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Browse entries in the PDBbind-CN Database

HEADER    HYDROLASE                               26-JAN-16   5HSW              
TITLE     KSHV SOX RNA COMPLEX                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ORF 37;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RNA (5'-                                                   
COMPND   7 R(P*UP*CP*UP*UP*GP*AP*AP*GP*CP*AP*GP*CP*UP*UP*CP*CP*AP*G)-3');       
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8 TYPE M;                     
SOURCE   3 ORGANISM_TAXID: 435895;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;                            
SOURCE   9 ORGANISM_TAXID: 37296                                                
KEYWDS    KSHV, EXONUCLEASE, ENDONUCLEASE, COMPLEX, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.E.BARRETT                                                           
REVDAT   4   17-MAY-17 5HSW    1       JRNL                                     
REVDAT   3   15-FEB-17 5HSW    1       JRNL                                     
REVDAT   2   08-FEB-17 5HSW    1       JRNL                                     
REVDAT   1   01-FEB-17 5HSW    0                                                
JRNL        AUTH   H.LEE,A.O.M.PATSCHULL,C.BAGNERIS,H.RYAN,C.M.SANDERSON,       
JRNL        AUTH 2 B.EBRAHIMI,I.NOBELI,T.E.BARRETT                              
JRNL        TITL   KSHV SOX MEDIATED HOST SHUTOFF: THE MOLECULAR MECHANISM      
JRNL        TITL 2 UNDERLYING MRNA TRANSCRIPT PROCESSING.                       
JRNL        REF    NUCLEIC ACIDS RES.            V.  45  4756 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28132029                                                     
JRNL        DOI    10.1093/NAR/GKW1340                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 9406                           
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)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.262                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.830                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 454                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.70                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2629                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2265                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2496                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2214                   
REMARK   3   BIN FREE R VALUE                        : 0.3172                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.06                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3232                                    
REMARK   3   NUCLEIC ACID ATOMS       : 380                                     
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -21.76490                                            
REMARK   3    B22 (A**2) : -3.03710                                             
REMARK   3    B33 (A**2) : 24.80200                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 14.77590                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.450               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.524               
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      : 0.898                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3743   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5175   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1105   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 59     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 518    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3743   ; 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   : 516    ; 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   : 4141   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.04                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.58                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   31.5075  -12.9032   98.8108           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1001 T22:   -0.2673                                    
REMARK   3     T33:   -0.3202 T12:    0.0224                                    
REMARK   3     T13:   -0.0221 T23:    0.0172                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6189 L22:    2.5652                                    
REMARK   3     L33:    5.3450 L12:    0.2424                                    
REMARK   3     L13:   -0.4382 L23:   -1.2527                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0135 S12:    0.0671 S13:    0.0587                     
REMARK   3     S21:   -0.0131 S22:    0.0869 S23:    0.1490                     
REMARK   3     S31:   -0.0730 S32:   -0.0948 S33:   -0.0734                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   13.9169   -1.9524   81.3492           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0777 T22:    0.1282                                    
REMARK   3     T33:    0.0692 T12:    0.0311                                    
REMARK   3     T13:   -0.0216 T23:   -0.0583                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2936 L22:    0.0000                                    
REMARK   3     L33:    0.0075 L12:   -4.9189                                    
REMARK   3     L13:    2.1494 L23:   -0.1731                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0053 S12:    0.0884 S13:    0.1502                     
REMARK   3     S21:   -0.0900 S22:    0.0281 S23:    0.0568                     
REMARK   3     S31:   -0.0813 S32:   -0.0607 S33:   -0.0228                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HSW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217702.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9408                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
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) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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: 3POV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM ACETATE, 0.1 M MES, PH   
REMARK 280  6.5, 10% W/V PEG 10,000, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       99.10000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       99.10000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     GLN A    28                                                      
REMARK 465     GLN A    29                                                      
REMARK 465     THR A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     TRP A   165                                                      
REMARK 465     PRO A   166                                                      
REMARK 465     ILE A   167                                                      
REMARK 465     THR A   168                                                      
REMARK 465     ASN A   169                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     PHE A   172                                                      
REMARK 465     VAL A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     PRO A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     LYS A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     PRO A   323                                                      
REMARK 465     LEU A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     ILE A   394                                                      
REMARK 465     PRO A   395                                                      
REMARK 465     ARG A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     VAL A   482                                                      
REMARK 465     PRO A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     PRO A   486                                                      
REMARK 465       G B     1                                                      
REMARK 465       A B     2                                                      
REMARK 465       G B     6                                                      
REMARK 465       A B     7                                                      
REMARK 465       G B     8                                                      
REMARK 465       C B     9                                                      
REMARK 465       C B    10                                                      
REMARK 465       A B    11                                                      
REMARK 465       U B    12                                                      
REMARK 465       A B    19                                                      
REMARK 465       A B    29                                                      
REMARK 465       U B    30                                                      
REMARK 465       C B    31                                                      
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     THR A   6    OG1  CG2                                            
REMARK 470     LEU A  10    CG   CD1  CD2                                       
REMARK 470     ASP A  14    CG   OD1  OD2                                       
REMARK 470     LYS A  39    CG   CD   CE   NZ                                   
REMARK 470     LEU A  41    CG   CD1  CD2                                       
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     LYS A  45    CG   CD   CE   NZ                                   
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  48    CG   OD1  OD2                                       
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     TRP A 150    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 150    CZ3  CH2                                            
REMARK 470     GLN A 155    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 156    CG   OD1  ND2                                       
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     ARG A 182    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 227    CG   CD   CE   NZ                                   
REMARK 470     ASP A 229    CG   OD1  OD2                                       
REMARK 470     THR A 230    OG1  CG2                                            
REMARK 470     ARG A 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 234    CG   CD1  CD2                                       
REMARK 470     GLN A 235    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 239    CG   OD1  ND2                                       
REMARK 470     LYS A 241    CG   CD   CE   NZ                                   
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 324    CG   CD1  CD2                                       
REMARK 470     ARG A 329    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 354    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 385    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 401    CG   CD   CE   NZ                                   
REMARK 470     LEU A 427    CG   CD1  CD2                                       
REMARK 470     ARG A 446    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 450    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 451    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 462    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 465    CG   CD   CE   NZ                                   
REMARK 470     ASP A 466    CG   OD1  OD2                                       
REMARK 470     LYS A 472    CG   CD   CE   NZ                                   
REMARK 470     TYR A 477    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 481    CG   OD1  ND2                                       
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    SER A  34       33.85    -89.36                                   
REMARK 500    GLN A 129      -60.68    -14.57                                   
REMARK 500    SER A 130       43.33   -154.89                                   
REMARK 500    ALA A 178        1.15    -62.54                                   
REMARK 500    CYS A 183      -70.41   -130.59                                   
REMARK 500    ASN A 213      -39.24   -132.32                                   
REMARK 500    ARG A 233     -168.13     60.34                                   
REMARK 500    LYS A 255       77.26    -69.30                                   
REMARK 500    ASP A 259      126.57    -35.74                                   
REMARK 500    ALA A 271       73.59   -160.36                                   
REMARK 500    LEU A 294       51.40   -101.24                                   
REMARK 500    LYS A 296        7.17    -49.81                                   
REMARK 500    LEU A 297      128.29     81.98                                   
REMARK 500    PRO A 298     -158.03    -95.72                                   
REMARK 500    GLU A 300       23.38    -70.34                                   
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 ACT A 501                 
DBREF  5HSW A    1   486  UNP    P88925   P88925_HHV8      1    486             
DBREF  5HSW B    1    31  PDB    5HSW     5HSW             1     31             
SEQADV 5HSW GLY A   -1  UNP  P88925              EXPRESSION TAG                 
SEQADV 5HSW ALA A    0  UNP  P88925              EXPRESSION TAG                 
SEQADV 5HSW SER A  244  UNP  P88925    GLU   244 ENGINEERED MUTATION            
SEQRES   1 A  488  GLY ALA MET GLU ALA THR PRO THR PRO ALA ASP LEU PHE          
SEQRES   2 A  488  SER GLU ASP TYR LEU VAL ASP THR LEU ASP GLY LEU THR          
SEQRES   3 A  488  VAL ASP ASP GLN GLN ALA VAL LEU ALA SER LEU SER PHE          
SEQRES   4 A  488  SER LYS PHE LEU LYS HIS ALA LYS VAL ARG ASP TRP CYS          
SEQRES   5 A  488  ALA GLN ALA LYS ILE GLN PRO SER MET PRO ALA LEU ARG          
SEQRES   6 A  488  MET ALA TYR ASN TYR PHE LEU PHE SER LYS VAL GLY GLU          
SEQRES   7 A  488  PHE ILE GLY SER GLU ASP VAL CYS ASN PHE PHE VAL ASP          
SEQRES   8 A  488  ARG VAL PHE GLY GLY VAL ARG LEU LEU ASP VAL ALA SER          
SEQRES   9 A  488  VAL TYR ALA ALA CYS SER GLN MET ASN ALA HIS GLN ARG          
SEQRES  10 A  488  HIS HIS ILE CYS CYS LEU VAL GLU ARG ALA THR SER SER          
SEQRES  11 A  488  GLN SER LEU ASN PRO VAL TRP ASP ALA LEU ARG ASP GLY          
SEQRES  12 A  488  ILE ILE SER SER SER LYS PHE HIS TRP ALA VAL LYS GLN          
SEQRES  13 A  488  GLN ASN THR SER LYS LYS ILE PHE SER PRO TRP PRO ILE          
SEQRES  14 A  488  THR ASN ASN HIS PHE VAL ALA GLY PRO LEU ALA PHE GLY          
SEQRES  15 A  488  LEU ARG CYS GLU GLU VAL VAL LYS THR LEU LEU ALA THR          
SEQRES  16 A  488  LEU LEU HIS PRO ASP GLU THR ASN CYS LEU ASP TYR GLY          
SEQRES  17 A  488  PHE MET GLN SER PRO GLN ASN GLY ILE PHE GLY VAL SER          
SEQRES  18 A  488  LEU ASP PHE ALA ALA ASN VAL LYS THR ASP THR GLU GLY          
SEQRES  19 A  488  ARG LEU GLN PHE ASP PRO ASN CYS LYS VAL TYR SER ILE          
SEQRES  20 A  488  LYS CYS ARG PHE LYS TYR THR PHE ALA LYS MET GLU CYS          
SEQRES  21 A  488  ASP PRO ILE TYR ALA ALA TYR GLN ARG LEU TYR GLU ALA          
SEQRES  22 A  488  PRO GLY LYS LEU ALA LEU LYS ASP PHE PHE TYR SER ILE          
SEQRES  23 A  488  SER LYS PRO ALA VAL GLU TYR VAL GLY LEU GLY LYS LEU          
SEQRES  24 A  488  PRO SER GLU SER ASP TYR LEU VAL ALA TYR ASP GLN GLU          
SEQRES  25 A  488  TRP GLU ALA CYS PRO ARG LYS LYS ARG LYS LEU THR PRO          
SEQRES  26 A  488  LEU HIS ASN LEU ILE ARG GLU CYS ILE LEU HIS ASN SER          
SEQRES  27 A  488  THR THR GLU SER ASP VAL TYR VAL LEU THR ASP PRO GLN          
SEQRES  28 A  488  ASP THR ARG GLY GLN ILE SER ILE LYS ALA ARG PHE LYS          
SEQRES  29 A  488  ALA ASN LEU PHE VAL ASN VAL ARG HIS SER TYR PHE TYR          
SEQRES  30 A  488  GLN VAL LEU LEU GLN SER SER ILE VAL GLU GLU TYR ILE          
SEQRES  31 A  488  GLY LEU ASP SER GLY ILE PRO ARG LEU GLY SER PRO LYS          
SEQRES  32 A  488  TYR TYR ILE ALA THR GLY PHE PHE ARG LYS ARG GLY TYR          
SEQRES  33 A  488  GLN ASP PRO VAL ASN CYS THR ILE GLY GLY ASP ALA LEU          
SEQRES  34 A  488  ASP PRO HIS VAL GLU ILE PRO THR LEU LEU ILE VAL THR          
SEQRES  35 A  488  PRO VAL TYR PHE PRO ARG GLY ALA LYS HIS ARG LEU LEU          
SEQRES  36 A  488  HIS GLN ALA ALA ASN PHE TRP SER ARG SER ALA LYS ASP          
SEQRES  37 A  488  THR PHE PRO TYR ILE LYS TRP ASP PHE SER TYR LEU SER          
SEQRES  38 A  488  ALA ASN VAL PRO HIS SER PRO                                  
SEQRES   1 B   31    G   A   U   C   U   G   A   G   C   C   A   U   U          
SEQRES   2 B   31    G   A   A   G   C   A   A   G   C   U   U   C   C          
SEQRES   3 B   31    A   G   A   U   C                                          
HET    ACT  A 501       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4  HOH   *9(H2 O)                                                      
HELIX    1 AA1 SER A   36  HIS A   43  1                                   8    
HELIX    2 AA2 HIS A   43  ALA A   51  1                                   9    
HELIX    3 AA3 PRO A   60  ILE A   78  1                                  19    
HELIX    4 AA4 GLU A   81  ARG A   90  1                                  10    
HELIX    5 AA5 ASP A   99  GLN A  109  1                                  11    
HELIX    6 AA6 ASN A  111  THR A  126  1                                  16    
HELIX    7 AA7 PRO A  133  ASP A  140  1                                   8    
HELIX    8 AA8 LYS A  147  GLN A  154  1                                   8    
HELIX    9 AA9 CYS A  183  LEU A  195  1                                  13    
HELIX   10 AB1 PHE A  249  THR A  252  5                                   4    
HELIX   11 AB2 ASP A  259  GLU A  270  1                                  12    
HELIX   12 AB3 GLY A  273  TYR A  282  1                                  10    
HELIX   13 AB4 ASP A  308  GLU A  312  5                                   5    
HELIX   14 AB5 HIS A  325  SER A  336  1                                  12    
HELIX   15 AB6 HIS A  371  GLY A  389  1                                  19    
HELIX   16 AB7 PRO A  445  PHE A  468  1                                  24    
HELIX   17 AB8 TYR A  477  ASN A  481  5                                   5    
SHEET    1 AA1 3 ILE A 143  SER A 144  0                                        
SHEET    2 AA1 3 PHE A 216  VAL A 218  1  O  GLY A 217   N  ILE A 143           
SHEET    3 AA1 3 MET A 208  GLN A 209 -1  N  MET A 208   O  VAL A 218           
SHEET    1 AA2 7 ASN A 201  CYS A 202  0                                        
SHEET    2 AA2 7 PHE A 222  ALA A 224 -1  O  ALA A 223   N  CYS A 202           
SHEET    3 AA2 7 LYS A 241  CYS A 247 -1  O  TYR A 243   N  PHE A 222           
SHEET    4 AA2 7 LYS A 401  ARG A 410  1  O  TYR A 403   N  SER A 244           
SHEET    5 AA2 7 ILE A 433  VAL A 442 -1  O  THR A 435   N  PHE A 408           
SHEET    6 AA2 7 SER A 340  LEU A 345 -1  N  TYR A 343   O  LEU A 437           
SHEET    7 AA2 7 ILE A 357  ALA A 363 -1  O  ALA A 359   N  VAL A 344           
SHEET    1 AA3 2 LYS A 227  THR A 228  0                                        
SHEET    2 AA3 2 LEU A 234  GLN A 235 -1  O  GLN A 235   N  LYS A 227           
SHEET    1 AA4 2 LEU A 304  VAL A 305  0                                        
SHEET    2 AA4 2 PHE A 366  VAL A 367 -1  O  PHE A 366   N  VAL A 305           
SHEET    1 AA5 3 GLN A 354  ILE A 355  0                                        
SHEET    2 AA5 3 CYS A 420  ILE A 422  1  O  THR A 421   N  ILE A 355           
SHEET    3 AA5 3 ASP A 425  LEU A 427 -1  O  ASP A 425   N  ILE A 422           
SSBOND   1 CYS A  183    CYS A  247                          1555   1555  2.04  
CISPEP   1 MET A   59    PRO A   60          0         4.71                     
SITE     1 AC1  6 ARG A 139  SER A 144  SER A 145  SER A 146                    
SITE     2 AC1  6 PHE A 207  SER A 219                                          
CRYST1  198.200   45.900   67.600  90.00  90.10  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005045  0.000000  0.000009        0.00000                         
SCALE2      0.000000  0.021786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014793        0.00000                         
ATOM      1  N   THR A   6       5.645 -28.847 106.579  1.00168.83           N  
ANISOU    1  N   THR A   6    20427  24631  19091  -5400      2   2709       N  
ATOM      2  CA  THR A   6       5.549 -29.260 107.976  1.00169.24           C  
ANISOU    2  CA  THR A   6    20579  24613  19112  -5419    276   2721       C  
ATOM      3  C   THR A   6       6.252 -28.261 108.919  1.00169.50           C  
ANISOU    3  C   THR A   6    20660  24453  19290  -4736    542   2614       C  
ATOM      4  O   THR A   6       7.345 -27.794 108.580  1.00165.03           O  
ANISOU    4  O   THR A   6    20407  23521  18774  -4373    486   2418       O  
ATOM      5  CB  THR A   6       6.088 -30.682 108.141  1.00177.20           C  
ANISOU    5  CB  THR A   6    22253  25166  19909  -5872    214   2576       C  
ATOM      6  N   PRO A   7       5.660 -27.923 110.099  1.00167.56           N  
ANISOU    6  N   PRO A   7    20126  24443  19094  -4567    834   2740       N  
ATOM      7  CA  PRO A   7       6.329 -26.967 111.006  1.00164.16           C  
ANISOU    7  CA  PRO A   7    19801  23804  18769  -3942   1081   2631       C  
ATOM      8  C   PRO A   7       7.602 -27.524 111.654  1.00163.78           C  
ANISOU    8  C   PRO A   7    20441  23154  18634  -3872   1121   2381       C  
ATOM      9  O   PRO A   7       7.540 -28.326 112.593  1.00164.37           O  
ANISOU    9  O   PRO A   7    20749  23106  18598  -4087   1259   2378       O  
ATOM     10  CB  PRO A   7       5.237 -26.597 112.019  1.00169.41           C  
ANISOU   10  CB  PRO A   7    19995  24902  19472  -3851   1378   2852       C  
ATOM     11  CG  PRO A   7       4.299 -27.743 112.009  1.00178.15           C  
ANISOU   11  CG  PRO A   7    20949  26285  20454  -4510   1322   3016       C  
ATOM     12  CD  PRO A   7       4.362 -28.376 110.648  1.00174.02           C  
ANISOU   12  CD  PRO A   7    20522  25734  19863  -4943    958   2990       C  
ATOM     13  N   ALA A   8       8.766 -27.106 111.115  1.00155.71           N  
ANISOU   13  N   ALA A   8    19736  21772  17655  -3576    993   2182       N  
ATOM     14  CA  ALA A   8      10.094 -27.533 111.561  1.00151.72           C  
ANISOU   14  CA  ALA A   8    19844  20725  17079  -3453    995   1952       C  
ATOM     15  C   ALA A   8      10.452 -27.007 112.955  1.00152.90           C  
