77.755  1.00202.46           C  
ANISOU 4982  CB  SER B 247    32082  25218  19627   -913  -1568   1182       C  
ATOM   4983  OG  SER B 247      -6.767   3.847 -78.395  1.00211.19           O  
ANISOU 4983  OG  SER B 247    33414  26207  20623  -1046  -1382   1066       O  
ATOM   4984  N   GLY B 248     -10.429   3.829 -79.084  1.00205.16           N  
ANISOU 4984  N   GLY B 248    32433  25994  19523  -1001  -2269   1219       N  
ATOM   4985  CA  GLY B 248     -11.248   2.842 -79.771  1.00207.30           C  
ANISOU 4985  CA  GLY B 248    32764  26419  19582  -1146  -2512   1144       C  
ATOM   4986  C   GLY B 248     -10.842   1.409 -79.499  1.00210.84           C  
ANISOU 4986  C   GLY B 248    33201  26825  20084  -1348  -2415    950       C  
ATOM   4987  O   GLY B 248     -10.311   1.099 -78.427  1.00207.71           O  
ANISOU 4987  O   GLY B 248    32615  26347  19957  -1362  -2245    879       O  
ATOM   4988  N   SER B 249     -11.099   0.527 -80.486  1.00209.95           N  
ANISOU 4988  N   SER B 249    33307  26763  19701  -1503  -2526    865       N  
ATOM   4989  CA  SER B 249     -10.839  -0.915 -80.436  1.00209.43           C  
ANISOU 4989  CA  SER B 249    33286  26661  19626  -1710  -2455    679       C  
ATOM   4990  C   SER B 249      -9.326  -1.237 -80.406  1.00212.14           C  
ANISOU 4990  C   SER B 249    33811  26760  20033  -1736  -2075    600       C  
ATOM   4991  O   SER B 249      -8.625  -0.976 -81.390  1.00213.45           O  
ANISOU 4991  O   SER B 249    34301  26804  19994  -1725  -1931    624       O  
ATOM   4992  CB  SER B 249     -11.503  -1.613 -81.625  1.00215.37           C  
ANISOU 4992  CB  SER B 249    34273  27521  20038  -1862  -2673    623       C  
ATOM   4993  OG  SER B 249     -12.862  -1.237 -81.781  1.00224.28           O  
ANISOU 4993  OG  SER B 249    35243  28884  21091  -1827  -3035    709       O  
ATOM   4994  N   LYS B 250      -8.833  -1.802 -79.267  1.00205.58           N  
ANISOU 4994  N   LYS B 250    32765  25859  19486  -1766  -1912    509       N  
ATOM   4995  CA  LYS B 250      -7.428  -2.197 -79.074  1.00203.46           C  
ANISOU 4995  CA  LYS B 250    32604  25379  19324  -1786  -1563    429       C  
ATOM   4996  C   LYS B 250      -7.236  -3.201 -77.917  1.00204.50           C  
ANISOU 4996  C   LYS B 250    32506  25487  19708  -1860  -1478    304       C  
ATOM   4997  O   LYS B 250      -8.013  -3.225 -76.958  1.00202.63           O  
ANISOU 4997  O   LYS B 250    31973  25368  19649  -1843  -1634    309       O  
ATOM   4998  CB  LYS B 250      -6.526  -0.972 -78.843  1.00204.52           C  
ANISOU 4998  CB  LYS B 250    32732  25386  19592  -1620  -1356    540       C  
ATOM   4999  N   GLU B 251      -6.179  -4.028 -78.041  1.00200.50           N  
ANISOU 4999  N   GLU B 251    32153  24818  19209  -1933  -1216    196       N  
ATOM   5000  CA  GLU B 251      -5.720  -5.035 -77.081  1.00198.44           C  
ANISOU 5000  CA  GLU B 251    31745  24490  19162  -1990  -1073     77       C  
ATOM   5001  C   GLU B 251      -4.786  -4.359 -76.080  1.00199.76           C  
ANISOU 5001  C   GLU B 251    31720  24558  19622  -1849   -875    126       C  
ATOM   5002  O   GLU B 251      -4.690  -4.785 -74.925  1.00197.03           O  
ANISOU 5002  O   GLU B 251    31141  24209  19513  -1839   -840     76       O  
ATOM   5003  CB  GLU B 251      -5.001  -6.192 -77.816  1.00200.87           C  
ANISOU 5003  CB  GLU B 251    32343  24664  19317  -2119   -876    -49       C  
ATOM   5004  CG  GLU B 251      -4.706  -7.413 -76.953  1.00209.55           C  
ANISOU 5004  CG  GLU B 251    33327  25704  20587  -2191   -758   -178       C  
ATOM   5005  CD  GLU B 251      -3.895  -8.515 -77.612  1.00226.67           C  
ANISOU 5005  CD  GLU B 251    35780  27716  22629  -2294   -523   -294       C  
ATOM   5006  OE1 GLU B 251      -2.709  -8.273 -77.934  1.00218.11           O1-
ANISOU 5006  OE1 GLU B 251    34829  26477  21567  -2226   -256   -275       O1-
ATOM   5007  OE2 GLU B 251      -4.432  -9.637 -77.763  1.00220.30           O  
ANISOU 5007  OE2 GLU B 251    35057  26934  21715  -2445   -592   -405       O  
ATOM   5008  N   LYS B 252      -4.089  -3.293 -76.533  1.00196.81           N  
ANISOU 5008  N   LYS B 252    31455  24100  19225  -1744   -746    223       N  
ATOM   5009  CA  LYS B 252      -3.158  -2.503 -75.722  1.00194.77           C  
ANISOU 5009  CA  LYS B 252    31038  23744  19221  -1621   -559    275       C  
ATOM   5010  C   LYS B 252      -3.914  -1.466 -74.837  1.00196.97           C  
ANISOU 5010  C   LYS B 252    31048  24134  19656  -1508   -740    380       C  
ATOM   5011  O   LYS B 252      -3.278  -0.741 -74.063  1.00194.93           O  
ANISOU 5011  O   LYS B 252    30643  23809  19613  -1412   -618    423       O  
ATOM   5012  CB  LYS B 252      -2.106  -1.820 -76.622  1.00198.25           C  
ANISOU 5012  CB  LYS B 252    31721  24037  19568  -1576   -326    327       C  
ATOM   5013  CG  LYS B 252      -0.660  -2.233 -76.323  1.00208.06           C  
ANISOU 5013  CG  LYS B 252    32963  25110  20979  -1576     -4    257       C  
ATOM   5014  CD  LYS B 252      -0.251  -3.561 -76.972  1.00215.75           C  
ANISOU 5014  CD  LYS B 252    34151  26005  21817  -1693    130    137       C  
ATOM   5015  CE  LYS B 252       1.159  -3.956 -76.599  1.00221.72           C  
ANISOU 5015  CE  LYS B 252    34869  26604  22768  -1671    445     79       C  
ATOM   5016  NZ  LYS B 252       1.520  -5.299 -77.123  1.00228.46           N  
ANISOU 5016  NZ  LYS B 252    35919  27376  23509  -1771    585    -36       N  
ATOM   5017  N   ASP B 253      -5.271  -1.431 -74.938  1.00193.68           N  
ANISOU 5017  N   ASP B 253    30566  23888  19138  -1525  -1028    416       N  
ATOM   5018  CA  ASP B 253      -6.179  -0.577 -74.159  1.00192.23           C  
ANISOU 5018  CA  ASP B 253    30131  23825  19084  -1421  -1218    514       C  
ATOM   5019  C   ASP B 253      -6.702  -1.361 -72.946  1.00191.64           C  
ANISOU 5019  C   ASP B 253    29784  23821  19209  -1465  -1300    435       C  
ATOM   5020  O   ASP B 253      -6.737  -0.825 -71.836  1.00189.37           O  
ANISOU 5020  O   ASP B 253    29267  23537  19149  -1374  -1294    474       O  
ATOM   5021  CB  ASP B 253      -7.331  -0.048 -75.034  1.00196.73           C  
ANISOU 5021  CB  ASP B 253    30783  24540  19427  -1399  -1476    611       C  
ATOM   5022  CG  ASP B 253      -6.962   1.106 -75.961  1.00211.43           C  
ANISOU 5022  CG  ASP B 253    32866  26337  21133  -1298  -1414    734       C  
ATOM   5023  OD1 ASP B 253      -5.892   1.731 -75.746  1.00211.18           O  
ANISOU 5023  OD1 ASP B 253    32869  26153  21216  -1228  -1175    762       O  
ATOM   5024  OD2 ASP B 253      -7.771   1.427 -76.861  1.00220.77           O1-
ANISOU 5024  OD2 ASP B 253    34175  27623  22085  -1283  -1610    809       O1-
ATOM   5025  N   ARG B 254      -7.061  -2.649 -73.162  1.00186.71           N  
ANISOU 5025  N   ARG B 254    29208  23238  18495  -1612  -1358    317       N  
ATOM   5026  CA  ARG B 254      -7.454  -3.619 -72.135  1.00184.16           C  
ANISOU 5026  CA  ARG B 254    28683  22954  18334  -1681  -1397    220       C  
ATOM   5027  C   ARG B 254      -6.223  -3.936 -71.239  1.00183.34           C  
ANISOU 5027  C   ARG B 254    28518  22697  18448  -1645  -1139    160       C  
ATOM   5028  O   ARG B 254      -6.366  -4.371 -70.091  1.00181.38           O  
ANISOU 5028  O   ARG B 254    28066  22457  18394  -1641  -1139    115       O  
ATOM   5029  CB  ARG B 254      -7.997  -4.889 -72.813  1.00185.37           C  
ANISOU 5029  CB  ARG B 254    28972  23160  18298  -1860  -1488    107       C  
ATOM   5030  CG  ARG B 254      -9.084  -5.613 -72.015  1.00195.05           C  
ANISOU 5030  CG  ARG B 254    29977  24509  19625  -1940  -1656     46       C  
ATOM   5031  CD  ARG B 254     -10.457  -4.955 -72.110  1.00205.15           C  
ANISOU 5031  CD  ARG B 254    31102  25981  20864  -1913  -1945    138       C  
ATOM   5032  NE  ARG B 254     -10.936  -4.496 -70.802  1.00209.15           N  
ANISOU 5032  NE  ARG B 254    31299  26539  21630  -1813  -1991    189       N  
ATOM   5033  CZ  ARG B 254     -12.110  -3.908 -70.589  1.00220.66           C  
ANISOU 5033  CZ  ARG B 254    32561  28156  23124  -1762  -2211    274       C  
ATOM   5034  NH1 ARG B 254     -12.948  -3.699 -71.598  1.00211.90           N1+
ANISOU 5034  NH1 ARG B 254    31517  27186  21809  -1799  -2428    322       N1+
ATOM   5035  NH2 ARG B 254     -12.456  -3.524 -69.368  1.00200.59           N  
ANISOU 5035  NH2 ARG B 254    29761  25635  20821  -1670  -2215    315       N  
ATOM   5036  N   SER B 255      -5.011  -3.677 -71.793  1.00177.60           N  
ANISOU 5036  N   SER B 255    27968  21829  17683  -1614   -921    166       N  
ATOM   5037  CA  SER B 255      -3.693  -3.807 -71.164  1.00174.45           C  
ANISOU 5037  CA  SER B 255    27527  21283  17471  -1568   -668    127       C  
ATOM   5038  C   SER B 255      -3.534  -2.808 -70.026  1.00173.20           C  
ANISOU 5038  C   SER B 255    27130  21124  17552  -1441   -665    201       C  
ATOM   5039  O   SER B 255      -2.925  -3.147 -69.017  1.00170.83           O  
ANISOU 5039  O   SER B 255    26688  20766  17454  -1415   -559    152       O  
ATOM   5040  CB  SER B 255      -2.595  -3.586 -72.202  1.00178.76           C  
ANISOU 5040  CB  SER B 255    28322  21700  17901  -1566   -456    135       C  
ATOM   5041  OG  SER B 255      -1.316  -3.380 -71.631  1.00185.86           O  
ANISOU 5041  OG  SER B 255    29146  22471  18999  -1499   -223    126       O  
ATOM   5042  N   LEU B 256      -4.063  -1.580 -70.190  1.00167.77           N  
ANISOU 5042  N   LEU B 256    26413  20497  16835  -1358   -778    319       N  
ATOM   5043  CA  LEU B 256      -3.985  -0.530 -69.177  1.00164.94           C  
ANISOU 5043  CA  LEU B 256    25858  20131  16682  -1241   -777    395       C  
ATOM   5044  C   LEU B 256      -5.053  -0.729 -68.102  1.00165.03           C  
ANISOU 5044  C   LEU B 256    25634  20254  16817  -1227   -955    392       C  
ATOM   5045  O   LEU B 256      -4.872  -0.255 -66.980  1.00163.54           O  
ANISOU 5045  O   LEU B 256    25269  20039  16830  -1151   -924    412       O  
ATOM   5046  CB  LEU B 256      -4.096   0.870 -69.811  1.00165.96           C  
ANISOU 5046  CB  LEU B 256    26076  20259  16723  -1151   -799    527       C  
ATOM   5047  CG  LEU B 256      -2.979   1.276 -70.789  1.00171.51           C  
ANISOU 5047  CG  LEU B 256    27009  20831  17327  -1151   -592    544       C  
ATOM   5048  CD1 LEU B 256      -3.448   2.368 -71.722  1.00173.44           C  
ANISOU 5048  CD1 LEU B 256    27407  21100  17392  -1087   -666    670       C  
ATOM   5049  CD2 LEU B 256      -1.729   1.722 -70.066  1.00171.75           C  
ANISOU 5049  CD2 LEU B 256    26951  20732  17575  -1107   -374    531       C  
ATOM   5050  N   ARG B 257      -6.141  -1.462 -68.433  1.00160.02           N  
ANISOU 5050  N   ARG B 257    25000  19738  16061  -1309  -1132    360       N  
ATOM   5051  CA  ARG B 257      -7.234  -1.771 -67.504  1.00158.17           C  
ANISOU 5051  CA  ARG B 257    24548  19613  15936  -1315  -1294    349       C  
ATOM   5052  C   ARG B 257      -6.778  -2.757 -66.425  1.00157.72           C  
ANISOU 5052  C   ARG B 257    24385  19492  16050  -1354  -1187    240       C  
ATOM   5053  O   ARG B 257      -7.352  -2.793 -65.334  1.00155.61           O  
ANISOU 5053  O   ARG B 257    23923  19268  15936  -1323  -1253    240       O  
ATOM   5054  CB  ARG B 257      -8.444  -2.332 -68.270  1.00160.29           C  
ANISOU 5054  CB  ARG B 257    24855  20025  16022  -1415  -1504    334       C  
ATOM   5055  N   ARG B 258      -5.743  -3.553 -66.755  1.00152.97           N  
ANISOU 5055  N   ARG B 258    23925  18782  15415  -1413  -1014    153       N  
ATOM   5056  CA  ARG B 258      -5.102  -4.558 -65.908  1.00150.86           C  
ANISOU 5056  CA  ARG B 258    23604  18432  15283  -1439   -884     53       C  
ATOM   5057  C   ARG B 258      -4.313  -3.868 -64.790  1.00150.76           C  
ANISOU 5057  C   ARG B 258    23444  18347  15492  -1322   -782     87       C  
ATOM   5058  O   ARG B 258      -4.372  -4.305 -63.643  1.00149.04           O  
ANISOU 5058  O   ARG B 258    23083  18119  15426  -1303   -778     47       O  
ATOM   5059  CB  ARG B 258      -4.177  -5.443 -66.773  1.00152.81           C  
ANISOU 5059  CB  ARG B 258    24069  18580  15413  -1516   -716    -29       C  
ATOM   5060  CG  ARG B 258      -3.521  -6.620 -66.054  1.00165.72           C  
ANISOU 5060  CG  ARG B 258    25680  20126  17159  -1539   -574   -132       C  
ATOM   5061  CD  ARG B 258      -2.070  -6.810 -66.480  1.00181.49           C  
ANISOU 5061  CD  ARG B 258    27805  21987  19165  -1515   -338   -160       C  
ATOM   5062  NE  ARG B 258      -1.176  -5.847 -65.827  1.00194.97           N  
ANISOU 5062  NE  ARG B 258    29383  23642  21054  -1396   -248   -101       N  
ATOM   5063  CZ  ARG B 258       0.121  -5.716 -66.097  1.00209.55           C  
ANISOU 5063  CZ  ARG B 258    31287  25383  22951  -1357    -48   -105       C  
ATOM   5064  NH1 ARG B 258       0.698  -6.483 -67.016  1.00196.57           N  
ANISOU 5064  NH1 ARG B 258    29837  23663  21189  -1414     99   -160       N  
ATOM   5065  NH2 ARG B 258       0.850  -4.812 -65.452  1.00194.14           N1+
ANISOU 5065  NH2 ARG B 258    29198  23397  21170  -1267     11    -56       N1+
ATOM   5066  N   ILE B 259      -3.582  -2.792 -65.141  1.00146.06           N  
ANISOU 5066  N   ILE B 259    22894  17696  14905  -1250   -698    158       N  
ATOM   5067  CA  ILE B 259      -2.749  -1.984 -64.244  1.00144.09           C  
ANISOU 5067  CA  ILE B 259    22527  17375  14848  -1154   -600    192       C  
ATOM   5068  C   ILE B 259      -3.645  -1.226 -63.265  1.00145.21           C  
ANISOU 5068  C   ILE B 259    22490  17584  15098  -1083   -740    257       C  
ATOM   5069  O   ILE B 259      -3.281  -1.100 -62.101  1.00143.00           O  
ANISOU 5069  O   ILE B 259    22076  17265  14993  -1032   -701    242       O  
ATOM   5070  CB  ILE B 259      -1.828  -1.027 -65.072  1.00148.20           C  
ANISOU 5070  CB  ILE B 259    23169  17817  15321  -1121   -469    249       C  
ATOM   5071  CG1 ILE B 259      -0.996  -1.820 -66.114  1.00149.69           C  
ANISOU 5071  CG1 ILE B 259    23551  17933  15391  -1192   -315    186       C  
ATOM   5072  CG2 ILE B 259      -0.915  -0.172 -64.173  1.00147.78           C  
ANISOU 5072  CG2 ILE B 259    22993  17687  15468  -1044   -365    273       C  
ATOM   5073  CD1 ILE B 259      -0.700  -1.078 -67.417  1.00157.51           C  
ANISOU 5073  CD1 ILE B 259    24741  18886  16219  -1195   -247    248       C  
ATOM   5074  N   THR B 260      -4.819  -0.756 -63.730  1.00142.20           N  
ANISOU 5074  N   THR B 260    22112  17306  14610  -1078   -902    327       N  