ANISOU   15  C   ALA A   8    20103  20740  17252  -3074   1263   1903       C  
ATOM     16  O   ALA A   8      10.708 -25.810 113.133  1.00150.63           O  
ANISOU   16  O   ALA A   8    19676  20480  17078  -2613   1357   1877       O  
ATOM     17  CB  ALA A   8      11.151 -27.129 110.540  1.00149.11           C  
ANISOU   17  CB  ALA A   8    19721  20137  16798  -3231    796   1789       C  
ATOM     18  N   ASP A   9      10.443 -27.918 113.946  1.00149.57           N  
ANISOU   18  N   ASP A   9    19965  20165  16701  -3290   1385   1895       N  
ATOM     19  CA  ASP A   9      10.756 -27.629 115.344  1.00148.14           C  
ANISOU   19  CA  ASP A   9    19957  19833  16495  -3007   1632   1851       C  
ATOM     20  C   ASP A   9      12.198 -28.049 115.641  1.00147.28           C  
ANISOU   20  C   ASP A   9    20443  19209  16307  -2878   1554   1635       C  
ATOM     21  O   ASP A   9      12.543 -29.220 115.478  1.00146.98           O  
ANISOU   21  O   ASP A   9    20771  18934  16140  -3190   1437   1579       O  
ATOM     22  CB  ASP A   9       9.762 -28.356 116.279  1.00153.67           C  
ANISOU   22  CB  ASP A   9    20572  20725  17091  -3331   1829   2004       C  
ATOM     23  CG  ASP A   9       9.712 -27.870 117.723  1.00164.47           C  
ANISOU   23  CG  ASP A   9    21981  22071  18439  -3034   2132   2018       C  
ATOM     24  OD1 ASP A   9      10.726 -27.320 118.206  1.00162.06           O  
ANISOU   24  OD1 ASP A   9    21966  21462  18146  -2644   2164   1863       O  
ATOM     25  OD2 ASP A   9       8.671 -28.078 118.383  1.00174.01           O  
ANISOU   25  OD2 ASP A   9    22951  23564  19601  -3218   2336   2186       O  
ATOM     26  N   LEU A  10      13.036 -27.083 116.065  1.00140.09           N  
ANISOU   26  N   LEU A  10    19634  18132  15461  -2417   1615   1524       N  
ATOM     27  CA  LEU A  10      14.442 -27.311 116.410  1.00136.48           C  
ANISOU   27  CA  LEU A  10    19670  17246  14939  -2239   1543   1339       C  
ATOM     28  C   LEU A  10      14.595 -27.844 117.847  1.00140.32           C  
ANISOU   28  C   LEU A  10    20469  17557  15291  -2250   1717   1328       C  
ATOM     29  O   LEU A  10      15.692 -28.268 118.228  1.00138.31           O  
ANISOU   29  O   LEU A  10    20641  16961  14949  -2156   1654   1202       O  
ATOM     30  CB  LEU A  10      15.265 -26.031 116.203  1.00133.57           C  
ANISOU   30  CB  LEU A  10    19262  16805  14685  -1797   1509   1237       C  
ATOM     31  N   PHE A  11      13.488 -27.836 118.630  1.00138.79           N  
ANISOU   31  N   PHE A  11    20051  17612  15069  -2359   1939   1472       N  
ATOM     32  CA  PHE A  11      13.417 -28.328 120.014  1.00139.33           C  
ANISOU   32  CA  PHE A  11    20381  17561  14997  -2404   2136   1490       C  
ATOM     33  C   PHE A  11      12.706 -29.688 120.087  1.00144.86           C  
ANISOU   33  C   PHE A  11    21175  18300  15565  -2911   2149   1591       C  
ATOM     34  O   PHE A  11      12.415 -30.185 121.179  1.00146.03           O  
ANISOU   34  O   PHE A  11    21497  18402  15586  -3021   2330   1641       O  
ATOM     35  CB  PHE A  11      12.739 -27.295 120.933  1.00142.31           C  
ANISOU   35  CB  PHE A  11    20493  18164  15413  -2132   2415   1577       C  
ATOM     36  CG  PHE A  11      13.361 -25.921 120.872  1.00141.32           C  
ANISOU   36  CG  PHE A  11    20314  17989  15391  -1663   2415   1486       C  
ATOM     37  CD1 PHE A  11      14.561 -25.654 121.519  1.00141.86           C  
ANISOU   37  CD1 PHE A  11    20785  17721  15395  -1411   2386   1333       C  
ATOM     38  CD2 PHE A  11      12.753 -24.897 120.159  1.00143.96           C  
ANISOU   38  CD2 PHE A  11    20207  18619  15873  -1487   2438   1565       C  
ATOM     39  CE1 PHE A  11      15.145 -24.390 121.445  1.00140.90           C  
ANISOU   39  CE1 PHE A  11    20644  17546  15347  -1032   2376   1251       C  
ATOM     40  CE2 PHE A  11      13.330 -23.626 120.101  1.00144.85           C  
ANISOU   40  CE2 PHE A  11    20327  18653  16058  -1071   2445   1482       C  
ATOM     41  CZ  PHE A  11      14.520 -23.380 120.747  1.00140.58           C  
ANISOU   41  CZ  PHE A  11    20206  17765  15444   -867   2415   1322       C  
ATOM     42  N   SER A  12      12.461 -30.294 118.909  1.00141.33           N  
ANISOU   42  N   SER A  12    20653  17917  15128  -3236   1951   1617       N  
ATOM     43  CA  SER A  12      11.832 -31.601 118.732  1.00143.79           C  
ANISOU   43  CA  SER A  12    21095  18242  15298  -3781   1910   1702       C  
ATOM     44  C   SER A  12      12.876 -32.719 118.930  1.00146.05           C  
ANISOU   44  C   SER A  12    22053  18032  15408  -3866   1807   1565       C  
ATOM     45  O   SER A  12      14.022 -32.433 119.289  1.00143.05           O  
ANISOU   45  O   SER A  12    21959  17366  15030  -3490   1785   1428       O  
ATOM     46  CB  SER A  12      11.210 -31.687 117.339  1.00148.21           C  
ANISOU   46  CB  SER A  12    21339  19052  15922  -4071   1716   1774       C  
ATOM     47  OG  SER A  12      10.428 -32.858 117.176  1.00160.14           O  
ANISOU   47  OG  SER A  12    22934  20627  17283  -4654   1677   1879       O  
ATOM     48  N   GLU A  13      12.481 -33.987 118.707  1.00144.24           N  
ANISOU   48  N   GLU A  13    22085  17706  15012  -4356   1745   1613       N  
ATOM     49  CA  GLU A  13      13.366 -35.147 118.830  1.00143.06           C  
ANISOU   49  CA  GLU A  13    22607  17080  14670  -4447   1658   1504       C  
ATOM     50  C   GLU A  13      13.151 -36.112 117.649  1.00147.36           C  
ANISOU   50  C   GLU A  13    23347  17536  15109  -4888   1459   1507       C  
ATOM     51  O   GLU A  13      12.560 -37.184 117.805  1.00150.10           O  
ANISOU   51  O   GLU A  13    23943  17818  15269  -5369   1481   1583       O  
ATOM     52  CB  GLU A  13      13.206 -35.822 120.206  1.00146.26           C  
ANISOU   52  CB  GLU A  13    23340  17334  14900  -4563   1854   1550       C  
ATOM     53  CG  GLU A  13      14.024 -35.156 121.304  1.00152.94           C  
ANISOU   53  CG  GLU A  13    24295  18039  15775  -4064   1975   1472       C  
ATOM     54  CD  GLU A  13      13.425 -35.145 122.699  1.00173.68           C  
ANISOU   54  CD  GLU A  13    26966  20725  18300  -4121   2233   1564       C  
ATOM     55  OE1 GLU A  13      12.590 -36.026 123.008  1.00176.55           O  
ANISOU   55  OE1 GLU A  13    27434  21130  18519  -4576   2321   1677       O  
ATOM     56  OE2 GLU A  13      13.815 -34.263 123.497  1.00162.01           O  
ANISOU   56  OE2 GLU A  13    25447  19239  16869  -3725   2348   1523       O  
ATOM     57  N   ASP A  14      13.611 -35.691 116.452  1.00140.99           N  
ANISOU   57  N   ASP A  14    22433  16728  14409  -4738   1268   1426       N  
ATOM     58  CA  ASP A  14      13.497 -36.444 115.202  1.00159.98           C  
ANISOU   58  CA  ASP A  14    25023  19045  16719  -5099   1063   1411       C  
ATOM     59  C   ASP A  14      14.713 -36.205 114.313  1.00172.78           C  
ANISOU   59  C   ASP A  14    26852  20408  18390  -4735    903   1250       C  
ATOM     60  O   ASP A  14      14.974 -36.989 113.404  1.00132.18           O  
ANISOU   60  O   ASP A  14    22059  15046  13119  -4942    752   1196       O  
ATOM     61  CB  ASP A  14      12.209 -36.061 114.458  1.00163.98           C  
ANISOU   61  CB  ASP A  14    24951  20037  17317  -5445   1003   1561       C  
ATOM     62  N   ALA A  30      14.623 -28.081 101.645  1.00115.21           N  
ANISOU   62  N   ALA A  30    16635  14918  12222  -3679   -667   1230       N  
ATOM     63  CA  ALA A  30      13.165 -27.988 101.671  1.00118.37           C  
ANISOU   63  CA  ALA A  30    16573  15764  12640  -3977   -717   1437       C  
ATOM     64  C   ALA A  30      12.663 -27.529 103.051  1.00122.58           C  
ANISOU   64  C   ALA A  30    16787  16497  13292  -3806   -492   1531       C  
ATOM     65  O   ALA A  30      12.489 -26.327 103.261  1.00121.34           O  
ANISOU   65  O   ALA A  30    16248  16557  13298  -3441   -403   1596       O  
ATOM     66  CB  ALA A  30      12.542 -29.324 101.273  1.00122.43           C  
ANISOU   66  CB  ALA A  30    17316  16265  12938  -4586   -863   1482       C  
ATOM     67  N   VAL A  31      12.459 -28.474 103.990  1.00120.41           N  
ANISOU   67  N   VAL A  31    16710  16123  12919  -4053   -387   1537       N  
ATOM     68  CA  VAL A  31      12.015 -28.192 105.359  1.00120.60           C  
ANISOU   68  CA  VAL A  31    16508  16293  13020  -3921   -155   1617       C  
ATOM     69  C   VAL A  31      13.265 -27.962 106.236  1.00120.43           C  
ANISOU   69  C   VAL A  31    16829  15892  13039  -3502      4   1443       C  
ATOM     70  O   VAL A  31      13.156 -27.484 107.365  1.00119.54           O  
ANISOU   70  O   VAL A  31    16577  15842  13002  -3266    204   1472       O  
ATOM     71  CB  VAL A  31      11.057 -29.288 105.920  1.00128.32           C  
ANISOU   71  CB  VAL A  31    17490  17402  13862  -4435   -122   1737       C  
ATOM     72  CG1 VAL A  31      10.288 -28.785 107.141  1.00129.50           C  
ANISOU   72  CG1 VAL A  31    17239  17856  14110  -4304    116   1879       C  
ATOM     73  CG2 VAL A  31      10.075 -29.771 104.851  1.00131.71           C  
ANISOU   73  CG2 VAL A  31    17733  18119  14193  -4953   -351   1874       C  
ATOM     74  N   LEU A  32      14.457 -28.265 105.680  1.00114.67           N  
ANISOU   74  N   LEU A  32    16534  14787  12249  -3400    -89   1270       N  
ATOM     75  CA  LEU A  32      15.756 -28.064 106.329  1.00111.43           C  
ANISOU   75  CA  LEU A  32    16432  14039  11866  -3015     17   1113       C  
ATOM     76  C   LEU A  32      16.139 -26.572 106.295  1.00112.12           C  
ANISOU   76  C   LEU A  32    16241  14229  12131  -2556     67   1094       C  
ATOM     77  O   LEU A  32      16.865 -26.097 107.173  1.00109.54           O  
ANISOU   77  O   LEU A  32    16008  13757  11854  -2240    197   1020       O  
ATOM     78  CB  LEU A  32      16.834 -28.931 105.648  1.00110.50           C  
ANISOU   78  CB  LEU A  32    16833  13537  11614  -3062    -96    964       C  
ATOM     79  CG  LEU A  32      18.017 -29.382 106.522  1.00113.53           C  
ANISOU   79  CG  LEU A  32    17632  13562  11941  -2834     11    838       C  
ATOM     80  CD1 LEU A  32      17.597 -30.449 107.538  1.00115.74           C  
ANISOU   80  CD1 LEU A  32    18137  13750  12088  -3097    108    880       C  
ATOM     81  CD2 LEU A  32      19.135 -29.940 105.670  1.00114.77           C  
ANISOU   81  CD2 LEU A  32    18210  13401  11998  -2761    -86    708       C  
ATOM     82  N   ALA A  33      15.619 -25.837 105.289  1.00108.50           N  
ANISOU   82  N   ALA A  33    15459  14017  11749  -2540    -42   1168       N  
ATOM     83  CA  ALA A  33      15.811 -24.397 105.106  1.00106.24           C  
ANISOU   83  CA  ALA A  33    14912  13841  11611  -2143     -6   1174       C  
ATOM     84  C   ALA A  33      14.935 -23.598 106.093  1.00109.69           C  
ANISOU   84  C   ALA A  33    14982  14552  12143  -1970    182   1304       C  
ATOM     85  O   ALA A  33      15.247 -22.444 106.399  1.00107.78           O  
ANISOU   85  O   ALA A  33    14647  14306  11997  -1590    282   1283       O  
ATOM     86  CB  ALA A  33      15.468 -24.013 103.675  1.00107.58           C  
ANISOU   86  CB  ALA A  33    14894  14181  11802  -2210   -191   1227       C  
ATOM     87  N   SER A  34      13.845 -24.225 106.592  1.00107.63           N  
ANISOU   87  N   SER A  34    14534  14523  11838  -2257    239   1441       N  
ATOM     88  CA  SER A  34      12.902 -23.630 107.538  1.00108.59           C  
ANISOU   88  CA  SER A  34    14296  14936  12027  -2121    443   1588       C  
ATOM     89  C   SER A  34      13.309 -23.867 109.012  1.00109.93           C  
ANISOU   89  C   SER A  34    14712  14899  12159  -2011    655   1518       C  
ATOM     90  O   SER A  34      12.448 -24.008 109.889  1.00112.09           O  
ANISOU   90  O   SER A  34    14795  15374  12418  -2086    823   1640       O  
ATOM     91  CB  SER A  34      11.481 -24.112 107.252  1.00116.31           C  
ANISOU   91  CB  SER A  34    14885  16330  12977  -2491    398   1798       C  
ATOM     92  OG  SER A  34      11.321 -25.490 107.547  1.00126.74           O  
ANISOU   92  OG  SER A  34    16438  17557  14159  -2943    368   1792       O  
ATOM     93  N   LEU A  35      14.633 -23.893 109.270  1.00101.42           N  
ANISOU   93  N   LEU A  35    14044  13435  11056  -1829    645   1333       N  
ATOM     94  CA  LEU A  35      15.245 -24.045 110.599  1.00 98.83           C  
ANISOU   94  CA  LEU A  35    13999  12872  10679  -1689    806   1248       C  
ATOM     95  C   LEU A  35      16.073 -22.771 110.878  1.00 96.86           C  
ANISOU   95  C   LEU A  35    13797  12497  10507  -1246    870   1157       C  
ATOM     96  O   LEU A  35      17.226 -22.827 111.314  1.00 93.62           O  
ANISOU   96  O   LEU A  35    13719  11794  10058  -1112    861   1018       O  
ATOM     97  CB  LEU A  35      16.118 -25.319 110.651  1.00 97.82           C  
ANISOU   97  CB  LEU A  35    14336  12409  10423  -1897    713   1125       C  
ATOM     98  CG  LEU A  35      15.389 -26.667 110.628  1.00104.84           C  
ANISOU   98  CG  LEU A  35    15308  13338  11188  -2358    678   1200       C  
ATOM     99  CD1 LEU A  35      16.309 -27.762 110.147  1.00104.05           C  
ANISOU   99  CD1 LEU A  35    15678  12894  10963  -2515    537   1075       C  
ATOM    100  CD2 LEU A  35      14.815 -27.021 111.998  1.00108.63           C  
ANISOU  100  CD2 LEU A  35    15796  13870  11609  -2440    883   1274       C  
ATOM    101  N   SER A  36      15.451 -21.619 110.596  1.00 92.39           N  
ANISOU  101  N   SER A  36    12896  12170  10039  -1028    930   1250       N  
ATOM    102  CA  SER A  36      16.017 -20.278 110.680  1.00 89.81           C  
ANISOU  102  CA  SER A  36    12589  11758   9775   -633    988   1191       C  
ATOM    103  C   SER A  36      16.288 -19.787 112.103  1.00 91.37           C  
ANISOU  103  C   SER A  36    12960  11822   9933   -401   1197   1148       C  
ATOM    104  O   SER A  36      15.738 -20.321 113.074  1.00 92.19           O  
ANISOU  104  O   SER A  36    13066  11984   9979   -497   1346   1206       O  
ATOM    105  CB  SER A  36      15.096 -19.289 109.969  1.00 94.90           C  
ANISOU  105  CB  SER A  36    12840  12708  10511   -476   1005   1332       C  
ATOM    106  OG  SER A  36      14.654 -19.773 108.712  1.00105.04           O  
ANISOU  106  OG  SER A  36    13936  14160  11816   -717    806   1397       O  
ATOM    107  N   PHE A  37      17.127 -18.731 112.208  1.00 84.50           N  
ANISOU  107  N   PHE A  37    12249  10776   9080   -109   1208   1051       N  
ATOM    108  CA  PHE A  37      17.442 -18.029 113.453  1.00 83.22           C  
ANISOU  108  CA  PHE A  37    12286  10472   8863    132   1388   1003       C  
ATOM    109  C   PHE A  37      16.211 -17.192 113.838  1.00 89.38           C  
ANISOU  109  C   PHE A  37    12795  11498   9669    343   1614   1152       C  
ATOM    110  O   PHE A  37      15.991 -16.905 115.017  1.00 89.50           O  
ANISOU  110  O   PHE A  37    12918  11475   9614    482   1826   1165       O  
ATOM    111  CB  PHE A  37      18.691 -17.149 113.265  1.00 82.18           C  
ANISOU  111  CB  PHE A  37    12399  10098   8729    322   1299    865       C  
ATOM    112  CG  PHE A  37      19.067 -16.271 114.435  1.00 83.36           C  
ANISOU  112  CG  PHE A  37    12791  10084   8798    551   1456    810       C  
ATOM    113  CD1 PHE A  37      19.235 -16.810 115.706  1.00 86.55           C  
ANISOU  113  CD1 PHE A  37    13410  10379   9098    498   1555    777       C  
ATOM    114  CD2 PHE A  37      19.288 -14.911 114.261  1.00 85.20           C  
ANISOU  114  CD2 PHE A  37    13085  10250   9036    804   1496    787       C  
ATOM    115  CE1 PHE A  37      19.591 -16.001 116.788  1.00 87.70           C  
ANISOU  115  CE1 PHE A  37    13817  10363   9143    688   1688    722       C  
ATOM    116  CE2 PHE A  37      19.656 -14.102 115.341  1.00 88.45           C  
ANISOU  116  CE2 PHE A  37    13782  10482   9342    985   1633    728       C  
ATOM    117  CZ  PHE A  37      19.801 -14.652 116.598  1.00 86.87           C  
ANISOU  117  CZ  PHE A  37    13785  10186   9036    922   1725    696       C  
ATOM    118  N   SER A  38      15.396 -16.833 112.818  1.00 87.58           N  
ANISOU  118  N   SER A  38    12214  11533   9529    374   1568   1276       N  
ATOM    119  CA  SER A  38      14.133 -16.106 112.933  1.00 90.16           C  
ANISOU  119  CA  SER A  38    12198  12167   9894    587   1758   1457       C  
ATOM    120  C   SER A  38      13.085 -17.053 113.520  1.00 96.09           C  
ANISOU  120  C   SER A  38    12713  13177  10620    363   1880   1595       C  
ATOM    121  O   SER A  38      12.358 -16.658 114.427  1.00 97.67           O  
ANISOU  121  O   SER A  38    12806  13514  10790    553   2140   1698       O  
ATOM    122  CB  SER A  38      13.677 -15.605 111.564  1.00 94.02           C  
ANISOU  122  CB  SER A  38    12376  12872  10474    636   1616   1555       C  
ATOM    123  OG  SER A  38      14.624 -14.728 110.979  1.00 99.09           O  
ANISOU  123  OG  SER A  38    13238  13280  11132    821   1510   1437       O  
ATOM    124  N   LYS A  39      13.033 -18.308 113.016  1.00 92.61           N  
ANISOU  124  N   LYS A  39    12223  12789  10175    -49   1702   1598       N  
ATOM    125  CA  LYS A  39      12.125 -19.366 113.469  1.00 95.13           C  
ANISOU  125  CA  LYS A  39    12362  13330  10451   -364   1776   1721       C  
ATOM    126  C   LYS A  39      12.443 -19.755 114.913  1.00 99.48           C  
ANISOU  126  C   LYS A  39    13221  13677  10898   -359   1965   1652       C  
ATOM    127  O   LYS A  39      11.522 -19.994 115.702  1.00101.55           O  
ANISOU  127  O   LYS A  39    13306  14154  11124   -404   2177   1785       O  
ATOM    128  CB  LYS A  39      12.223 -20.591 112.545  1.00 97.29           C  
ANISOU  128  CB  LYS A  39    12651  13605  10709   -815   1516   1701       C  
ATOM    129  N   PHE A  40      13.752 -19.789 115.255  1.00 93.86           N  
ANISOU  129  N   PHE A  40    12959  12569  10133   -297   1890   1456       N  
ATOM    130  CA  PHE A  40      14.271 -20.086 116.594  1.00 93.49           C  
ANISOU  130  CA  PHE A  40    13268  12283   9972   -270   2027   1370       C  
ATOM    131  C   PHE A  40      13.833 -18.996 117.580  1.00 99.48           C  
ANISOU  131  C   PHE A  40    14005  13092  10701     86   2311   1421       C  
ATOM    132  O   PHE A  40      13.252 -19.324 118.611  1.00101.04           O  
ANISOU  132  O   PHE A  40    14203  13368  10822     52   2526   1495       O  
ATOM    133  CB  PHE A  40      15.809 -20.245 116.560  1.00 91.83           C  
ANISOU  133  CB  PHE A  40    13483  11689   9718   -257   1844   1169       C  
ATOM    134  CG  PHE A  40      16.526 -20.168 117.891  1.00 92.51           C  
ANISOU  134  CG  PHE A  40    13948  11517   9686   -135   1953   1071       C  
ATOM    135  CD1 PHE A  40      16.628 -21.285 118.710  1.00 96.12           C  
ANISOU  135  CD1 PHE A  40    14623  11866  10031   -346   1985   1060       C  
ATOM    136  CD2 PHE A  40      17.126 -18.986 118.309  1.00 93.74           C  
ANISOU  136  CD2 PHE A  40    14275  11521   9819    172   2009    991       C  
ATOM    137  CE1 PHE A  40      17.295 -21.214 119.937  1.00 96.69           C  
ANISOU  137  CE1 PHE A  40    15053  11707   9979   -234   2068    977       C  
ATOM    138  CE2 PHE A  40      17.790 -18.914 119.538  1.00 96.39           C  
ANISOU  138  CE2 PHE A  40    14976  11624  10023    254   2086    904       C  
ATOM    139  CZ  PHE A  40      17.875 -20.030 120.342  1.00 95.00           C  
ANISOU  139  CZ  PHE A  40    14987  11364   9743     58   2110    900       C  
ATOM    140  N   LEU A  41      14.095 -17.708 117.248  1.00 95.90           N  
ANISOU  140  N   LEU A  41    13556  12587  10293    422   2324   1387       N  
ATOM    141  CA  LEU A  41      13.729 -16.552 118.073  1.00 97.63           C  
ANISOU  141  CA  LEU A  41    13821  12809  10463    801   2596   1427       C  
ATOM    142  C   LEU A  41      12.204 -16.399 118.221  1.00106.73           C  
ANISOU  142  C   LEU A  41    14536  14369  11648    899   2841   1655       C  
ATOM    143  O   LEU A  41      11.738 -16.075 119.314  1.00108.31           O  
ANISOU  143  O   LEU A  41    14803  14589  11759   1088   3128   1707       O  
ATOM    144  CB  LEU A  41      14.366 -15.264 117.529  1.00 96.06           C  
ANISOU  144  CB  LEU A  41    13758  12447  10294   1100   2530   1345       C  
ATOM    145  N   LYS A  42      11.431 -16.672 117.139  1.00105.54           N  
ANISOU  145  N   LYS A  42    13935  14554  11610    758   2727   1797       N  
ATOM    146  CA  LYS A  42       9.962 -16.584 117.128  1.00109.65           C  
ANISOU  146  CA  LYS A  42    13950  15539  12172    818   2919   2044       C  
ATOM    147  C   LYS A  42       9.262 -17.757 117.832  1.00116.78           C  
ANISOU  147  C   LYS A  42    14716  16635  13019    475   3030   2146       C  
ATOM    148  O   LYS A  42       8.081 -17.633 118.173  1.00120.14           O  
ANISOU  148  O   LYS A  42    14762  17438  13450    558   3266   2355       O  
ATOM    149  CB  LYS A  42       9.418 -16.398 115.701  1.00112.71           C  
ANISOU  149  CB  LYS A  42    13905  16235  12685    784   2729   2171       C  
ATOM    150  N   HIS A  43       9.989 -18.880 118.058  1.00111.94           N  
ANISOU  150  N   HIS A  43    14417  15769  12344    103   2874   2011       N  
ATOM    151  CA  HIS A  43       9.479 -20.088 118.722  1.00113.96           C  
ANISOU  151  CA  HIS A  43    14647  16130  12520   -271   2955   2084       C  
ATOM    152  C   HIS A  43       8.924 -19.793 120.124  1.00119.79           C  
ANISOU  152  C   HIS A  43    15418  16933  13163    -65   3329   2163       C  
ATOM    153  O   HIS A  43       9.477 -18.956 120.842  1.00118.21           O  
ANISOU  153  O   HIS A  43    15534  16479  12903    294   3471   2059       O  
ATOM    154  CB  HIS A  43      10.560 -21.182 118.776  1.00112.16           C  
ANISOU  154  CB  HIS A  43    14873  15526  12218   -597   2738   1900       C  
ATOM    155  CG  HIS A  43      10.032 -22.544 119.110  1.00117.78           C  
ANISOU  155  CG  HIS A  43    15566  16338  12848  -1054   2754   1981       C  
ATOM    156  ND1 HIS A  43       9.698 -23.451 118.119  1.00120.33           N  
ANISOU  156  ND1 HIS A  43    15719  16806  13195  -1476   2533   2039       N  
ATOM    157  CD2 HIS A  43       9.795 -23.109 120.316  1.00121.20           C  
ANISOU  157  CD2 HIS A  43    16165  16729  13157  -1159   2967   2012       C  
ATOM    158  CE1 HIS A  43       9.271 -24.532 118.751  1.00121.81           C  
ANISOU  158  CE1 HIS A  43    15980  17029  13272  -1834   2618   2104       C  
ATOM    159  NE2 HIS A  43       9.315 -24.375 120.074  1.00122.70           N  
ANISOU  159  NE2 HIS A  43    16287  17037  13298  -1655   2880   2093       N  
ATOM    160  N   ALA A  44       7.816 -20.475 120.488  1.00119.51           N  
ANISOU  160  N   ALA A  44    15062  17248  13100   -311   3489   2354       N  
ATOM    161  CA  ALA A  44       7.099 -20.328 121.760  1.00122.39           C  
ANISOU  161  CA  ALA A  44    15381  17753  13368   -165   3870   2471       C  
ATOM    162  C   ALA A  44       7.959 -20.523 123.018  1.00124.19           C  
ANISOU  162  C   ALA A  44    16207  17542  13439   -110   3983   2296       C  
ATOM    163  O   ALA A  44       7.775 -19.783 123.985  1.00124.98           O  
ANISOU  163  O   ALA A  44    16426  17604  13458    244   4283   2312       O  
ATOM    164  CB  ALA A  44       5.897 -21.257 121.793  1.00127.06           C  
ANISOU  164  CB  ALA A  44    15541  18785  13952   -567   3956   2696       C  
ATOM    165  N   LYS A  45       8.890 -21.506 123.000  1.00117.90           N  
ANISOU  165  N   LYS A  45    15797  16417  12583   -443   3745   2138       N  
ATOM    166  CA  LYS A  45       9.801 -21.817 124.109  1.00116.00           C  
ANISOU  166  CA  LYS A  45    16129  15761  12186   -429   3789   1976       C  
ATOM    167  C   LYS A  45      10.756 -20.654 124.383  1.00117.71           C  
ANISOU  167  C   LYS A  45    16683  15662  12380     -4   3782   1810       C  
ATOM    168  O   LYS A  45      11.010 -20.327 125.544  1.00117.23           O  
ANISOU  168  O   LYS A  45    16963  15404  12177    181   3975   1753       O  
ATOM    169  CB  LYS A  45      10.584 -23.106 123.823  1.00116.26           C  
ANISOU  169  CB  LYS A  45    16461  15540  12172   -841   3506   1864       C  
ATOM    170  N   VAL A  46      11.264 -20.021 123.307  1.00112.85           N  
ANISOU  170  N   VAL A  46    15987  15002  11888    127   3558   1739       N  
ATOM    171  CA  VAL A  46      12.152 -18.857 123.376  1.00110.79           C  
ANISOU  171  CA  VAL A  46    16016  14466  11612    487   3524   1593       C  
ATOM    172  C   VAL A  46      11.318 -17.640 123.815  1.00119.33           C  
ANISOU  172  C   VAL A  46    16949  15715  12676    904   3853   1703       C  
ATOM    173  O   VAL A  46      11.772 -16.867 124.661  1.00118.96           O  
ANISOU  173  O   VAL A  46    17280  15416  12505   1176   3994   1611       O  
ATOM    174  CB  VAL A  46      12.932 -18.639 122.047  1.00110.91           C  
ANISOU  174  CB  VAL A  46    15995  14390  11757    462   3190   1494       C  
ATOM    175  CG1 VAL A  46      13.734 -17.340 122.068  1.00108.89           C  
ANISOU  175  CG1 VAL A  46    16002  13890  11481    813   3174   1368       C  
ATOM    176  CG2 VAL A  46      13.853 -19.821 121.763  1.00108.16           C  
ANISOU  176  CG2 VAL A  46    15874  13830  11391    115   2908   1376       C  
ATOM    177  N   ARG A  47      10.075 -17.519 123.286  1.00119.91           N  
ANISOU  177  N   ARG A  47    16487  16222  12853    947   3983   1913       N  
ATOM    178  CA  ARG A  47       9.121 -16.455 123.620  1.00123.56           C  
ANISOU  178  CA  ARG A  47    16734  16912  13302   1373   4323   2064       C  
ATOM    179  C   ARG A  47       8.777 -16.482 125.116  1.00131.40           C  
ANISOU  179  C   ARG A  47    17958  17851  14118   1487   4682   2095       C  
ATOM    180  O   ARG A  47       8.698 -15.423 125.745  1.00132.58           O  
ANISOU  180  O   ARG A  47    18313  17892  14169   1909   4940   2087       O  
ATOM    181  CB  ARG A  47       7.852 -16.575 122.764  1.00126.54           C  
ANISOU  181  CB  ARG A  47    16432  17825  13822   1332   4359   2311       C  
ATOM    182  N   ASP A  48       8.615 -17.696 125.686  1.00129.38           N  
ANISOU  182  N   ASP A  48    17725  17636  13798   1108   4699   2122       N  
ATOM    183  CA  ASP A  48       8.337 -17.898 127.110  1.00131.78           C  
ANISOU  183  CA  ASP A  48    18278  17876  13918   1149   5020   2148       C  
ATOM    184  C   ASP A  48       9.601 -17.641 127.944  1.00133.80           C  
ANISOU  184  C   ASP A  48    19223  17607  14009   1240   4955   1912       C  
ATOM    185  O   ASP A  48       9.488 -17.231 129.101  1.00135.33           O  
ANISOU  185  O   ASP A  48    19717  17676  14027   1461   5247   1903       O  
ATOM    186  CB  ASP A  48       7.785 -19.310 127.370  1.00135.14           C  
ANISOU  186  CB  ASP A  48    18525  18502  14321    675   5034   2257       C  
ATOM    187  N   TRP A  49      10.799 -17.875 127.352  1.00126.60           N  
ANISOU  187  N   TRP A  49    18554  16406  13143   1070   4574   1730       N  
ATOM    188  CA  TRP A  49      12.089 -17.643 128.008  1.00124.06           C  
ANISOU  188  CA  TRP A  49    18831  15630  12676   1123   4449   1519       C  
ATOM    189  C   TRP A  49      12.364 -16.140 128.132  1.00128.40           C  
ANISOU  189  C   TRP A  49    19602  16012  13171   1551   4555   1449       C  
ATOM    190  O   TRP A  49      12.760 -15.683 129.204  1.00128.63           O  
ANISOU  190  O   TRP A  49    20092  15778  13001   1704   4697   1362       O  
ATOM    191  CB  TRP A  49      13.234 -18.373 127.274  1.00118.97           C  
ANISOU  191  CB  TRP A  49    18312  14787  12103    831   4027   1377       C  
ATOM    192  CG  TRP A  49      14.606 -18.055 127.803  1.00117.56           C  
ANISOU  192  CG  TRP A  49    18669  14204  11796    894   3861   1181       C  
ATOM    193  CD1 TRP A  49      15.113 -18.389 129.025  1.00120.80           C  
ANISOU  193  CD1 TRP A  49    19524  14374  12002    848   3914   1108       C  
ATOM    194  CD2 TRP A  49      15.641 -17.332 127.122  1.00114.58           C  
ANISOU  194  CD2 TRP A  49    18424  13640  11474    997   3608   1046       C  
ATOM    195  NE1 TRP A  49      16.396 -17.909 129.152  1.00117.96           N  
ANISOU  195  NE1 TRP A  49    19544  13710  11567    911   3696    943       N  
ATOM    196  CE2 TRP A  49      16.748 -17.260 127.997  1.00117.39           C  
ANISOU  196  CE2 TRP A  49    19284  13667  11652    994   3512    902       C  
ATOM    197  CE3 TRP A  49      15.744 -16.741 125.853  1.00114.28           C  
ANISOU  197  CE3 TRP A  49    18126  13689  11607   1077   3450   1040       C  
ATOM    198  CZ2 TRP A  49      17.939 -16.618 127.646  1.00114.24           C  
ANISOU  198  CZ2 TRP A  49    19106  13051  11249   1047   3264    761       C  
ATOM    199  CZ3 TRP A  49      16.920 -16.094 125.512  1.00113.25           C  
ANISOU  199  CZ3 TRP A  49    18244  13319  11469   1144   3225    893       C  
ATOM    200  CH2 TRP A  49      18.002 -16.040 126.400  1.00112.97           C  
ANISOU  200  CH2 TRP A  49    18681  12982  11262   1118   3134    759       C  
ATOM    201  N   CYS A  50      12.121 -15.374 127.047  1.00124.92           N  
ANISOU  201  N   CYS A  50    18861  15718  12886   1735   4491   1493       N  
ATOM    202  CA  CYS A  50      12.310 -13.921 126.998  1.00125.29           C  
ANISOU  202  CA  CYS A  50    19111  15609  12884   2141   4588   1442       C  
ATOM    203  C   CYS A  50      11.294 -13.179 127.866  1.00133.17           C  
ANISOU  203  C   CYS A  50    20129  16715  13754   2520   5045   1568       C  
ATOM    204  O   CYS A  50      11.549 -12.042 128.266  1.00133.64           O  
ANISOU  204  O   CYS A  50    20568  16531  13678   2851   5184   1497       O  
ATOM    205  CB  CYS A  50      12.283 -13.421 125.557  1.00124.53           C  
ANISOU  205  CB  CYS A  50    18679  15653  12985   2218   4394   1473       C  
ATOM    206  SG  CYS A  50      13.595 -14.104 124.511  1.00123.83           S  
ANISOU  206  SG  CYS A  50    18627  15402  13023   1838   3887   1313       S  
ATOM    207  N   ALA A  51      10.153 -13.836 128.167  1.00132.44           N  
ANISOU  207  N   ALA A  51    19647  16983  13689   2460   5284   1759       N  
ATOM    208  CA  ALA A  51       9.062 -13.313 128.991  1.00136.71           C  
ANISOU  208  CA  ALA A  51    20119  17709  14118   2809   5754   1918       C  
ATOM    209  C   ALA A  51       9.469 -13.030 130.449  1.00141.30           C  
ANISOU  209  C   ALA A  51    21335  17934  14421   2936   5982   1804       C  
ATOM    210  O   ALA A  51       8.805 -12.232 131.113  1.00144.41           O  
ANISOU  210  O   ALA A  51    21835  18356  14679   3337   6376   1887       O  
ATOM    211  CB  ALA A  51       7.876 -14.262 128.947  1.00140.23           C  
ANISOU  211  CB  ALA A  51    19981  18643  14657   2610   5907   2147       C  
ATOM    212  N   GLN A  52      10.549 -13.676 130.940  1.00134.79           N  
ANISOU  212  N   GLN A  52    20938  16779  13495   2617   5739   1623       N  
ATOM    213  CA  GLN A  52      11.080 -13.478 132.297  1.00135.11           C  
ANISOU  213  CA  GLN A  52    21619  16462  13255   2680   5884   1501       C  
ATOM    214  C   GLN A  52      11.765 -12.107 132.395  1.00138.13           C  
ANISOU  214  C   GLN A  52    22488  16488  13505   2996   5876   1358       C  
ATOM    215  O   GLN A  52      12.303 -11.615 131.395  1.00135.40           O  
ANISOU  215  O   GLN A  52    22070  16084  13293   3014   5614   1291       O  
ATOM    216  CB  GLN A  52      12.049 -14.609 132.682  1.00133.68           C  
ANISOU  216  CB  GLN A  52    21706  16070  13015   2244   5584   1372       C  
ATOM    217  CG  GLN A  52      11.358 -15.939 132.993  1.00147.50           C  
ANISOU  217  CG  GLN A  52    23165  18081  14797   1938   5673   1505       C  
ATOM    218  CD  GLN A  52      12.200 -17.146 132.641  1.00160.81           C  
ANISOU  218  CD  GLN A  52    24896  19660  16546   1499   5280   1416       C  
ATOM    219  OE1 GLN A  52      13.359 -17.281 133.051  1.00154.21           O  
ANISOU  219  OE1 GLN A  52    24524  18481  15587   1401   5055   1250       O  
ATOM    220  NE2 GLN A  52      11.618 -18.078 131.900  1.00151.13           N  
ANISOU  220  NE2 GLN A  52    23200  18731  15493   1224   5196   1534       N  
ATOM    221  N   ALA A  53      11.725 -11.489 133.595  1.00136.63           N  
ANISOU  221  N   ALA A  53    22818  16058  13036   3233   6174   1315       N  
ATOM    222  CA  ALA A  53      12.275 -10.154 133.866  1.00136.62           C  
ANISOU  222  CA  ALA A  53    23375  15688  12846   3529   6224   1186       C  
ATOM    223  C   ALA A  53      13.805 -10.050 133.804  1.00136.02           C  
ANISOU  223  C   ALA A  53    23752  15231  12700   3261   5792    960       C  
ATOM    224  O   ALA A  53      14.321  -9.059 133.275  1.00134.77           O  
ANISOU  224  O   ALA A  53    23786  14885  12537   3393   5668    874       O  
ATOM    225  CB  ALA A  53      11.768  -9.642 135.203  1.00141.41           C  
ANISOU  225  CB  ALA A  53    24439  16144  13148   3825   6672   1208       C  
ATOM    226  N   LYS A  54      14.522 -11.054 134.354  1.00129.67           N  
ANISOU  226  N   LYS A  54    23116  14323  11829   2892   5572    877       N  
ATOM    227  CA  LYS A  54      15.989 -11.097 134.404  1.00125.81           C  
ANISOU  227  CA  LYS A  54    23014  13528  11261   2621   5160    689       C  
ATOM    228  C   LYS A  54      16.667 -11.251 133.036  1.00124.44           C  
ANISOU  228  C   LYS A  54    22496  13437  11351   2442   4759    647       C  
ATOM    229  O   LYS A  54      17.796 -10.789 132.862  1.00121.78           O  
ANISOU  229  O   LYS A  54    22456  12861  10955   2338   4474    507       O  
ATOM    230  CB  LYS A  54      16.441 -12.211 135.335  1.00126.03           C  
ANISOU  230  CB  LYS A  54    23245  13481  11159   2321   5056    652       C  
ATOM    231  N   ILE A  55      15.975 -11.903 132.079  1.00119.57           N  
ANISOU  231  N   ILE A  55    21259  13166  11007   2388   4741    775       N  
ATOM    232  CA  ILE A  55      16.459 -12.226 130.734  1.00115.78           C  
ANISOU  232  CA  ILE A  55    20405  12803  10782   2208   4390    756       C  
ATOM    233  C   ILE A  55      16.661 -10.988 129.849  1.00118.62           C  
ANISOU  233  C   ILE A  55    20769  13092  11208   2424   4330    720       C  
ATOM    234  O   ILE A  55      15.701 -10.297 129.501  1.00120.34           O  
ANISOU  234  O   ILE A  55    20775  13463  11484   2729   4583    832       O  
ATOM    235  CB  ILE A  55      15.556 -13.303 130.053  1.00118.70           C  
ANISOU  235  CB  ILE A  55    20161  13557  11383   2065   4410    912       C  
ATOM    236  CG1 ILE A  55      15.424 -14.596 130.913  1.00119.63           C  
ANISOU  236  CG1 ILE A  55    20323  13714  11419   1806   4452    945       C  
ATOM    237  CG2 ILE A  55      15.996 -13.619 128.614  1.00116.33           C  
ANISOU  237  CG2 ILE A  55    19502  13370  11327   1890   4063    894       C  
ATOM    238  CD1 ILE A  55      16.757 -15.322 131.369  1.00124.87           C  
ANISOU  238  CD1 ILE A  55    21351  14113  11979   1516   4126    800       C  
ATOM    239  N   GLN A  56      17.933 -10.752 129.465  1.00112.06           N  
ANISOU  239  N   GLN A  56    20163  12047  10369   2256   3987    574       N  
ATOM    240  CA  GLN A  56      18.386  -9.670 128.583  1.00110.67           C  
ANISOU  240  CA  GLN A  56    20043  11762  10243   2369   3857    516       C  
ATOM    241  C   GLN A  56      19.356 -10.266 127.531  1.00110.74           C  
ANISOU  241  C   GLN A  56    19811  11824  10440   2072   3440    455       C  
ATOM    242  O   GLN A  56      20.577 -10.197 127.721  1.00108.89           O  
ANISOU  242  O   GLN A  56    19880  11385  10110   1883   3184    328       O  
ATOM    243  CB  GLN A  56      19.032  -8.524 129.389  1.00113.20           C  
ANISOU  243  CB  GLN A  56    21021  11711  10281   2471   3905    392       C  
ATOM    244  CG  GLN A  56      18.020  -7.611 130.078  1.00123.47           C  
ANISOU  244  CG  GLN A  56    22571  12936  11405   2862   4343    457       C  
ATOM    245  CD  GLN A  56      18.674  -6.646 131.032  1.00135.19           C  
ANISOU  245  CD  GLN A  56    24792  14015  12559   2904   4388    323       C  
ATOM    246  OE1 GLN A  56      19.347  -5.688 130.635  1.00128.48           O  
ANISOU  246  OE1 GLN A  56    24236  12943  11638   2908   4252    233       O  
ATOM    247  NE2 GLN A  56      18.468  -6.867 132.318  1.00127.91           N  
ANISOU  247  NE2 GLN A  56    24209  12983  11408   2917   4585    311       N  
ATOM    248  N   PRO A  57      18.832 -10.902 126.442  1.00105.66           N  
ANISOU  248  N   PRO A  57    18625  11469  10050   2017   3368    552       N  
ATOM    249  CA  PRO A  57      19.721 -11.564 125.469  1.00101.70           C  
ANISOU  249  CA  PRO A  57    17921  11012   9708   1749   3003    497       C  
ATOM    250  C   PRO A  57      20.662 -10.648 124.694  1.00102.03           C  
ANISOU  250  C   PRO A  57    18099  10901   9768   1748   2784    400       C  
ATOM    251  O   PRO A  57      20.243  -9.640 124.121  1.00102.33           O  
ANISOU  251  O   PRO A  57    18102  10940   9840   1964   2882    431       O  
ATOM    252  CB  PRO A  57      18.750 -12.311 124.544  1.00103.44           C  
ANISOU  252  CB  PRO A  57    17586  11564  10154   1718   3030    633       C  
ATOM    253  CG  PRO A  57      17.478 -12.407 125.309  1.00111.20           C  
ANISOU  253  CG  PRO A  57    18470  12699  11081   1873   3380    760       C  
ATOM    254  CD  PRO A  57      17.418 -11.129 126.085  1.00109.08           C  
ANISOU  254  CD  PRO A  57    18607  12220  10619   2172   3611    724       C  
ATOM    255  N   SER A  58      21.949 -11.029 124.686  1.00 95.14           N  
ANISOU  255  N   SER A  58    17375   9910   8864   1505   2489    294       N  
ATOM    256  CA  SER A  58      23.038 -10.323 124.020  1.00 92.83           C  
ANISOU  256  CA  SER A  58    17202   9492   8576   1428   2248    203       C  
ATOM    257  C   SER A  58      23.522 -11.093 122.794  1.00 92.75           C  
ANISOU  257  C   SER A  58    16818   9644   8780   1259   1991    211       C  
ATOM    258  O   SER A  58      23.320 -12.307 122.698  1.00 92.00           O  
ANISOU  258  O   SER A  58    16483   9694   8778   1143   1947    256       O  
ATOM    259  CB  SER A  58      24.207 -10.134 124.984  1.00 96.51           C  
ANISOU  259  CB  SER A  58    18111   9734   8824   1274   2102     93       C  
ATOM    260  OG  SER A  58      25.088 -11.248 124.973  1.00102.84           O  
ANISOU  260  OG  SER A  58    18805  10599   9669   1039   1846     68       O  
ATOM    261  N   MET A  59      24.207 -10.389 121.886  1.00 86.29           N  
ANISOU  261  N   MET A  59    15994   8779   8013   1234   1826    164       N  
ATOM    262  CA  MET A  59      24.794 -10.973 120.686  1.00 82.47           C  
ANISOU  262  CA  MET A  59    15210   8421   7705   1087   1587    160       C  
ATOM    263  C   MET A  59      26.327 -10.958 120.846  1.00 82.92           C  
ANISOU  263  C   MET A  59    15468   8365   7674    893   1329     65       C  
ATOM    264  O   MET A  59      26.850 -10.009 121.443  1.00 83.31           O  
ANISOU  264  O   MET A  59    15862   8238   7554    886   1325      4       O  
ATOM    265  CB  MET A  59      24.355 -10.197 119.436  1.00 84.38           C  
ANISOU  265  CB  MET A  59    15253   8730   8076   1212   1606    200       C  
ATOM    266  CG  MET A  59      22.870 -10.330 119.112  1.00 88.95           C  
ANISOU  266  CG  MET A  59    15536   9497   8765   1390   1817    323       C  
ATOM    267  SD  MET A  59      22.349 -11.982 118.575  1.00 91.93           S  
ANISOU  267  SD  MET A  59    15485  10134   9311   1218   1743    400       S  
ATOM    268  CE  MET A  59      23.095 -12.066 116.956  1.00 86.16           C  
ANISOU  268  CE  MET A  59    14549   9457   8729   1098   1473    370       C  
ATOM    269  N   PRO A  60      27.076 -11.994 120.395  1.00 76.09           N  
ANISOU  269  N   PRO A  60    14419   7598   6895    735   1119     58       N  
ATOM    270  CA  PRO A  60      26.656 -13.192 119.640  1.00 74.05           C  
ANISOU  270  CA  PRO A  60    13825   7509   6804    697   1087    116       C  
ATOM    271  C   PRO A  60      26.115 -14.373 120.448  1.00 76.78           C  
ANISOU  271  C   PRO A  60    14166   7891   7115    661   1176    158       C  
ATOM    272  O   PRO A  60      25.854 -15.414 119.850  1.00 75.92           O  
ANISOU  272  O   PRO A  60    13837   7894   7116    590   1134    200       O  
ATOM    273  CB  PRO A  60      27.940 -13.583 118.899  1.00 74.25           C  
ANISOU  273  CB  PRO A  60    13767   7565   6880    565    828     76       C  
ATOM    274  CG  PRO A  60      29.031 -13.198 119.841  1.00 79.52           C  
ANISOU  274  CG  PRO A  60    14720   8118   7375    488    718     18       C  
ATOM    275  CD  PRO A  60      28.546 -11.952 120.549  1.00 76.86           C  
ANISOU  275  CD  PRO A  60    14658   7639   6907    574    879     -6       C  
ATOM    276  N   ALA A  61      25.954 -14.228 121.778  1.00 73.53           N  
ANISOU  276  N   ALA A  61    14028   7373   6537    694   1299    148       N  
ATOM    277  CA  ALA A  61      25.488 -15.288 122.687  1.00 73.40           C  
ANISOU  277  CA  ALA A  61    14068   7368   6454    650   1395    188       C  
ATOM    278  C   ALA A  61      24.225 -16.023 122.229  1.00 75.16           C  
ANISOU  278  C   ALA A  61    13999   7754   6804    650   1546    283       C  
ATOM    279  O   ALA A  61      24.216 -17.253 122.262  1.00 74.19           O  
ANISOU  279  O   ALA A  61    13823   7669   6695    524   1498    312       O  
ATOM    280  CB  ALA A  61      25.299 -14.742 124.094  1.00 76.17           C  
ANISOU  280  CB  ALA A  61    14764   7578   6598    719   1555    168       C  
ATOM    281  N   LEU A  62      23.185 -15.292 121.773  1.00 71.20           N  
ANISOU  281  N   LEU A  62    13313   7355   6384    783   1717    341       N  
ATOM    282  CA  LEU A  62      21.954 -15.924 121.297  1.00 71.38           C  
ANISOU  282  CA  LEU A  62    13011   7586   6524    758   1842    453       C  
ATOM    283  C   LEU A  62      22.179 -16.662 119.976  1.00 74.68           C  
ANISOU  283  C   LEU A  62    13170   8109   7096    611   1639    462       C  
ATOM    284  O   LEU A  62      21.632 -17.755 119.797  1.00 74.79           O  
ANISOU  284  O   LEU A  62    13034   8232   7152    461   1646    524       O  
ATOM    285  CB  LEU A  62      20.785 -14.931 121.200  1.00 72.97           C  
ANISOU  285  CB  LEU A  62    13062   7904   6758    974   2083    537       C  
ATOM    286  CG  LEU A  62      19.378 -15.557 121.160  1.00 79.08           C  
ANISOU  286  CG  LEU A  62    13507   8933   7605    950   2266    682       C  
ATOM    287  CD1 LEU A  62      18.953 -16.049 122.520  1.00 81.06           C  
ANISOU  287  CD1 LEU A  62    13917   9162   7719    922   2467    717       C  
ATOM    288  CD2 LEU A  62      18.354 -14.571 120.660  1.00 82.73           C  
ANISOU  288  CD2 LEU A  62    13730   9564   8140   1190   2439    783       C  
ATOM    289  N   ARG A  63      23.009 -16.082 119.071  1.00 70.02           N  
ANISOU  289  N   ARG A  63    12562   7473   6568    636   1462    398       N  
ATOM    290  CA  ARG A  63      23.378 -16.681 117.779  1.00 68.16           C  
ANISOU  290  CA  ARG A  63    12133   7309   6456    517   1269    393       C  
ATOM    291  C   ARG A  63      24.140 -17.993 118.012  1.00 71.56           C  
ANISOU  291  C   ARG A  63    12687   7665   6838    359   1133    358       C  
ATOM    292  O   ARG A  63      23.833 -18.999 117.372  1.00 71.49           O  
ANISOU  292  O   ARG A  63    12550   7727   6887    227   1080    395       O  
ATOM    293  CB  ARG A  63      24.213 -15.701 116.925  1.00 66.05           C  
ANISOU  293  CB  ARG A  63    11866   6993   6237    587   1134    333       C  
ATOM    294  CG  ARG A  63      24.524 -16.194 115.508  1.00 71.56           C  
ANISOU  294  CG  ARG A  63    12368   7768   7054    489    961    331       C  
ATOM    295  CD  ARG A  63      23.416 -15.884 114.521  1.00 77.31           C  
ANISOU  295  CD  ARG A  63    12813   8664   7896    525   1015    415       C  
ATOM    296  NE  ARG A  63      23.345 -16.884 113.458  1.00 84.24           N  