ATOM   5075  CA  THR B 260      -5.780  -0.023 -62.909  1.00141.40           C  
ANISOU 5075  CA  THR B 260    21850  17274  14604  -1002  -1029    400       C  
ATOM   5076  C   THR B 260      -6.487  -0.994 -61.940  1.00145.03           C  
ANISOU 5076  C   THR B 260    22168  17783  15153  -1041  -1101    331       C  
ATOM   5077  O   THR B 260      -6.828  -0.582 -60.825  1.00144.31           O  
ANISOU 5077  O   THR B 260    21930  17694  15208   -973  -1127    358       O  
ATOM   5078  CB  THR B 260      -6.755   0.775 -63.788  1.00149.98           C  
ANISOU 5078  CB  THR B 260    22981  18457  15548   -970  -1172    506       C  
ATOM   5079  OG1 THR B 260      -6.006   1.512 -64.754  1.00149.94           O  
ANISOU 5079  OG1 THR B 260    23145  18386  15439   -945  -1080    558       O  
ATOM   5080  CG2 THR B 260      -7.589   1.773 -62.977  1.00148.97           C  
ANISOU 5080  CG2 THR B 260    22696  18375  15531   -860  -1265    602       C  
ATOM   5081  N   ARG B 261      -6.682  -2.275 -62.331  1.00141.32           N  
ANISOU 5081  N   ARG B 261    21759  17340  14598  -1152  -1115    240       N  
ATOM   5082  CA  ARG B 261      -7.297  -3.243 -61.411  1.00140.08           C  
ANISOU 5082  CA  ARG B 261    21486  17211  14527  -1197  -1157    169       C  
ATOM   5083  C   ARG B 261      -6.286  -3.678 -60.360  1.00141.85           C  
ANISOU 5083  C   ARG B 261    21673  17321  14902  -1163  -1010    107       C  
ATOM   5084  O   ARG B 261      -6.672  -3.966 -59.222  1.00140.87           O  
ANISOU 5084  O   ARG B 261    21426  17196  14901  -1140  -1029     85       O  
ATOM   5085  CB  ARG B 261      -7.866  -4.469 -62.138  1.00140.81           C  
ANISOU 5085  CB  ARG B 261    21665  17360  14479  -1337  -1214     87       C  
ATOM   5086  N   MET B 262      -4.992  -3.672 -60.748  1.00137.32           N  
ANISOU 5086  N   MET B 262    21203  16652  14319  -1152   -865     85       N  
ATOM   5087  CA  MET B 262      -3.832  -4.027 -59.933  1.00135.51           C  
ANISOU 5087  CA  MET B 262    20944  16318  14223  -1111   -724     33       C  
ATOM   5088  C   MET B 262      -3.611  -3.039 -58.787  1.00134.70           C  
ANISOU 5088  C   MET B 262    20704  16191  14286  -1008   -727     85       C  
ATOM   5089  O   MET B 262      -3.192  -3.458 -57.706  1.00133.10           O  
ANISOU 5089  O   MET B 262    20428  15939  14207   -974   -683     41       O  
ATOM   5090  CB  MET B 262      -2.565  -4.105 -60.812  1.00138.77           C  
ANISOU 5090  CB  MET B 262    21491  16652  14584  -1123   -570     11       C  
ATOM   5091  CG  MET B 262      -1.336  -4.609 -60.085  1.00142.06           C  
ANISOU 5091  CG  MET B 262    21868  16972  15135  -1082   -427    -45       C  
ATOM   5092  SD  MET B 262      -1.699  -6.119 -59.167  1.00146.39           S  
ANISOU 5092  SD  MET B 262    22382  17511  15730  -1109   -433   -136       S  
ATOM   5093  CE  MET B 262      -0.559  -5.960 -57.855  1.00142.11           C  
ANISOU 5093  CE  MET B 262    21713  16893  15389  -1001   -351   -145       C  
ATOM   5094  N   VAL B 263      -3.878  -1.741 -59.023  1.00128.87           N  
ANISOU 5094  N   VAL B 263    19948  15477  13539   -957   -777    177       N  
ATOM   5095  CA  VAL B 263      -3.680  -0.703 -58.016  1.00126.76           C  
ANISOU 5095  CA  VAL B 263    19576  15174  13411   -868   -773    227       C  
ATOM   5096  C   VAL B 263      -4.822  -0.788 -56.965  1.00129.12           C  
ANISOU 5096  C   VAL B 263    19754  15524  13781   -839   -880    239       C  
ATOM   5097  O   VAL B 263      -4.582  -0.504 -55.786  1.00127.41           O  
ANISOU 5097  O   VAL B 263    19456  15260  13695   -782   -859    235       O  
ATOM   5098  CB  VAL B 263      -3.472   0.709 -58.635  1.00130.81           C  
ANISOU 5098  CB  VAL B 263    20139  15672  13893   -823   -757    320       C  
ATOM   5099  CG1 VAL B 263      -4.705   1.226 -59.354  1.00131.83           C  
ANISOU 5099  CG1 VAL B 263    20292  15893  13904   -812   -883    404       C  
ATOM   5100  CG2 VAL B 263      -2.984   1.717 -57.607  1.00129.70           C  
ANISOU 5100  CG2 VAL B 263    19917  15465  13899   -751   -716    351       C  
ATOM   5101  N   LEU B 264      -6.023  -1.267 -57.374  1.00125.65           N  
ANISOU 5101  N   LEU B 264    19304  15178  13257   -887   -988    244       N  
ATOM   5102  CA  LEU B 264      -7.134  -1.467 -56.442  1.00124.44           C  
ANISOU 5102  CA  LEU B 264    19030  15074  13177   -871  -1071    249       C  
ATOM   5103  C   LEU B 264      -6.825  -2.651 -55.537  1.00123.12           C  
ANISOU 5103  C   LEU B 264    18844  14854  13083   -902  -1011    152       C  
ATOM   5104  O   LEU B 264      -7.076  -2.576 -54.333  1.00121.55           O  
ANISOU 5104  O   LEU B 264    18560  14627  12996   -851  -1010    151       O  
ATOM   5105  CB  LEU B 264      -8.477  -1.663 -57.169  1.00126.24           C  
ANISOU 5105  CB  LEU B 264    19233  15428  13306   -924  -1206    279       C  
ATOM   5106  CG  LEU B 264      -9.741  -1.695 -56.279  1.00131.66           C  
ANISOU 5106  CG  LEU B 264    19769  16175  14081   -902  -1289    301       C  
ATOM   5107  CD1 LEU B 264      -9.976  -0.355 -55.553  1.00131.65           C  
ANISOU 5107  CD1 LEU B 264    19686  16152  14182   -774  -1294    400       C  
ATOM   5108  CD2 LEU B 264     -10.958  -2.071 -57.089  1.00136.44           C  
ANISOU 5108  CD2 LEU B 264    20337  16915  14590   -978  -1425    312       C  
ATOM   5109  N   VAL B 265      -6.243  -3.725 -56.110  1.00117.22           N  
ANISOU 5109  N   VAL B 265    18193  14081  12264   -978   -948     72       N  
ATOM   5110  CA  VAL B 265      -5.832  -4.909 -55.347  1.00115.37           C  
ANISOU 5110  CA  VAL B 265    17969  13783  12086   -997   -873    -18       C  
ATOM   5111  C   VAL B 265      -4.871  -4.454 -54.237  1.00117.13           C  
ANISOU 5111  C   VAL B 265    18142  13921  12443   -899   -805    -12       C  
ATOM   5112  O   VAL B 265      -5.133  -4.720 -53.061  1.00116.47           O  
ANISOU 5112  O   VAL B 265    17997  13809  12446   -862   -809    -30       O  
ATOM   5113  CB  VAL B 265      -5.199  -6.006 -56.251  1.00119.04           C  
ANISOU 5113  CB  VAL B 265    18567  14216  12448  -1078   -791    -94       C  
ATOM   5114  CG1 VAL B 265      -4.527  -7.098 -55.423  1.00117.62           C  
ANISOU 5114  CG1 VAL B 265    18406  13948  12337  -1063   -689   -172       C  
ATOM   5115  CG2 VAL B 265      -6.232  -6.615 -57.182  1.00120.24           C  
ANISOU 5115  CG2 VAL B 265    18775  14449  12463  -1195   -870   -118       C  
ATOM   5116  N   VAL B 266      -3.813  -3.702 -54.628  1.00111.49           N  
ANISOU 5116  N   VAL B 266    17454  13167  11739   -863   -747     14       N  
ATOM   5117  CA  VAL B 266      -2.753  -3.162 -53.781  1.00109.57           C  
ANISOU 5117  CA  VAL B 266    17164  12852  11614   -788   -689     17       C  
ATOM   5118  C   VAL B 266      -3.320  -2.349 -52.595  1.00113.11           C  
ANISOU 5118  C   VAL B 266    17523  13297  12156   -722   -753     61       C  
ATOM   5119  O   VAL B 266      -2.903  -2.605 -51.463  1.00113.70           O  
ANISOU 5119  O   VAL B 266    17562  13321  12320   -677   -733     27       O  
ATOM   5120  CB  VAL B 266      -1.773  -2.331 -54.646  1.00113.07           C  
ANISOU 5120  CB  VAL B 266    17649  13271  12042   -786   -623     48       C  
ATOM   5121  CG1 VAL B 266      -0.957  -1.351 -53.819  1.00111.85           C  
ANISOU 5121  CG1 VAL B 266    17426  13063  12010   -723   -597     69       C  
ATOM   5122  CG2 VAL B 266      -0.858  -3.245 -55.437  1.00113.55           C  
ANISOU 5122  CG2 VAL B 266    17792  13299  12054   -828   -517    -11       C  
ATOM   5123  N   VAL B 267      -4.270  -1.409 -52.847  1.00107.28           N  
ANISOU 5123  N   VAL B 267    16759  12611  11392   -709   -825    137       N  
ATOM   5124  CA  VAL B 267      -4.855  -0.538 -51.816  1.00105.01           C  
ANISOU 5124  CA  VAL B 267    16402  12311  11187   -640   -867    188       C  
ATOM   5125  C   VAL B 267      -5.820  -1.304 -50.872  1.00106.17           C  
ANISOU 5125  C   VAL B 267    16499  12471  11370   -637   -903    160       C  
ATOM   5126  O   VAL B 267      -5.828  -1.024 -49.668  1.00104.32           O  
ANISOU 5126  O   VAL B 267    16232  12185  11221   -580   -895    161       O  
ATOM   5127  CB  VAL B 267      -5.511   0.723 -52.424  1.00109.31           C  
ANISOU 5127  CB  VAL B 267    16942  12896  11695   -610   -915    287       C  
ATOM   5128  CG1 VAL B 267      -6.858   0.436 -53.098  1.00110.00           C  
ANISOU 5128  CG1 VAL B 267    17005  13088  11703   -640  -1005    323       C  
ATOM   5129  CG2 VAL B 267      -5.611   1.853 -51.394  1.00108.64           C  
ANISOU 5129  CG2 VAL B 267    16818  12758  11704   -529   -911    338       C  
ATOM   5130  N   VAL B 268      -6.604  -2.270 -51.401  1.00102.23           N  
ANISOU 5130  N   VAL B 268    16003  12034  10804   -707   -936    131       N  
ATOM   5131  CA  VAL B 268      -7.520  -3.058 -50.575  1.00101.22           C  
ANISOU 5131  CA  VAL B 268    15831  11913  10714   -721   -951     99       C  
ATOM   5132  C   VAL B 268      -6.686  -3.976 -49.659  1.00105.63           C  
ANISOU 5132  C   VAL B 268    16433  12383  11320   -706   -875     21       C  
ATOM   5133  O   VAL B 268      -6.978  -4.079 -48.456  1.00105.91           O  
ANISOU 5133  O   VAL B 268    16444  12372  11426   -660   -863     13       O  
ATOM   5134  CB  VAL B 268      -8.559  -3.826 -51.422  1.00104.85           C  
ANISOU 5134  CB  VAL B 268    16281  12466  11093   -818  -1008     81       C  
ATOM   5135  CG1 VAL B 268      -9.417  -4.729 -50.536  1.00104.18           C  
ANISOU 5135  CG1 VAL B 268    16153  12373  11058   -847   -998     36       C  
ATOM   5136  CG2 VAL B 268      -9.447  -2.855 -52.192  1.00105.39           C  
ANISOU 5136  CG2 VAL B 268    16290  12631  11121   -809  -1103    171       C  
ATOM   5137  N   ALA B 269      -5.614  -4.587 -50.226  1.00101.59           N  
ANISOU 5137  N   ALA B 269    15990  11841  10766   -734   -819    -30       N  
ATOM   5138  CA  ALA B 269      -4.666  -5.436 -49.500  1.00100.74           C  
ANISOU 5138  CA  ALA B 269    15924  11654  10699   -702   -747    -94       C  
ATOM   5139  C   ALA B 269      -3.959  -4.621 -48.437  1.00103.40           C  
ANISOU 5139  C   ALA B 269    16225  11935  11128   -610   -747    -72       C  
ATOM   5140  O   ALA B 269      -3.878  -5.061 -47.292  1.00102.65           O  
ANISOU 5140  O   ALA B 269    16137  11786  11082   -562   -733    -99       O  
ATOM   5141  CB  ALA B 269      -3.651  -6.028 -50.460  1.00101.87           C  
ANISOU 5141  CB  ALA B 269    16136  11783  10788   -737   -680   -135       C  
ATOM   5142  N   PHE B 270      -3.505  -3.400 -48.806  1.00 99.02           N  
ANISOU 5142  N   PHE B 270    15642  11390  10590   -590   -762    -21       N  
ATOM   5143  CA  PHE B 270      -2.824  -2.492 -47.894  1.00 98.05           C  
ANISOU 5143  CA  PHE B 270    15490  11216  10549   -524   -767     -4       C  
ATOM   5144  C   PHE B 270      -3.702  -2.176 -46.685  1.00101.09           C  
ANISOU 5144  C   PHE B 270    15857  11576  10976   -477   -804     18       C  
ATOM   5145  O   PHE B 270      -3.220  -2.300 -45.562  1.00 99.96           O  
ANISOU 5145  O   PHE B 270    15724  11373  10883   -428   -800    -10       O  
ATOM   5146  CB  PHE B 270      -2.389  -1.197 -48.604  1.00100.10           C  
ANISOU 5146  CB  PHE B 270    15737  11486  10810   -530   -766     48       C  
ATOM   5147  CG  PHE B 270      -1.504  -0.300 -47.772  1.00101.55           C  
ANISOU 5147  CG  PHE B 270    15897  11612  11077   -487   -762     50       C  
ATOM   5148  CD1 PHE B 270      -0.121  -0.468 -47.765  1.00104.21           C  
ANISOU 5148  CD1 PHE B 270    16217  11921  11458   -488   -722      7       C  
ATOM   5149  CD2 PHE B 270      -2.050   0.698 -46.979  1.00104.23           C  
ANISOU 5149  CD2 PHE B 270    16229  11923  11451   -449   -796     93       C  
ATOM   5150  CE1 PHE B 270       0.700   0.347 -46.981  1.00106.96           C  
ANISOU 5150  CE1 PHE B 270    16532  12224  11885   -465   -733      0       C  
ATOM   5151  CE2 PHE B 270      -1.230   1.508 -46.189  1.00105.21           C  
ANISOU 5151  CE2 PHE B 270    16346  11988  11640   -426   -795     84       C  
ATOM   5152  CZ  PHE B 270       0.140   1.330 -46.201  1.00104.85           C  
ANISOU 5152  CZ  PHE B 270    16275  11926  11638   -441   -772     35       C  
ATOM   5153  N   VAL B 271      -4.981  -1.813 -46.907  1.00 98.15           N  
ANISOU 5153  N   VAL B 271    15459  11249  10583   -490   -837     68       N  
ATOM   5154  CA  VAL B 271      -5.912  -1.446 -45.833  1.00 98.09           C  
ANISOU 5154  CA  VAL B 271    15432  11215  10622   -442   -852     97       C  
ATOM   5155  C   VAL B 271      -6.228  -2.637 -44.933  1.00102.63           C  
ANISOU 5155  C   VAL B 271    16034  11753  11209   -439   -825     41       C  
ATOM   5156  O   VAL B 271      -6.073  -2.520 -43.714  1.00101.48           O  
ANISOU 5156  O   VAL B 271    15917  11535  11106   -381   -812     31       O  
ATOM   5157  CB  VAL B 271      -7.206  -0.800 -46.379  1.00102.64           C  
ANISOU 5157  CB  VAL B 271    15954  11860  11186   -447   -889    172       C  
ATOM   5158  CG1 VAL B 271      -8.288  -0.716 -45.305  1.00102.25           C  
ANISOU 5158  CG1 VAL B 271    15876  11785  11191   -403   -881    195       C  
ATOM   5159  CG2 VAL B 271      -6.914   0.578 -46.936  1.00103.02           C  
ANISOU 5159  CG2 VAL B 271    16001  11913  11230   -418   -902    241       C  
ATOM   5160  N   VAL B 272      -6.650  -3.782 -45.529  1.00100.54           N  
ANISOU 5160  N   VAL B 272    15775  11528  10897   -505   -813      2       N  
ATOM   5161  CA  VAL B 272      -7.029  -4.992 -44.786  1.00100.93           C  
ANISOU 5161  CA  VAL B 272    15864  11534  10950   -515   -769    -53       C  
ATOM   5162  C   VAL B 272      -5.867  -5.490 -43.891  1.00107.65           C  
ANISOU 5162  C   VAL B 272    16787  12298  11818   -453   -733   -100       C  
ATOM   5163  O   VAL B 272      -6.137  -5.996 -42.801  1.00107.33           O  
ANISOU 5163  O   VAL B 272    16793  12193  11796   -415   -702   -120       O  
ATOM   5164  CB  VAL B 272      -7.577  -6.103 -45.733  1.00104.26           C  
ANISOU 5164  CB  VAL B 272    16294  12010  11309   -617   -757    -94       C  
ATOM   5165  CG1 VAL B 272      -7.502  -7.494 -45.128  1.00103.51           C  
ANISOU 5165  CG1 VAL B 272    16277  11846  11204   -631   -686   -166       C  
ATOM   5166  CG2 VAL B 272      -8.983  -5.777 -46.206  1.00104.61           C  
ANISOU 5166  CG2 VAL B 272    16254  12140  11351   -671   -806    -52       C  
ATOM   5167  N   CYS B 273      -4.604  -5.292 -44.320  1.00106.06           N  
ANISOU 5167  N   CYS B 273    16590  12095  11614   -437   -737   -111       N  
ATOM   5168  CA  CYS B 273      -3.410  -5.734 -43.595  1.00106.66           C  
ANISOU 5168  CA  CYS B 273    16707  12108  11712   -373   -719   -150       C  
ATOM   5169  C   CYS B 273      -2.909  -4.729 -42.594  1.00108.55           C  
ANISOU 5169  C   CYS B 273    16935  12308  12002   -304   -763   -128       C  
ATOM   5170  O   CYS B 273      -2.295  -5.132 -41.605  1.00108.91           O  
ANISOU 5170  O   CYS B 273    17022  12296  12061   -241   -766   -156       O  
ATOM   5171  CB  CYS B 273      -2.298  -6.074 -44.573  1.00108.37           C  
ANISOU 5171  CB  CYS B 273    16917  12346  11912   -392   -693   -174       C  
ATOM   5172  SG  CYS B 273      -2.659  -7.482 -45.647  1.00113.60           S  
ANISOU 5172  SG  CYS B 273    17639  13028  12497   -472   -625   -219       S  
ATOM   5173  N   TRP B 274      -3.076  -3.437 -42.872  1.00102.90           N  
ANISOU 5173  N   TRP B 274    16172  11617  11307   -317   -796    -79       N  
ATOM   5174  CA  TRP B 274      -2.507  -2.426 -42.006  1.00101.86           C  
ANISOU 5174  CA  TRP B 274    16043  11442  11219   -270   -832    -67       C  
ATOM   5175  C   TRP B 274      -3.491  -1.798 -41.024  1.00103.63           C  
ANISOU 5175  C   TRP B 274    16300  11620  11453   -235   -838    -34       C  
ATOM   5176  O   TRP B 274      -3.061  -1.498 -39.910  1.00103.05           O  
ANISOU 5176  O   TRP B 274    16275  11484  11397   -187   -860    -49       O  
ATOM   5177  CB  TRP B 274      -1.814  -1.353 -42.836  1.00100.98           C  
ANISOU 5177  CB  TRP B 274    15880  11361  11128   -302   -843    -42       C  
ATOM   5178  CG  TRP B 274      -0.456  -1.795 -43.295  1.00102.20           C  
ANISOU 5178  CG  TRP B 274    16004  11528  11299   -311   -832    -83       C  
ATOM   5179  CD1 TRP B 274      -0.085  -2.140 -44.563  1.00105.35           C  
ANISOU 5179  CD1 TRP B 274    16379  11972  11677   -357   -790    -88       C  
ATOM   5180  CD2 TRP B 274       0.693  -2.018 -42.466  1.00102.16           C  
ANISOU 5180  CD2 TRP B 274    15988  11491  11337   -266   -858   -125       C  
ATOM   5181  NE1 TRP B 274       1.242  -2.512 -44.584  1.00105.11           N  
ANISOU 5181  NE1 TRP B 274    16316  11935  11687   -341   -773   -126       N  
ATOM   5182  CE2 TRP B 274       1.740  -2.453 -43.309  1.00106.66           C  
ANISOU 5182  CE2 TRP B 274    16508  12092  11927   -283   -823   -149       C  
ATOM   5183  CE3 TRP B 274       0.947  -1.865 -41.090  1.00103.21           C  
ANISOU 5183  CE3 TRP B 274    16152  11573  11490   -211   -912   -143       C  
ATOM   5184  CZ2 TRP B 274       3.016  -2.746 -42.821  1.00106.60           C  
ANISOU 5184  CZ2 TRP B 274    16455  12076  11973   -241   -844   -185       C  
ATOM   5185  CZ3 TRP B 274       2.202  -2.175 -40.605  1.00105.20           C  
ANISOU 5185  CZ3 TRP B 274    16371  11820  11779   -174   -949   -182       C  
ATOM   5186  CH2 TRP B 274       3.226  -2.588 -41.467  1.00106.49           C  
ANISOU 5186  CH2 TRP B 274    16458  12025  11978   -187   -918   -201       C  
ATOM   5187  N   ALA B 275      -4.787  -1.608 -41.397  1.00 98.91           N  
ANISOU 5187  N   ALA B 275    15679  11053  10848   -257   -819     10       N  
ATOM   5188  CA  ALA B 275      -5.794  -1.027 -40.489  1.00 97.75           C  
ANISOU 5188  CA  ALA B 275    15557  10860  10723   -216   -803     48       C  
ATOM   5189  C   ALA B 275      -5.863  -1.793 -39.129  1.00100.45           C  
ANISOU 5189  C   ALA B 275    15987  11120  11061   -168   -776      8       C  
ATOM   5190  O   ALA B 275      -5.725  -1.124 -38.105  1.00 98.47           O  
ANISOU 5190  O   ALA B 275    15798  10795  10819   -119   -780     14       O  
ATOM   5191  CB  ALA B 275      -7.168  -0.963 -41.153  1.00 98.43           C  
ANISOU 5191  CB  ALA B 275    15579  11008  10812   -243   -787     99       C  
ATOM   5192  N   PRO B 276      -5.931  -3.161 -39.088  1.00 98.31           N  
ANISOU 5192  N   PRO B 276    15743  10847  10765   -181   -747    -38       N  
ATOM   5193  CA  PRO B 276      -5.961  -3.873 -37.793  1.00 98.64           C  
ANISOU 5193  CA  PRO B 276    15890  10797  10791   -126   -714    -71       C  
ATOM   5194  C   PRO B 276      -4.907  -3.441 -36.749  1.00103.37           C  
ANISOU 5194  C   PRO B 276    16566  11329  11381    -58   -762    -89       C  
ATOM   5195  O   PRO B 276      -5.283  -3.097 -35.619  1.00102.86           O  
ANISOU 5195  O   PRO B 276    16588  11185  11308    -11   -745    -80       O  
ATOM   5196  CB  PRO B 276      -5.727  -5.320 -38.213  1.00100.33           C  
ANISOU 5196  CB  PRO B 276    16122  11024  10973   -152   -682   -119       C  
ATOM   5197  CG  PRO B 276      -6.396  -5.418 -39.517  1.00104.70           C  
ANISOU 5197  CG  PRO B 276    16585  11667  11528   -239   -674   -105       C  
ATOM   5198  CD  PRO B 276      -6.080  -4.129 -40.201  1.00100.12           C  
ANISOU 5198  CD  PRO B 276    15929  11144  10969   -248   -731    -61       C  
ATOM   5199  N   ILE B 277      -3.605  -3.454 -37.116  1.00 99.91           N  
ANISOU 5199  N   ILE B 277    16095  10922  10943    -57   -820   -115       N  
ATOM   5200  CA  ILE B 277      -2.540  -3.070 -36.194  1.00 99.58           C  
ANISOU 5200  CA  ILE B 277    16101  10836  10897     -5   -887   -137       C  
ATOM   5201  C   ILE B 277      -2.577  -1.560 -35.929  1.00105.11           C  
ANISOU 5201  C   ILE B 277    16799  11518  11621    -19   -918   -109       C  
ATOM   5202  O   ILE B 277      -2.315  -1.165 -34.800  1.00106.02           O  
ANISOU 5202  O   ILE B 277    17003  11565  11715     22   -953   -122       O  
ATOM   5203  CB  ILE B 277      -1.124  -3.565 -36.618  1.00102.33           C  
ANISOU 5203  CB  ILE B 277    16395  11229  11258      3   -936   -173       C  
ATOM   5204  CG1 ILE B 277      -0.075  -3.408 -35.479  1.00102.85           C  
ANISOU 5204  CG1 ILE B 277    16508  11255  11315     67  -1022   -201       C  
ATOM   5205  CG2 ILE B 277      -0.631  -2.942 -37.924  1.00102.91           C  
ANISOU 5205  CG2 ILE B 277    16348  11380  11373    -64   -942   -161       C  
ATOM   5206  CD1 ILE B 277      -0.299  -4.309 -34.233  1.00107.43           C  
ANISOU 5206  CD1 ILE B 277    17228  11756  11833    153  -1018   -217       C  
ATOM   5207  N   HIS B 278      -2.932  -0.724 -36.921  1.00102.26           N  
ANISOU 5207  N   HIS B 278    16358  11207  11291    -72   -902    -69       N  
ATOM   5208  CA  HIS B 278      -2.986   0.723 -36.688  1.00102.82           C  
ANISOU 5208  CA  HIS B 278    16444  11243  11380    -80   -913    -39       C  
ATOM   5209  C   HIS B 278      -4.113   1.066 -35.697  1.00109.70           C  
ANISOU 5209  C   HIS B 278    17410  12033  12236    -36   -862    -10       C  
ATOM   5210  O   HIS B 278      -3.918   1.950 -34.861  1.00109.37           O  
ANISOU 5210  O   HIS B 278    17450  11918  12186    -19   -875    -11       O  
ATOM   5211  CB  HIS B 278      -3.109   1.522 -37.993  1.00102.93           C  
ANISOU 5211  CB  HIS B 278    16366  11320  11421   -133   -897      6       C  
ATOM   5212  CG  HIS B 278      -1.798   1.694 -38.693  1.00106.12           C  
ANISOU 5212  CG  HIS B 278    16706  11769  11848   -177   -936    -23       C  
ATOM   5213  ND1 HIS B 278      -0.764   2.410 -38.120  1.00108.29           N  
ANISOU 5213  ND1 HIS B 278    16997  12006  12142   -188   -984    -54       N  
ATOM   5214  CD2 HIS B 278      -1.390   1.230 -39.897  1.00107.63           C  
ANISOU 5214  CD2 HIS B 278    16818  12033  12043   -216   -925    -26       C  
ATOM   5215  CE1 HIS B 278       0.235   2.361 -38.990  1.00107.78           C  
ANISOU 5215  CE1 HIS B 278    16845  11996  12108   -232   -995    -73       C  
ATOM   5216  NE2 HIS B 278      -0.098   1.670 -40.079  1.00107.72           N  
ANISOU 5216  NE2 HIS B 278    16788  12051  12090   -246   -954    -55       N  
ATOM   5217  N   ILE B 279      -5.242   0.306 -35.741  1.00107.76           N  
ANISOU 5217  N   ILE B 279    17162  11794  11988    -23   -798     10       N  
ATOM   5218  CA  ILE B 279      -6.396   0.462 -34.843  1.00108.12           C  
ANISOU 5218  CA  ILE B 279    17284  11762  12033     20   -724     38       C  
ATOM   5219  C   ILE B 279      -6.010  -0.038 -33.443  1.00114.19           C  
ANISOU 5219  C   ILE B 279    18201  12433  12752     72   -728     -7       C  
ATOM   5220  O   ILE B 279      -6.350   0.603 -32.446  1.00113.91           O  
ANISOU 5220  O   ILE B 279    18276  12304  12699    111   -695      4       O  
ATOM   5221  CB  ILE B 279      -7.648  -0.266 -35.414  1.00110.79           C  
ANISOU 5221  CB  ILE B 279    17548  12152  12397      1   -657     66       C  
ATOM   5222  CG1 ILE B 279      -8.171   0.466 -36.669  1.00110.97           C  
ANISOU 5222  CG1 ILE B 279    17440  12265  12457    -35   -664    125       C  
ATOM   5223  CG2 ILE B 279      -8.759  -0.380 -34.366  1.00111.82           C  
ANISOU 5223  CG2 ILE B 279    17756  12196  12536     47   -562     84       C  
ATOM   5224  CD1 ILE B 279      -8.936  -0.381 -37.649  1.00118.38           C  
ANISOU 5224  CD1 ILE B 279    18273  13298  13406    -86   -653    133       C  
ATOM   5225  N   PHE B 280      -5.268  -1.161 -33.385  1.00112.37           N  
ANISOU 5225  N   PHE B 280    17983  12221  12491     79   -767    -57       N  
ATOM   5226  CA  PHE B 280      -4.796  -1.779 -32.148  1.00112.96           C  
ANISOU 5226  CA  PHE B 280    18200  12213  12505    140   -787    -97       C  
ATOM   5227  C   PHE B 280      -3.822  -0.894 -31.355  1.00116.45           C  
ANISOU 5227  C   PHE B 280    18718  12613  12917    160   -879   -119       C  
ATOM   5228  O   PHE B 280      -3.977  -0.800 -30.143  1.00117.46           O  
ANISOU 5228  O   PHE B 280    19000  12642  12988    209   -870   -128       O  
ATOM   5229  CB  PHE B 280      -4.137  -3.133 -32.420  1.00115.16           C  
ANISOU 5229  CB  PHE B 280    18464  12529  12762    154   -810   -135       C  
ATOM   5230  CG  PHE B 280      -4.608  -4.173 -31.442  1.00117.78           C  
ANISOU 5230  CG  PHE B 280    18940  12773  13040    212   -744   -149       C  
ATOM   5231  CD1 PHE B 280      -4.098  -4.218 -30.149  1.00121.81           C  
ANISOU 5231  CD1 PHE B 280    19606  13195  13480    287   -786   -169       C  
ATOM   5232  CD2 PHE B 280      -5.601  -5.078 -31.793  1.00121.20           C  
ANISOU 5232  CD2 PHE B 280    19362  13202  13485    187   -637   -144       C  
ATOM   5233  CE1 PHE B 280      -4.561  -5.163 -29.231  1.00123.75           C  
ANISOU 5233  CE1 PHE B 280    20010  13346  13665    348   -712   -177       C  
ATOM   5234  CE2 PHE B 280      -6.059  -6.028 -30.875  1.00125.04           C  
ANISOU 5234  CE2 PHE B 280    19995  13591  13922    236   -556   -158       C  
ATOM   5235  CZ  PHE B 280      -5.534  -6.065 -29.599  1.00123.55           C  
ANISOU 5235  CZ  PHE B 280    19975  13310  13660    321   -588   -171       C  
ATOM   5236  N   VAL B 281      -2.831  -0.259 -32.012  1.00111.32           N  
ANISOU 5236  N   VAL B 281    17968  12030  12299    115   -962   -130       N  
ATOM   5237  CA  VAL B 281      -1.860   0.609 -31.331  1.00111.04           C  
ANISOU 5237  CA  VAL B 281    17984  11962  12244    108  -1057   -161       C  
ATOM   5238  C   VAL B 281      -2.599   1.854 -30.744  1.00116.53           C  
ANISOU 5238  C   VAL B 281    18782  12568  12927    101  -1004   -133       C  
ATOM   5239  O   VAL B 281      -2.211   2.322 -29.670  1.00117.42           O  
ANISOU 5239  O   VAL B 281    19027  12603  12984    115  -1053   -163       O  
ATOM   5240  CB  VAL B 281      -0.650   0.989 -32.232  1.00113.84           C  
ANISOU 5240  CB  VAL B 281    18193  12408  12653     49  -1137   -182       C  
ATOM   5241  CG1 VAL B 281       0.423   1.711 -31.434  1.00113.99           C  
ANISOU 5241  CG1 VAL B 281    18255  12401  12653     31  -1248   -226       C  
ATOM   5242  CG2 VAL B 281      -0.041  -0.246 -32.887  1.00113.36           C  
ANISOU 5242  CG2 VAL B 281    18035  12427  12610     66  -1157   -200       C  
ATOM   5243  N   ILE B 282      -3.695   2.332 -31.409  1.00112.84           N  
ANISOU 5243  N   ILE B 282    18265  12106  12505     86   -903    -75       N  
ATOM   5244  CA  ILE B 282      -4.539   3.459 -30.954  1.00112.85           C  
ANISOU 5244  CA  ILE B 282    18355  12018  12506     97   -824    -35       C  
ATOM   5245  C   ILE B 282      -5.273   3.044 -29.666  1.00118.12           C  
ANISOU 5245  C   ILE B 282    19191  12573  13115    164   -756    -37       C  
ATOM   5246  O   ILE B 282      -5.173   3.730 -28.644  1.00118.16           O  
ANISOU 5246  O   ILE B 282    19355  12473  13067    181   -754    -53       O  
ATOM   5247  CB  ILE B 282      -5.561   3.929 -32.057  1.00115.21           C  
ANISOU 5247  CB  ILE B 282    18535  12368  12873     86   -738     39       C  
ATOM   5248  CG1 ILE B 282      -4.872   4.455 -33.360  1.00115.58           C  
ANISOU 5248  CG1 ILE B 282    18444  12509  12963     22   -790     49       C  
ATOM   5249  CG2 ILE B 282      -6.595   4.941 -31.526  1.00115.04           C  
ANISOU 5249  CG2 ILE B 282    18603  12247  12859    126   -632     94       C  
ATOM   5250  CD1 ILE B 282      -3.889   5.651 -33.287  1.00125.48           C  
ANISOU 5250  CD1 ILE B 282    19734  13729  14216    -26   -839     27       C  
ATOM   5251  N   VAL B 283      -6.011   1.913 -29.737  1.00114.94           N  
ANISOU 5251  N   VAL B 283    18764  12187  12720    195   -692    -26       N  
ATOM   5252  CA  VAL B 283      -6.818   1.359 -28.646  1.00115.39           C  
ANISOU 5252  CA  VAL B 283    18971  12140  12734    255   -598    -24       C  
ATOM   5253  C   VAL B 283      -5.930   1.042 -27.417  1.00121.98           C  
ANISOU 5253  C   VAL B 283    19988  12896  13464    293   -675    -81       C  
ATOM   5254  O   VAL B 283      -6.315   1.397 -26.306  1.00122.31           O  
ANISOU 5254  O   VAL B 283    20214  12814  13446    334   -619    -81       O  
ATOM   5255  CB  VAL B 283      -7.642   0.136 -29.133  1.00118.21           C  
ANISOU 5255  CB  VAL B 283    19244  12543  13127    256   -520    -10       C  
ATOM   5256  CG1 VAL B 283      -8.278  -0.620 -27.971  1.00118.47           C  
ANISOU 5256  CG1 VAL B 283    19444  12461  13110    312   -420    -20       C  
ATOM   5257  CG2 VAL B 283      -8.714   0.566 -30.133  1.00117.58           C  
ANISOU 5257  CG2 VAL B 283    19006  12530  13140    225   -446     51       C  
ATOM   5258  N   TRP B 284      -4.733   0.447 -27.627  1.00119.97           N  
ANISOU 5258  N   TRP B 284    19684  12711  13186    284   -805   -125       N  
ATOM   5259  CA  TRP B 284      -3.781   0.106 -26.566  1.00121.13           C  
ANISOU 5259  CA  TRP B 284    19976  12811  13237    328   -911   -175       C  