ANISOU  296  NE  ARG A  63    13529   9629   8850    364    886    436       N  
ATOM    297  CZ  ARG A  63      22.538 -16.804 112.406  1.00 99.12           C  
ANISOU  297  CZ  ARG A  63    15165  11670  10826    340    866    506       C  
ATOM    298  NH1 ARG A  63      21.736 -15.758 112.254  1.00 92.06           N  
ANISOU  298  NH1 ARG A  63    14128  10878   9974    501    968    572       N  
ATOM    299  NH2 ARG A  63      22.539 -17.760 111.488  1.00 80.49           N  
ANISOU  299  NH2 ARG A  63    12722   9360   8501    166    741    515       N  
ATOM    300  N   MET A  64      25.100 -17.980 118.953  1.00 67.75           N  
ANISOU  300  N   MET A  64    12474   7037   6230    376   1079    296       N  
ATOM    301  CA  MET A  64      25.885 -19.150 119.345  1.00 67.43           C  
ANISOU  301  CA  MET A  64    12586   6919   6117    282    960    276       C  
ATOM    302  C   MET A  64      24.979 -20.228 119.940  1.00 72.94           C  
ANISOU  302  C   MET A  64    13317   7630   6766    182   1089    341       C  
ATOM    303  O   MET A  64      25.173 -21.413 119.655  1.00 72.07           O  
ANISOU  303  O   MET A  64    13238   7496   6651     73   1009    354       O  
ATOM    304  CB  MET A  64      26.987 -18.757 120.339  1.00 69.79           C  
ANISOU  304  CB  MET A  64    13147   7095   6276    329    876    217       C  
ATOM    305  CG  MET A  64      28.097 -17.948 119.719  1.00 72.18           C  
ANISOU  305  CG  MET A  64    13421   7395   6608    361    710    161       C  
ATOM    306  SD  MET A  64      29.315 -18.998 118.925  1.00 75.10           S  
ANISOU  306  SD  MET A  64    13723   7794   7017    320    484    154       S  
ATOM    307  CE  MET A  64      28.749 -18.940 117.236  1.00 70.74           C  
ANISOU  307  CE  MET A  64    12885   7343   6650    302    491    170       C  
ATOM    308  N   ALA A  65      23.967 -19.809 120.737  1.00 71.13           N  
ANISOU  308  N   ALA A  65    13094   7440   6492    222   1304    388       N  
ATOM    309  CA  ALA A  65      22.979 -20.712 121.328  1.00 72.46           C  
ANISOU  309  CA  ALA A  65    13264   7655   6613    108   1460    466       C  
ATOM    310  C   ALA A  65      22.152 -21.362 120.205  1.00 76.34           C  
ANISOU  310  C   ALA A  65    13471   8304   7230    -42   1447    536       C  
ATOM    311  O   ALA A  65      22.030 -22.589 120.178  1.00 76.22           O  
ANISOU  311  O   ALA A  65    13523   8260   7178   -221   1409    562       O  
ATOM    312  CB  ALA A  65      22.080 -19.956 122.300  1.00 74.89           C  
ANISOU  312  CB  ALA A  65    13597   8004   6854    215   1714    511       C  
ATOM    313  N   TYR A  66      21.668 -20.545 119.237  1.00 72.08           N  
ANISOU  313  N   TYR A  66    12650   7915   6823     24   1455    564       N  
ATOM    314  CA  TYR A  66      20.896 -21.009 118.088  1.00 72.03           C  
ANISOU  314  CA  TYR A  66    12358   8082   6929   -123   1414    635       C  
ATOM    315  C   TYR A  66      21.690 -22.031 117.281  1.00 74.29           C  
ANISOU  315  C   TYR A  66    12740   8267   7219   -271   1203    583       C  
ATOM    316  O   TYR A  66      21.123 -23.041 116.860  1.00 74.70           O  
ANISOU  316  O   TYR A  66    12733   8378   7272   -488   1181    637       O  
ATOM    317  CB  TYR A  66      20.450 -19.822 117.213  1.00 73.32           C  
ANISOU  317  CB  TYR A  66    12249   8396   7214     24   1426    665       C  
ATOM    318  CG  TYR A  66      20.257 -20.158 115.747  1.00 75.27           C  
ANISOU  318  CG  TYR A  66    12268   8761   7569   -104   1274    693       C  
ATOM    319  CD1 TYR A  66      19.164 -20.907 115.319  1.00 78.96           C  
ANISOU  319  CD1 TYR A  66    12508   9425   8067   -313   1302    803       C  
ATOM    320  CD2 TYR A  66      21.171 -19.730 114.788  1.00 74.32           C  
ANISOU  320  CD2 TYR A  66    12168   8564   7505    -38   1102    614       C  
ATOM    321  CE1 TYR A  66      18.999 -21.244 113.976  1.00 79.57           C  
ANISOU  321  CE1 TYR A  66    12416   9601   8216   -459   1144    827       C  
ATOM    322  CE2 TYR A  66      21.013 -20.055 113.442  1.00 75.01           C  
ANISOU  322  CE2 TYR A  66    12084   8745   7670   -157    966    636       C  
ATOM    323  CZ  TYR A  66      19.919 -20.803 113.039  1.00 83.88           C  
ANISOU  323  CZ  TYR A  66    13011  10049   8813   -367    981    740       C  
ATOM    324  OH  TYR A  66      19.760 -21.119 111.711  1.00 84.26           O  
ANISOU  324  OH  TYR A  66    12921  10181   8912   -506    832    761       O  
ATOM    325  N   ASN A  67      23.002 -21.766 117.085  1.00 69.13           N  
ANISOU  325  N   ASN A  67    12245   7467   6554   -158   1056    485       N  
ATOM    326  CA  ASN A  67      23.948 -22.620 116.356  1.00 67.89           C  
ANISOU  326  CA  ASN A  67    12201   7205   6390   -222    874    434       C  
ATOM    327  C   ASN A  67      24.005 -24.037 116.932  1.00 73.77           C  
ANISOU  327  C   ASN A  67    13185   7829   7015   -362    877    450       C  
ATOM    328  O   ASN A  67      24.238 -24.978 116.179  1.00 72.67           O  
ANISOU  328  O   ASN A  67    13117   7631   6863   -473    781    445       O  
ATOM    329  CB  ASN A  67      25.343 -21.992 116.353  1.00 65.90           C  
ANISOU  329  CB  ASN A  67    12054   6857   6129    -55    751    350       C  
ATOM    330  CG  ASN A  67      25.745 -21.277 115.081  1.00 81.07           C  
ANISOU  330  CG  ASN A  67    13800   8842   8161      1    645    320       C  
ATOM    331  OD1 ASN A  67      24.947 -20.622 114.393  1.00 71.54           O  
ANISOU  331  OD1 ASN A  67    12376   7759   7047     -6    688    356       O  
ATOM    332  ND2 ASN A  67      27.028 -21.341 114.780  1.00 71.77           N  
ANISOU  332  ND2 ASN A  67    12710   7592   6967     69    508    263       N  
ATOM    333  N   TYR A  68      23.773 -24.192 118.260  1.00 72.92           N  
ANISOU  333  N   TYR A  68    13238   7666   6802   -357    998    471       N  
ATOM    334  CA  TYR A  68      23.756 -25.498 118.921  1.00 74.14           C  
ANISOU  334  CA  TYR A  68    13656   7692   6823   -488   1022    497       C  
ATOM    335  C   TYR A  68      22.519 -26.296 118.501  1.00 80.09           C  
ANISOU  335  C   TYR A  68    14307   8539   7584   -756   1100    579       C  
ATOM    336  O   TYR A  68      22.670 -27.399 117.981  1.00 80.23           O  
ANISOU  336  O   TYR A  68    14481   8455   7549   -908   1017    580       O  
ATOM    337  CB  TYR A  68      23.871 -25.371 120.453  1.00 76.17           C  
ANISOU  337  CB  TYR A  68    14121   7868   6952   -409   1129    500       C  
ATOM    338  CG  TYR A  68      23.612 -26.670 121.182  1.00 80.24           C  
ANISOU  338  CG  TYR A  68    14904   8261   7321   -564   1190    545       C  
ATOM    339  CD1 TYR A  68      24.555 -27.694 121.180  1.00 82.45           C  
ANISOU  339  CD1 TYR A  68    15474   8353   7499   -547   1061    520       C  
ATOM    340  CD2 TYR A  68      22.409 -26.892 121.844  1.00 83.27           C  
ANISOU  340  CD2 TYR A  68    15256   8724   7660   -719   1386    625       C  
ATOM    341  CE1 TYR A  68      24.307 -28.909 121.819  1.00 85.62           C  
ANISOU  341  CE1 TYR A  68    16171   8613   7749   -689   1120    567       C  
ATOM    342  CE2 TYR A  68      22.153 -28.099 122.494  1.00 86.28           C  
ANISOU  342  CE2 TYR A  68    15906   8983   7892   -894   1447    672       C  
ATOM    343  CZ  TYR A  68      23.108 -29.104 122.483  1.00 94.91           C  
ANISOU  343  CZ  TYR A  68    17331   9855   8877   -880   1309    639       C  
ATOM    344  OH  TYR A  68      22.866 -30.292 123.131  1.00 99.29           O  
ANISOU  344  OH  TYR A  68    18202  10259   9266  -1044   1372    688       O  
ATOM    345  N   PHE A  69      21.310 -25.720 118.695  1.00 78.15           N  
ANISOU  345  N   PHE A  69    13803   8496   7394   -814   1258    657       N  
ATOM    346  CA  PHE A  69      20.019 -26.329 118.347  1.00 80.21           C  
ANISOU  346  CA  PHE A  69    13889   8922   7667  -1094   1334    763       C  
ATOM    347  C   PHE A  69      19.903 -26.664 116.860  1.00 85.00           C  
ANISOU  347  C   PHE A  69    14358   9591   8349  -1246   1174    764       C  
ATOM    348  O   PHE A  69      19.262 -27.654 116.499  1.00 86.37           O  
ANISOU  348  O   PHE A  69    14566   9784   8466  -1548   1156    822       O  
ATOM    349  CB  PHE A  69      18.852 -25.434 118.790  1.00 83.35           C  
ANISOU  349  CB  PHE A  69    13968   9577   8125  -1050   1536    861       C  
ATOM    350  CG  PHE A  69      18.776 -25.203 120.282  1.00 85.67           C  
ANISOU  350  CG  PHE A  69    14425   9810   8315   -933   1727    870       C  
ATOM    351  CD1 PHE A  69      18.248 -26.174 121.128  1.00 90.32           C  
ANISOU  351  CD1 PHE A  69    15176  10366   8774  -1139   1849    934       C  
ATOM    352  CD2 PHE A  69      19.220 -24.012 120.841  1.00 86.42           C  
ANISOU  352  CD2 PHE A  69    14549   9868   8421   -636   1786    815       C  
ATOM    353  CE1 PHE A  69      18.178 -25.958 122.506  1.00 91.76           C  
ANISOU  353  CE1 PHE A  69    15534  10487   8844  -1029   2032    943       C  
ATOM    354  CE2 PHE A  69      19.150 -23.799 122.218  1.00 89.95           C  
ANISOU  354  CE2 PHE A  69    15190  10242   8744   -536   1962    820       C  
ATOM    355  CZ  PHE A  69      18.622 -24.769 123.039  1.00 89.78           C  
ANISOU  355  CZ  PHE A  69    15314  10197   8600   -723   2086    884       C  
ATOM    356  N   LEU A  70      20.532 -25.844 116.006  1.00 80.44           N  
ANISOU  356  N   LEU A  70    13654   9030   7878  -1059   1059    702       N  
ATOM    357  CA  LEU A  70      20.560 -26.042 114.563  1.00 80.37           C  
ANISOU  357  CA  LEU A  70    13543   9062   7931  -1165    903    691       C  
ATOM    358  C   LEU A  70      21.389 -27.293 114.241  1.00 86.22           C  
ANISOU  358  C   LEU A  70    14649   9551   8557  -1265    783    628       C  
ATOM    359  O   LEU A  70      20.932 -28.129 113.462  1.00 87.98           O  
ANISOU  359  O   LEU A  70    14915   9773   8740  -1518    715    656       O  
ATOM    360  CB  LEU A  70      21.140 -24.779 113.868  1.00 78.32           C  
ANISOU  360  CB  LEU A  70    13106   8856   7796   -911    829    637       C  
ATOM    361  CG  LEU A  70      21.084 -24.614 112.318  1.00 82.03           C  
ANISOU  361  CG  LEU A  70    13411   9409   8346   -972    683    633       C  
ATOM    362  CD1 LEU A  70      22.278 -25.231 111.632  1.00 80.68           C  
ANISOU  362  CD1 LEU A  70    13502   9027   8126   -948    538    538       C  
ATOM    363  CD2 LEU A  70      19.759 -25.055 111.708  1.00 86.08           C  
ANISOU  363  CD2 LEU A  70    13705  10131   8870  -1258    679    745       C  
ATOM    364  N   PHE A  71      22.578 -27.442 114.866  1.00 81.87           N  
ANISOU  364  N   PHE A  71    14374   8793   7938  -1065    761    553       N  
ATOM    365  CA  PHE A  71      23.474 -28.572 114.622  1.00 81.77           C  
ANISOU  365  CA  PHE A  71    14721   8540   7810  -1070    666    503       C  
ATOM    366  C   PHE A  71      23.141 -29.823 115.448  1.00 87.69           C  
ANISOU  366  C   PHE A  71    15798   9130   8391  -1253    738    543       C  
ATOM    367  O   PHE A  71      23.649 -30.899 115.134  1.00 87.55           O  
ANISOU  367  O   PHE A  71    16116   8897   8253  -1288    676    518       O  
ATOM    368  CB  PHE A  71      24.944 -28.157 114.782  1.00 81.95           C  
ANISOU  368  CB  PHE A  71    14840   8459   7839   -754    589    426       C  
ATOM    369  CG  PHE A  71      25.484 -27.427 113.572  1.00 82.15           C  
ANISOU  369  CG  PHE A  71    14674   8559   7980   -638    482    380       C  
ATOM    370  CD1 PHE A  71      26.080 -28.121 112.528  1.00 85.56           C  
ANISOU  370  CD1 PHE A  71    15257   8881   8373   -638    387    346       C  
ATOM    371  CD2 PHE A  71      25.374 -26.045 113.466  1.00 83.20           C  
ANISOU  371  CD2 PHE A  71    14510   8859   8243   -527    491    372       C  
ATOM    372  CE1 PHE A  71      26.566 -27.444 111.404  1.00 85.29           C  
ANISOU  372  CE1 PHE A  71    15053   8920   8434   -538    303    308       C  
ATOM    373  CE2 PHE A  71      25.854 -25.371 112.341  1.00 84.70           C  
ANISOU  373  CE2 PHE A  71    14545   9111   8527   -438    398    335       C  
ATOM    374  CZ  PHE A  71      26.457 -26.072 111.323  1.00 82.83           C  
ANISOU  374  CZ  PHE A  71    14435   8780   8256   -448    305    304       C  
ATOM    375  N   SER A  72      22.262 -29.712 116.464  1.00 86.11           N  
ANISOU  375  N   SER A  72    15523   9027   8168  -1369    882    611       N  
ATOM    376  CA  SER A  72      21.848 -30.893 117.231  1.00 88.34           C  
ANISOU  376  CA  SER A  72    16116   9167   8282  -1586    963    661       C  
ATOM    377  C   SER A  72      20.830 -31.672 116.399  1.00 94.54           C  
ANISOU  377  C   SER A  72    16879  10011   9032  -1976    944    722       C  
ATOM    378  O   SER A  72      20.665 -32.881 116.577  1.00 96.12           O  
ANISOU  378  O   SER A  72    17433  10023   9067  -2204    952    743       O  
ATOM    379  CB  SER A  72      21.287 -30.508 118.601  1.00 92.74           C  
ANISOU  379  CB  SER A  72    16616   9809   8811  -1573   1137    716       C  
ATOM    380  OG  SER A  72      20.086 -29.761 118.516  1.00103.20           O  
ANISOU  380  OG  SER A  72    17538  11428  10244  -1692   1249    795       O  
ATOM    381  N   LYS A  73      20.201 -30.968 115.445  1.00 90.82           N  
ANISOU  381  N   LYS A  73    16014   9791   8703  -2052    904    751       N  
ATOM    382  CA  LYS A  73      19.212 -31.489 114.519  1.00 92.69           C  
ANISOU  382  CA  LYS A  73    16143  10152   8922  -2430    851    820       C  
ATOM    383  C   LYS A  73      19.838 -31.827 113.168  1.00 96.95           C  
ANISOU  383  C   LYS A  73    16840  10552   9444  -2440    675    745       C  
ATOM    384  O   LYS A  73      19.656 -32.942 112.675  1.00 98.54           O  
ANISOU  384  O   LYS A  73    17351  10593   9496  -2728    617    750       O  
ATOM    385  CB  LYS A  73      18.085 -30.463 114.340  1.00 95.35           C  
ANISOU  385  CB  LYS A  73    15932  10880   9414  -2479    910    918       C  
ATOM    386  CG  LYS A  73      16.706 -30.994 114.677  1.00107.14           C  
ANISOU  386  CG  LYS A  73    17270  12587  10850  -2872   1011   1062       C  
ATOM    387  CD  LYS A  73      16.391 -30.902 116.165  1.00112.25           C  
ANISOU  387  CD  LYS A  73    17941  13256  11452  -2813   1225   1113       C  
ATOM    388  CE  LYS A  73      14.972 -31.317 116.437  1.00119.47           C  
ANISOU  388  CE  LYS A  73    18630  14441  12321  -3204   1340   1275       C  
ATOM    389  NZ  LYS A  73      14.782 -32.786 116.309  1.00126.00           N  
ANISOU  389  NZ  LYS A  73    19829  15087  12958  -3651   1277   1295       N  
ATOM    390  N   VAL A  74      20.574 -30.875 112.569  1.00 92.00           N  
ANISOU  390  N   VAL A  74    16038   9967   8949  -2135    599    677       N  
ATOM    391  CA  VAL A  74      21.168 -31.079 111.253  1.00 91.82           C  
ANISOU  391  CA  VAL A  74    16129   9840   8917  -2113    452    610       C  
ATOM    392  C   VAL A  74      22.490 -31.891 111.308  1.00 96.58           C  
ANISOU  392  C   VAL A  74    17199  10102   9393  -1912    419    520       C  
ATOM    393  O   VAL A  74      22.722 -32.695 110.404  1.00 96.86           O  
ANISOU  393  O   VAL A  74    17508   9970   9323  -2016    339    486       O  
ATOM    394  CB  VAL A  74      21.300 -29.747 110.449  1.00 94.04           C  
ANISOU  394  CB  VAL A  74    16013  10333   9384  -1910    390    593       C  
ATOM    395  CG1 VAL A  74      22.580 -28.972 110.773  1.00 91.32           C  
ANISOU  395  CG1 VAL A  74    15677   9908   9112  -1500    394    509       C  
ATOM    396  CG2 VAL A  74      21.182 -29.996 108.952  1.00 94.33           C  
ANISOU  396  CG2 VAL A  74    16058  10379   9405  -2072    248    579       C  
ATOM    397  N   GLY A  75      23.297 -31.689 112.360  1.00 93.35           N  
ANISOU  397  N   GLY A  75    16883   9604   8980  -1630    482    493       N  
ATOM    398  CA  GLY A  75      24.608 -32.304 112.568  1.00 93.35           C  
ANISOU  398  CA  GLY A  75    17250   9344   8876  -1369    455    433       C  
ATOM    399  C   GLY A  75      24.726 -33.789 112.296  1.00101.18           C  
ANISOU  399  C   GLY A  75    18744  10044   9657  -1513    443    429       C  
ATOM    400  O   GLY A  75      25.628 -34.204 111.562  1.00100.67           O  
ANISOU  400  O   GLY A  75    18900   9817   9532  -1343    385    377       O  
ATOM    401  N   GLU A  76      23.816 -34.596 112.888  1.00101.23           N  
ANISOU  401  N   GLU A  76    18952   9974   9535  -1826    512    487       N  
ATOM    402  CA  GLU A  76      23.773 -36.054 112.726  1.00104.15           C  
ANISOU  402  CA  GLU A  76    19867  10037   9670  -2030    516    491       C  
ATOM    403  C   GLU A  76      23.459 -36.442 111.271  1.00110.89           C  
ANISOU  403  C   GLU A  76    20818  10843  10471  -2261    422    466       C  
ATOM    404  O   GLU A  76      24.053 -37.384 110.740  1.00111.76           O  
ANISOU  404  O   GLU A  76    21405  10652  10406  -2213    400    424       O  
ATOM    405  CB  GLU A  76      22.746 -36.674 113.686  1.00107.79           C  
ANISOU  405  CB  GLU A  76    20449  10486  10021  -2385    613    572       C  
ATOM    406  N   PHE A  77      22.551 -35.688 110.626  1.00108.13           N  
ANISOU  406  N   PHE A  77    20031  10790  10262  -2489    369    496       N  
ATOM    407  CA  PHE A  77      22.141 -35.897 109.245  1.00109.26           C  
ANISOU  407  CA  PHE A  77    20199  10948  10366  -2744    259    484       C  
ATOM    408  C   PHE A  77      23.262 -35.549 108.264  1.00112.71           C  
ANISOU  408  C   PHE A  77    20667  11308  10849  -2402    191    396       C  
ATOM    409  O   PHE A  77      23.610 -36.389 107.438  1.00114.04           O  
ANISOU  409  O   PHE A  77    21251  11228  10850  -2454    150    351       O  
ATOM    410  CB  PHE A  77      20.850 -35.111 108.937  1.00111.46           C  
ANISOU  410  CB  PHE A  77    19943  11616  10789  -3044    219    567       C  
ATOM    411  CG  PHE A  77      20.491 -34.991 107.472  1.00113.79           C  
ANISOU  411  CG  PHE A  77    20152  12002  11081  -3255     76    561       C  
ATOM    412  CD1 PHE A  77      19.836 -36.024 106.811  1.00120.18           C  
ANISOU  412  CD1 PHE A  77    21301  12680  11682  -3710     -1    582       C  
ATOM    413  CD2 PHE A  77      20.789 -33.834 106.758  1.00113.62           C  
ANISOU  413  CD2 PHE A  77    19738  12188  11245  -3020     12    537       C  
ATOM    414  CE1 PHE A  77      19.510 -35.913 105.455  1.00121.80           C  
ANISOU  414  CE1 PHE A  77    21450  12967  11860  -3921   -149    578       C  
ATOM    415  CE2 PHE A  77      20.465 -33.726 105.403  1.00117.05           C  
ANISOU  415  CE2 PHE A  77    20113  12701  11660  -3212   -127    536       C  
ATOM    416  CZ  PHE A  77      19.825 -34.764 104.761  1.00118.20           C  
ANISOU  416  CZ  PHE A  77    20590  12724  11595  -3660   -211    557       C  
ATOM    417  N   ILE A  78      23.842 -34.330 108.363  1.00107.27           N  
ANISOU  417  N   ILE A  78    19566  10821  10369  -2059    192    375       N  
ATOM    418  CA  ILE A  78      24.889 -33.849 107.444  1.00105.58           C  
ANISOU  418  CA  ILE A  78    19305  10590  10220  -1744    138    305       C  
ATOM    419  C   ILE A  78      26.256 -34.575 107.620  1.00110.52           C  
ANISOU  419  C   ILE A  78    20348  10927  10718  -1397    181    255       C  
ATOM    420  O   ILE A  78      27.241 -34.189 106.985  1.00108.82           O  
ANISOU  420  O   ILE A  78    20082  10713  10551  -1097    160    209       O  
ATOM    421  CB  ILE A  78      25.042 -32.297 107.449  1.00105.96           C  
ANISOU  421  CB  ILE A  78    18808  10940  10513  -1530    122    306       C  
ATOM    422  CG1 ILE A  78      25.439 -31.733 108.840  1.00105.21           C  
ANISOU  422  CG1 ILE A  78    18565  10910  10498  -1307    204    322       C  
ATOM    423  CG2 ILE A  78      23.781 -31.630 106.894  1.00107.01           C  
ANISOU  423  CG2 ILE A  78    18566  11345  10749  -1818     65    361       C  
ATOM    424  CD1 ILE A  78      25.910 -30.238 108.851  1.00110.11           C  
ANISOU  424  CD1 ILE A  78    18792  11735  11310  -1031    192    302       C  
ATOM    425  N   GLY A  79      26.280 -35.640 108.419  1.00109.73           N  
ANISOU  425  N   GLY A  79    20660  10590  10443  -1442    246    275       N  
ATOM    426  CA  GLY A  79      27.469 -36.454 108.636  1.00110.76           C  
ANISOU  426  CA  GLY A  79    21225  10438  10422  -1109    294    251       C  
ATOM    427  C   GLY A  79      28.282 -36.100 109.861  1.00114.69           C  
ANISOU  427  C   GLY A  79    21612  10985  10980   -760    337    274       C  
ATOM    428  O   GLY A  79      28.342 -36.889 110.809  1.00115.93           O  
ANISOU  428  O   GLY A  79    22090  10961  10996   -744    395    308       O  
ATOM    429  N   SER A  80      28.925 -34.914 109.846  1.00109.48           N  
ANISOU  429  N   SER A  80    20524  10562  10510   -495    302    260       N  
ATOM    430  CA  SER A  80      29.786 -34.464 110.942  1.00108.63           C  
ANISOU  430  CA  SER A  80    20291  10530  10452   -182    314    283       C  
ATOM    431  C   SER A  80      29.028 -33.821 112.115  1.00111.45           C  
ANISOU  431  C   SER A  80    20402  11045  10898   -337    339    314       C  
ATOM    432  O   SER A  80      28.322 -32.816 111.949  1.00109.55           O  
ANISOU  432  O   SER A  80    19781  11028  10815   -492    326    310       O  
ATOM    433  CB  SER A  80      30.891 -33.544 110.431  1.00110.96           C  
ANISOU  433  CB  SER A  80    20287  10998  10877    142    264    261       C  
ATOM    434  OG  SER A  80      32.140 -33.895 111.008  1.00121.33           O  
ANISOU  434  OG  SER A  80    21756  12239  12104    506    271    292       O  
ATOM    435  N   GLU A  81      29.199 -34.426 113.308  1.00108.63           N  
ANISOU  435  N   GLU A  81    20294  10559  10421   -270    385    353       N  
ATOM    436  CA  GLU A  81      28.603 -33.995 114.571  1.00107.91           C  
ANISOU  436  CA  GLU A  81    20068  10569  10364   -379    433    388       C  