ATOM   5260  C   TRP B 284      -3.357   1.355 -25.796  1.00126.59           C  
ANISOU 5260  C   TRP B 284    20788  13433  13879    307   -972   -196       C  
ATOM   5261  O   TRP B 284      -3.273   1.306 -24.566  1.00127.41           O  
ANISOU 5261  O   TRP B 284    21095  13435  13878    354   -991   -219       O  
ATOM   5262  CB  TRP B 284      -2.545  -0.588 -27.153  1.00120.19           C  
ANISOU 5262  CB  TRP B 284    19729  12804  13134    321  -1040   -208       C  
ATOM   5263  CG  TRP B 284      -1.821  -1.456 -26.170  1.00122.40           C  
ANISOU 5263  CG  TRP B 284    20138  13048  13319    399  -1125   -242       C  
ATOM   5264  CD1 TRP B 284      -0.919  -1.060 -25.229  1.00126.37           C  
ANISOU 5264  CD1 TRP B 284    20747  13522  13745    419  -1260   -279       C  
ATOM   5265  CD2 TRP B 284      -1.936  -2.871 -26.048  1.00122.44           C  
ANISOU 5265  CD2 TRP B 284    20185  13044  13292    469  -1085   -240       C  
ATOM   5266  NE1 TRP B 284      -0.471  -2.146 -24.517  1.00126.54           N  
ANISOU 5266  NE1 TRP B 284    20873  13523  13685    511  -1315   -294       N  
ATOM   5267  CE2 TRP B 284      -1.086  -3.271 -24.993  1.00127.38           C  
ANISOU 5267  CE2 TRP B 284    20951  13633  13817    547  -1199   -268       C  
ATOM   5268  CE3 TRP B 284      -2.687  -3.847 -26.716  1.00123.45           C  
ANISOU 5268  CE3 TRP B 284    20257  13188  13461    470   -963   -219       C  
ATOM   5269  CZ2 TRP B 284      -0.962  -4.604 -24.599  1.00127.37           C  
ANISOU 5269  CZ2 TRP B 284    21040  13602  13755    641  -1184   -267       C  
ATOM   5270  CZ3 TRP B 284      -2.565  -5.171 -26.322  1.00125.47           C  
ANISOU 5270  CZ3 TRP B 284    20606  13408  13660    546   -939   -228       C  
ATOM   5271  CH2 TRP B 284      -1.706  -5.539 -25.282  1.00127.16           C  
ANISOU 5271  CH2 TRP B 284    20963  13577  13773    638  -1043   -247       C  
ATOM   5272  N   THR B 285      -3.132   2.475 -26.527  1.00123.28           N  
ANISOU 5272  N   THR B 285    20258  13058  13525    234   -992   -187       N  
ATOM   5273  CA  THR B 285      -2.723   3.786 -26.017  1.00124.32           C  
ANISOU 5273  CA  THR B 285    20486  13127  13625    188  -1036   -210       C  
ATOM   5274  C   THR B 285      -3.774   4.342 -25.037  1.00130.11           C  
ANISOU 5274  C   THR B 285    21430  13705  14299    228   -906   -185       C  
ATOM   5275  O   THR B 285      -3.420   4.787 -23.941  1.00129.21           O  
ANISOU 5275  O   THR B 285    21511  13494  14087    230   -952   -225       O  
ATOM   5276  CB  THR B 285      -2.481   4.746 -27.218  1.00131.64           C  
ANISOU 5276  CB  THR B 285    21241  14127  14648    107  -1037   -190       C  
ATOM   5277  OG1 THR B 285      -1.324   4.314 -27.948  1.00131.19           O  
ANISOU 5277  OG1 THR B 285    21017  14194  14634     66  -1158   -224       O  
ATOM   5278  CG2 THR B 285      -2.324   6.233 -26.808  1.00130.06           C  
ANISOU 5278  CG2 THR B 285    21151  13839  14427     51  -1031   -203       C  
ATOM   5279  N   LEU B 286      -5.053   4.295 -25.434  1.00129.20           N  
ANISOU 5279  N   LEU B 286    21274  13570  14245    260   -746   -121       N  
ATOM   5280  CA  LEU B 286      -6.173   4.846 -24.673  1.00130.94           C  
ANISOU 5280  CA  LEU B 286    21659  13650  14441    305   -588    -84       C  
ATOM   5281  C   LEU B 286      -6.786   3.818 -23.697  1.00139.12           C  
ANISOU 5281  C   LEU B 286    22848  14600  15409    381   -508    -87       C  
ATOM   5282  O   LEU B 286      -6.593   3.955 -22.488  1.00140.39           O  
ANISOU 5282  O   LEU B 286    23244  14642  15457    410   -514   -120       O  
ATOM   5283  CB  LEU B 286      -7.248   5.393 -25.640  1.00130.44           C  
ANISOU 5283  CB  LEU B 286    21448  13618  14493    306   -457     -6       C  
ATOM   5284  CG  LEU B 286      -6.756   6.164 -26.887  1.00134.02           C  
ANISOU 5284  CG  LEU B 286    21722  14177  15024    241   -520     11       C  
ATOM   5285  CD1 LEU B 286      -7.801   6.152 -27.983  1.00133.73           C  
ANISOU 5285  CD1 LEU B 286    21504  14216  15091    257   -425     91       C  
ATOM   5286  CD2 LEU B 286      -6.343   7.573 -26.549  1.00135.49           C  
ANISOU 5286  CD2 LEU B 286    22025  14276  15179    204   -525      0       C  
ATOM   5287  N   VAL B 287      -7.509   2.804 -24.218  1.00137.32           N  
ANISOU 5287  N   VAL B 287    22503  14428  15246    405   -429    -55       N  
ATOM   5288  CA  VAL B 287      -8.195   1.745 -23.460  1.00138.58           C  
ANISOU 5288  CA  VAL B 287    22784  14509  15362    467   -323    -54       C  
ATOM   5289  C   VAL B 287      -7.096   0.874 -22.810  1.00146.59           C  
ANISOU 5289  C   VAL B 287    23935  15507  16257    498   -446   -112       C  
ATOM   5290  O   VAL B 287      -6.110   0.515 -23.462  1.00145.58           O  
ANISOU 5290  O   VAL B 287    23689  15491  16134    473   -598   -142       O  
ATOM   5291  CB  VAL B 287      -9.116   0.900 -24.391  1.00141.44           C  
ANISOU 5291  CB  VAL B 287    22953  14955  15834    457   -225    -15       C  
ATOM   5292  CG1 VAL B 287      -9.934  -0.128 -23.612  1.00141.49           C  
ANISOU 5292  CG1 VAL B 287    23087  14865  15809    506    -83    -13       C  
ATOM   5293  CG2 VAL B 287     -10.033   1.792 -25.222  1.00141.15           C  
ANISOU 5293  CG2 VAL B 287    22756  14961  15915    434   -137     49       C  
ATOM   5294  N   ASP B 288      -7.278   0.549 -21.524  1.00147.54           N  
ANISOU 5294  N   ASP B 288    24305  15484  16269    562   -373   -122       N  
ATOM   5295  CA  ASP B 288      -6.395  -0.345 -20.763  1.00149.58           C  
ANISOU 5295  CA  ASP B 288    24729  15706  16397    617   -470   -164       C  
ATOM   5296  C   ASP B 288      -7.007  -1.730 -20.971  1.00153.65           C  
ANISOU 5296  C   ASP B 288    25193  16241  16944    649   -379   -150       C  
ATOM   5297  O   ASP B 288      -8.011  -2.082 -20.345  1.00153.72           O  
ANISOU 5297  O   ASP B 288    25338  16137  16934    689   -205   -130       O  
ATOM   5298  CB  ASP B 288      -6.263   0.055 -19.268  1.00153.52           C  
ANISOU 5298  CB  ASP B 288    25557  16032  16743    670   -437   -182       C  
ATOM   5299  CG  ASP B 288      -5.289  -0.776 -18.452  1.00170.17           C  
ANISOU 5299  CG  ASP B 288    27778  18005  18874    679   -221   -143       C  
ATOM   5300  OD1 ASP B 288      -4.657  -1.698 -19.034  1.00171.64           O  
ANISOU 5300  OD1 ASP B 288    27952  18175  19087    637   -221   -137       O  
ATOM   5301  OD2 ASP B 288      -5.168  -0.520 -17.231  1.00178.13           O1-
ANISOU 5301  OD2 ASP B 288    28892  18916  19875    729    -41   -118       O1-
ATOM   5302  N   ILE B 289      -6.483  -2.420 -21.989  1.00149.39           N  
ANISOU 5302  N   ILE B 289    24445  15845  16471    619   -475   -159       N  
ATOM   5303  CA  ILE B 289      -6.944  -3.735 -22.421  1.00148.58           C  
ANISOU 5303  CA  ILE B 289    24271  15776  16405    630   -403   -153       C  
ATOM   5304  C   ILE B 289      -6.021  -4.748 -21.684  1.00154.09           C  
ANISOU 5304  C   ILE B 289    25129  16440  16979    714   -496   -183       C  
ATOM   5305  O   ILE B 289      -4.849  -4.428 -21.424  1.00154.61           O  
ANISOU 5305  O   ILE B 289    25215  16547  16983    735   -679   -209       O  
ATOM   5306  CB  ILE B 289      -6.851  -3.746 -23.986  1.00149.86           C  
ANISOU 5306  CB  ILE B 289    24138  16103  16700    551   -443   -144       C  
ATOM   5307  CG1 ILE B 289      -7.740  -4.831 -24.609  1.00149.55           C  
ANISOU 5307  CG1 ILE B 289    24013  16083  16726    525   -307   -132       C  
ATOM   5308  CG2 ILE B 289      -5.429  -3.806 -24.522  1.00149.50           C  
ANISOU 5308  CG2 ILE B 289    23984  16171  16648    543   -634   -174       C  
ATOM   5309  CD1 ILE B 289      -8.801  -4.293 -25.552  1.00152.16           C  
ANISOU 5309  CD1 ILE B 289    24152  16478  17183    450   -217    -95       C  
ATOM   5310  N   ASP B 290      -6.573  -5.922 -21.271  1.00150.43           N  
ANISOU 5310  N   ASP B 290    24791  15890  16473    764   -365   -177       N  
ATOM   5311  CA  ASP B 290      -5.792  -6.927 -20.542  1.00150.68           C  
ANISOU 5311  CA  ASP B 290    24999  15874  16379    863   -433   -193       C  
ATOM   5312  C   ASP B 290      -4.749  -7.548 -21.461  1.00154.08           C  
ANISOU 5312  C   ASP B 290    25246  16444  16851    865   -569   -207       C  
ATOM   5313  O   ASP B 290      -5.083  -8.349 -22.339  1.00152.50           O  
ANISOU 5313  O   ASP B 290    24921  16291  16729    830   -485   -203       O  
ATOM   5314  CB  ASP B 290      -6.676  -8.014 -19.902  1.00152.77           C  
ANISOU 5314  CB  ASP B 290    25458  15997  16590    913   -234   -181       C  
ATOM   5315  CG  ASP B 290      -6.060  -8.676 -18.673  1.00160.56           C  
ANISOU 5315  CG  ASP B 290    26735  16872  17400   1041   -282   -186       C  
ATOM   5316  OD1 ASP B 290      -4.823  -8.908 -18.669  1.00160.26           O1-
ANISOU 5316  OD1 ASP B 290    26679  16908  17304   1100   -477   -198       O1-
ATOM   5317  OD2 ASP B 290      -6.812  -8.975 -17.723  1.00166.80           O  
ANISOU 5317  OD2 ASP B 290    27767  17501  18108   1085   -124   -175       O  
ATOM   5318  N   ARG B 291      -3.480  -7.158 -21.247  1.00151.69           N  
ANISOU 5318  N   ARG B 291    24930  16205  16498    901   -778   -226       N  
ATOM   5319  CA  ARG B 291      -2.321  -7.606 -22.015  1.00151.75           C  
ANISOU 5319  CA  ARG B 291    24762  16346  16549    915   -921   -237       C  
ATOM   5320  C   ARG B 291      -2.051  -9.108 -21.847  1.00157.92           C  
ANISOU 5320  C   ARG B 291    25638  17091  17272   1019   -883   -229       C  
ATOM   5321  O   ARG B 291      -1.374  -9.697 -22.692  1.00157.92           O  
ANISOU 5321  O   ARG B 291    25482  17189  17332   1027   -931   -232       O  
ATOM   5322  CB  ARG B 291      -1.080  -6.805 -21.606  1.00152.05           C  
ANISOU 5322  CB  ARG B 291    24781  16448  16544    932  -1147   -260       C  
ATOM   5323  N   ARG B 292      -2.594  -9.721 -20.776  1.00155.49           N  
ANISOU 5323  N   ARG B 292    25598  16634  16848   1099   -780   -217       N  
ATOM   5324  CA  ARG B 292      -2.421 -11.135 -20.459  1.00155.91           C  
ANISOU 5324  CA  ARG B 292    25795  16619  16825   1210   -720   -204       C  
ATOM   5325  C   ARG B 292      -3.532 -12.033 -21.045  1.00159.20           C  
ANISOU 5325  C   ARG B 292    26204  16979  17307   1154   -484   -200       C  
ATOM   5326  O   ARG B 292      -3.274 -13.214 -21.286  1.00159.01           O  
ANISOU 5326  O   ARG B 292    26213  16937  17266   1211   -433   -195       O  
ATOM   5327  CB  ARG B 292      -2.351 -11.312 -18.938  1.00157.57           C  
ANISOU 5327  CB  ARG B 292    26328  16687  16857   1331   -738   -193       C  
ATOM   5328  N   ASP B 293      -4.745 -11.486 -21.281  1.00155.48           N  
ANISOU 5328  N   ASP B 293    25684  16478  16911   1042   -340   -201       N  
ATOM   5329  CA  ASP B 293      -5.899 -12.227 -21.820  1.00155.24           C  
ANISOU 5329  CA  ASP B 293    25625  16405  16956    965   -123   -202       C  
ATOM   5330  C   ASP B 293      -5.539 -12.998 -23.109  1.00158.86           C  
ANISOU 5330  C   ASP B 293    25892  16971  17496    918   -130   -217       C  
ATOM   5331  O   ASP B 293      -4.844 -12.451 -23.973  1.00157.65           O  
ANISOU 5331  O   ASP B 293    25528  16960  17411    879   -270   -223       O  
ATOM   5332  CB  ASP B 293      -7.082 -11.280 -22.087  1.00156.74           C  
ANISOU 5332  CB  ASP B 293    25706  16601  17245    849    -22   -197       C  
ATOM   5333  CG  ASP B 293      -8.417 -11.975 -22.282  1.00167.46           C  
ANISOU 5333  CG  ASP B 293    27075  17888  18666    776    212   -198       C  
ATOM   5334  OD1 ASP B 293      -8.659 -12.502 -23.391  1.00167.17           O1-
ANISOU 5334  OD1 ASP B 293    26862  17936  18720    688    250   -213       O1-
ATOM   5335  OD2 ASP B 293      -9.227 -11.973 -21.335  1.00174.65           O1-
ANISOU 5335  OD2 ASP B 293    28167  18659  19534    798    359   -187       O1-
ATOM   5336  N   PRO B 294      -5.994 -14.266 -23.253  1.00156.40           N  
ANISOU 5336  N   PRO B 294    25667  16585  17175    916     30   -225       N  
ATOM   5337  CA  PRO B 294      -5.634 -15.041 -24.460  1.00155.73           C  
ANISOU 5337  CA  PRO B 294    25431  16586  17152    870     34   -243       C  
ATOM   5338  C   PRO B 294      -6.267 -14.519 -25.757  1.00156.01           C  
ANISOU 5338  C   PRO B 294    25207  16746  17325    706     51   -259       C  
ATOM   5339  O   PRO B 294      -5.641 -14.629 -26.808  1.00154.93           O  
ANISOU 5339  O   PRO B 294    24907  16721  17237    672    -24   -271       O  
ATOM   5340  CB  PRO B 294      -6.121 -16.461 -24.139  1.00158.65           C  
ANISOU 5340  CB  PRO B 294    26001  16814  17466    897    227   -252       C  
ATOM   5341  CG  PRO B 294      -7.184 -16.283 -23.111  1.00163.92           C  
ANISOU 5341  CG  PRO B 294    26842  17343  18097    890    369   -243       C  
ATOM   5342  CD  PRO B 294      -6.794 -15.077 -22.308  1.00159.32           C  
ANISOU 5342  CD  PRO B 294    26293  16773  17466    956    223   -220       C  
ATOM   5343  N   LEU B 295      -7.487 -13.957 -25.687  1.00150.48           N  
ANISOU 5343  N   LEU B 295    24468  16025  16683    613    151   -256       N  
ATOM   5344  CA  LEU B 295      -8.186 -13.420 -26.854  1.00148.83           C  
ANISOU 5344  CA  LEU B 295    24017  15935  16596    468    160   -262       C  
ATOM   5345  C   LEU B 295      -7.456 -12.182 -27.394  1.00149.11           C  
ANISOU 5345  C   LEU B 295    23876  16105  16673    463    -24   -246       C  
ATOM   5346  O   LEU B 295      -7.340 -12.031 -28.614  1.00148.74           O  
ANISOU 5346  O   LEU B 295    23637  16181  16697    380    -74   -254       O  
ATOM   5347  CB  LEU B 295      -9.641 -13.082 -26.485  1.00149.52           C  
ANISOU 5347  CB  LEU B 295    24109  15962  16738    397    309   -251       C  
ATOM   5348  CG  LEU B 295     -10.503 -12.434 -27.572  1.00154.21           C  
ANISOU 5348  CG  LEU B 295    24452  16680  17459    262    313   -245       C  
ATOM   5349  CD1 LEU B 295     -11.370 -13.467 -28.272  1.00154.90           C  
ANISOU 5349  CD1 LEU B 295    24481  16774  17599    143    447   -279       C  
ATOM   5350  CD2 LEU B 295     -11.343 -11.300 -26.997  1.00156.62           C  
ANISOU 5350  CD2 LEU B 295    24737  16959  17811    264    353   -208       C  
ATOM   5351  N   VAL B 296      -6.947 -11.324 -26.473  1.00142.38           N  
ANISOU 5351  N   VAL B 296    23109  15220  15768    547   -121   -228       N  
ATOM   5352  CA  VAL B 296      -6.208 -10.084 -26.749  1.00139.82           C  