ATOM    437  C   GLU A  81      29.650 -33.276 115.456  1.00109.56           C  
ANISOU  437  C   GLU A  81    20134  10877  10616    -51    396    394       C  
ATOM    438  O   GLU A  81      29.536 -33.277 116.685  1.00109.80           O  
ANISOU  438  O   GLU A  81    20246  10888  10584    -45    434    428       O  
ATOM    439  CB  GLU A  81      27.986 -35.209 115.292  1.00111.69           C  
ANISOU  439  CB  GLU A  81    20968  10821  10647   -593    513    433       C  
ATOM    440  N   ASP A  82      30.656 -32.646 114.817  1.00103.61           N  
ANISOU  440  N   ASP A  82    19167  10243   9959    196    316    366       N  
ATOM    441  CA  ASP A  82      31.756 -31.941 115.483  1.00102.06           C  
ANISOU  441  CA  ASP A  82    18807  10173   9796    476    250    379       C  
ATOM    442  C   ASP A  82      31.352 -30.646 116.181  1.00102.65           C  
ANISOU  442  C   ASP A  82    18566  10446   9992    393    247    366       C  
ATOM    443  O   ASP A  82      31.982 -30.287 117.176  1.00102.33           O  
ANISOU  443  O   ASP A  82    18513  10456   9913    535    206    388       O  
ATOM    444  CB  ASP A  82      32.913 -31.683 114.503  1.00103.48           C  
ANISOU  444  CB  ASP A  82    18849  10437  10031    727    176    367       C  
ATOM    445  CG  ASP A  82      33.618 -32.940 114.027  1.00118.17           C  
ANISOU  445  CG  ASP A  82    21061  12099  11739    930    193    394       C  
ATOM    446  OD1 ASP A  82      33.852 -33.847 114.864  1.00121.16           O  
ANISOU  446  OD1 ASP A  82    21770  12309  11956   1034    217    444       O  
ATOM    447  OD2 ASP A  82      33.969 -33.005 112.828  1.00123.95           O  
ANISOU  447  OD2 ASP A  82    21759  12837  12501   1009    191    370       O  
ATOM    448  N   VAL A  83      30.327 -29.941 115.659  1.00 96.84           N  
ANISOU  448  N   VAL A  83    17590   9820   9383    177    289    338       N  
ATOM    449  CA  VAL A  83      29.825 -28.672 116.208  1.00 94.84           C  
ANISOU  449  CA  VAL A  83    17063   9735   9235    116    318    327       C  
ATOM    450  C   VAL A  83      29.248 -28.896 117.610  1.00 98.18           C  
ANISOU  450  C   VAL A  83    17646  10100   9559     35    407    362       C  
ATOM    451  O   VAL A  83      29.611 -28.166 118.536  1.00 97.65           O  
ANISOU  451  O   VAL A  83    17533  10091   9480    129    397    360       O  
ATOM    452  CB  VAL A  83      28.826 -27.950 115.250  1.00 97.89           C  
ANISOU  452  CB  VAL A  83    17171  10255   9768    -58    352    310       C  
ATOM    453  CG1 VAL A  83      28.274 -26.670 115.874  1.00 97.14           C  
ANISOU  453  CG1 VAL A  83    16846  10305   9756    -79    413    310       C  
ATOM    454  CG2 VAL A  83      29.474 -27.639 113.904  1.00 96.58           C  
ANISOU  454  CG2 VAL A  83    16862  10145   9688     31    263    274       C  
ATOM    455  N   CYS A  84      28.389 -29.923 117.773  1.00 94.74           N  
ANISOU  455  N   CYS A  84    17423   9541   9033   -157    493    397       N  
ATOM    456  CA  CYS A  84      27.776 -30.253 119.062  1.00 95.06           C  
ANISOU  456  CA  CYS A  84    17637   9519   8963   -260    600    439       C  
ATOM    457  C   CYS A  84      28.744 -30.885 120.049  1.00 95.76           C  
ANISOU  457  C   CYS A  84    18039   9457   8888    -76    556    461       C  
ATOM    458  O   CYS A  84      28.593 -30.656 121.247  1.00 95.79           O  
ANISOU  458  O   CYS A  84    18115   9460   8820    -74    611    481       O  
ATOM    459  CB  CYS A  84      26.524 -31.100 118.883  1.00 97.41           C  
ANISOU  459  CB  CYS A  84    18041   9758   9211   -567    705    481       C  
ATOM    460  SG  CYS A  84      25.036 -30.132 118.542  1.00101.37           S  
ANISOU  460  SG  CYS A  84    18127  10520   9870   -796    816    508       S  
ATOM    461  N   ASN A  85      29.735 -31.663 119.560  1.00 89.85           N  
ANISOU  461  N   ASN A  85    17480   8589   8070    100    462    464       N  
ATOM    462  CA  ASN A  85      30.755 -32.284 120.409  1.00 89.53           C  
ANISOU  462  CA  ASN A  85    17715   8431   7870    329    401    505       C  
ATOM    463  C   ASN A  85      31.572 -31.205 121.121  1.00 90.65           C  
ANISOU  463  C   ASN A  85    17654   8740   8048    502    307    500       C  
ATOM    464  O   ASN A  85      31.820 -31.335 122.317  1.00 91.31           O  
ANISOU  464  O   ASN A  85    17914   8778   8001    565    295    537       O  
ATOM    465  CB  ASN A  85      31.658 -33.237 119.617  1.00 88.12           C  
ANISOU  465  CB  ASN A  85    17742   8122   7619    533    335    521       C  
ATOM    466  CG  ASN A  85      31.010 -34.543 119.215  1.00 92.28           C  
ANISOU  466  CG  ASN A  85    18638   8401   8023    373    420    535       C  
ATOM    467  OD1 ASN A  85      30.231 -35.149 119.959  1.00 75.76           O  
ANISOU  467  OD1 ASN A  85    16797   6174   5815    174    511    565       O  
ATOM    468  ND2 ASN A  85      31.350 -35.022 118.027  1.00 85.16           N  
ANISOU  468  ND2 ASN A  85    17809   7424   7123    448    396    515       N  
ATOM    469  N   PHE A  86      31.922 -30.112 120.407  1.00 84.13           N  
ANISOU  469  N   PHE A  86    16480   8102   7382    544    241    455       N  
ATOM    470  CA  PHE A  86      32.638 -28.970 120.984  1.00 82.73           C  
ANISOU  470  CA  PHE A  86    16114   8085   7234    643    146    444       C  
ATOM    471  C   PHE A  86      31.735 -28.245 121.989  1.00 85.79           C  
ANISOU  471  C   PHE A  86    16503   8488   7605    487    246    427       C  
ATOM    472  O   PHE A  86      32.193 -27.912 123.081  1.00 85.89           O  
ANISOU  472  O   PHE A  86    16614   8511   7511    547    196    443       O  
ATOM    473  CB  PHE A  86      33.110 -27.993 119.892  1.00 82.74           C  
ANISOU  473  CB  PHE A  86    15779   8259   7400    682     72    401       C  
ATOM    474  CG  PHE A  86      34.018 -26.897 120.401  1.00 83.65           C  
ANISOU  474  CG  PHE A  86    15733   8530   7518    761    -50    396       C  
ATOM    475  CD1 PHE A  86      35.397 -27.049 120.376  1.00 87.31           C  
ANISOU  475  CD1 PHE A  86    16153   9089   7932    955   -202    444       C  
ATOM    476  CD2 PHE A  86      33.494 -25.722 120.922  1.00 84.94           C  
ANISOU  476  CD2 PHE A  86    15804   8752   7717    636    -11    354       C  
ATOM    477  CE1 PHE A  86      36.235 -26.042 120.856  1.00 88.26           C  
ANISOU  477  CE1 PHE A  86    16123   9375   8038    971   -334    450       C  
ATOM    478  CE2 PHE A  86      34.331 -24.716 121.401  1.00 87.90           C  
ANISOU  478  CE2 PHE A  86    16088   9245   8065    665   -132    347       C  
ATOM    479  CZ  PHE A  86      35.697 -24.880 121.362  1.00 86.72           C  
ANISOU  479  CZ  PHE A  86    15879   9203   7866    806   -304    395       C  
ATOM    480  N   PHE A  87      30.458 -28.001 121.613  1.00 81.20           N  
ANISOU  480  N   PHE A  87    15813   7922   7117    296    388    405       N  
ATOM    481  CA  PHE A  87      29.455 -27.347 122.456  1.00 80.69           C  
ANISOU  481  CA  PHE A  87    15732   7885   7041    172    530    402       C  
ATOM    482  C   PHE A  87      29.195 -28.104 123.760  1.00 85.01           C  
ANISOU  482  C   PHE A  87    16603   8296   7402    135    608    449       C  
ATOM    483  O   PHE A  87      29.061 -27.476 124.801  1.00 84.93           O  
ANISOU  483  O   PHE A  87    16659   8296   7316    141    660    446       O  
ATOM    484  CB  PHE A  87      28.132 -27.153 121.694  1.00 81.98           C  
ANISOU  484  CB  PHE A  87    15693   8122   7334     -7    669    402       C  
ATOM    485  CG  PHE A  87      27.965 -25.834 120.977  1.00 81.95           C  
ANISOU  485  CG  PHE A  87    15371   8275   7491     18    664    362       C  
ATOM    486  CD1 PHE A  87      28.174 -24.629 121.640  1.00 84.78           C  
ANISOU  486  CD1 PHE A  87    15684   8685   7841     97    679    333       C  
ATOM    487  CD2 PHE A  87      27.515 -25.792 119.665  1.00 83.35           C  
ANISOU  487  CD2 PHE A  87    15332   8531   7807    -53    654    356       C  
ATOM    488  CE1 PHE A  87      27.997 -23.408 120.982  1.00 84.64           C  
ANISOU  488  CE1 PHE A  87    15426   8782   7953    126    685    300       C  
ATOM    489  CE2 PHE A  87      27.339 -24.570 119.007  1.00 85.08           C  
ANISOU  489  CE2 PHE A  87    15281   8885   8162    -18    652    328       C  
ATOM    490  CZ  PHE A  87      27.583 -23.387 119.670  1.00 82.85           C  
ANISOU  490  CZ  PHE A  87    14972   8637   7871     78    673    301       C  
ATOM    491  N   VAL A  88      29.147 -29.442 123.706  1.00 82.01           N  
ANISOU  491  N   VAL A  88    16463   7769   6928     98    619    491       N  
ATOM    492  CA  VAL A  88      28.869 -30.278 124.872  1.00 83.46           C  
ANISOU  492  CA  VAL A  88    16990   7800   6921     48    698    543       C  
ATOM    493  C   VAL A  88      30.137 -30.574 125.696  1.00 87.99           C  
ANISOU  493  C   VAL A  88    17797   8300   7337    270    549    572       C  
ATOM    494  O   VAL A  88      30.143 -30.301 126.896  1.00 87.90           O  
ANISOU  494  O   VAL A  88    17931   8267   7200    279    573    587       O  
ATOM    495  CB  VAL A  88      28.091 -31.556 124.461  1.00 88.40           C  
ANISOU  495  CB  VAL A  88    17809   8284   7495   -140    794    583       C  
ATOM    496  CG1 VAL A  88      28.068 -32.598 125.575  1.00 90.49           C  
ANISOU  496  CG1 VAL A  88    18502   8347   7534   -163    848    644       C  
ATOM    497  CG2 VAL A  88      26.671 -31.208 124.026  1.00 88.09           C  
ANISOU  497  CG2 VAL A  88    17533   8364   7571   -403    953    586       C  
ATOM    498  N   ASP A  89      31.194 -31.116 125.059  1.00 85.09           N  
ANISOU  498  N   ASP A  89    17460   7906   6964    458    401    587       N  
ATOM    499  CA  ASP A  89      32.441 -31.514 125.725  1.00 86.32           C  
ANISOU  499  CA  ASP A  89    17801   8028   6969    699    248    642       C  
ATOM    500  C   ASP A  89      33.402 -30.363 126.094  1.00 89.93           C  
ANISOU  500  C   ASP A  89    18035   8683   7451    822     85    630       C  
ATOM    501  O   ASP A  89      34.389 -30.618 126.788  1.00 90.69           O  
ANISOU  501  O   ASP A  89    18252   8795   7410   1001    -59    693       O  
ATOM    502  CB  ASP A  89      33.181 -32.575 124.892  1.00 88.86           C  
ANISOU  502  CB  ASP A  89    18247   8256   7259    888    178    683       C  
ATOM    503  N   ARG A  90      33.135 -29.118 125.654  1.00 85.47           N  
ANISOU  503  N   ARG A  90    17166   8269   7041    719     99    561       N  
ATOM    504  CA  ARG A  90      34.015 -27.983 125.967  1.00 85.20           C  
ANISOU  504  CA  ARG A  90    16957   8403   7011    778    -55    545       C  
ATOM    505  C   ARG A  90      33.283 -26.728 126.428  1.00 88.01           C  
ANISOU  505  C   ARG A  90    17242   8799   7399    617     39    479       C  
ATOM    506  O   ARG A  90      33.872 -25.937 127.163  1.00 88.35           O  
ANISOU  506  O   ARG A  90    17311   8907   7352    622    -68    473       O  
ATOM    507  CB  ARG A  90      34.959 -27.650 124.795  1.00 86.16           C  
ANISOU  507  CB  ARG A  90    16779   8689   7271    892   -192    539       C  
ATOM    508  CG  ARG A  90      36.121 -28.626 124.616  1.00102.39           C  
ANISOU  508  CG  ARG A  90    18888  10766   9248   1135   -329    626       C  
ATOM    509  CD  ARG A  90      37.415 -28.084 125.193  1.00117.94           C  
ANISOU  509  CD  ARG A  90    20748  12929  11134   1246   -546    682       C  
ATOM    510  NE  ARG A  90      38.494 -29.073 125.141  1.00130.11           N  
ANISOU  510  NE  ARG A  90    22331  14518  12587   1523   -663    793       N  
ATOM    511  CZ  ARG A  90      38.843 -29.861 126.155  1.00144.43           C  
ANISOU  511  CZ  ARG A  90    24414  16258  14207   1662   -724    883       C  
ATOM    512  NH1 ARG A  90      38.201 -29.790 127.315  1.00129.17           N  
ANISOU  512  NH1 ARG A  90    22744  14193  12142   1524   -677    868       N  
ATOM    513  NH2 ARG A  90      39.841 -30.724 126.017  1.00132.96           N  
ANISOU  513  NH2 ARG A  90    22977  14862  12677   1959   -821    997       N  
ATOM    514  N   VAL A  91      32.025 -26.526 125.995  1.00 83.53           N  
ANISOU  514  N   VAL A  91    16593   8201   6945    480    234    439       N  
ATOM    515  CA  VAL A  91      31.236 -25.343 126.369  1.00 83.16           C  
ANISOU  515  CA  VAL A  91    16481   8188   6928    376    362    388       C  
ATOM    516  C   VAL A  91      30.233 -25.679 127.499  1.00 89.03           C  
ANISOU  516  C   VAL A  91    17475   8816   7537    289    557    413       C  
ATOM    517  O   VAL A  91      29.983 -24.825 128.356  1.00 89.17           O  
ANISOU  517  O   VAL A  91    17586   8826   7470    266    630    388       O  
ATOM    518  CB  VAL A  91      30.587 -24.650 125.130  1.00 85.28           C  
ANISOU  518  CB  VAL A  91    16438   8552   7412    321    441    345       C  
ATOM    519  CG1 VAL A  91      29.513 -23.634 125.518  1.00 85.12           C  
ANISOU  519  CG1 VAL A  91    16380   8549   7414    251    632    316       C  
ATOM    520  CG2 VAL A  91      31.651 -23.989 124.262  1.00 83.90           C  
ANISOU  520  CG2 VAL A  91    16049   8495   7335    396    257    315       C  
ATOM    521  N   PHE A  92      29.695 -26.916 127.522  1.00 86.85           N  
ANISOU  521  N   PHE A  92    17338   8440   7220    233    648    463       N  
ATOM    522  CA  PHE A  92      28.741 -27.345 128.553  1.00 88.50           C  
ANISOU  522  CA  PHE A  92    17782   8550   7295    126    845    500       C  
ATOM    523  C   PHE A  92      29.385 -28.245 129.630  1.00 93.93           C  
ANISOU  523  C   PHE A  92    18844   9092   7752    187    767    553       C  
ATOM    524  O   PHE A  92      28.761 -28.520 130.659  1.00 94.54           O  
ANISOU  524  O   PHE A  92    19163   9077   7680    109    917    584       O  
ATOM    525  CB  PHE A  92      27.497 -28.030 127.937  1.00 90.77           C  
ANISOU  525  CB  PHE A  92    17981   8834   7671    -44   1030    533       C  
ATOM    526  CG  PHE A  92      26.744 -27.371 126.794  1.00 91.30           C  
ANISOU  526  CG  PHE A  92    17677   9055   7956   -115   1103    508       C  
ATOM    527  CD1 PHE A  92      26.778 -25.992 126.611  1.00 93.53           C  
ANISOU  527  CD1 PHE A  92    17745   9457   8336    -36   1107    458       C  
ATOM    528  CD2 PHE A  92      25.968 -28.130 125.923  1.00 93.66           C  
ANISOU  528  CD2 PHE A  92    17871   9375   8342   -272   1167    542       C  
ATOM    529  CE1 PHE A  92      26.075 -25.389 125.561  1.00 93.51           C  
ANISOU  529  CE1 PHE A  92    17413   9595   8521    -77   1172    448       C  
ATOM    530  CE2 PHE A  92      25.264 -27.526 124.877  1.00 95.54           C  
ANISOU  530  CE2 PHE A  92    17760   9774   8766   -339   1215    533       C  
ATOM    531  CZ  PHE A  92      25.323 -26.160 124.701  1.00 92.57           C  
ANISOU  531  CZ  PHE A  92    17159   9519   8492   -223   1219    490       C  
ATOM    532  N   GLY A  93      30.621 -28.679 129.383  1.00 91.12           N  
ANISOU  532  N   GLY A  93    18527   8732   7364    340    542    573       N  
ATOM    533  CA  GLY A  93      31.379 -29.536 130.288  1.00 93.16           C  
ANISOU  533  CA  GLY A  93    19115   8876   7406    449    431    640       C  
ATOM    534  C   GLY A  93      30.798 -30.930 130.415  1.00 99.84           C  
ANISOU  534  C   GLY A  93    20245   9535   8156    389    550    700       C  
ATOM    535  O   GLY A  93      30.440 -31.355 131.517  1.00101.27           O  
ANISOU  535  O   GLY A  93    20739   9590   8147    336    639    742       O  
ATOM    536  N   GLY A  94      30.675 -31.618 129.278  1.00 96.57           N  
ANISOU  536  N   GLY A  94    19748   9089   7854    377    560    703       N  
ATOM    537  CA  GLY A  94      30.139 -32.973 129.188  1.00 98.01           C  
ANISOU  537  CA  GLY A  94    20224   9073   7944    287    663    754       C  
ATOM    538  C   GLY A  94      28.624 -33.087 129.168  1.00102.60           C  
ANISOU  538  C   GLY A  94    20791   9630   8561    -16    903    751       C  
ATOM    539  O   GLY A  94      28.093 -34.088 128.679  1.00103.42           O  
ANISOU  539  O   GLY A  94    21049   9606   8639   -160    978    780       O  
ATOM    540  N   VAL A  95      27.916 -32.074 129.712  1.00 98.57           N  
ANISOU  540  N   VAL A  95    20110   9246   8095   -118   1031    724       N  
ATOM    541  CA  VAL A  95      26.450 -32.030 129.800  1.00 98.81           C  
ANISOU  541  CA  VAL A  95    20057   9323   8164   -380   1278    742       C  
ATOM    542  C   VAL A  95      25.845 -31.765 128.422  1.00101.76           C  
ANISOU  542  C   VAL A  95    20061   9839   8762   -498   1302    715       C  
ATOM    543  O   VAL A  95      26.282 -30.844 127.735  1.00 99.23           O  
ANISOU  543  O   VAL A  95    19448   9654   8601   -373   1198    658       O  
ATOM    544  CB  VAL A  95      25.945 -30.986 130.837  1.00102.51           C  
ANISOU  544  CB  VAL A  95    20470   9886   8591   -384   1424    731       C  
ATOM    545  CG1 VAL A  95      24.485 -31.235 131.197  1.00103.88           C  
ANISOU  545  CG1 VAL A  95    20637  10094   8737   -630   1707    789       C  
ATOM    546  CG2 VAL A  95      26.809 -30.975 132.094  1.00103.19           C  
ANISOU  546  CG2 VAL A  95    20886   9859   8463   -230   1331    739       C  
ATOM    547  N   ARG A  96      24.839 -32.564 128.025  1.00 99.95           N  
ANISOU  547  N   ARG A  96    19856   9586   8534   -760   1432    763       N  
ATOM    548  CA  ARG A  96      24.148 -32.390 126.748  1.00 99.09           C  
ANISOU  548  CA  ARG A  96    19409   9626   8614   -916   1449    754       C  
ATOM    549  C   ARG A  96      22.891 -31.531 126.973  1.00103.56           C  
ANISOU  549  C   ARG A  96    19655  10421   9274  -1054   1656    786       C  
ATOM    550  O   ARG A  96      21.766 -32.036 126.881  1.00104.88           O  
ANISOU  550  O   ARG A  96    19761  10656   9433  -1333   1803    857       O  
ATOM    551  CB  ARG A  96      23.817 -33.752 126.114  1.00100.80           C  
ANISOU  551  CB  ARG A  96    19846   9694   8760  -1146   1442    793       C  
ATOM    552  N   LEU A  97      23.106 -30.226 127.300  1.00 98.60           N  
ANISOU  552  N   LEU A  97    18836   9913   8717   -853   1671    742       N  
ATOM    553  CA  LEU A  97      22.068 -29.228 127.598  1.00 98.71           C  
ANISOU  553  CA  LEU A  97    18570  10131   8804   -877   1879    770       C  
ATOM    554  C   LEU A  97      20.921 -29.232 126.594  1.00102.58           C  
ANISOU  554  C   LEU A  97    18692  10833   9450  -1080   1965    827       C  
ATOM    555  O   LEU A  97      21.156 -29.277 125.387  1.00100.26           O  
ANISOU  555  O   LEU A  97    18232  10578   9285  -1100   1813    797       O  
ATOM    556  CB  LEU A  97      22.654 -27.818 127.765  1.00 97.25           C  
ANISOU  556  CB  LEU A  97    18263  10005   8681   -616   1832    696       C  
ATOM    557  CG  LEU A  97      23.607 -27.566 128.945  1.00102.15           C  
ANISOU  557  CG  LEU A  97    19214  10472   9127   -446   1769    653       C  
ATOM    558  CD1 LEU A  97      24.065 -26.130 128.957  1.00101.06           C  
ANISOU  558  CD1 LEU A  97    18948  10401   9049   -256   1723    582       C  
ATOM    559  CD2 LEU A  97      22.949 -27.867 130.281  1.00107.26           C  
ANISOU  559  CD2 LEU A  97    20110  11058   9585   -519   1988    710       C  
ATOM    560  N   LEU A  98      19.678 -29.228 127.112  1.00101.73           N  
ANISOU  560  N   LEU A  98    18460  10875   9316  -1237   2210    921       N  
ATOM    561  CA  LEU A  98      18.455 -29.344 126.317  1.00102.86           C  
ANISOU  561  CA  LEU A  98    18237  11267   9579  -1473   2303   1012       C  
ATOM    562  C   LEU A  98      17.588 -28.084 126.228  1.00107.12           C  
ANISOU  562  C   LEU A  98    18349  12100  10253  -1349   2473   1061       C  
ATOM    563  O   LEU A  98      16.947 -27.885 125.194  1.00106.82           O  
ANISOU  563  O   LEU A  98    17940  12282  10365  -1443   2447   1110       O  
ATOM    564  CB  LEU A  98      17.606 -30.519 126.832  1.00105.83           C  
ANISOU  564  CB  LEU A  98    18768  11632   9812  -1816   2447   1119       C  
ATOM    565  CG  LEU A  98      18.268 -31.898 126.799  1.00110.78           C  
ANISOU  565  CG  LEU A  98    19840  11962  10290  -1977   2299   1094       C  
ATOM    566  CD1 LEU A  98      17.703 -32.795 127.874  1.00114.03           C  
ANISOU  566  CD1 LEU A  98    20538  12290  10500  -2222   2480   1183       C  
ATOM    567  CD2 LEU A  98      18.152 -32.544 125.425  1.00112.90           C  
ANISOU  567  CD2 LEU A  98    20011  12244  10640  -2188   2131   1091       C  
ATOM    568  N   ASP A  99      17.528 -27.262 127.296  1.00103.97           N  
ANISOU  568  N   ASP A  99    18019  11700   9783  -1137   2653   1057       N  
ATOM    569  CA  ASP A  99      16.699 -26.049 127.296  1.00104.42           C  
ANISOU  569  CA  ASP A  99    17727  12010   9939   -966   2854   1111       C  
ATOM    570  C   ASP A  99      17.463 -24.782 126.906  1.00104.74           C  
ANISOU  570  C   ASP A  99    17718  12006  10071   -648   2744   1006       C  
ATOM    571  O   ASP A  99      18.660 -24.672 127.179  1.00102.36           O  
ANISOU  571  O   ASP A  99    17721  11471   9702   -526   2579    892       O  
ATOM    572  CB  ASP A  99      15.995 -25.864 128.648  1.00109.15           C  
ANISOU  572  CB  ASP A  99    18428  12654  10390   -925   3171   1187       C  
ATOM    573  CG  ASP A  99      16.935 -25.499 129.776  1.00119.48           C  
ANISOU  573  CG  ASP A  99    20175  13693  11529   -711   3174   1085       C  
ATOM    574  OD1 ASP A  99      17.847 -26.303 130.070  1.00119.02           O  
ANISOU  574  OD1 ASP A  99    20475  13387  11360   -781   2992   1018       O  
ATOM    575  OD2 ASP A  99      16.775 -24.400 130.347  1.00126.92           O  
ANISOU  575  OD2 ASP A  99    21117  14670  12435   -467   3357   1078       O  
ATOM    576  N   VAL A 100      16.734 -23.820 126.300  1.00100.97           N  
ANISOU  576  N   VAL A 100    16856  11771   9738   -523   2843   1061       N  
ATOM    577  CA  VAL A 100      17.179 -22.499 125.821  1.00 98.88           C  