ANISOU 5352  CA  VAL B 296    22658  14996  15471    544   -287   -217       C  
ATOM   5353  C   VAL B 296      -4.850 -10.418 -27.383  1.00140.66           C  
ANISOU 5353  C   VAL B 296    22675  15195  15573    577   -422   -232       C  
ATOM   5354  O   VAL B 296      -4.441  -9.746 -28.335  1.00140.18           O  
ANISOU 5354  O   VAL B 296    22427  15253  15582    516   -508   -232       O  
ATOM   5355  CB  VAL B 296      -6.042  -9.228 -25.467  1.00143.57           C  
ANISOU 5355  CB  VAL B 296    23290  15387  15873    617   -339   -205       C  
ATOM   5356  CG1 VAL B 296      -5.188  -7.988 -25.724  1.00143.02           C  
ANISOU 5356  CG1 VAL B 296    23103  15411  15826    603   -510   -203       C  
ATOM   5357  CG2 VAL B 296      -7.398  -8.834 -24.890  1.00143.44           C  
ANISOU 5357  CG2 VAL B 296    23355  15274  15873    589   -184   -185       C  
ATOM   5358  N   VAL B 297      -4.171 -11.458 -26.867  1.00134.69           N  
ANISOU 5358  N   VAL B 297    22057  14381  14739    678   -428   -241       N  
ATOM   5359  CA  VAL B 297      -2.872 -11.923 -27.355  1.00133.49           C  
ANISOU 5359  CA  VAL B 297    21832  14304  14585    735   -536   -249       C  
ATOM   5360  C   VAL B 297      -3.028 -12.545 -28.792  1.00135.02           C  
ANISOU 5360  C   VAL B 297    21874  14572  14854    645   -463   -265       C  
ATOM   5361  O   VAL B 297      -2.182 -12.314 -29.664  1.00134.93           O  
ANISOU 5361  O   VAL B 297    21705  14668  14894    628   -551   -269       O  
ATOM   5362  CB  VAL B 297      -2.244 -12.888 -26.322  1.00137.98           C  
ANISOU 5362  CB  VAL B 297    22609  14776  15043    888   -546   -243       C  
ATOM   5363  CG1 VAL B 297      -1.149 -13.760 -26.940  1.00138.25           C  
ANISOU 5363  CG1 VAL B 297    22576  14865  15085    955   -591   -245       C  
ATOM   5364  CG2 VAL B 297      -1.714 -12.112 -25.118  1.00138.08           C  
ANISOU 5364  CG2 VAL B 297    22730  14758  14977    972   -684   -232       C  
ATOM   5365  N   ALA B 298      -4.132 -13.281 -29.033  1.00128.79           N  
ANISOU 5365  N   ALA B 298    21136  13725  14072    576   -300   -276       N  
ATOM   5366  CA  ALA B 298      -4.446 -13.877 -30.334  1.00126.64           C  
ANISOU 5366  CA  ALA B 298    20750  13513  13854    471   -226   -299       C  
ATOM   5367  C   ALA B 298      -4.761 -12.798 -31.358  1.00125.32           C  
ANISOU 5367  C   ALA B 298    20370  13473  13773    353   -286   -293       C  
ATOM   5368  O   ALA B 298      -4.332 -12.903 -32.503  1.00124.61           O  
ANISOU 5368  O   ALA B 298    20155  13472  13719    300   -314   -305       O  
ATOM   5369  CB  ALA B 298      -5.624 -14.830 -30.205  1.00127.79           C  
ANISOU 5369  CB  ALA B 298    21007  13562  13987    410    -44   -318       C  
ATOM   5370  N   ALA B 299      -5.495 -11.756 -30.940  1.00118.41           N  
ANISOU 5370  N   ALA B 299    19469  12596  12925    322   -297   -271       N  
ATOM   5371  CA  ALA B 299      -5.863 -10.664 -31.819  1.00116.73           C  
ANISOU 5371  CA  ALA B 299    19073  12492  12788    229   -348   -255       C  
ATOM   5372  C   ALA B 299      -4.642  -9.829 -32.174  1.00119.73           C  
ANISOU 5372  C   ALA B 299    19353  12955  13183    258   -494   -247       C  
ATOM   5373  O   ALA B 299      -4.401  -9.612 -33.359  1.00119.82           O  
ANISOU 5373  O   ALA B 299    19222  13065  13239    191   -527   -249       O  
ATOM   5374  CB  ALA B 299      -6.936  -9.803 -31.173  1.00117.27           C  
ANISOU 5374  CB  ALA B 299    19158  12520  12881    212   -304   -226       C  
ATOM   5375  N   LEU B 300      -3.839  -9.425 -31.162  1.00115.00           N  
ANISOU 5375  N   LEU B 300    18838  12314  12543    354   -581   -242       N  
ATOM   5376  CA  LEU B 300      -2.638  -8.609 -31.345  1.00114.10           C  
ANISOU 5376  CA  LEU B 300    18631  12274  12449    375   -723   -241       C  
ATOM   5377  C   LEU B 300      -1.643  -9.259 -32.299  1.00118.81           C  
ANISOU 5377  C   LEU B 300    19128  12944  13070    379   -752   -258       C  
ATOM   5378  O   LEU B 300      -1.254  -8.616 -33.272  1.00118.82           O  
ANISOU 5378  O   LEU B 300    18979  13036  13129    316   -797   -255       O  
ATOM   5379  CB  LEU B 300      -1.955  -8.305 -29.999  1.00114.53           C  
ANISOU 5379  CB  LEU B 300    18811  12265  12440    476   -815   -243       C  
ATOM   5380  CG  LEU B 300      -0.582  -7.616 -30.045  1.00119.38           C  
ANISOU 5380  CG  LEU B 300    19330  12953  13074    498   -973   -252       C  
ATOM   5381  CD1 LEU B 300      -0.658  -6.238 -30.683  1.00118.89           C  
ANISOU 5381  CD1 LEU B 300    19134  12958  13081    401  -1013   -244       C  
ATOM   5382  CD2 LEU B 300       0.017  -7.501 -28.667  1.00123.02           C  
ANISOU 5382  CD2 LEU B 300    19934  13353  13456    594  -1073   -259       C  
ATOM   5383  N   HIS B 301      -1.253 -10.528 -32.039  1.00115.58           N  
ANISOU 5383  N   HIS B 301    18814  12485  12615    456   -711   -271       N  
ATOM   5384  CA  HIS B 301      -0.268 -11.263 -32.844  1.00115.30           C  
ANISOU 5384  CA  HIS B 301    18707  12501  12600    483   -717   -283       C  
ATOM   5385  C   HIS B 301      -0.747 -11.586 -34.264  1.00117.12           C  
ANISOU 5385  C   HIS B 301    18849  12784  12868    369   -626   -296       C  
ATOM   5386  O   HIS B 301       0.083 -11.737 -35.167  1.00116.10           O  
ANISOU 5386  O   HIS B 301    18622  12719  12773    360   -639   -303       O  
ATOM   5387  CB  HIS B 301       0.214 -12.512 -32.108  1.00117.25           C  
ANISOU 5387  CB  HIS B 301    19103  12666  12782    613   -685   -286       C  
ATOM   5388  CG  HIS B 301       1.153 -12.147 -31.005  1.00121.92           C  
ANISOU 5388  CG  HIS B 301    19735  13249  13341    733   -822   -273       C  
ATOM   5389  ND1 HIS B 301       0.688 -11.741 -29.764  1.00124.33           N  
ANISOU 5389  ND1 HIS B 301    20181  13479  13581    770   -853   -265       N  
ATOM   5390  CD2 HIS B 301       2.499 -12.021 -31.024  1.00124.54           C  
ANISOU 5390  CD2 HIS B 301    19969  13648  13701    807   -942   -270       C  
ATOM   5391  CE1 HIS B 301       1.764 -11.432 -29.059  1.00124.45           C  
ANISOU 5391  CE1 HIS B 301    20195  13518  13574    864  -1001   -260       C  
ATOM   5392  NE2 HIS B 301       2.876 -11.574 -29.779  1.00125.00           N  
ANISOU 5392  NE2 HIS B 301    20109  13680  13707    888  -1064   -263       N  
ATOM   5393  N   LEU B 302      -2.073 -11.595 -34.474  1.00113.35           N  
ANISOU 5393  N   LEU B 302    18396  12285  12388    278   -542   -297       N  
ATOM   5394  CA  LEU B 302      -2.673 -11.788 -35.789  1.00113.21           C  
ANISOU 5394  CA  LEU B 302    18294  12326  12395    155   -479   -309       C  
ATOM   5395  C   LEU B 302      -2.650 -10.485 -36.574  1.00115.35           C  
ANISOU 5395  C   LEU B 302    18407  12700  12719     85   -558   -288       C  
ATOM   5396  O   LEU B 302      -2.631 -10.486 -37.805  1.00113.90           O  
ANISOU 5396  O   LEU B 302    18138  12586  12551      8   -546   -295       O  
ATOM   5397  CB  LEU B 302      -4.115 -12.249 -35.645  1.00113.84           C  
ANISOU 5397  CB  LEU B 302    18438  12355  12460     83   -375   -318       C  
ATOM   5398  CG  LEU B 302      -4.834 -12.404 -36.963  1.00120.08           C  
ANISOU 5398  CG  LEU B 302    19219  13164  13241    -20   -285   -352       C  
ATOM   5399  CD1 LEU B 302      -4.186 -13.475 -37.814  1.00121.47           C  
ANISOU 5399  CD1 LEU B 302    19556  13226  13372    -12   -156   -381       C  
ATOM   5400  CD2 LEU B 302      -6.317 -12.638 -36.760  1.00123.12           C  
ANISOU 5400  CD2 LEU B 302    19474  13641  13665   -152   -300   -342       C  
ATOM   5401  N   CYS B 303      -2.680  -9.376 -35.841  1.00111.98           N  
ANISOU 5401  N   CYS B 303    17965  12271  12311    112   -630   -262       N  
ATOM   5402  CA  CYS B 303      -2.632  -8.046 -36.405  1.00111.76           C  
ANISOU 5402  CA  CYS B 303    17814  12319  12330     59   -698   -237       C  
ATOM   5403  C   CYS B 303      -1.197  -7.762 -36.814  1.00113.52           C  
ANISOU 5403  C   CYS B 303    17959  12593  12580     86   -771   -245       C  
ATOM   5404  O   CYS B 303      -0.987  -7.268 -37.927  1.00114.68           O  
ANISOU 5404  O   CYS B 303    18001  12813  12759     20   -779   -237       O  
ATOM   5405  CB  CYS B 303      -3.160  -6.992 -35.438  1.00112.83           C  
ANISOU 5405  CB  CYS B 303    17985  12413  12472     80   -729   -210       C  
ATOM   5406  SG  CYS B 303      -4.944  -7.092 -35.139  1.00117.14           S  
ANISOU 5406  SG  CYS B 303    18576  12915  13018     37   -627   -190       S  
ATOM   5407  N   ILE B 304      -0.212  -8.089 -35.937  1.00106.30           N  
ANISOU 5407  N   ILE B 304    17094  11643  11653    184   -823   -259       N  
ATOM   5408  CA  ILE B 304       1.221  -7.879 -36.179  1.00105.23           C  
ANISOU 5408  CA  ILE B 304    16867  11558  11558    220   -897   -268       C  
ATOM   5409  C   ILE B 304       1.639  -8.632 -37.431  1.00109.99           C  
ANISOU 5409  C   ILE B 304    17406  12206  12180    192   -829   -279       C  
ATOM   5410  O   ILE B 304       2.340  -8.072 -38.279  1.00109.30           O  
ANISOU 5410  O   ILE B 304    17201  12183  12144    151   -849   -278       O  
ATOM   5411  CB  ILE B 304       2.082  -8.293 -34.959  1.00108.30           C  
ANISOU 5411  CB  ILE B 304    17323  11904  11921    342   -970   -277       C  
ATOM   5412  CG1 ILE B 304       1.803  -7.412 -33.739  1.00108.37           C  
ANISOU 5412  CG1 ILE B 304    17407  11867  11900    361  -1048   -271       C  
ATOM   5413  CG2 ILE B 304       3.580  -8.299 -35.293  1.00109.36           C  
ANISOU 5413  CG2 ILE B 304    17335  12103  12113    384  -1038   -287       C  
ATOM   5414  CD1 ILE B 304       2.163  -8.057 -32.448  1.00115.49           C  
ANISOU 5414  CD1 ILE B 304    18442  12702  12736    481  -1096   -277       C  
ATOM   5415  N   ALA B 305       1.191  -9.900 -37.544  1.00107.87           N  
ANISOU 5415  N   ALA B 305    17230  11891  11866    208   -735   -293       N  
ATOM   5416  CA  ALA B 305       1.500 -10.783 -38.669  1.00107.97           C  
ANISOU 5416  CA  ALA B 305    17225  11922  11876    183   -649   -311       C  
ATOM   5417  C   ALA B 305       0.905 -10.262 -39.963  1.00111.15           C  
ANISOU 5417  C   ALA B 305    17557  12389  12287     53   -618   -308       C  
ATOM   5418  O   ALA B 305       1.589 -10.282 -40.977  1.00111.30           O  
ANISOU 5418  O   ALA B 305    17510  12452  12327     26   -593   -313       O  
ATOM   5419  CB  ALA B 305       1.001 -12.186 -38.388  1.00108.95           C  
ANISOU 5419  CB  ALA B 305    17492  11964  11938    216   -548   -330       C  
ATOM   5420  N   LEU B 306      -0.334  -9.738 -39.924  1.00107.20           N  
ANISOU 5420  N   LEU B 306    17067  11894  11770    -21   -623   -294       N  
ATOM   5421  CA  LEU B 306      -0.999  -9.194 -41.112  1.00107.08           C  
ANISOU 5421  CA  LEU B 306    16987  11947  11754   -134   -612   -282       C  
ATOM   5422  C   LEU B 306      -0.166  -8.077 -41.789  1.00111.94           C  
ANISOU 5422  C   LEU B 306    17492  12626  12414   -152   -665   -260       C  
ATOM   5423  O   LEU B 306      -0.069  -8.051 -43.023  1.00111.86           O  
ANISOU 5423  O   LEU B 306    17446  12663  12392   -219   -632   -260       O  
ATOM   5424  CB  LEU B 306      -2.405  -8.683 -40.772  1.00106.41           C  
ANISOU 5424  CB  LEU B 306    16908  11861  11661   -183   -622   -259       C  
ATOM   5425  CG  LEU B 306      -3.525  -9.702 -40.884  1.00109.70           C  
ANISOU 5425  CG  LEU B 306    17390  12254  12037   -241   -546   -282       C  
ATOM   5426  CD1 LEU B 306      -4.811  -9.130 -40.359  1.00109.43           C  
ANISOU 5426  CD1 LEU B 306    17341  12218  12019   -269   -555   -254       C  
ATOM   5427  CD2 LEU B 306      -3.712 -10.161 -42.313  1.00110.31           C  
ANISOU 5427  CD2 LEU B 306    17444  12389  12079   -342   -512   -302       C  
ATOM   5428  N   GLY B 307       0.455  -7.219 -40.970  1.00107.80           N  
ANISOU 5428  N   GLY B 307    16931  12094  11935    -98   -739   -246       N  
ATOM   5429  CA  GLY B 307       1.334  -6.145 -41.421  1.00107.30           C  
ANISOU 5429  CA  GLY B 307    16769  12075  11925   -117   -782   -233       C  
ATOM   5430  C   GLY B 307       2.561  -6.704 -42.108  1.00110.19           C  
ANISOU 5430  C   GLY B 307    17084  12463  12320    -98   -744   -254       C  
ATOM   5431  O   GLY B 307       2.927  -6.243 -43.192  1.00110.11           O  
ANISOU 5431  O   GLY B 307    17013  12495  12328   -157   -714   -246       O  
ATOM   5432  N   TYR B 308       3.164  -7.750 -41.504  1.00105.64           N  
ANISOU 5432  N   TYR B 308    16544  11851  11744    -10   -732   -278       N  
ATOM   5433  CA  TYR B 308       4.319  -8.445 -42.059  1.00105.85           C  
ANISOU 5433  CA  TYR B 308    16524  11888  11804     32   -679   -294       C  
ATOM   5434  C   TYR B 308       3.960  -9.084 -43.393  1.00111.91           C  
ANISOU 5434  C   TYR B 308    17332  12663  12526    -37   -567   -303       C  
ATOM   5435  O   TYR B 308       4.751  -8.996 -44.334  1.00113.20           O  
ANISOU 5435  O   TYR B 308    17434  12854  12721    -57   -515   -305       O  
ATOM   5436  CB  TYR B 308       4.830  -9.508 -41.091  1.00107.07           C  
ANISOU 5436  CB  TYR B 308    16733  11996  11954    158   -684   -306       C  
ATOM   5437  CG  TYR B 308       5.801  -8.998 -40.055  1.00109.59           C  
ANISOU 5437  CG  TYR B 308    16978  12329  12332    240   -798   -302       C  
ATOM   5438  CD1 TYR B 308       7.095  -8.622 -40.410  1.00112.42           C  
ANISOU 5438  CD1 TYR B 308    17191  12741  12781    257   -821   -304       C  
ATOM   5439  CD2 TYR B 308       5.458  -8.970 -38.704  1.00110.23           C  
ANISOU 5439  CD2 TYR B 308    17138  12369  12376    302   -881   -300       C  
ATOM   5440  CE1 TYR B 308       8.003  -8.168 -39.455  1.00113.73           C  
ANISOU 5440  CE1 TYR B 308    17276  12933  13005    321   -943   -307       C  
ATOM   5441  CE2 TYR B 308       6.360  -8.523 -37.739  1.00111.68           C  
ANISOU 5441  CE2 TYR B 308    17265  12569  12598    372  -1003   -301       C  
ATOM   5442  CZ  TYR B 308       7.635  -8.133 -38.119  1.00119.35           C  
ANISOU 5442  CZ  TYR B 308    18076  13608  13665    378  -1042   -306       C  
ATOM   5443  OH  TYR B 308       8.535  -7.707 -37.176  1.00119.71           O  
ANISOU 5443  OH  TYR B 308    18052  13682  13751    435  -1178   -313       O  
ATOM   5444  N   ILE B 309       2.739  -9.676 -43.485  1.00108.22           N  
ANISOU 5444  N   ILE B 309    16969  12170  11982    -84   -530   -312       N  
ATOM   5445  CA  ILE B 309       2.205 -10.337 -44.681  1.00108.32           C  
ANISOU 5445  CA  ILE B 309    17041  12186  11928   -170   -439   -330       C  
ATOM   5446  C   ILE B 309       2.125  -9.335 -45.841  1.00113.64           C  
ANISOU 5446  C   ILE B 309    17652  12926  12600   -263   -449   -308       C  
ATOM   5447  O   ILE B 309       2.552  -9.670 -46.940  1.00113.21           O  
ANISOU 5447  O   ILE B 309    17613  12880  12522   -301   -372   -321       O  
ATOM   5448  CB  ILE B 309       0.834 -11.041 -44.416  1.00110.64           C  
ANISOU 5448  CB  ILE B 309    17439  12447  12151   -218   -416   -347       C  
ATOM   5449  CG1 ILE B 309       1.016 -12.304 -43.566  1.00110.75           C  
ANISOU 5449  CG1 ILE B 309    17555  12377  12148   -132   -358   -373       C  
ATOM   5450  CG2 ILE B 309       0.103 -11.401 -45.724  1.00111.51           C  
ANISOU 5450  CG2 ILE B 309    17593  12587  12189   -343   -360   -366       C  
ATOM   5451  CD1 ILE B 309      -0.129 -12.640 -42.654  1.00114.26           C  
ANISOU 5451  CD1 ILE B 309    18079  12774  12560   -140   -362   -378       C  
ATOM   5452  N   ASN B 310       1.617  -8.112 -45.598  1.00111.29           N  
ANISOU 5452  N   ASN B 310    17299  12664  12323   -293   -532   -274       N  
ATOM   5453  CA  ASN B 310       1.490  -7.119 -46.664  1.00111.75           C  
ANISOU 5453  CA  ASN B 310    17315  12775  12370   -370   -539   -244       C  
ATOM   5454  C   ASN B 310       2.833  -6.699 -47.235  1.00119.22           C  
ANISOU 5454  C   ASN B 310    18195  13730  13372   -357   -501   -243       C  
ATOM   5455  O   ASN B 310       2.915  -6.500 -48.445  1.00120.61           O  
ANISOU 5455  O   ASN B 310    18385  13931  13512   -420   -448   -235       O  
ATOM   5456  CB  ASN B 310       0.723  -5.883 -46.214  1.00108.92           C  
ANISOU 5456  CB  ASN B 310    16920  12439  12027   -385   -622   -201       C  
ATOM   5457  CG  ASN B 310       0.434  -4.896 -47.334  1.00131.34           C  
ANISOU 5457  CG  ASN B 310    19737  15328  14840   -454   -627   -160       C  
ATOM   5458  OD1 ASN B 310       1.001  -3.797 -47.384  1.00128.31           O  
ANISOU 5458  OD1 ASN B 310    19302  14947  14503   -450   -643   -134       O  
ATOM   5459  ND2 ASN B 310      -0.407  -5.278 -48.292  1.00121.23           N  
ANISOU 5459  ND2 ASN B 310    18502  14083  13476   -522   -610   -156       N  
ATOM   5460  N   SER B 311       3.876  -6.571 -46.407  1.00116.90           N  
ANISOU 5460  N   SER B 311    17832  13419  13164   -282   -525   -252       N  
ATOM   5461  CA  SER B 311       5.161  -6.116 -46.925  1.00118.50           C  
ANISOU 5461  CA  SER B 311    17946  13637  13441   -279   -485   -252       C  
ATOM   5462  C   SER B 311       6.025  -7.249 -47.478  1.00124.11           C  
ANISOU 5462  C   SER B 311    18666  14329  14162   -239   -377   -279       C  
ATOM   5463  O   SER B 311       6.834  -6.998 -48.374  1.00125.30           O  
ANISOU 5463  O   SER B 311    18770  14491  14349   -264   -299   -277       O  
ATOM   5464  CB  SER B 311       5.919  -5.323 -45.870  1.00124.04           C  
ANISOU 5464  CB  SER B 311    18548  14342  14239   -233   -571   -251       C  
ATOM   5465  OG  SER B 311       5.406  -3.999 -45.772  1.00135.23           O  
ANISOU 5465  OG  SER B 311    19954  15770  15657   -291   -629   -222       O  
ATOM   5466  N   SER B 312       5.840  -8.484 -46.999  1.00120.44           N  
ANISOU 5466  N   SER B 312    18272  13827  13663   -177   -354   -302       N  
ATOM   5467  CA  SER B 312       6.618  -9.620 -47.492  1.00121.41           C  
ANISOU 5467  CA  SER B 312    18422  13917  13791   -125   -235   -324       C  
ATOM   5468  C   SER B 312       5.933 -10.368 -48.658  1.00125.89           C  
ANISOU 5468  C   SER B 312    19125  14462  14246   -205   -129   -343       C  
ATOM   5469  O   SER B 312       6.607 -10.750 -49.608  1.00126.65           O  
ANISOU 5469  O   SER B 312    19240  14542  14340   -211    -11   -353       O  
ATOM   5470  CB  SER B 312       6.899 -10.598 -46.359  1.00125.61           C  
ANISOU 5470  CB  SER B 312    18976  14407  14342     -3   -253   -335       C  
ATOM   5471  OG  SER B 312       5.723 -11.212 -45.857  1.00134.56           O  
ANISOU 5471  OG  SER B 312    20235  15503  15387    -15   -271   -346       O  
ATOM   5472  N   LEU B 313       4.640 -10.708 -48.489  1.00121.58           N  
ANISOU 5472  N   LEU B 313    18678  13907  13609   -258   -165   -353       N  
ATOM   5473  CA  LEU B 313       3.791 -11.457 -49.424  1.00121.28           C  
ANISOU 5473  CA  LEU B 313    18774  13854  13454   -352    -95   -380       C  
ATOM   5474  C   LEU B 313       2.799 -10.450 -50.079  1.00121.60           C  
ANISOU 5474  C   LEU B 313    18806  13959  13438   -466   -170   -355       C  
ATOM   5475  O   LEU B 313       1.570 -10.625 -50.085  1.00120.22           O  
ANISOU 5475  O   LEU B 313    18686  13802  13192   -535   -216   -362       O  
ATOM   5476  CB  LEU B 313       3.099 -12.594 -48.614  1.00121.77           C  
ANISOU 5476  CB  LEU B 313    18934  13859  13473   -325    -84   -410       C  
ATOM   5477  CG  LEU B 313       2.303 -13.723 -49.318  1.00127.71           C  
ANISOU 5477  CG  LEU B 313    19842  14572  14112   -416      3   -457       C  
ATOM   5478  CD1 LEU B 313       3.107 -14.396 -50.438  1.00129.44           C  
ANISOU 5478  CD1 LEU B 313    20138  14751  14291   -425    145   -482       C  
ATOM   5479  CD2 LEU B 313       1.840 -14.771 -48.302  1.00129.50           C  
ANISOU 5479  CD2 LEU B 313    20155  14726  14324   -370     28   -483       C  
ATOM   5480  N   ASN B 314       3.390  -9.369 -50.617  1.00116.58           N  
ANISOU 5480  N   ASN B 314    18094  13360  12842   -478   -180   -323       N  
ATOM   5481  CA  ASN B 314       2.726  -8.245 -51.261  1.00115.66           C  
ANISOU 5481  CA  ASN B 314    17962  13299  12683   -557   -242   -285       C  
ATOM   5482  C   ASN B 314       2.058  -8.667 -52.577  1.00120.93           C  
ANISOU 5482  C   ASN B 314    18747  13984  13218   -659   -200   -298       C  
ATOM   5483  O   ASN B 314       2.602  -9.557 -53.243  1.00122.03           O  
ANISOU 5483  O   ASN B 314    18968  14082  13315   -669    -87   -335       O  
ATOM   5484  CB  ASN B 314       3.760  -7.151 -51.513  1.00114.81           C  
ANISOU 5484  CB  ASN B 314    17765  13202  12657   -538   -225   -254       C  
ATOM   5485  CG  ASN B 314       3.191  -5.798 -51.854  1.00143.01           C  
ANISOU 5485  CG  ASN B 314    21312  16817  16209   -588   -295   -203       C  
ATOM   5486  OD1 ASN B 314       3.379  -5.296 -52.961  1.00141.63           O  
ANISOU 5486  OD1 ASN B 314    21172  16653  15989   -639   -245   -182       O  
ATOM   5487  ND2 ASN B 314       2.473  -5.173 -50.923  1.00134.31           N  
ANISOU 5487  ND2 ASN B 314    20166  15732  15135   -569   -400   -178       N  
ATOM   5488  N   PRO B 315       0.909  -8.041 -52.989  1.00116.83           N  
ANISOU 5488  N   PRO B 315    18240  13524  12625   -732   -288   -267       N  
ATOM   5489  CA  PRO B 315       0.261  -8.427 -54.267  1.00117.08           C  
ANISOU 5489  CA  PRO B 315    18385  13584  12517   -835   -273   -281       C  
ATOM   5490  C   PRO B 315       1.086  -8.157 -55.539  1.00120.74           C  
ANISOU 5490  C   PRO B 315    18915  14035  12927   -864   -179   -274       C  
ATOM   5491  O   PRO B 315       0.798  -8.777 -56.560  1.00121.09           O  
ANISOU 5491  O   PRO B 315    19085  14078  12845   -943   -137   -303       O  
ATOM   5492  CB  PRO B 315      -1.015  -7.581 -54.295  1.00118.52           C  
ANISOU 5492  CB  PRO B 315    18526  13845  12662   -878   -407   -233       C  
ATOM   5493  CG  PRO B 315      -1.231  -7.157 -52.907  1.00122.07           C  
ANISOU 5493  CG  PRO B 315    18869  14288  13222   -804   -470   -211       C  
ATOM   5494  CD  PRO B 315       0.118  -6.998 -52.304  1.00117.40           C  
ANISOU 5494  CD  PRO B 315    18230  13641  12738   -718   -408   -218       C  
ATOM   5495  N   VAL B 316       2.076  -7.232 -55.496  1.00116.29           N  
ANISOU 5495  N   VAL B 316    18276  13457  12453   -809   -143   -238       N  
ATOM   5496  CA  VAL B 316       2.957  -6.932 -56.633  1.00116.26           C  
ANISOU 5496  CA  VAL B 316    18329  13428  12418   -831    -29   -229       C  
ATOM   5497  C   VAL B 316       4.049  -8.019 -56.710  1.00120.69           C  
ANISOU 5497  C   VAL B 316    18922  13917  13018   -792    123   -281       C  
ATOM   5498  O   VAL B 316       4.445  -8.413 -57.808  1.00121.06           O  
ANISOU 5498  O   VAL B 316    19085  13928  12983   -832    243   -299       O  
ATOM   5499  CB  VAL B 316       3.571  -5.511 -56.605  1.00119.66           C  
ANISOU 5499  CB  VAL B 316    18669  13864  12934   -803    -31   -174       C  
ATOM   5500  CG1 VAL B 316       4.212  -5.191 -57.946  1.00120.93           C  
ANISOU 5500  CG1 VAL B 316    18923  13997  13030   -845     92   -161       C  
ATOM   5501  CG2 VAL B 316       2.535  -4.449 -56.256  1.00118.50           C  
ANISOU 5501  CG2 VAL B 316    18480  13773  12773   -811   -174   -118       C  
ATOM   5502  N   LEU B 317       4.525  -8.501 -55.539  1.00117.35           N  
ANISOU 5502  N   LEU B 317    18405  13469  12714   -706    121   -302       N  
ATOM   5503  CA  LEU B 317       5.503  -9.592 -55.441  1.00118.03           C  
ANISOU 5503  CA  LEU B 317    18508  13489  12848   -642    255   -342       C  
ATOM   5504  C   LEU B 317       4.853 -10.893 -55.888  1.00120.93           C  
ANISOU 5504  C   LEU B 317    19042  13820  13087   -693    308   -392       C  
ATOM   5505  O   LEU B 317       5.503 -11.696 -56.549  1.00121.01           O  
ANISOU 5505  O   LEU B 317    19146  13767  13065   -685    460   -423       O  
ATOM   5506  CB  LEU B 317       6.065  -9.732 -54.016  1.00117.86           C  
ANISOU 5506  CB  LEU B 317    18350  13459  12972   -528    210   -343       C  
ATOM   5507  CG  LEU B 317       7.070  -8.669 -53.593  1.00123.10           C  
ANISOU 5507  CG  LEU B 317    18847  14144  13780   -477    191   -311       C  
ATOM   5508  CD1 LEU B 317       7.136  -8.549 -52.081  1.00123.02           C  
ANISOU 5508  CD1 LEU B 317    18722  14149  13870   -395     73   -308       C  
ATOM   5509  CD2 LEU B 317       8.437  -8.933 -54.183  1.00126.16           C  
ANISOU 5509  CD2 LEU B 317    19197  14494  14243   -436    350   -319       C  
ATOM   5510  N   TYR B 318       3.561 -11.080 -55.555  1.00116.57           N  
ANISOU 5510  N   TYR B 318    18527  13303  12460   -751    192   -403       N  
ATOM   5511  CA  TYR B 318       2.787 -12.227 -55.991  1.00117.38           C  
ANISOU 5511  CA  TYR B 318    18786  13378  12433   -831    225   -457       C  
ATOM   5512  C   TYR B 318       2.653 -12.190 -57.515  1.00122.80           C  
ANISOU 5512  C   TYR B 318    19614  14070  12974   -937    282   -467       C  
ATOM   5513  O   TYR B 318       2.804 -13.229 -58.149  1.00124.17           O  
ANISOU 5513  O   TYR B 318    19941  14178  13059   -978    401   -520       O  
ATOM   5514  CB  TYR B 318       1.399 -12.255 -55.316  1.00118.71           C  
ANISOU 5514  CB  TYR B 318    18934  13598  12574   -882     82   -461       C  
ATOM   5515  CG  TYR B 318       0.509 -13.400 -55.775  1.00123.14           C  
ANISOU 5515  CG  TYR B 318    19646  14137  13004   -992    107   -524       C  
ATOM   5516  CD1 TYR B 318      -0.286 -13.283 -56.911  1.00126.36           C  
ANISOU 5516  CD1 TYR B 318    20144  14598  13269  -1126     60   -536       C  
ATOM   5517  CD2 TYR B 318       0.449 -14.594 -55.059  1.00124.49           C  
ANISOU 5517  CD2 TYR B 318    19876  14234  13189   -967    174   -574       C  
ATOM   5518  CE1 TYR B 318      -1.081 -14.341 -57.354  1.00128.68           C  
ANISOU 5518  CE1 TYR B 318    20577  14876  13440  -1247     77   -605       C  
ATOM   5519  CE2 TYR B 318      -0.368 -15.648 -55.475  1.00126.42           C  
ANISOU 5519  CE2 TYR B 318    20269  14450  13317  -1085    208   -641       C  
ATOM   5520  CZ  TYR B 318      -1.133 -15.516 -56.624  1.00136.89           C  
ANISOU 5520  CZ  TYR B 318    21673  15834  14504  -1233    155   -660       C  
ATOM   5521  OH  TYR B 318      -1.940 -16.547 -57.052  1.00142.57           O  
ANISOU 5521  OH  TYR B 318    22536  16530  15105  -1370    179   -735       O  
ATOM   5522  N   ALA B 319       2.369 -11.005 -58.096  1.00119.07           N  
ANISOU 5522  N   ALA B 319    19109  13665  12468   -978    201   -417       N  
ATOM   5523  CA  ALA B 319       2.166 -10.812 -59.536  1.00120.09           C  
ANISOU 5523  CA  ALA B 319    19381  13807  12442  -1075    230   -415       C  
ATOM   5524  C   ALA B 319       3.451 -10.974 -60.352  1.00125.78           C  
ANISOU 5524  C   ALA B 319    20182  14447  13161  -1047    424   -423       C  
ATOM   5525  O   ALA B 319       3.383 -11.542 -61.448  1.00126.94           O  
ANISOU 5525  O   ALA B 319    20515  14558  13160  -1125    509   -458       O  
ATOM   5526  CB  ALA B 319       1.559  -9.450 -59.803  1.00120.59           C  
ANISOU 5526  CB  ALA B 319    19382  13956  12479  -1099     94   -346       C  
ATOM   5527  N   PHE B 320       4.607 -10.468 -59.838  1.00122.13           N  
ANISOU 5527  N   PHE B 320    19582  13957  12864   -942    496   -393       N  
ATOM   5528  CA  PHE B 320       5.920 -10.593 -60.493  1.00123.03           C  
ANISOU 5528  CA  PHE B 320    19731  13995  13018   -902    695   -397       C  
ATOM   5529  C   PHE B 320       6.287 -12.076 -60.605  1.00127.59           C  
ANISOU 5529  C   PHE B 320    20428  14486  13565   -882    844   -459       C  
ATOM   5530  O   PHE B 320       6.753 -12.506 -61.659  1.00128.98           O  
ANISOU 5530  O   PHE B 320    20759  14595  13654   -914   1007   -481       O  
ATOM   5531  CB  PHE B 320       7.021  -9.807 -59.735  1.00124.49           C  
ANISOU 5531  CB  PHE B 320    19707  14184  13411   -799    718   -359       C  
ATOM   5532  CG  PHE B 320       8.440 -10.059 -60.212  1.00127.50           C  
ANISOU 5532  CG  PHE B 320    20077  14490  13876   -743    932   -365       C  
ATOM   5533  CD1 PHE B 320       8.996  -9.295 -61.230  1.00132.02           C  
ANISOU 5533  CD1 PHE B 320    20692  15041  14429   -781   1042   -338       C  
ATOM   5534  CD2 PHE B 320       9.221 -11.059 -59.639  1.00130.27           C  
ANISOU 5534  CD2 PHE B 320    20376  14789  14330   -644   1032   -394       C  
ATOM   5535  CE1 PHE B 320      10.307  -9.529 -61.669  1.00134.21           C  
ANISOU 5535  CE1 PHE B 320    20948  15248  14800   -729   1258   -343       C  
ATOM   5536  CE2 PHE B 320      10.524 -11.305 -60.094  1.00134.31           C  
ANISOU 5536  CE2 PHE B 320    20862  15236  14933   -582   1238   -394       C  
ATOM   5537  CZ  PHE B 320      11.060 -10.531 -61.098  1.00133.31           C  
ANISOU 5537  CZ  PHE B 320    20764  15090  14797   -629   1353   -371       C  