ANISOU  577  CA  VAL A 100    16501  11501   9567   -236   2783    988       C  
ATOM    578  C   VAL A 100      17.992 -21.741 126.881  1.00101.72           C  
ANISOU  578  C   VAL A 100    17245  11625   9778     -7   2818    886       C  
ATOM    579  O   VAL A 100      19.085 -21.260 126.572  1.00 99.30           O  
ANISOU  579  O   VAL A 100    17086  11160   9484     91   2605    771       O  
ATOM    580  CB  VAL A 100      15.962 -21.647 125.342  1.00104.44           C  
ANISOU  580  CB  VAL A 100    16764  12519  10398   -109   2975   1107       C  
ATOM    581  CG1 VAL A 100      16.397 -20.299 124.769  1.00102.66           C  
ANISOU  581  CG1 VAL A 100    16489  12261  10258    183   2907   1036       C  
ATOM    582  CG2 VAL A 100      15.106 -22.408 124.338  1.00105.13           C  
ANISOU  582  CG2 VAL A 100    16459  12872  10611   -377   2917   1224       C  
ATOM    583  N   ALA A 101      17.447 -21.629 128.114  1.00 99.72           N  
ANISOU  583  N   ALA A 101    17156  11361   9373     58   3087    933       N  
ATOM    584  CA  ALA A 101      18.058 -20.913 129.234  1.00 99.60           C  
ANISOU  584  CA  ALA A 101    17542  11125   9176    249   3150    847       C  
ATOM    585  C   ALA A 101      19.480 -21.374 129.551  1.00100.93           C  
ANISOU  585  C   ALA A 101    18080  11029   9241    181   2866    728       C  
ATOM    586  O   ALA A 101      20.393 -20.545 129.574  1.00 98.72           O  
ANISOU  586  O   ALA A 101    17964  10614   8930    317   2723    627       O  
ATOM    587  CB  ALA A 101      17.174 -21.017 130.467  1.00103.55           C  
ANISOU  587  CB  ALA A 101    18174  11658   9511    271   3485    931       C  
ATOM    588  N   SER A 102      19.666 -22.699 129.759  1.00 97.78           N  
ANISOU  588  N   SER A 102    17803  10567   8782    -34   2779    752       N  
ATOM    589  CA  SER A 102      20.955 -23.327 130.069  1.00 96.35           C  
ANISOU  589  CA  SER A 102    17952  10165   8493    -83   2520    673       C  
ATOM    590  C   SER A 102      21.954 -23.151 128.932  1.00 97.01           C  
ANISOU  590  C   SER A 102    17910  10231   8717    -49   2219    598       C  
ATOM    591  O   SER A 102      23.114 -22.822 129.190  1.00 95.95           O  
ANISOU  591  O   SER A 102    17987   9962   8508     37   2028    517       O  
ATOM    592  CB  SER A 102      20.773 -24.810 130.380  1.00101.46           C  
ANISOU  592  CB  SER A 102    18740  10757   9055   -303   2523    737       C  
ATOM    593  OG  SER A 102      20.092 -25.006 131.608  1.00115.26           O  
ANISOU  593  OG  SER A 102    20689  12479  10626   -339   2781    798       O  
ATOM    594  N   VAL A 103      21.496 -23.354 127.678  1.00 91.43           N  
ANISOU  594  N   VAL A 103    16857   9679   8205   -129   2178    632       N  
ATOM    595  CA  VAL A 103      22.312 -23.204 126.473  1.00 88.14           C  
ANISOU  595  CA  VAL A 103    16291   9267   7930   -102   1925    571       C  
ATOM    596  C   VAL A 103      22.768 -21.748 126.325  1.00 88.73           C  
ANISOU  596  C   VAL A 103    16326   9343   8045     95   1888    500       C  
ATOM    597  O   VAL A 103      23.955 -21.526 126.091  1.00 86.94           O  
ANISOU  597  O   VAL A 103    16198   9025   7810    145   1665    425       O  
ATOM    598  CB  VAL A 103      21.617 -23.780 125.208  1.00 91.99           C  
ANISOU  598  CB  VAL A 103    16455   9911   8585   -256   1902    629       C  
ATOM    599  CG1 VAL A 103      22.424 -23.501 123.940  1.00 89.55           C  
ANISOU  599  CG1 VAL A 103    15996   9612   8416   -204   1669    565       C  
ATOM    600  CG2 VAL A 103      21.381 -25.279 125.358  1.00 92.92           C  
ANISOU  600  CG2 VAL A 103    16715   9967   8625   -484   1896    682       C  
ATOM    601  N   TYR A 104      21.859 -20.765 126.532  1.00 84.64           N  
ANISOU  601  N   TYR A 104    15695   8919   7544    210   2114    533       N  
ATOM    602  CA  TYR A 104      22.222 -19.346 126.452  1.00 83.23           C  
ANISOU  602  CA  TYR A 104    15555   8701   7369    397   2106    468       C  
ATOM    603  C   TYR A 104      23.255 -18.984 127.514  1.00 86.23           C  
ANISOU  603  C   TYR A 104    16342   8875   7548    441   2020    385       C  
ATOM    604  O   TYR A 104      24.235 -18.305 127.197  1.00 84.71           O  
ANISOU  604  O   TYR A 104    16218   8613   7357    480   1829    307       O  
ATOM    605  CB  TYR A 104      20.998 -18.411 126.555  1.00 85.89           C  
ANISOU  605  CB  TYR A 104    15740   9160   7734    557   2398    533       C  
ATOM    606  CG  TYR A 104      21.381 -16.943 126.604  1.00 87.47           C  
ANISOU  606  CG  TYR A 104    16090   9257   7887    758   2412    463       C  
ATOM    607  CD1 TYR A 104      21.577 -16.213 125.434  1.00 88.09           C  
ANISOU  607  CD1 TYR A 104    15962   9393   8114    832   2305    442       C  
ATOM    608  CD2 TYR A 104      21.588 -16.295 127.819  1.00 89.65           C  
ANISOU  608  CD2 TYR A 104    16762   9354   7948    856   2524    413       C  
ATOM    609  CE1 TYR A 104      21.952 -14.870 125.473  1.00 88.87           C  
ANISOU  609  CE1 TYR A 104    16249   9367   8149    993   2317    378       C  
ATOM    610  CE2 TYR A 104      21.979 -14.959 127.870  1.00 90.84           C  
ANISOU  610  CE2 TYR A 104    17120   9373   8024   1006   2527    342       C  
ATOM    611  CZ  TYR A 104      22.153 -14.247 126.694  1.00 97.63           C  
ANISOU  611  CZ  TYR A 104    17774  10285   9035   1072   2427    326       C  
ATOM    612  OH  TYR A 104      22.523 -12.926 126.751  1.00 99.99           O  
ANISOU  612  OH  TYR A 104    18323  10429   9239   1202   2439    258       O  
ATOM    613  N   ALA A 105      23.020 -19.416 128.771  1.00 83.51           N  
ANISOU  613  N   ALA A 105    16266   8445   7020    417   2160    408       N  
ATOM    614  CA  ALA A 105      23.911 -19.142 129.896  1.00 83.57           C  
ANISOU  614  CA  ALA A 105    16688   8263   6801    438   2080    342       C  
ATOM    615  C   ALA A 105      25.312 -19.703 129.664  1.00 84.69           C  
ANISOU  615  C   ALA A 105    16904   8343   6930    353   1738    294       C  
ATOM    616  O   ALA A 105      26.291 -19.021 129.968  1.00 84.11           O  
ANISOU  616  O   ALA A 105    17018   8184   6756    375   1573    227       O  
ATOM    617  CB  ALA A 105      23.323 -19.689 131.183  1.00 86.59           C  
ANISOU  617  CB  ALA A 105    17325   8581   6995    409   2291    391       C  
ATOM    618  N   ALA A 106      25.408 -20.916 129.086  1.00 79.57           N  
ANISOU  618  N   ALA A 106    16107   7748   6377    256   1634    336       N  
ATOM    619  CA  ALA A 106      26.685 -21.556 128.775  1.00 77.81           C  
ANISOU  619  CA  ALA A 106    15923   7491   6153    222   1337    314       C  
ATOM    620  C   ALA A 106      27.381 -20.843 127.626  1.00 79.71           C  
ANISOU  620  C   ALA A 106    15934   7807   6545    263   1156    264       C  
ATOM    621  O   ALA A 106      28.602 -20.690 127.659  1.00 79.17           O  
ANISOU  621  O   ALA A 106    15943   7716   6420    274    926    231       O  
ATOM    622  CB  ALA A 106      26.466 -23.016 128.425  1.00 78.34           C  
ANISOU  622  CB  ALA A 106    15936   7564   6264    131   1322    375       C  
ATOM    623  N   CYS A 107      26.596 -20.397 126.622  1.00 74.86           N  
ANISOU  623  N   CYS A 107    15031   7299   6113    279   1260    271       N  
ATOM    624  CA  CYS A 107      27.073 -19.707 125.429  1.00 72.71           C  
ANISOU  624  CA  CYS A 107    14531   7101   5995    312   1123    232       C  
ATOM    625  C   CYS A 107      27.553 -18.302 125.699  1.00 76.45           C  
ANISOU  625  C   CYS A 107    15126   7524   6399    374   1092    170       C  
ATOM    626  O   CYS A 107      28.439 -17.820 124.990  1.00 75.05           O  
ANISOU  626  O   CYS A 107    14863   7374   6279    366    904    131       O  
ATOM    627  CB  CYS A 107      26.018 -19.733 124.333  1.00 72.57           C  
ANISOU  627  CB  CYS A 107    14193   7212   6169    305   1240    273       C  
ATOM    628  SG  CYS A 107      25.904 -21.318 123.470  1.00 75.93           S  
ANISOU  628  SG  CYS A 107    14469   7689   6691    176   1161    324       S  
ATOM    629  N   SER A 108      26.955 -17.632 126.703  1.00 74.38           N  
ANISOU  629  N   SER A 108    15083   7178   5999    428   1286    163       N  
ATOM    630  CA  SER A 108      27.333 -16.275 127.105  1.00 74.52           C  
ANISOU  630  CA  SER A 108    15319   7097   5899    475   1283     99       C  
ATOM    631  C   SER A 108      28.671 -16.301 127.845  1.00 78.60           C  
ANISOU  631  C   SER A 108    16099   7531   6236    379   1040     57       C  
ATOM    632  O   SER A 108      29.396 -15.304 127.835  1.00 78.17           O  
ANISOU  632  O   SER A 108    16169   7425   6107    342    919      1       O  
ATOM    633  CB  SER A 108      26.245 -15.641 127.964  1.00 79.19           C  
ANISOU  633  CB  SER A 108    16105   7611   6374    587   1590    111       C  
ATOM    634  OG  SER A 108      25.919 -16.465 129.068  1.00 88.36           O  
ANISOU  634  OG  SER A 108    17461   8722   7388    555   1693    145       O  
ATOM    635  N   GLN A 109      29.010 -17.466 128.438  1.00 75.78           N  
ANISOU  635  N   GLN A 109    15818   7172   5802    328    957     93       N  
ATOM    636  CA  GLN A 109      30.252 -17.726 129.174  1.00 76.49           C  
ANISOU  636  CA  GLN A 109    16116   7228   5719    253    710     85       C  
ATOM    637  C   GLN A 109      31.426 -18.155 128.253  1.00 80.25           C  
ANISOU  637  C   GLN A 109    16345   7835   6312    222    427    100       C  
ATOM    638  O   GLN A 109      32.526 -18.414 128.749  1.00 80.99           O  
ANISOU  638  O   GLN A 109    16540   7955   6278    176    201    116       O  
ATOM    639  CB  GLN A 109      30.009 -18.779 130.268  1.00 78.80           C  
ANISOU  639  CB  GLN A 109    16633   7451   5857    249    772    132       C  
ATOM    640  CG  GLN A 109      29.252 -18.259 131.485  1.00 86.01           C  
ANISOU  640  CG  GLN A 109    17885   8226   6571    266   1005    116       C  
ATOM    641  CD  GLN A 109      28.534 -19.353 132.248  1.00 99.28           C  
ANISOU  641  CD  GLN A 109    19682   9863   8176    272   1177    178       C  
ATOM    642  OE1 GLN A 109      29.032 -20.474 132.419  1.00 91.85           O  
ANISOU  642  OE1 GLN A 109    18772   8927   7199    238   1039    224       O  
ATOM    643  NE2 GLN A 109      27.338 -19.046 132.737  1.00 91.44           N  
ANISOU  643  NE2 GLN A 109    18768   8827   7146    323   1496    190       N  
ATOM    644  N   MET A 110      31.195 -18.214 126.927  1.00 75.44           N  
ANISOU  644  N   MET A 110    15411   7322   5931    255    442    104       N  
ATOM    645  CA  MET A 110      32.209 -18.599 125.943  1.00 74.50           C  
ANISOU  645  CA  MET A 110    15048   7329   5928    252    221    121       C  
ATOM    646  C   MET A 110      33.239 -17.504 125.726  1.00 78.70           C  
ANISOU  646  C   MET A 110    15559   7917   6426    180     36     85       C  
ATOM    647  O   MET A 110      32.873 -16.335 125.592  1.00 78.93           O  
ANISOU  647  O   MET A 110    15640   7892   6457    149    120     34       O  
ATOM    648  CB  MET A 110      31.562 -18.907 124.586  1.00 75.46           C  
ANISOU  648  CB  MET A 110    14870   7520   6282    292    309    130       C  
ATOM    649  CG  MET A 110      30.847 -20.221 124.531  1.00 79.52           C  
ANISOU  649  CG  MET A 110    15359   8015   6840    311    416    179       C  
ATOM    650  SD  MET A 110      29.927 -20.379 122.986  1.00 82.82           S  
ANISOU  650  SD  MET A 110    15455   8515   7496    308    520    186       S  
ATOM    651  CE  MET A 110      31.206 -20.995 121.901  1.00 78.32           C  
ANISOU  651  CE  MET A 110    14731   8021   7007    341    290    193       C  
ATOM    652  N   ASN A 111      34.521 -17.883 125.630  1.00 74.96           N  
ANISOU  652  N   ASN A 111    14999   7562   5921    158   -210    122       N  
ATOM    653  CA  ASN A 111      35.578 -16.924 125.323  1.00 74.92           C  
ANISOU  653  CA  ASN A 111    14921   7656   5889     50   -403    106       C  
ATOM    654  C   ASN A 111      35.667 -16.771 123.788  1.00 77.01           C  
ANISOU  654  C   ASN A 111    14858   8026   6377     80   -403    101       C  
ATOM    655  O   ASN A 111      35.040 -17.559 123.076  1.00 75.17           O  
ANISOU  655  O   ASN A 111    14477   7791   6293    184   -287    115       O  
ATOM    656  CB  ASN A 111      36.912 -17.322 125.983  1.00 76.85           C  
ANISOU  656  CB  ASN A 111    15191   8027   5982      3   -668    170       C  
ATOM    657  CG  ASN A 111      37.578 -18.563 125.447  1.00 98.72           C  
ANISOU  657  CG  ASN A 111    17724  10947   8839    140   -777    254       C  
ATOM    658  OD1 ASN A 111      38.101 -18.587 124.333  1.00 94.91           O  
ANISOU  658  OD1 ASN A 111    16956  10604   8503    175   -837    273       O  
ATOM    659  ND2 ASN A 111      37.690 -19.579 126.281  1.00 90.02           N  
ANISOU  659  ND2 ASN A 111    16765   9819   7618    227   -814    313       N  
ATOM    660  N   ALA A 112      36.409 -15.755 123.281  1.00 73.93           N  
ANISOU  660  N   ALA A 112    14380   7717   5993    -34   -528     82       N  
ATOM    661  CA  ALA A 112      36.539 -15.494 121.837  1.00 72.19           C  
ANISOU  661  CA  ALA A 112    13876   7590   5961    -20   -528     77       C  
ATOM    662  C   ALA A 112      37.141 -16.644 121.051  1.00 76.34           C  
ANISOU  662  C   ALA A 112    14132   8271   6604     92   -609    141       C  
ATOM    663  O   ALA A 112      36.677 -16.892 119.938  1.00 74.84           O  
ANISOU  663  O   ALA A 112    13768   8090   6579    164   -516    133       O  
ATOM    664  CB  ALA A 112      37.306 -14.212 121.575  1.00 73.45           C  
ANISOU  664  CB  ALA A 112    14039   7802   6069   -195   -652     54       C  
ATOM    665  N   HIS A 113      38.133 -17.374 121.626  1.00 74.44           N  
ANISOU  665  N   HIS A 113    13873   8148   6264    124   -774    211       N  
ATOM    666  CA  HIS A 113      38.739 -18.535 120.958  1.00 74.30           C  
ANISOU  666  CA  HIS A 113    13643   8262   6326    284   -832    284       C  
ATOM    667  C   HIS A 113      37.683 -19.631 120.740  1.00 74.53           C  
ANISOU  667  C   HIS A 113    13742   8143   6431    421   -654    275       C  
ATOM    668  O   HIS A 113      37.660 -20.253 119.676  1.00 73.19           O  
ANISOU  668  O   HIS A 113    13418   8005   6387    518   -610    287       O  
ATOM    669  CB  HIS A 113      39.994 -19.047 121.716  1.00 77.92           C  
ANISOU  669  CB  HIS A 113    14082   8886   6639    323  -1042    381       C  
ATOM    670  CG  HIS A 113      40.387 -20.475 121.425  1.00 82.47           C  
ANISOU  670  CG  HIS A 113    14569   9525   7241    561  -1055    465       C  
ATOM    671  ND1 HIS A 113      40.697 -20.901 120.136  1.00 83.93           N  
ANISOU  671  ND1 HIS A 113    14520   9805   7567    689  -1023    491       N  
ATOM    672  CD2 HIS A 113      40.523 -21.526 122.272  1.00 85.76           C  
ANISOU  672  CD2 HIS A 113    15140   9908   7536    698  -1093    532       C  
ATOM    673  CE1 HIS A 113      40.987 -22.192 120.244  1.00 84.18           C  
ANISOU  673  CE1 HIS A 113    14591   9838   7555    911  -1029    567       C  
ATOM    674  NE2 HIS A 113      40.899 -22.612 121.507  1.00 85.62           N  
ANISOU  674  NE2 HIS A 113    15004   9946   7583    926  -1074    598       N  
ATOM    675  N   GLN A 114      36.774 -19.802 121.720  1.00 69.43           N  
ANISOU  675  N   GLN A 114    13345   7335   5700    401   -542    251       N  
ATOM    676  CA  GLN A 114      35.684 -20.776 121.690  1.00 67.98           C  
ANISOU  676  CA  GLN A 114    13256   7014   5558    467   -369    249       C  
ATOM    677  C   GLN A 114      34.607 -20.426 120.667  1.00 68.63           C  
ANISOU  677  C   GLN A 114    13213   7057   5807    431   -210    201       C  
ATOM    678  O   GLN A 114      34.117 -21.325 119.992  1.00 67.79           O  
ANISOU  678  O   GLN A 114    13054   6922   5782    477   -139    216       O  
ATOM    679  CB  GLN A 114      35.061 -20.940 123.082  1.00 70.59           C  
ANISOU  679  CB  GLN A 114    13875   7210   5736    432   -287    247       C  
ATOM    680  CG  GLN A 114      35.969 -21.637 124.092  1.00 91.52           C  
ANISOU  680  CG  GLN A 114    16680   9883   8210    492   -438    313       C  
ATOM    681  CD  GLN A 114      35.338 -21.747 125.457  1.00113.55           C  
ANISOU  681  CD  GLN A 114    19782  12530  10832    447   -351    309       C  
ATOM    682  OE1 GLN A 114      34.782 -20.783 125.997  1.00109.77           O  
ANISOU  682  OE1 GLN A 114    19424  11985  10299    347   -265    254       O  
ATOM    683  NE2 GLN A 114      35.444 -22.922 126.064  1.00107.06           N  
ANISOU  683  NE2 GLN A 114    19127  11649   9903    533   -367    371       N  
ATOM    684  N   ARG A 115      34.228 -19.139 120.551  1.00 63.69           N  
ANISOU  684  N   ARG A 115    12561   6424   5214    350   -159    150       N  
ATOM    685  CA  ARG A 115      33.213 -18.714 119.583  1.00 62.25           C  
ANISOU  685  CA  ARG A 115    12244   6227   5180    339    -20    121       C  
ATOM    686  C   ARG A 115      33.759 -18.838 118.168  1.00 66.23           C  
ANISOU  686  C   ARG A 115    12513   6833   5816    365   -101    127       C  
ATOM    687  O   ARG A 115      33.033 -19.271 117.273  1.00 64.92           O  
ANISOU  687  O   ARG A 115    12244   6661   5760    380    -20    131       O  
ATOM    688  CB  ARG A 115      32.720 -17.290 119.856  1.00 62.51           C  
ANISOU  688  CB  ARG A 115    12351   6210   5191    290     62     77       C  
ATOM    689  CG  ARG A 115      32.024 -17.118 121.208  1.00 78.16           C  
ANISOU  689  CG  ARG A 115    14590   8076   7032    287    189     69       C  
ATOM    690  CD  ARG A 115      31.394 -15.742 121.383  1.00 89.88           C  
ANISOU  690  CD  ARG A 115    16180   9483   8486    287    317     29       C  
ATOM    691  NE  ARG A 115      32.315 -14.658 121.032  1.00 97.10           N  
ANISOU  691  NE  ARG A 115    17111  10411   9373    215    179     -8       N  
ATOM    692  CZ  ARG A 115      33.191 -14.113 121.868  1.00112.96           C  
ANISOU  692  CZ  ARG A 115    19332  12380  11209    116     55    -31       C  
ATOM    693  NH1 ARG A 115      33.271 -14.530 123.127  1.00100.75           N  
ANISOU  693  NH1 ARG A 115    18012  10771   9498    100     51    -24       N  
ATOM    694  NH2 ARG A 115      33.997 -13.144 121.451  1.00100.08           N  
ANISOU  694  NH2 ARG A 115    17701  10773   9552      8    -72    -56       N  
ATOM    695  N   HIS A 116      35.060 -18.503 117.988  1.00 63.76           N  
ANISOU  695  N   HIS A 116    12120   6628   5476    358   -265    137       N  
ATOM    696  CA  HIS A 116      35.809 -18.591 116.729  1.00 62.81           C  
ANISOU  696  CA  HIS A 116    11782   6629   5454    393   -344    154       C  
ATOM    697  C   HIS A 116      35.874 -20.039 116.244  1.00 68.35           C  
ANISOU  697  C   HIS A 116    12460   7327   6182    515   -332    193       C  
ATOM    698  O   HIS A 116      35.582 -20.286 115.077  1.00 66.83           O  
ANISOU  698  O   HIS A 116    12157   7142   6093    540   -288    185       O  
ATOM    699  CB  HIS A 116      37.214 -17.986 116.914  1.00 63.92           C  
ANISOU  699  CB  HIS A 116    11846   6917   5526    343   -518    179       C  
ATOM    700  CG  HIS A 116      38.218 -18.349 115.864  1.00 66.74           C  
ANISOU  700  CG  HIS A 116    11975   7437   5947    415   -601    225       C  
ATOM    701  ND1 HIS A 116      39.393 -18.998 116.191  1.00 69.62           N  
ANISOU  701  ND1 HIS A 116    12268   7948   6237    507   -727    303       N  
ATOM    702  CD2 HIS A 116      38.212 -18.104 114.534  1.00 66.96           C  
ANISOU  702  CD2 HIS A 116    11837   7511   6093    419   -566    212       C  
ATOM    703  CE1 HIS A 116      40.053 -19.139 115.054  1.00 68.53           C  
ANISOU  703  CE1 HIS A 116    11916   7945   6176    577   -746    336       C  
ATOM    704  NE2 HIS A 116      39.378 -18.625 114.030  1.00 67.32           N  
ANISOU  704  NE2 HIS A 116    11715   7728   6137    517   -651    278       N  
ATOM    705  N   HIS A 117      36.209 -20.986 117.152  1.00 68.14           N  
ANISOU  705  N   HIS A 117    12579   7267   6042    589   -367    236       N  
ATOM    706  CA  HIS A 117      36.298 -22.426 116.892  1.00 69.53           C  
ANISOU  706  CA  HIS A 117    12826   7395   6199    722   -348    278       C  
ATOM    707  C   HIS A 117      34.966 -22.985 116.394  1.00 71.19           C  
ANISOU  707  C   HIS A 117    13111   7465   6472    666   -199    249       C  
ATOM    708  O   HIS A 117      34.979 -23.765 115.445  1.00 70.64           O  
ANISOU  708  O   HIS A 117    13032   7368   6438    724   -178    258       O  
ATOM    709  CB  HIS A 117      36.765 -23.186 118.147  1.00 73.17           C  
ANISOU  709  CB  HIS A 117    13476   7823   6504    806   -408    334       C  
ATOM    710  CG  HIS A 117      37.287 -24.574 117.886  1.00 78.75           C  
ANISOU  710  CG  HIS A 117    14265   8498   7158    996   -422    397       C  
ATOM    711  ND1 HIS A 117      36.511 -25.545 117.257  1.00 80.82           N  
ANISOU  711  ND1 HIS A 117    14659   8603   7445   1011   -301    383       N  
ATOM    712  CD2 HIS A 117      38.466 -25.133 118.248  1.00 82.82           C  
ANISOU  712  CD2 HIS A 117    14779   9111   7577   1181   -537    482       C  
ATOM    713  CE1 HIS A 117      37.258 -26.639 117.220  1.00 81.78           C  
ANISOU  713  CE1 HIS A 117    14894   8699   7480   1214   -334    449       C  
ATOM    714  NE2 HIS A 117      38.442 -26.442 117.804  1.00 83.32           N  
ANISOU  714  NE2 HIS A 117    14997   9055   7606   1346   -470    516       N  
ATOM    715  N   ILE A 118      33.828 -22.594 117.018  1.00 66.73           N  
ANISOU  715  N   ILE A 118    12622   6825   5908    548    -92    222       N  
ATOM    716  CA  ILE A 118      32.491 -23.036 116.598  1.00 66.22           C  
ANISOU  716  CA  ILE A 118    12578   6682   5901    458     44    214       C  
ATOM    717  C   ILE A 118      32.208 -22.560 115.175  1.00 69.41           C  
ANISOU  717  C   ILE A 118    12777   7154   6443    423     48    189       C  