ATOM   5538  N   LEU B 321       6.073 -12.846 -59.513  1.00122.71           N  
ANISOU 5538  N   LEU B 321    19753  13859  13012   -825    798   -485       N  
ATOM   5539  CA  LEU B 321       6.342 -14.281 -59.449  1.00122.95           C  
ANISOU 5539  CA  LEU B 321    19899  13797  13018   -793    935   -539       C  
ATOM   5540  C   LEU B 321       5.335 -15.047 -60.283  1.00127.78           C  
ANISOU 5540  C   LEU B 321    20740  14388  13425   -932    941   -595       C  
ATOM   5541  O   LEU B 321       5.638 -16.158 -60.707  1.00129.19           O  
ANISOU 5541  O   LEU B 321    21080  14468  13538   -937   1102   -645       O  
ATOM   5542  CB  LEU B 321       6.333 -14.804 -58.003  1.00122.14           C  
ANISOU 5542  CB  LEU B 321    19684  13689  13033   -690    875   -543       C  
ATOM   5543  CG  LEU B 321       7.493 -14.380 -57.102  1.00126.35           C  
ANISOU 5543  CG  LEU B 321    20010  14230  13768   -539    885   -501       C  
ATOM   5544  CD1 LEU B 321       7.172 -14.654 -55.650  1.00125.14           C  
ANISOU 5544  CD1 LEU B 321    19762  14093  13692   -459    766   -498       C  
ATOM   5545  CD2 LEU B 321       8.799 -15.059 -57.502  1.00130.51           C  
ANISOU 5545  CD2 LEU B 321    20557  14671  14359   -444   1101   -507       C  
ATOM   5546  N   ASP B 322       4.138 -14.473 -60.515  1.00123.66           N  
ANISOU 5546  N   ASP B 322    20231  13954  12800  -1045    767   -589       N  
ATOM   5547  CA  ASP B 322       3.130 -15.112 -61.356  1.00124.58           C  
ANISOU 5547  CA  ASP B 322    20548  14071  12717  -1196    743   -645       C  
ATOM   5548  C   ASP B 322       3.522 -14.911 -62.808  1.00130.48           C  
ANISOU 5548  C   ASP B 322    21463  14786  13327  -1261    850   -647       C  
ATOM   5549  O   ASP B 322       3.324 -15.799 -63.643  1.00131.26           O  
ANISOU 5549  O   ASP B 322    21783  14823  13268  -1355    941   -709       O  
ATOM   5550  CB  ASP B 322       1.725 -14.567 -61.075  1.00125.83           C  
ANISOU 5550  CB  ASP B 322    20636  14346  12826  -1284    513   -631       C  
ATOM   5551  CG  ASP B 322       0.643 -15.612 -61.280  1.00140.42           C  
ANISOU 5551  CG  ASP B 322    22626  16189  14537  -1420    476   -707       C  
ATOM   5552  OD1 ASP B 322       0.502 -16.109 -62.424  1.00142.74           O  
ANISOU 5552  OD1 ASP B 322    23123  16452  14660  -1532    538   -755       O  
ATOM   5553  OD2 ASP B 322      -0.058 -15.943 -60.295  1.00147.51           O1-
ANISOU 5553  OD2 ASP B 322    23441  17110  15496  -1421    392   -722       O1-
ATOM   5554  N   LYS B 323       4.123 -13.746 -63.089  1.00127.16           N  
ANISOU 5554  N   LYS B 323    20950  14398  12968  -1211    851   -580       N  
ATOM   5555  CA  LYS B 323       4.620 -13.356 -64.397  1.00128.14           C  
ANISOU 5555  CA  LYS B 323    21218  14486  12983  -1252    966   -567       C  
ATOM   5556  C   LYS B 323       5.774 -14.305 -64.811  1.00133.23           C  
ANISOU 5556  C   LYS B 323    21985  14994  13644  -1200   1234   -607       C  
ATOM   5557  O   LYS B 323       5.585 -15.119 -65.715  1.00134.55           O  
ANISOU 5557  O   LYS B 323    22393  15093  13637  -1288   1333   -663       O  
ATOM   5558  CB  LYS B 323       5.049 -11.861 -64.365  1.00129.71           C  
ANISOU 5558  CB  LYS B 323    21262  14739  13281  -1196    918   -483       C  
ATOM   5559  CG  LYS B 323       5.923 -11.359 -65.519  1.00144.06           C  
ANISOU 5559  CG  LYS B 323    23192  16497  15047  -1201   1089   -458       C  
ATOM   5560  CD  LYS B 323       6.589 -10.028 -65.165  1.00153.04           C  
ANISOU 5560  CD  LYS B 323    24138  17665  16347  -1126   1080   -385       C  
ATOM   5561  CE  LYS B 323       7.648  -9.599 -66.155  1.00160.37           C  
ANISOU 5561  CE  LYS B 323    25151  18513  17269  -1118   1292   -363       C  
ATOM   5562  NZ  LYS B 323       9.021  -9.939 -65.692  1.00165.55           N1+
ANISOU 5562  NZ  LYS B 323    25673  19097  18129  -1015   1482   -373       N1+
ATOM   5563  N   ASN B 324       6.917 -14.245 -64.104  1.00128.84           N  
ANISOU 5563  N   ASN B 324    21260  14398  13294  -1059   1344   -580       N  
ATOM   5564  CA  ASN B 324       8.145 -14.968 -64.422  1.00129.85           C  
ANISOU 5564  CA  ASN B 324    21449  14406  13481   -977   1605   -598       C  
ATOM   5565  C   ASN B 324       8.074 -16.490 -64.278  1.00136.14           C  
ANISOU 5565  C   ASN B 324    22396  15107  14225   -968   1718   -665       C  
ATOM   5566  O   ASN B 324       8.848 -17.179 -64.950  1.00137.72           O  
ANISOU 5566  O   ASN B 324    22742  15190  14394   -939   1953   -689       O  
ATOM   5567  CB  ASN B 324       9.292 -14.430 -63.596  1.00127.82           C  
ANISOU 5567  CB  ASN B 324    20931  14160  13474   -829   1650   -547       C  
ATOM   5568  CG  ASN B 324       9.634 -13.021 -63.993  1.00150.95           C  
ANISOU 5568  CG  ASN B 324    23761  17142  16452   -846   1623   -489       C  
ATOM   5569  OD1 ASN B 324      10.416 -12.785 -64.916  1.00149.92           O  
ANISOU 5569  OD1 ASN B 324    23704  16949  16310   -849   1807   -478       O  
ATOM   5570  ND2 ASN B 324       8.982 -12.054 -63.369  1.00140.50           N  
ANISOU 5570  ND2 ASN B 324    22297  15923  15166   -866   1406   -453       N  
ATOM   5571  N   PHE B 325       7.160 -17.022 -63.452  1.00132.84           N  
ANISOU 5571  N   PHE B 325    21960  14724  13791   -994   1573   -696       N  
ATOM   5572  CA  PHE B 325       7.040 -18.479 -63.264  1.00134.06           C  
ANISOU 5572  CA  PHE B 325    22271  14774  13890   -991   1687   -761       C  
ATOM   5573  C   PHE B 325       5.671 -19.003 -63.759  1.00139.60           C  
ANISOU 5573  C   PHE B 325    23178  15490  14375  -1179   1586   -830       C  
ATOM   5574  O   PHE B 325       5.168 -20.005 -63.239  1.00139.32           O  
ANISOU 5574  O   PHE B 325    23217  15408  14312  -1202   1591   -883       O  
ATOM   5575  CB  PHE B 325       7.263 -18.857 -61.783  1.00134.78           C  
ANISOU 5575  CB  PHE B 325    22181  14868  14161   -851   1643   -744       C  
ATOM   5576  CG  PHE B 325       8.633 -18.574 -61.208  1.00136.36           C  
ANISOU 5576  CG  PHE B 325    22180  15053  14576   -663   1738   -686       C  
ATOM   5577  CD1 PHE B 325       8.962 -17.306 -60.738  1.00138.52           C  
ANISOU 5577  CD1 PHE B 325    22210  15431  14991   -614   1610   -624       C  
ATOM   5578  CD2 PHE B 325       9.569 -19.590 -61.069  1.00139.50           C  
ANISOU 5578  CD2 PHE B 325    22626  15336  15043   -533   1949   -694       C  
ATOM   5579  CE1 PHE B 325      10.221 -17.049 -60.191  1.00139.47           C  
ANISOU 5579  CE1 PHE B 325    22129  15548  15315   -457   1682   -578       C  
ATOM   5580  CE2 PHE B 325      10.829 -19.331 -60.522  1.00142.53           C  
ANISOU 5580  CE2 PHE B 325    22797  15722  15636   -357   2021   -639       C  
ATOM   5581  CZ  PHE B 325      11.145 -18.063 -60.085  1.00139.64           C  
ANISOU 5581  CZ  PHE B 325    22180  15469  15407   -327   1880   -584       C  
ATOM   5582  N   LYS B 326       5.100 -18.337 -64.793  1.00137.07           N  
ANISOU 5582  N   LYS B 326    22954  15229  13896  -1313   1501   -830       N  
ATOM   5583  CA  LYS B 326       3.790 -18.618 -65.383  1.00137.40           C  
ANISOU 5583  CA  LYS B 326    23162  15317  13728  -1503   1368   -888       C  
ATOM   5584  C   LYS B 326       3.646 -20.062 -65.877  1.00143.41           C  
ANISOU 5584  C   LYS B 326    24201  15949  14340  -1594   1525   -986       C  
ATOM   5585  O   LYS B 326       2.759 -20.761 -65.387  1.00142.58           O  
ANISOU 5585  O   LYS B 326    24126  15851  14196  -1676   1443  -1042       O  
ATOM   5586  CB  LYS B 326       3.483 -17.636 -66.526  1.00140.32           C  
ANISOU 5586  CB  LYS B 326    23605  15760  13952  -1597   1282   -858       C  
ATOM   5587  N   ARG B 327       4.525 -20.519 -66.802  1.00142.44           N  
ANISOU 5587  N   ARG B 327    24284  15698  14140  -1579   1766  -1009       N  
ATOM   5588  CA  ARG B 327       4.479 -21.861 -67.417  1.00144.40           C  
ANISOU 5588  CA  ARG B 327    24839  15800  14226  -1668   1949  -1104       C  
ATOM   5589  C   ARG B 327       4.587 -23.011 -66.386  1.00149.10           C  
ANISOU 5589  C   ARG B 327    25426  16301  14926  -1591   2048  -1140       C  
ATOM   5590  O   ARG B 327       4.236 -24.151 -66.714  1.00150.04           O  
ANISOU 5590  O   ARG B 327    25794  16311  14905  -1694   2156  -1229       O  
ATOM   5591  CB  ARG B 327       5.571 -22.017 -68.498  1.00146.04           C  
ANISOU 5591  CB  ARG B 327    25244  15876  14366  -1627   2220  -1104       C  
ATOM   5592  CG  ARG B 327       5.365 -21.129 -69.733  1.00156.06           C  
ANISOU 5592  CG  ARG B 327    26629  17202  15463  -1737   2158  -1087       C  
ATOM   5593  CD  ARG B 327       6.342 -21.435 -70.859  1.00168.13           C  
ANISOU 5593  CD  ARG B 327    28409  18578  16895  -1718   2450  -1101       C  
ATOM   5594  NE  ARG B 327       6.252 -20.452 -71.943  1.00178.99           N  
ANISOU 5594  NE  ARG B 327    29878  20006  18125  -1794   2396  -1068       N  
ATOM   5595  CZ  ARG B 327       6.731 -20.625 -73.174  1.00195.39           C  
ANISOU 5595  CZ  ARG B 327    32242  21967  20030  -1842   2600  -1092       C  
ATOM   5596  NH1 ARG B 327       7.337 -21.763 -73.501  1.00185.89           N1+
ANISOU 5596  NH1 ARG B 327    31263  20584  18781  -1823   2881  -1152       N1+
ATOM   5597  NH2 ARG B 327       6.601 -19.673 -74.088  1.00178.67           N  
ANISOU 5597  NH2 ARG B 327    30206  19901  17778  -1903   2534  -1053       N  
ATOM   5598  N   CYS B 328       5.027 -22.699 -65.142  1.00144.61           N  
ANISOU 5598  N   CYS B 328    24584  15772  14587  -1417   2003  -1074       N  
ATOM   5599  CA  CYS B 328       5.201 -23.656 -64.044  1.00144.12           C  
ANISOU 5599  CA  CYS B 328    24491  15630  14640  -1308   2082  -1088       C  
ATOM   5600  C   CYS B 328       3.949 -23.789 -63.199  1.00145.27           C  
ANISOU 5600  C   CYS B 328    24565  15854  14778  -1401   1874  -1118       C  
ATOM   5601  O   CYS B 328       3.653 -24.894 -62.750  1.00145.29           O  
ANISOU 5601  O   CYS B 328    24691  15759  14756  -1419   1956  -1175       O  
ATOM   5602  CB  CYS B 328       6.393 -23.269 -63.176  1.00144.07           C  
ANISOU 5602  CB  CYS B 328    24241  15624  14874  -1067   2143  -1000       C  
ATOM   5603  SG  CYS B 328       7.970 -23.224 -64.065  1.00149.72           S  
ANISOU 5603  SG  CYS B 328    25011  16237  15641   -939   2426   -963       S  
ATOM   5604  N   PHE B 329       3.243 -22.675 -62.944  1.00139.90           N  
ANISOU 5604  N   PHE B 329    23687  15339  14130  -1451   1623  -1076       N  
ATOM   5605  CA  PHE B 329       2.057 -22.672 -62.086  1.00138.52           C  
ANISOU 5605  CA  PHE B 329    23409  15248  13974  -1526   1426  -1093       C  
ATOM   5606  C   PHE B 329       0.733 -22.697 -62.864  1.00143.06           C  
ANISOU 5606  C   PHE B 329    24102  15897  14358  -1768   1281  -1159       C  
ATOM   5607  O   PHE B 329      -0.253 -23.192 -62.310  1.00143.37           O  
ANISOU 5607  O   PHE B 329    24137  15954  14383  -1864   1195  -1207       O  
ATOM   5608  CB  PHE B 329       2.092 -21.489 -61.109  1.00138.20           C  
ANISOU 5608  CB  PHE B 329    23062  15336  14113  -1408   1248  -1001       C  
ATOM   5609  CG  PHE B 329       3.314 -21.551 -60.228  1.00139.11           C  
ANISOU 5609  CG  PHE B 329    23052  15390  14415  -1183   1362   -945       C  
ATOM   5610  CD1 PHE B 329       3.496 -22.602 -59.334  1.00142.32           C  
ANISOU 5610  CD1 PHE B 329    23502  15692  14880  -1093   1465   -967       C  
ATOM   5611  CD2 PHE B 329       4.311 -20.591 -60.328  1.00140.92           C  
ANISOU 5611  CD2 PHE B 329    23128  15660  14756  -1063   1373   -872       C  
ATOM   5612  CE1 PHE B 329       4.649 -22.685 -58.551  1.00143.05           C  
ANISOU 5612  CE1 PHE B 329    23479  15735  15136   -876   1558   -911       C  
ATOM   5613  CE2 PHE B 329       5.464 -20.675 -59.542  1.00143.74           C  
ANISOU 5613  CE2 PHE B 329    23355  15971  15288   -863   1468   -824       C  
ATOM   5614  CZ  PHE B 329       5.623 -21.717 -58.655  1.00141.91           C  
ANISOU 5614  CZ  PHE B 329    23161  15650  15110   -765   1550   -841       C  
ATOM   5615  N   ARG B 330       0.707 -22.220 -64.136  1.00138.77           N  
ANISOU 5615  N   ARG B 330    23670  15390  13665  -1868   1260  -1164       N  
ATOM   5616  CA  ARG B 330      -0.508 -22.236 -64.957  1.00138.57           C  
ANISOU 5616  CA  ARG B 330    23760  15446  13444  -2095   1107  -1225       C  
ATOM   5617  C   ARG B 330      -0.860 -23.668 -65.374  1.00142.16           C  
ANISOU 5617  C   ARG B 330    24498  15774  13744  -2248   1240  -1347       C  
ATOM   5618  O   ARG B 330      -0.007 -24.401 -65.886  1.00142.73           O  
ANISOU 5618  O   ARG B 330    24785  15690  13755  -2214   1479  -1382       O  
ATOM   5619  CB  ARG B 330      -0.375 -21.332 -66.190  1.00139.18           C  
ANISOU 5619  CB  ARG B 330    23901  15590  13391  -2144   1051  -1190       C  
ATOM   5620  N   GLN B 331      -2.109 -24.069 -65.094  1.00137.72           N  
ANISOU 5620  N   GLN B 331    23927  15270  13129  -2413   1097  -1411       N  
ATOM   5621  CA  GLN B 331      -2.671 -25.381 -65.417  1.00138.69           C  
ANISOU 5621  CA  GLN B 331    24302  15290  13106  -2600   1189  -1537       C  
ATOM   5622  C   GLN B 331      -4.149 -25.236 -65.743  1.00142.40           C  
ANISOU 5622  C   GLN B 331    24737  15907  13462  -2835    942  -1593       C  
ATOM   5623  O   GLN B 331      -4.813 -24.368 -65.174  1.00140.54           O  
ANISOU 5623  O   GLN B 331    24237  15830  13332  -2814    727  -1530       O  
ATOM   5624  CB  GLN B 331      -2.442 -26.408 -64.290  1.00139.48           C  
ANISOU 5624  CB  GLN B 331    24418  15249  13329  -2514   1355  -1566       C  
ATOM   5625  CG  GLN B 331      -2.953 -26.018 -62.904  1.00149.70           C  
ANISOU 5625  CG  GLN B 331    25432  16632  14817  -2430   1216  -1512       C  
ATOM   5626  CD  GLN B 331      -2.311 -26.865 -61.830  1.00170.72           C  
ANISOU 5626  CD  GLN B 331    28121  19138  17607  -2269   1412  -1507       C  
ATOM   5627  OE1 GLN B 331      -1.083 -26.913 -61.698  1.00168.06           O  
ANISOU 5627  OE1 GLN B 331    27800  18708  17346  -2071   1576  -1453       O  
ATOM   5628  NE2 GLN B 331      -3.123 -27.527 -61.012  1.00160.59           N  
ANISOU 5628  NE2 GLN B 331    26834  17826  16357  -2343   1399  -1557       N  
ATOM   5629  N   LEU B 332      -4.655 -26.068 -66.671  1.00140.89           N  
ANISOU 5629  N   LEU B 332    24811  15664  13055  -3061    972  -1710       N  
ATOM   5630  CA  LEU B 332      -6.050 -26.047 -67.124  1.00141.78           C  