ATOM    718  O   ILE A 118      31.790 -23.359 114.341  1.00 68.82           O  
ANISOU  718  O   ILE A 118    12709   7040   6398    392     75    196       O  
ATOM    719  CB  ILE A 118      31.385 -22.614 117.610  1.00 69.81           C  
ANISOU  719  CB  ILE A 118    13111   7091   6323    365    172    210       C  
ATOM    720  CG1 ILE A 118      31.379 -23.530 118.854  1.00 72.05           C  
ANISOU  720  CG1 ILE A 118    13648   7270   6457    374    199    244       C  
ATOM    721  CG2 ILE A 118      29.983 -22.524 116.970  1.00 69.95           C  
ANISOU  721  CG2 ILE A 118    13010   7126   6441    258    302    215       C  
ATOM    722  CD1 ILE A 118      30.982 -25.056 118.630  1.00 84.05           C  
ANISOU  722  CD1 ILE A 118    15322   8682   7932    342    244    280       C  
ATOM    723  N   CYS A 119      32.493 -21.271 114.900  1.00 65.74           N  
ANISOU  723  N   CYS A 119    12164   6776   6039    417     14    162       N  
ATOM    724  CA  CYS A 119      32.317 -20.617 113.604  1.00 64.44           C  
ANISOU  724  CA  CYS A 119    11814   6677   5992    392     10    143       C  
ATOM    725  C   CYS A 119      33.085 -21.296 112.490  1.00 66.99           C  
ANISOU  725  C   CYS A 119    12083   7029   6339    453    -58    149       C  
ATOM    726  O   CYS A 119      32.556 -21.405 111.388  1.00 66.26           O  
ANISOU  726  O   CYS A 119    11916   6941   6319    411    -32    142       O  
ATOM    727  CB  CYS A 119      32.656 -19.137 113.702  1.00 64.63           C  
ANISOU  727  CB  CYS A 119    11765   6757   6037    378    -18    117       C  
ATOM    728  SG  CYS A 119      31.524 -18.199 114.756  1.00 69.20           S  
ANISOU  728  SG  CYS A 119    12436   7274   6584    341    114    106       S  
ATOM    729  N   CYS A 120      34.303 -21.790 112.780  1.00 63.90           N  
ANISOU  729  N   CYS A 120    11737   6666   5877    563   -141    173       N  
ATOM    730  CA  CYS A 120      35.127 -22.517 111.815  1.00 64.23           C  
ANISOU  730  CA  CYS A 120    11750   6737   5919    675   -178    192       C  
ATOM    731  C   CYS A 120      34.527 -23.880 111.504  1.00 69.60           C  
ANISOU  731  C   CYS A 120    12617   7274   6554    686   -113    199       C  
ATOM    732  O   CYS A 120      34.431 -24.239 110.329  1.00 69.20           O  
ANISOU  732  O   CYS A 120    12561   7200   6533    689    -94    188       O  
ATOM    733  CB  CYS A 120      36.567 -22.635 112.297  1.00 65.52           C  
ANISOU  733  CB  CYS A 120    11876   7008   6010    817   -276    239       C  
ATOM    734  SG  CYS A 120      37.414 -21.046 112.462  1.00 69.36           S  
ANISOU  734  SG  CYS A 120    12149   7677   6526    739   -376    237       S  
ATOM    735  N   LEU A 121      34.093 -24.622 112.555  1.00 67.36           N  
ANISOU  735  N   LEU A 121    12529   6881   6182    669    -77    218       N  
ATOM    736  CA  LEU A 121      33.447 -25.937 112.441  1.00 68.10           C  
ANISOU  736  CA  LEU A 121    12860   6811   6204    631    -12    228       C  
ATOM    737  C   LEU A 121      32.186 -25.842 111.578  1.00 71.00           C  
ANISOU  737  C   LEU A 121    13171   7160   6647    434     45    202       C  
ATOM    738  O   LEU A 121      31.919 -26.746 110.788  1.00 71.59           O  
ANISOU  738  O   LEU A 121    13380   7138   6682    391     62    200       O  
ATOM    739  CB  LEU A 121      33.064 -26.505 113.824  1.00 69.30           C  
ANISOU  739  CB  LEU A 121    13220   6861   6250    601     27    256       C  
ATOM    740  CG  LEU A 121      34.172 -26.857 114.814  1.00 75.43           C  
ANISOU  740  CG  LEU A 121    14102   7643   6917    786    -40    299       C  
ATOM    741  CD1 LEU A 121      33.582 -27.424 116.093  1.00 76.59           C  
ANISOU  741  CD1 LEU A 121    14495   7659   6947    728     14    324       C  
ATOM    742  CD2 LEU A 121      35.170 -27.846 114.222  1.00 80.40           C  
ANISOU  742  CD2 LEU A 121    14821   8247   7480   1011    -81    337       C  
ATOM    743  N   VAL A 122      31.423 -24.740 111.742  1.00 65.70           N  
ANISOU  743  N   VAL A 122    12310   6584   6068    322     71    190       N  
ATOM    744  CA  VAL A 122      30.201 -24.430 111.007  1.00 64.86           C  
ANISOU  744  CA  VAL A 122    12077   6522   6043    155    114    189       C  
ATOM    745  C   VAL A 122      30.576 -24.179 109.555  1.00 68.99           C  
ANISOU  745  C   VAL A 122    12494   7091   6627    181     57    167       C  
ATOM    746  O   VAL A 122      29.920 -24.717 108.665  1.00 69.68           O  
ANISOU  746  O   VAL A 122    12616   7148   6710     60     59    170       O  
ATOM    747  CB  VAL A 122      29.454 -23.240 111.664  1.00 68.03           C  
ANISOU  747  CB  VAL A 122    12313   7022   6514    115    170    196       C  
ATOM    748  CG1 VAL A 122      28.398 -22.636 110.743  1.00 67.38           C  
ANISOU  748  CG1 VAL A 122    12028   7041   6534     12    195    211       C  
ATOM    749  CG2 VAL A 122      28.830 -23.659 112.990  1.00 68.87           C  
ANISOU  749  CG2 VAL A 122    12547   7076   6546     59    259    224       C  
ATOM    750  N   GLU A 123      31.667 -23.423 109.322  1.00 64.86           N  
ANISOU  750  N   GLU A 123    11861   6642   6139    319      2    149       N  
ATOM    751  CA  GLU A 123      32.184 -23.117 107.985  1.00 64.30           C  
ANISOU  751  CA  GLU A 123    11692   6625   6116    359    -40    132       C  
ATOM    752  C   GLU A 123      32.602 -24.403 107.258  1.00 70.05           C  
ANISOU  752  C   GLU A 123    12611   7247   6758    414    -39    132       C  
ATOM    753  O   GLU A 123      32.304 -24.559 106.078  1.00 69.76           O  
ANISOU  753  O   GLU A 123    12581   7193   6730    350    -44    118       O  
ATOM    754  CB  GLU A 123      33.332 -22.094 108.081  1.00 65.05           C  
ANISOU  754  CB  GLU A 123    11643   6830   6243    471    -90    127       C  
ATOM    755  CG  GLU A 123      34.137 -21.867 106.810  1.00 74.88           C  
ANISOU  755  CG  GLU A 123    12796   8140   7516    534   -121    120       C  
ATOM    756  CD  GLU A 123      35.380 -22.726 106.655  1.00 93.24           C  
ANISOU  756  CD  GLU A 123    15192  10470   9764    710   -131    144       C  
ATOM    757  OE1 GLU A 123      36.065 -22.999 107.671  1.00 74.75           O  
ANISOU  757  OE1 GLU A 123    12882   8154   7367    812   -156    175       O  
ATOM    758  OE2 GLU A 123      35.693 -23.089 105.498  1.00 88.26           O  
ANISOU  758  OE2 GLU A 123    14587   9827   9121    761   -112    139       O  
ATOM    759  N   ARG A 124      33.264 -25.330 107.964  1.00 68.16           N  
ANISOU  759  N   ARG A 124    12559   6922   6416    539    -29    151       N  
ATOM    760  CA  ARG A 124      33.671 -26.592 107.356  1.00 69.44           C  
ANISOU  760  CA  ARG A 124    12970   6947   6467    633     -5    155       C  
ATOM    761  C   ARG A 124      32.472 -27.511 107.127  1.00 76.14           C  
ANISOU  761  C   ARG A 124    14048   7636   7247    426     31    146       C  
ATOM    762  O   ARG A 124      32.463 -28.259 106.152  1.00 76.29           O  
ANISOU  762  O   ARG A 124    14264   7537   7185    414     45    132       O  
ATOM    763  CB  ARG A 124      34.798 -27.274 108.153  1.00 69.81           C  
ANISOU  763  CB  ARG A 124    13150   6961   6415    872     -5    196       C  
ATOM    764  CG  ARG A 124      36.147 -26.533 108.123  1.00 78.82           C  
ANISOU  764  CG  ARG A 124    14058   8291   7597   1072    -53    225       C  
ATOM    765  CD  ARG A 124      36.912 -26.698 106.813  1.00 90.61           C  
ANISOU  765  CD  ARG A 124    15532   9817   9080   1214    -24    228       C  
ATOM    766  NE  ARG A 124      36.442 -25.775 105.774  1.00 94.81           N  
ANISOU  766  NE  ARG A 124    15884  10422   9717   1058    -34    184       N  
ATOM    767  CZ  ARG A 124      36.499 -26.017 104.468  1.00106.01           C  
ANISOU  767  CZ  ARG A 124    17350  11810  11118   1085      4    166       C  
ATOM    768  NH1 ARG A 124      36.041 -25.122 103.603  1.00 90.17           N  
ANISOU  768  NH1 ARG A 124    15186   9874   9201    938    -17    134       N  
ATOM    769  NH2 ARG A 124      37.007 -27.157 104.016  1.00 94.39           N  
ANISOU  769  NH2 ARG A 124    16117  10223   9523   1272     69    183       N  
ATOM    770  N   ALA A 125      31.441 -27.413 107.991  1.00 74.94           N  
ANISOU  770  N   ALA A 125    13875   7486   7115    248     49    160       N  
ATOM    771  CA  ALA A 125      30.208 -28.204 107.884  1.00 77.04           C  
ANISOU  771  CA  ALA A 125    14308   7647   7316     -6     78    169       C  
ATOM    772  C   ALA A 125      29.359 -27.753 106.695  1.00 83.74           C  
ANISOU  772  C   ALA A 125    14999   8583   8234   -199     43    161       C  
ATOM    773  O   ALA A 125      28.641 -28.565 106.107  1.00 84.80           O  
ANISOU  773  O   ALA A 125    15313   8625   8283   -406     34    166       O  
ATOM    774  CB  ALA A 125      29.402 -28.105 109.170  1.00 77.96           C  
ANISOU  774  CB  ALA A 125    14393   7789   7439   -124    125    202       C  
ATOM    775  N   THR A 126      29.448 -26.460 106.347  1.00 81.15           N  
ANISOU  775  N   THR A 126    14358   8431   8044   -143     13    154       N  
ATOM    776  CA  THR A 126      28.717 -25.858 105.234  1.00 81.89           C  
ANISOU  776  CA  THR A 126    14272   8633   8209   -282    -31    158       C  
ATOM    777  C   THR A 126      29.677 -25.578 104.050  1.00 89.69           C  
ANISOU  777  C   THR A 126    15257   9619   9202   -145    -70    121       C  
ATOM    778  O   THR A 126      29.397 -24.715 103.216  1.00 88.44           O  
ANISOU  778  O   THR A 126    14915   9569   9118   -194   -111    123       O  
ATOM    779  CB  THR A 126      27.898 -24.636 105.730  1.00 83.19           C  
ANISOU  779  CB  THR A 126    14126   8980   8504   -321    -16    192       C  
ATOM    780  OG1 THR A 126      28.746 -23.729 106.443  1.00 76.36           O  
ANISOU  780  OG1 THR A 126    13166   8154   7693   -122      4    173       O  
ATOM    781  CG2 THR A 126      26.725 -25.036 106.615  1.00 82.12           C  
ANISOU  781  CG2 THR A 126    13976   8875   8352   -503     38    245       C  
ATOM    782  N   SER A 127      30.777 -26.368 103.949  1.00 90.42           N  
ANISOU  782  N   SER A 127    15567   9589   9200     33    -47     99       N  
ATOM    783  CA  SER A 127      31.816 -26.256 102.913  1.00 91.83           C  
ANISOU  783  CA  SER A 127    15764   9767   9360    197    -50     76       C  
ATOM    784  C   SER A 127      31.324 -26.486 101.471  1.00100.38           C  
ANISOU  784  C   SER A 127    16938  10806  10396     53    -81     56       C  
ATOM    785  O   SER A 127      32.117 -26.402 100.530  1.00100.02           O  
ANISOU  785  O   SER A 127    16921  10757  10323    179    -69     37       O  
ATOM    786  CB  SER A 127      32.990 -27.178 103.226  1.00 96.47           C  
ANISOU  786  CB  SER A 127    16583  10238   9835    437      3     79       C  
ATOM    787  OG  SER A 127      34.118 -26.832 102.441  1.00105.60           O  
ANISOU  787  OG  SER A 127    17646  11474  11004    645     19     77       O  
ATOM    788  N   SER A 128      30.025 -26.765 101.301  1.00100.64           N  
ANISOU  788  N   SER A 128    17002  10827  10410   -221   -124     70       N  
ATOM    789  CA  SER A 128      29.387 -26.960 100.006  1.00102.61           C  
ANISOU  789  CA  SER A 128    17322  11062  10604   -419   -187     64       C  
ATOM    790  C   SER A 128      28.715 -25.624  99.659  1.00108.84           C  
ANISOU  790  C   SER A 128    17738  12071  11545   -478   -246     95       C  
ATOM    791  O   SER A 128      27.564 -25.386 100.047  1.00108.61           O  
ANISOU  791  O   SER A 128    17526  12157  11582   -632   -271    144       O  
ATOM    792  CB  SER A 128      28.366 -28.088 100.089  1.00108.18           C  
ANISOU  792  CB  SER A 128    18247  11664  11192   -716   -217     84       C  
ATOM    793  OG  SER A 128      28.804 -29.153 100.917  1.00119.07           O  
ANISOU  793  OG  SER A 128    19956  12840  12446   -662   -149     71       O  
ATOM    794  N   GLN A 129      29.486 -24.734  98.972  1.00107.19           N  
ANISOU  794  N   GLN A 129    17422  11922  11384   -334   -252     76       N  
ATOM    795  CA  GLN A 129      29.182 -23.350  98.551  1.00107.15           C  
ANISOU  795  CA  GLN A 129    17117  12090  11504   -328   -295    102       C  
ATOM    796  C   GLN A 129      27.691 -22.953  98.627  1.00115.20           C  
ANISOU  796  C   GLN A 129    17945  13243  12582   -529   -359    165       C  
ATOM    797  O   GLN A 129      27.372 -22.031  99.372  1.00114.11           O  
ANISOU  797  O   GLN A 129    17576  13224  12558   -466   -334    199       O  
ATOM    798  CB  GLN A 129      29.751 -23.044  97.148  1.00108.16           C  
ANISOU  798  CB  GLN A 129    17289  12212  11595   -277   -318     79       C  
ATOM    799  CG  GLN A 129      30.195 -21.589  96.964  1.00113.06           C  
ANISOU  799  CG  GLN A 129    17663  12962  12334   -153   -314     90       C  
ATOM    800  CD  GLN A 129      31.664 -21.371  97.244  1.00122.19           C  
ANISOU  800  CD  GLN A 129    18820  14107  13498     57   -238     62       C  
ATOM    801  OE1 GLN A 129      32.480 -21.239  96.329  1.00116.12           O  
ANISOU  801  OE1 GLN A 129    18081  13343  12696    139   -215     48       O  
ATOM    802  NE2 GLN A 129      32.031 -21.288  98.514  1.00110.50           N  
ANISOU  802  NE2 GLN A 129    17291  12636  12057    142   -200     63       N  
ATOM    803  N   SER A 130      26.789 -23.642  97.882  1.00116.00           N  
ANISOU  803  N   SER A 130    18149  13334  12592   -770   -437    190       N  
ATOM    804  CA  SER A 130      25.347 -23.342  97.868  1.00117.95           C  
ANISOU  804  CA  SER A 130    18176  13759  12880   -978   -510    277       C  
ATOM    805  C   SER A 130      24.482 -24.566  97.479  1.00126.34           C  
ANISOU  805  C   SER A 130    19427  14778  13800  -1302   -589    302       C  
ATOM    806  O   SER A 130      23.539 -24.428  96.691  1.00127.75           O  
ANISOU  806  O   SER A 130    19496  15092  13952  -1507   -706    365       O  
ATOM    807  CB  SER A 130      25.058 -22.148  96.950  1.00121.16           C  
ANISOU  807  CB  SER A 130    18351  14324  13361   -933   -579    321       C  
ATOM    808  OG  SER A 130      23.707 -21.722  97.021  1.00130.38           O  
ANISOU  808  OG  SER A 130    19247  15708  14584  -1067   -638    429       O  
ATOM    809  N   LEU A 131      24.797 -25.761  98.028  1.00124.42           N  
ANISOU  809  N   LEU A 131    19483  14345  13448  -1362   -534    260       N  
ATOM    810  CA  LEU A 131      24.005 -26.956  97.714  1.00126.98           C  
ANISOU  810  CA  LEU A 131    20045  14595  13608  -1709   -606    281       C  
ATOM    811  C   LEU A 131      23.258 -27.515  98.936  1.00131.83           C  
ANISOU  811  C   LEU A 131    20628  15240  14220  -1872   -557    333       C  
ATOM    812  O   LEU A 131      22.301 -28.277  98.758  1.00134.06           O  
ANISOU  812  O   LEU A 131    20993  15549  14394  -2226   -631    386       O  
ATOM    813  CB  LEU A 131      24.810 -28.053  96.976  1.00128.08           C  
ANISOU  813  CB  LEU A 131    20679  14439  13546  -1721   -599    195       C  
ATOM    814  CG  LEU A 131      25.998 -28.699  97.681  1.00132.30           C  
ANISOU  814  CG  LEU A 131    21500  14738  14029  -1459   -463    125       C  
ATOM    815  CD1 LEU A 131      25.595 -30.003  98.383  1.00134.25           C  
ANISOU  815  CD1 LEU A 131    22077  14806  14127  -1662   -433    130       C  
ATOM    816  CD2 LEU A 131      27.116 -28.971  96.691  1.00135.01           C  
ANISOU  816  CD2 LEU A 131    22131  14903  14265  -1258   -425     52       C  
ATOM    817  N   ASN A 132      23.669 -27.131 100.159  1.00126.21           N  
ANISOU  817  N   ASN A 132    19809  14530  13613  -1641   -438    324       N  
ATOM    818  CA  ASN A 132      22.997 -27.595 101.372  1.00126.67           C  
ANISOU  818  CA  ASN A 132    19840  14621  13667  -1777   -374    377       C  
ATOM    819  C   ASN A 132      21.884 -26.630 101.823  1.00129.00           C  
ANISOU  819  C   ASN A 132    19674  15229  14109  -1820   -365    483       C  
ATOM    820  O   ASN A 132      22.084 -25.417 101.744  1.00126.76           O  
ANISOU  820  O   ASN A 132    19130  15071  13963  -1581   -348    488       O  
ATOM    821  CB  ASN A 132      23.990 -27.919 102.509  1.00127.57           C  
ANISOU  821  CB  ASN A 132    20157  14546  13766  -1542   -252    319       C  
ATOM    822  CG  ASN A 132      25.043 -26.873 102.797  1.00149.12           C  
ANISOU  822  CG  ASN A 132    22737  17300  16621  -1173   -200    274       C  
ATOM    823  OD1 ASN A 132      26.229 -27.053 102.500  1.00142.63           O  
ANISOU  823  OD1 ASN A 132    22110  16327  15756   -967   -184    208       O  
ATOM    824  ND2 ASN A 132      24.655 -25.801 103.461  1.00140.33           N  
ANISOU  824  ND2 ASN A 132    21295  16374  15649  -1082   -160    317       N  
ATOM    825  N   PRO A 133      20.702 -27.132 102.279  1.00126.66           N  
ANISOU  825  N   PRO A 133    19278  15070  13777  -2117   -367    578       N  
ATOM    826  CA  PRO A 133      19.635 -26.215 102.727  1.00126.41           C  
ANISOU  826  CA  PRO A 133    18785  15363  13881  -2110   -330    699       C  
ATOM    827  C   PRO A 133      19.925 -25.604 104.100  1.00126.29           C  
ANISOU  827  C   PRO A 133    18675  15346  13963  -1837   -162    689       C  
ATOM    828  O   PRO A 133      19.164 -24.758 104.578  1.00126.12           O  
ANISOU  828  O   PRO A 133    18312  15562  14047  -1758    -90    781       O  
ATOM    829  CB  PRO A 133      18.372 -27.094 102.729  1.00131.53           C  
ANISOU  829  CB  PRO A 133    19374  16166  14435  -2547   -384    811       C  
ATOM    830  CG  PRO A 133      18.800 -28.449 102.208  1.00137.28           C  
ANISOU  830  CG  PRO A 133    20593  16604  14962  -2801   -458    733       C  
ATOM    831  CD  PRO A 133      20.277 -28.536 102.430  1.00130.53           C  
ANISOU  831  CD  PRO A 133    20073  15431  14091  -2471   -388    592       C  
ATOM    832  N   VAL A 134      21.044 -26.029 104.719  1.00119.52           N  
ANISOU  832  N   VAL A 134    18133  14223  13056  -1678    -99    585       N  
ATOM    833  CA  VAL A 134      21.563 -25.545 105.999  1.00117.10           C  
ANISOU  833  CA  VAL A 134    17821  13866  12806  -1425     35    557       C  
ATOM    834  C   VAL A 134      21.977 -24.088 105.781  1.00116.17           C  
ANISOU  834  C   VAL A 134    17476  13841  12822  -1131     44    539       C  
ATOM    835  O   VAL A 134      21.660 -23.228 106.601  1.00115.66           O  
ANISOU  835  O   VAL A 134    17230  13882  12832   -984    147    575       O  
ATOM    836  CB  VAL A 134      22.768 -26.402 106.482  1.00120.38           C  
ANISOU  836  CB  VAL A 134    18634  13987  13117  -1324     58    460       C  
ATOM    837  CG1 VAL A 134      23.067 -26.149 107.955  1.00119.62           C  
ANISOU  837  CG1 VAL A 134    18552  13858  13041  -1152    180    454       C  
ATOM    838  CG2 VAL A 134      22.540 -27.889 106.228  1.00122.09           C  
ANISOU  838  CG2 VAL A 134    19181  14040  13166  -1605     21    460       C  
ATOM    839  N   TRP A 135      22.634 -23.823 104.633  1.00109.33           N  
ANISOU  839  N   TRP A 135    16650  12925  11966  -1061    -57    486       N  
ATOM    840  CA  TRP A 135      23.109 -22.528 104.148  1.00106.75           C  
ANISOU  840  CA  TRP A 135    16167  12654  11738   -830    -73    464       C  
ATOM    841  C   TRP A 135      21.978 -21.512 104.108  1.00108.90           C  
ANISOU  841  C   TRP A 135    16099  13172  12106   -805    -49    568       C  
ATOM    842  O   TRP A 135      22.200 -20.336 104.385  1.00107.56           O  
ANISOU  842  O   TRP A 135    15818  13036  12012   -578      5    565       O  
ATOM    843  CB  TRP A 135      23.657 -22.702 102.726  1.00105.23           C  
ANISOU  843  CB  TRP A 135    16083  12394  11507   -861   -191    417       C  
ATOM    844  CG  TRP A 135      24.479 -21.557 102.230  1.00104.60           C  
ANISOU  844  CG  TRP A 135    15929  12315  11500   -635   -203    377       C  
ATOM    845  CD1 TRP A 135      24.034 -20.444 101.578  1.00107.57           C  
ANISOU  845  CD1 TRP A 135    16085  12836  11952   -573   -236    426       C  
ATOM    846  CD2 TRP A 135      25.902 -21.448 102.289  1.00102.90           C  
ANISOU  846  CD2 TRP A 135    15870  11956  11271   -458   -186    290       C  
ATOM    847  NE1 TRP A 135      25.095 -19.632 101.253  1.00105.52           N  
ANISOU  847  NE1 TRP A 135    15864  12507  11723   -388   -235    367       N  
ATOM    848  CE2 TRP A 135      26.254 -20.222 101.683  1.00105.99           C  
ANISOU  848  CE2 TRP A 135    16130  12409  11733   -326   -207    286       C  
ATOM    849  CE3 TRP A 135      26.919 -22.265 102.808  1.00103.58           C  
ANISOU  849  CE3 TRP A 135    16186  11883  11286   -391   -156    229       C  
ATOM    850  CZ2 TRP A 135      27.580 -19.797 101.579  1.00104.04           C  
ANISOU  850  CZ2 TRP A 135    15957  12085  11488   -171   -199    224       C  
ATOM    851  CZ3 TRP A 135      28.231 -21.844 102.698  1.00103.86           C  
ANISOU  851  CZ3 TRP A 135    16264  11867  11331   -205   -152    177       C  
ATOM    852  CH2 TRP A 135      28.552 -20.625 102.091  1.00103.70           C  
ANISOU  852  CH2 TRP A 135    16092  11926  11382   -116   -174    174       C  
ATOM    853  N   ASP A 136      20.773 -21.970 103.736  1.00105.65           N  
ANISOU  853  N   ASP A 136    15533  12936  11675  -1042    -94    669       N  
ATOM    854  CA  ASP A 136      19.572 -21.152 103.622  1.00106.11           C  
ANISOU  854  CA  ASP A 136    15226  13280  11811  -1022    -77    802       C  
ATOM    855  C   ASP A 136      19.083 -20.694 104.993  1.00106.98           C  
ANISOU  855  C   ASP A 136    15204  13475  11969   -881    104    856       C  
ATOM    856  O   ASP A 136      18.750 -19.520 105.153  1.00106.78           O  
ANISOU  856  O   ASP A 136    14987  13565  12021   -644    181    908       O  
ATOM    857  CB  ASP A 136      18.468 -21.915 102.865  1.00110.89           C  
ANISOU  857  CB  ASP A 136    15695  14077  12361  -1362   -195    908       C  
ATOM    858  CG  ASP A 136      18.919 -22.639 101.601  1.00125.56           C  