ANISOU 5630  CA  LEU B 332    24912  15918  13039  -3312    737  -1778       C  
ATOM   5631  C   LEU B 332      -7.052 -26.277 -65.981  1.00144.62           C  
ANISOU 5631  C   LEU B 332    25064  16343  13543  -3366    627  -1797       C  
ATOM   5632  O   LEU B 332      -6.820 -27.126 -65.116  1.00144.15           O  
ANISOU 5632  O   LEU B 332    25044  16145  13583  -3315    801  -1830       O  
ATOM   5633  CB  LEU B 332      -6.281 -27.078 -68.238  1.00144.28           C  
ANISOU 5633  CB  LEU B 332    25585  16136  13101  -3547    826  -1916       C  
ATOM   5634  CG  LEU B 332      -6.034 -26.585 -69.657  1.00150.14           C  
ANISOU 5634  CG  LEU B 332    26506  16915  13626  -3609    779  -1912       C  
ATOM   5635  CD1 LEU B 332      -5.931 -27.731 -70.615  1.00152.88           C  
ANISOU 5635  CD1 LEU B 332    27250  17102  13736  -3795    949  -2047       C  
ATOM   5636  CD2 LEU B 332      -7.136 -25.665 -70.114  1.00152.98           C  
ANISOU 5636  CD2 LEU B 332    26704  17512  13909  -3734    440  -1885       C  
ATOM   5637  N   CYS B 333      -8.158 -25.496 -65.988  1.00140.02           N  
ANISOU 5637  N   CYS B 333    24262  15968  12971  -3461    346  -1770       N  
ATOM   5638  CA  CYS B 333      -9.240 -25.523 -65.003  1.00138.75           C  
ANISOU 5638  CA  CYS B 333    23871  15900  12948  -3523    214  -1778       C  
ATOM   5639  C   CYS B 333     -10.028 -26.838 -65.101  1.00144.58           C  
ANISOU 5639  C   CYS B 333    24783  16562  13589  -3780    273  -1931       C  
ATOM   5640  O   CYS B 333     -11.144 -26.855 -65.624  1.00146.02           O  
ANISOU 5640  O   CYS B 333    24931  16877  13673  -4006     81  -1994       O  
ATOM   5641  CB  CYS B 333     -10.150 -24.308 -65.179  1.00138.54           C  
ANISOU 5641  CB  CYS B 333    23582  16114  12942  -3550    -90  -1703       C  
ATOM   5642  SG  CYS B 333      -9.426 -22.746 -64.616  1.00139.67           S  
ANISOU 5642  SG  CYS B 333    23465  16339  13264  -3245   -154  -1521       S  
ATOM   5643  N   ARG B 334      -9.430 -27.935 -64.584  1.00140.71           N  
ANISOU 5643  N   ARG B 334    24477  15857  13130  -3740    542  -1989       N  
ATOM   5644  CA  ARG B 334      -9.972 -29.295 -64.576  1.00154.12           C  
ANISOU 5644  CA  ARG B 334    26385  17429  14746  -3960    667  -2135       C  
ATOM   5645  C   ARG B 334     -11.149 -29.406 -63.621  1.00168.28           C  
ANISOU 5645  C   ARG B 334    27958  19304  16676  -4063    556  -2159       C  
ATOM   5646  O   ARG B 334     -12.267 -29.054 -63.986  1.00126.85           O  
ANISOU 5646  O   ARG B 334    22570  14237  11390  -4251    322  -2190       O  
ATOM   5647  CB  ARG B 334      -8.878 -30.301 -64.185  1.00153.59           C  
ANISOU 5647  CB  ARG B 334    26560  17100  14697  -3828   1001  -2159       C  
TER    5648      ARG B 334                                                      
HETATM 5649  CBI OWY A1201       2.438 -40.250 -54.794  1.00115.32           C  
HETATM 5650  CBG OWY A1201       1.794 -39.555 -53.596  1.00114.76           C  
HETATM 5651  NBF OWY A1201       2.007 -40.204 -52.438  1.00116.10           N  
HETATM 5652  CBH OWY A1201       1.144 -41.201 -52.107  1.00114.97           C  
HETATM 5653  CBJ OWY A1201      -0.138 -40.803 -51.327  1.00113.42           C  
HETATM 5654  CBD OWY A1201       3.082 -39.835 -51.677  1.00117.66           C  
HETATM 5655  OBE OWY A1201       3.791 -38.935 -52.048  1.00119.43           O  
HETATM 5656  CAZ OWY A1201       3.485 -40.472 -50.392  1.00114.24           C  
HETATM 5657  CBA OWY A1201       4.647 -41.270 -50.340  1.00112.61           C  
HETATM 5658  CBB OWY A1201       5.070 -41.843 -49.123  1.00111.42           C  
HETATM 5659  CAY OWY A1201       2.787 -40.195 -49.205  1.00112.38           C  
HETATM 5660  CAX OWY A1201       3.190 -40.780 -47.996  1.00111.56           C  
HETATM 5661  CAR OWY A1201       4.349 -41.590 -47.938  1.00111.03           C  
HETATM 5662  CAP OWY A1201       4.792 -42.221 -46.661  1.00108.99           C  
HETATM 5663  CAQ OWY A1201       3.774 -43.222 -46.249  1.00107.59           C  
HETATM 5664  CAS OWY A1201       3.864 -44.497 -46.812  1.00107.15           C  
HETATM 5665  CAT OWY A1201       2.897 -45.468 -46.521  1.00107.47           C  
HETATM 5666  OBC OWY A1201       2.993 -46.692 -47.122  1.00107.36           O  
HETATM 5667  CAU OWY A1201       1.847 -45.186 -45.633  1.00107.52           C  
HETATM 5668  CAV OWY A1201       1.736 -43.904 -45.072  1.00107.57           C  
HETATM 5669  CAW OWY A1201       2.691 -42.922 -45.388  1.00107.68           C  
HETATM 5670  NAK OWY A1201       5.140 -41.265 -45.594  1.00105.88           N  
HETATM 5671  CAJ OWY A1201       5.698 -41.858 -44.386  1.00105.98           C  
HETATM 5672  CAI OWY A1201       5.645 -40.762 -43.290  1.00107.88           C  
HETATM 5673  CAO OWY A1201       7.092 -42.511 -44.506  1.00105.63           C  
HETATM 5674  CAL OWY A1201       5.982 -40.130 -46.071  1.00103.68           C  
HETATM 5675  CAM OWY A1201       5.824 -38.983 -45.023  1.00106.52           C  
HETATM 5676  CAN OWY A1201       4.403 -38.413 -45.120  1.00108.08           C  
HETATM 5677  NAH OWY A1201       6.218 -39.471 -43.698  1.00108.19           N  
HETATM 5678  CAG OWY A1201       6.023 -38.411 -42.656  1.00107.06           C  
HETATM 5679  CAB OWY A1201       6.519 -38.701 -41.289  1.00105.60           C  
HETATM 5680  CAA OWY A1201       5.683 -38.407 -40.190  1.00104.19           C  
HETATM 5681  CAF OWY A1201       6.112 -38.664 -38.869  1.00102.18           C  
HETATM 5682  CAE OWY A1201       7.395 -39.186 -38.632  1.00101.10           C  
HETATM 5683  CAD OWY A1201       8.248 -39.451 -39.724  1.00102.46           C  
HETATM 5684  CAC OWY A1201       7.817 -39.209 -41.048  1.00104.39           C  
HETATM 5685  CBI OWY B1201      -0.324  -2.694 -29.993  1.00123.27           C  
HETATM 5686  CBG OWY B1201       0.945  -2.349 -29.215  1.00123.74           C  
HETATM 5687  NBF OWY B1201       1.762  -3.390 -28.921  1.00124.67           N  
HETATM 5688  CBH OWY B1201       1.523  -4.081 -27.785  1.00127.24           C  
HETATM 5689  CBJ OWY B1201       2.174  -3.502 -26.504  1.00127.60           C  
HETATM 5690  CBD OWY B1201       2.819  -3.765 -29.704  1.00122.55           C  
HETATM 5691  OBE OWY B1201       3.506  -4.692 -29.369  1.00124.16           O  
HETATM 5692  CAZ OWY B1201       3.242  -3.100 -30.958  1.00118.72           C  
HETATM 5693  CBA OWY B1201       4.422  -2.321 -30.969  1.00116.24           C  
HETATM 5694  CBB OWY B1201       4.855  -1.703 -32.158  1.00113.86           C  
HETATM 5695  CAY OWY B1201       2.547  -3.326 -32.164  1.00117.49           C  
HETATM 5696  CAX OWY B1201       2.973  -2.706 -33.349  1.00115.90           C  
HETATM 5697  CAR OWY B1201       4.141  -1.904 -33.358  1.00114.01           C  
HETATM 5698  CAP OWY B1201       4.601  -1.230 -34.602  1.00112.14           C  
HETATM 5699  CAQ OWY B1201       3.591  -0.204 -34.988  1.00112.07           C  
HETATM 5700  CAS OWY B1201       3.661   1.055 -34.357  1.00112.00           C  
HETATM 5701  CAT OWY B1201       2.702   2.047 -34.616  1.00112.77           C  
HETATM 5702  OBC OWY B1201       2.789   3.259 -33.968  1.00114.53           O  
HETATM 5703  CAU OWY B1201       1.667   1.786 -35.539  1.00112.33           C  
HETATM 5704  CAV OWY B1201       1.576   0.528 -36.174  1.00112.07           C  
HETATM 5705  CAW OWY B1201       2.525  -0.469 -35.886  1.00111.83           C  
HETATM 5706  NAK OWY B1201       4.961  -2.146 -35.696  1.00108.82           N  
HETATM 5707  CAJ OWY B1201       5.553  -1.517 -36.863  1.00108.60           C  
HETATM 5708  CAI OWY B1201       5.532  -2.577 -37.994  1.00109.05           C  
HETATM 5709  CAO OWY B1201       6.956  -0.893 -36.688  1.00109.22           C  
HETATM 5710  CAL OWY B1201       5.783  -3.308 -35.252  1.00105.97           C  
HETATM 5711  CAM OWY B1201       5.650  -4.427 -36.336  1.00104.88           C  
HETATM 5712  CAN OWY B1201       4.222  -4.978 -36.305  1.00102.76           C  
HETATM 5713  NAH OWY B1201       6.083  -3.889 -37.622  1.00107.75           N  
HETATM 5714  CAG OWY B1201       5.917  -4.909 -38.710  1.00107.55           C  
HETATM 5715  CAB OWY B1201       6.453  -4.576 -40.051  1.00105.66           C  
HETATM 5716  CAA OWY B1201       5.638  -4.819 -41.169  1.00105.66           C  
HETATM 5717  CAF OWY B1201       6.099  -4.514 -42.463  1.00106.09           C  
HETATM 5718  CAE OWY B1201       7.396  -4.002 -42.655  1.00106.25           C  
HETATM 5719  CAD OWY B1201       8.227  -3.794 -41.537  1.00106.24           C  
HETATM 5720  CAC OWY B1201       7.759  -4.082 -40.242  1.00105.39           C  
CONECT 1412 1997                                                                
CONECT 1997 1412                                                                
CONECT 3999 4585                                                                
CONECT 4585 3999                                                                
CONECT 5649 5650                                                                
CONECT 5650 5649 5651                                                           
CONECT 5651 5650 5652 5654                                                      
CONECT 5652 5651 5653                                                           
CONECT 5653 5652                                                                
CONECT 5654 5651 5655 5656                                                      
CONECT 5655 5654                                                                
CONECT 5656 5654 5657 5659                                                      
CONECT 5657 5656 5658                                                           
CONECT 5658 5657 5661                                                           
CONECT 5659 5656 5660                                                           
CONECT 5660 5659 5661                                                           
CONECT 5661 5658 5660 5662                                                      
CONECT 5662 5661 5663 5670                                                      
CONECT 5663 5662 5664 5669                                                      
CONECT 5664 5663 5665                                                           
CONECT 5665 5664 5666 5667                                                      
CONECT 5666 5665                                                                
CONECT 5667 5665 5668                                                           
CONECT 5668 5667 5669                                                           
CONECT 5669 5663 5668                                                           
CONECT 5670 5662 5671 5674                                                      
CONECT 5671 5670 5672 5673                                                      
CONECT 5672 5671 5677                                                           
CONECT 5673 5671                                                                
CONECT 5674 5670 5675                                                           
CONECT 5675 5674 5676 5677                                                      
CONECT 5676 5675                                                                
CONECT 5677 5672 5675 5678                                                      
CONECT 5678 5677 5679                                                           
CONECT 5679 5678 5680 5684                                                      
CONECT 5680 5679 5681                                                           
CONECT 5681 5680 5682                                                           
CONECT 5682 5681 5683                                                           
CONECT 5683 5682 5684                                                           
CONECT 5684 5679 5683                                                           
CONECT 5685 5686                                                                
CONECT 5686 5685 5687                                                           
CONECT 5687 5686 5688 5690                                                      
CONECT 5688 5687 5689                                                           
CONECT 5689 5688                                                                
CONECT 5690 5687 5691 5692                                                      
CONECT 5691 5690                                                                
CONECT 5692 5690 5693 5695                                                      
CONECT 5693 5692 5694                                                           
CONECT 5694 5693 5697                                                           
CONECT 5695 5692 5696                                                           
CONECT 5696 5695 5697                                                           
CONECT 5697 5694 5696 5698                                                      
CONECT 5698 5697 5699 5706                                                      
CONECT 5699 5698 5700 5705                                                      
CONECT 5700 5699 5701                                                           
CONECT 5701 5700 5702 5703                                                      
CONECT 5702 5701                                                                
CONECT 5703 5701 5704                                                           
CONECT 5704 5703 5705                                                           
CONECT 5705 5699 5704                                                           
CONECT 5706 5698 5707 5710                                                      
CONECT 5707 5706 5708 5709                                                      
CONECT 5708 5707 5713                                                           
CONECT 5709 5707                                                                
CONECT 5710 5706 5711                                                           
CONECT 5711 5710 5712 5713                                                      
CONECT 5712 5711                                                                
CONECT 5713 5708 5711 5714                                                      
CONECT 5714 5713 5715                                                           
CONECT 5715 5714 5716 5720                                                      
CONECT 5716 5715 5717                                                           
CONECT 5717 5716 5718                                                           
CONECT 5718 5717 5719                                                           
CONECT 5719 5718 5720                                                           
CONECT 5720 5715 5719                                                           
MASTER      523    0    2   33    6    0    8    6 5718    2   76   70          
END