ANISOU  858  CG  ASP A 136    17783  15802  14120  -1558   -366    844       C  
ATOM    859  OD1 ASP A 136      19.998 -22.290 101.059  1.00125.00           O  
ANISOU  859  OD1 ASP A 136    17888  15553  14054  -1380   -395    739       O  
ATOM    860  OD2 ASP A 136      18.191 -23.549 101.149  1.00135.10           O  
ANISOU  860  OD2 ASP A 136    19009  17090  15235  -1901   -466    902       O  
ATOM    861  N   ALA A 137      19.072 -21.609 105.984  1.00101.01           N  
ANISOU  861  N   ALA A 137    14595  12636  11148  -1011    183    842       N  
ATOM    862  CA  ALA A 137      18.654 -21.327 107.359  1.00100.07           C  
ANISOU  862  CA  ALA A 137    14409  12570  11043   -903    368    885       C  
ATOM    863  C   ALA A 137      19.706 -20.499 108.111  1.00 98.84           C  
ANISOU  863  C   ALA A 137    14425  12224  10907   -597    454    782       C  
ATOM    864  O   ALA A 137      19.361 -19.747 109.028  1.00 98.74           O  
ANISOU  864  O   ALA A 137    14331  12268  10917   -420    609    821       O  
ATOM    865  CB  ALA A 137      18.392 -22.631 108.094  1.00101.97           C  
ANISOU  865  CB  ALA A 137    14808  12752  11186  -1164    409    896       C  
ATOM    866  N   LEU A 138      20.981 -20.639 107.707  1.00 91.40           N  
ANISOU  866  N   LEU A 138    13724  11063   9940   -546    356    659       N  
ATOM    867  CA  LEU A 138      22.147 -19.968 108.282  1.00 88.76           C  
ANISOU  867  CA  LEU A 138    13563  10558   9605   -320    390    561       C  
ATOM    868  C   LEU A 138      22.278 -18.502 107.873  1.00 91.06           C  
ANISOU  868  C   LEU A 138    13736  10894   9968   -105    396    562       C  
ATOM    869  O   LEU A 138      22.655 -17.679 108.703  1.00 89.97           O  
ANISOU  869  O   LEU A 138    13677  10685   9824     71    485    530       O  
ATOM    870  CB  LEU A 138      23.414 -20.738 107.891  1.00 87.41           C  
ANISOU  870  CB  LEU A 138    13644  10191   9376   -358    279    459       C  
ATOM    871  CG  LEU A 138      24.415 -21.067 108.995  1.00 91.58           C  
ANISOU  871  CG  LEU A 138    14412  10548   9836   -276    316    390       C  
ATOM    872  CD1 LEU A 138      23.769 -21.867 110.143  1.00 93.19           C  
ANISOU  872  CD1 LEU A 138    14696  10742   9973   -384    417    432       C  
ATOM    873  CD2 LEU A 138      25.582 -21.841 108.427  1.00 93.04           C  
ANISOU  873  CD2 LEU A 138    14796  10589   9966   -280    210    319       C  
ATOM    874  N   ARG A 139      21.998 -18.184 106.594  1.00 87.49           N  
ANISOU  874  N   ARG A 139    13138  10542   9563   -130    298    598       N  
ATOM    875  CA  ARG A 139      22.072 -16.825 106.054  1.00 86.88           C  
ANISOU  875  CA  ARG A 139    12973  10496   9540     64    296    609       C  
ATOM    876  C   ARG A 139      21.062 -15.891 106.725  1.00 91.68           C  
ANISOU  876  C   ARG A 139    13420  11235  10179    241    450    706       C  
ATOM    877  O   ARG A 139      21.421 -14.763 107.065  1.00 91.54           O  
ANISOU  877  O   ARG A 139    13490  11130  10160    450    521    678       O  
ATOM    878  CB  ARG A 139      21.896 -16.817 104.524  1.00 88.28           C  
ANISOU  878  CB  ARG A 139    13038  10761   9743    -17    153    641       C  
ATOM    879  CG  ARG A 139      23.167 -17.195 103.758  1.00100.08           C  
ANISOU  879  CG  ARG A 139    14731  12091  11203    -73     37    533       C  
ATOM    880  CD  ARG A 139      23.047 -16.975 102.257  1.00111.59           C  
ANISOU  880  CD  ARG A 139    16112  13615  12670   -120    -87    560       C  
ATOM    881  NE  ARG A 139      23.302 -15.583 101.880  1.00121.48           N  
ANISOU  881  NE  ARG A 139    17332  14862  13963     75    -74    564       N  
ATOM    882  CZ  ARG A 139      23.375 -15.142 100.628  1.00138.56           C  
ANISOU  882  CZ  ARG A 139    19462  17056  16128     79   -169    582       C  
ATOM    883  NH1 ARG A 139      23.214 -15.979  99.610  1.00131.57           N  
ANISOU  883  NH1 ARG A 139    18573  16215  15205   -102   -289    593       N  
ATOM    884  NH2 ARG A 139      23.612 -13.860 100.383  1.00122.75           N  
ANISOU  884  NH2 ARG A 139    17470  15023  14148    255   -143    589       N  
ATOM    885  N   ASP A 140      19.816 -16.371 106.934  1.00 88.84           N  
ANISOU  885  N   ASP A 140    12840  11083   9831    152    510    825       N  
ATOM    886  CA  ASP A 140      18.719 -15.632 107.567  1.00 90.05           C  
ANISOU  886  CA  ASP A 140    12794  11412  10009    331    683    947       C  
ATOM    887  C   ASP A 140      19.123 -15.092 108.934  1.00 91.16           C  
ANISOU  887  C   ASP A 140    13148  11387  10100    520    858    886       C  
ATOM    888  O   ASP A 140      19.662 -15.836 109.757  1.00 89.98           O  
ANISOU  888  O   ASP A 140    13195  11098   9895    412    874    807       O  
ATOM    889  CB  ASP A 140      17.465 -16.522 107.670  1.00 94.60           C  
ANISOU  889  CB  ASP A 140    13107  12248  10589    128    713   1081       C  
ATOM    890  CG  ASP A 140      16.390 -16.028 108.623  1.00110.66           C  
ANISOU  890  CG  ASP A 140    14939  14476  12631    299    936   1212       C  
ATOM    891  OD1 ASP A 140      16.476 -16.346 109.830  1.00111.56           O  
ANISOU  891  OD1 ASP A 140    15196  14498  12692    302   1081   1179       O  
ATOM    892  OD2 ASP A 140      15.446 -15.353 108.156  1.00120.18           O  
ANISOU  892  OD2 ASP A 140    15840  15937  13886    438    971   1359       O  
ATOM    893  N   GLY A 141      18.854 -13.807 109.148  1.00 87.00           N  
ANISOU  893  N   GLY A 141    12609  10868   9578    804    983    928       N  
ATOM    894  CA  GLY A 141      19.159 -13.112 110.394  1.00 86.45           C  
ANISOU  894  CA  GLY A 141    12781  10630   9435    998   1158    877       C  
ATOM    895  C   GLY A 141      20.558 -12.536 110.485  1.00 86.83           C  
ANISOU  895  C   GLY A 141    13166  10395   9430   1027   1080    725       C  
ATOM    896  O   GLY A 141      20.937 -11.995 111.531  1.00 86.23           O  
ANISOU  896  O   GLY A 141    13342  10154   9266   1137   1193    668       O  
ATOM    897  N   ILE A 142      21.328 -12.645 109.385  1.00 80.93           N  
ANISOU  897  N   ILE A 142    12427   9602   8721    915    887    668       N  
ATOM    898  CA  ILE A 142      22.702 -12.158 109.280  1.00 78.48           C  
ANISOU  898  CA  ILE A 142    12374   9076   8368    901    790    543       C  
ATOM    899  C   ILE A 142      22.867 -11.213 108.077  1.00 81.49           C  
ANISOU  899  C   ILE A 142    12728   9451   8784    985    713    555       C  
ATOM    900  O   ILE A 142      22.173 -11.367 107.067  1.00 81.12           O  
ANISOU  900  O   ILE A 142    12452   9565   8804    971    653    637       O  
ATOM    901  CB  ILE A 142      23.704 -13.363 109.292  1.00 79.49           C  
ANISOU  901  CB  ILE A 142    12581   9139   8484    680    650    455       C  
ATOM    902  CG1 ILE A 142      24.688 -13.252 110.463  1.00 79.57           C  
ANISOU  902  CG1 ILE A 142    12860   8974   8398    680    672    364       C  
ATOM    903  CG2 ILE A 142      24.438 -13.568 107.968  1.00 78.09           C  
ANISOU  903  CG2 ILE A 142    12366   8956   8347    581    477    417       C  
ATOM    904  CD1 ILE A 142      25.163 -14.580 111.053  1.00 88.14           C  
ANISOU  904  CD1 ILE A 142    14008  10034   9448    532    624    328       C  
ATOM    905  N   ILE A 143      23.770 -10.227 108.203  1.00 77.55           N  
ANISOU  905  N   ILE A 143    12478   8765   8222   1051    710    480       N  
ATOM    906  CA  ILE A 143      24.088  -9.308 107.115  1.00 77.20           C  
ANISOU  906  CA  ILE A 143    12469   8676   8188   1106    639    482       C  
ATOM    907  C   ILE A 143      25.199  -9.988 106.303  1.00 78.84           C  
ANISOU  907  C   ILE A 143    12668   8867   8420    897    458    407       C  
ATOM    908  O   ILE A 143      26.338 -10.095 106.771  1.00 77.49           O  
ANISOU  908  O   ILE A 143    12663   8583   8198    797    410    318       O  
ATOM    909  CB  ILE A 143      24.455  -7.877 107.610  1.00 81.31           C  
ANISOU  909  CB  ILE A 143    13296   8993   8606   1253    732    447       C  
ATOM    910  CG1 ILE A 143      23.249  -7.196 108.280  1.00 84.27           C  
ANISOU  910  CG1 ILE A 143    13688   9384   8945   1521    942    537       C  
ATOM    911  CG2 ILE A 143      25.001  -7.000 106.469  1.00 81.62           C  
ANISOU  911  CG2 ILE A 143    13420   8955   8638   1254    643    436       C  
ATOM    912  CD1 ILE A 143      23.620  -6.164 109.332  1.00 94.91           C  
ANISOU  912  CD1 ILE A 143    15423  10492  10147   1625   1069    477       C  
ATOM    913  N   SER A 144      24.830 -10.514 105.120  1.00 74.54           N  
ANISOU  913  N   SER A 144    11922   8455   7945    832    362    454       N  
ATOM    914  CA  SER A 144      25.732 -11.204 104.200  1.00 72.37           C  
ANISOU  914  CA  SER A 144    11638   8175   7684    666    215    398       C  
ATOM    915  C   SER A 144      26.447 -10.219 103.273  1.00 75.11           C  
ANISOU  915  C   SER A 144    12081   8446   8013    688    159    375       C  
ATOM    916  O   SER A 144      25.937  -9.120 103.053  1.00 75.34           O  
ANISOU  916  O   SER A 144    12144   8450   8030    831    213    427       O  
ATOM    917  CB  SER A 144      24.978 -12.267 103.407  1.00 75.70           C  
ANISOU  917  CB  SER A 144    11859   8751   8155    562    143    454       C  
ATOM    918  OG  SER A 144      23.951 -11.701 102.610  1.00 85.66           O  
ANISOU  918  OG  SER A 144    12958  10140   9450    650    142    560       O  
ATOM    919  N   SER A 145      27.638 -10.603 102.751  1.00 70.33           N  
ANISOU  919  N   SER A 145    11528   7800   7393    561     64    307       N  
ATOM    920  CA  SER A 145      28.472  -9.777 101.861  1.00 69.64           C  
ANISOU  920  CA  SER A 145    11529   7652   7279    538     13    285       C  
ATOM    921  C   SER A 145      27.677  -9.107 100.726  1.00 73.94           C  
ANISOU  921  C   SER A 145    12014   8238   7842    623     -2    360       C  
ATOM    922  O   SER A 145      27.809  -7.898 100.511  1.00 74.45           O  
ANISOU  922  O   SER A 145    12211   8211   7866    700     30    374       O  
ATOM    923  CB  SER A 145      29.663 -10.570 101.322  1.00 71.27           C  
ANISOU  923  CB  SER A 145    11725   7876   7478    405    -71    229       C  
ATOM    924  OG  SER A 145      29.289 -11.750 100.632  1.00 76.07           O  
ANISOU  924  OG  SER A 145    12219   8568   8116    356   -123    246       O  
ATOM    925  N   SER A 146      26.809  -9.886 100.055  1.00 69.44           N  
ANISOU  925  N   SER A 146    11267   7801   7317    601    -54    417       N  
ATOM    926  CA  SER A 146      25.932  -9.419  98.988  1.00 69.55           C  
ANISOU  926  CA  SER A 146    11185   7899   7344    674    -95    508       C  
ATOM    927  C   SER A 146      24.950  -8.390  99.538  1.00 74.35           C  
ANISOU  927  C   SER A 146    11780   8517   7953    889      9    594       C  
ATOM    928  O   SER A 146      24.901  -7.272  99.031  1.00 75.44           O  
ANISOU  928  O   SER A 146    12016   8590   8057   1012     23    633       O  
ATOM    929  CB  SER A 146      25.180 -10.593  98.375  1.00 73.39           C  
ANISOU  929  CB  SER A 146    11484   8542   7857    563   -182    555       C  
ATOM    930  OG  SER A 146      24.572 -11.390  99.379  1.00 83.47           O  
ANISOU  930  OG  SER A 146    12662   9891   9162    533   -131    570       O  
ATOM    931  N   LYS A 147      24.243  -8.737 100.630  1.00 70.70           N  
ANISOU  931  N   LYS A 147    11231   8118   7515    948    100    623       N  
ATOM    932  CA  LYS A 147      23.250  -7.891 101.291  1.00 71.98           C  
ANISOU  932  CA  LYS A 147    11370   8308   7671   1187    236    714       C  
ATOM    933  C   LYS A 147      23.827  -6.661 102.019  1.00 77.53           C  
ANISOU  933  C   LYS A 147    12378   8784   8295   1323    352    661       C  
ATOM    934  O   LYS A 147      23.045  -5.776 102.365  1.00 79.48           O  
ANISOU  934  O   LYS A 147    12670   9017   8512   1568    477    741       O  
ATOM    935  CB  LYS A 147      22.388  -8.730 102.249  1.00 74.36           C  
ANISOU  935  CB  LYS A 147    11489   8756   8011   1183    314    761       C  
ATOM    936  N   PHE A 148      25.170  -6.586 102.232  1.00 73.22           N  
ANISOU  936  N   PHE A 148    12049   8071   7702   1167    311    539       N  
ATOM    937  CA  PHE A 148      25.850  -5.502 102.966  1.00 73.70           C  
ANISOU  937  CA  PHE A 148    12434   7908   7660   1209    391    477       C  
ATOM    938  C   PHE A 148      25.579  -4.090 102.448  1.00 80.27           C  
ANISOU  938  C   PHE A 148    13461   8614   8422   1388    447    531       C  
ATOM    939  O   PHE A 148      25.356  -3.197 103.265  1.00 81.17           O  
ANISOU  939  O   PHE A 148    13821   8573   8447   1542    580    533       O  
ATOM    940  CB  PHE A 148      27.369  -5.727 103.073  1.00 73.98           C  
ANISOU  940  CB  PHE A 148    12600   7853   7658    967    298    363       C  
ATOM    941  CG  PHE A 148      28.081  -4.691 103.921  1.00 76.29           C  
ANISOU  941  CG  PHE A 148    13228   7934   7825    943    355    302       C  
ATOM    942  CD1 PHE A 148      28.034  -4.752 105.311  1.00 79.99           C  
ANISOU  942  CD1 PHE A 148    13823   8334   8235    965    439    266       C  
ATOM    943  CD2 PHE A 148      28.773  -3.641 103.329  1.00 78.73           C  
ANISOU  943  CD2 PHE A 148    13757   8105   8053    880    325    285       C  
ATOM    944  CE1 PHE A 148      28.672  -3.780 106.093  1.00 81.87           C  
ANISOU  944  CE1 PHE A 148    14416   8364   8329    913    479    209       C  
ATOM    945  CE2 PHE A 148      29.412  -2.672 104.111  1.00 82.68           C  
ANISOU  945  CE2 PHE A 148    14604   8398   8411    811    367    231       C  
ATOM    946  CZ  PHE A 148      29.358  -2.749 105.488  1.00 81.39           C  
ANISOU  946  CZ  PHE A 148    14576   8165   8183    825    437    192       C  
ATOM    947  N   HIS A 149      25.646  -3.869 101.126  1.00 78.14           N  
ANISOU  947  N   HIS A 149    13136   8382   8172   1369    351    570       N  
ATOM    948  CA  HIS A 149      25.413  -2.540 100.553  1.00 80.05           C  
ANISOU  948  CA  HIS A 149    13592   8490   8335   1542    398    629       C  
ATOM    949  C   HIS A 149      24.041  -1.974 100.956  1.00 84.91           C  
ANISOU  949  C   HIS A 149    14182   9142   8939   1888    543    751       C  
ATOM    950  O   HIS A 149      23.974  -0.830 101.401  1.00 85.59           O  
ANISOU  950  O   HIS A 149    14589   9020   8913   2066    672    759       O  
ATOM    951  CB  HIS A 149      25.602  -2.551  99.025  1.00 80.95           C  
ANISOU  951  CB  HIS A 149    13615   8670   8471   1469    266    665       C  
ATOM    952  CG  HIS A 149      25.612  -1.189  98.392  1.00 86.41           C  
ANISOU  952  CG  HIS A 149    14582   9190   9062   1605    299    715       C  
ATOM    953  ND1 HIS A 149      25.315  -1.020  97.049  1.00 88.94           N  
ANISOU  953  ND1 HIS A 149    14823   9582   9388   1643    208    793       N  
ATOM    954  CD2 HIS A 149      25.884   0.024  98.933  1.00 89.99           C  
ANISOU  954  CD2 HIS A 149    15419   9386   9386   1701    411    696       C  
ATOM    955  CE1 HIS A 149      25.414   0.280  96.817  1.00 90.16           C  
ANISOU  955  CE1 HIS A 149    15305   9524   9425   1773    272    824       C  
ATOM    956  NE2 HIS A 149      25.748   0.951  97.923  1.00 91.21           N  
ANISOU  956  NE2 HIS A 149    15740   9446   9471   1808    397    767       N  
ATOM    957  N   TRP A 150      22.974  -2.800 100.853  1.00 81.56           N  
ANISOU  957  N   TRP A 150    13386   8987   8618   1972    532    849       N  
ATOM    958  CA  TRP A 150      21.592  -2.455 101.201  1.00 83.60           C  
ANISOU  958  CA  TRP A 150    13506   9374   8885   2302    670    995       C  
ATOM    959  C   TRP A 150      21.473  -2.016 102.655  1.00 89.51           C  
ANISOU  959  C   TRP A 150    14473   9977   9560   2455    874    963       C  
ATOM    960  O   TRP A 150      20.804  -1.020 102.938  1.00 91.47           O  
ANISOU  960  O   TRP A 150    14876  10146   9731   2787   1038   1050       O  
ATOM    961  CB  TRP A 150      20.651  -3.638 100.922  1.00 82.18           C  
ANISOU  961  CB  TRP A 150    12857   9543   8826   2249    594   1094       C  
ATOM    962  N   ALA A 151      22.144  -2.754 103.568  1.00 85.36           N  
ANISOU  962  N   ALA A 151    13988   9404   9041   2228    868    842       N  
ATOM    963  CA  ALA A 151      22.167  -2.507 105.011  1.00 86.22           C  
ANISOU  963  CA  ALA A 151    14325   9370   9066   2314   1042    792       C  
ATOM    964  C   ALA A 151      22.870  -1.199 105.360  1.00 92.26           C  
ANISOU  964  C   ALA A 151    15603   9789   9663   2369   1118    717       C  
ATOM    965  O   ALA A 151      22.424  -0.511 106.275  1.00 93.99           O  
ANISOU  965  O   ALA A 151    16072   9868   9773   2596   1312    733       O  
ATOM    966  CB  ALA A 151      22.831  -3.668 105.734  1.00 84.85           C  
ANISOU  966  CB  ALA A 151    14069   9239   8932   2030    975    687       C  
ATOM    967  N   VAL A 152      23.954  -0.846 104.634  1.00 88.58           N  
ANISOU  967  N   VAL A 152    15314   9182   9159   2153    975    640       N  
ATOM    968  CA  VAL A 152      24.692   0.395 104.885  1.00 89.77           C  
ANISOU  968  CA  VAL A 152    15972   9003   9133   2135   1025    572       C  
ATOM    969  C   VAL A 152      23.923   1.615 104.327  1.00 97.37           C  
ANISOU  969  C   VAL A 152    17139   9844  10013   2479   1144    682       C  
ATOM    970  O   VAL A 152      24.069   2.715 104.860  1.00 98.64           O  
ANISOU  970  O   VAL A 152    17775   9708   9995   2594   1274    656       O  
ATOM    971  CB  VAL A 152      26.179   0.327 104.440  1.00 91.60           C  
ANISOU  971  CB  VAL A 152    16316   9149   9339   1747    843    458       C  
ATOM    972  CG1 VAL A 152      26.397   0.839 103.016  1.00 91.39           C  
ANISOU  972  CG1 VAL A 152    16294   9109   9319   1722    750    501       C  
ATOM    973  CG2 VAL A 152      27.061   1.070 105.425  1.00 92.22           C  
ANISOU  973  CG2 VAL A 152    16860   8946   9232   1597    883    355       C  
ATOM    974  N   LYS A 153      23.079   1.398 103.291  1.00 95.46           N  
ANISOU  974  N   LYS A 153    16557   9829   9884   2649   1099    812       N  
ATOM    975  CA  LYS A 153      22.226   2.417 102.672  1.00 98.45           C  
ANISOU  975  CA  LYS A 153    17044  10161  10203   3021   1195    951       C  
ATOM    976  C   LYS A 153      21.022   2.725 103.577  1.00107.92           C  
ANISOU  976  C   LYS A 153    18240  11400  11365   3438   1436   1060       C  
ATOM    977  O   LYS A 153      20.398   3.780 103.422  1.00110.28           O  
ANISOU  977  O   LYS A 153    18768  11575  11558   3812   1580   1165       O  
ATOM    978  CB  LYS A 153      21.723   1.939 101.298  1.00 99.74           C  
ANISOU  978  CB  LYS A 153    16788  10609  10499   3036   1039   1065       C  
ATOM    979  CG  LYS A 153      22.666   2.234 100.140  1.00107.35           C  
ANISOU  979  CG  LYS A 153    17897  11459  11433   2806    872   1015       C  
ATOM    980  CD  LYS A 153      21.962   2.022  98.800  1.00116.02           C  
ANISOU  980  CD  LYS A 153    18664  12802  12615   2905    747   1152       C  
ATOM    981  CE  LYS A 153      22.705   2.646  97.640  1.00123.46           C  
ANISOU  981  CE  LYS A 153    19844  13583  13481   2783    639   1134       C  
ATOM    982  NZ  LYS A 153      21.881   2.684  96.401  1.00128.82           N  
ANISOU  982  NZ  LYS A 153    20285  14463  14198   2956    539   1291       N  
ATOM    983  N   GLN A 154      20.708   1.790 104.520  1.00105.99           N  
ANISOU  983  N   GLN A 154    17745  11329  11198   3385   1492   1040       N  
ATOM    984  CA  GLN A 154      19.590   1.807 105.484  1.00109.03           C  
ANISOU  984  CA  GLN A 154    18041  11818  11567   3727   1729   1141       C  
ATOM    985  C   GLN A 154      18.229   1.745 104.751  1.00116.78           C  
ANISOU  985  C   GLN A 154    18578  13142  12649   4065   1764   1364       C  
ATOM    986  O   GLN A 154      17.337   2.568 104.997  1.00119.84           O  
ANISOU  986  O   GLN A 154    19065  13512  12955   4516   1979   1499       O  
ATOM    987  CB  GLN A 154      19.667   2.988 106.488  1.00112.95           C  
ANISOU  987  CB  GLN A 154    19133  11940  11842   3969   1970   1097       C  
ATOM    988  CG  GLN A 154      21.026   3.207 107.159  1.00129.35           C  
ANISOU  988  CG  GLN A 154    21683  13678  13786   3610   1908    891       C  
ATOM    989  CD  GLN A 154      21.309   2.256 108.292  1.00148.96           C  
ANISOU  989  CD  GLN A 154    24070  16230  16298   3391   1915    796       C  
ATOM    990  OE1 GLN A 154      20.587   2.199 109.295  1.00146.39           O  
ANISOU  990  OE1 GLN A 154    23763  15931  15927   3622   2127    838       O  
ATOM    991  NE2 GLN A 154      22.416   1.543 108.185  1.00139.36           N  
ANISOU  991  NE2 GLN A 154    22787  15027  15137   2953   1696    668       N  
ATOM    992  N   GLN A 155      18.088   0.756 103.837  1.00112.45           N  
ANISOU  992  N   GLN A 155    17548  12912  12266   3840   1548   1408       N  
ATOM    993  CA  GLN A 155      16.890   0.557 103.017  1.00114.28           C  
ANISOU  993  CA  GLN A 155    17306  13520  12597   4054   1509   1621       C  
ATOM    994  C   GLN A 155      16.245  -0.816 103.219  1.00117.73           C  
ANISOU  994  C   GLN A 155    17198  14353  13183   3866   1444   1680       C  
ATOM    995  O   GLN A 155      16.948  -1.799 103.483  1.00114.58           O  
ANISOU  995  O   GLN A 155    16754  13941  12840   3471   1321   1539       O  
ATOM    996  CB  GLN A 155      17.212   0.787 101.531  1.00114.94           C  
ANISOU  996  CB  GLN A 155    17374  13604  12695   3965   1290   1647       C  
ATOM    997  N   ASN A 156      14.902  -0.873 103.076  1.00117.07           N  
ANISOU  997  N   ASN A 156    16700  14629  13150   4150   1526   1903       N  
ATOM    998  CA  ASN A 156      14.100  -2.090 103.213  1.00145.11           C  
ANISOU  998  CA  ASN A 156    19710  18601  16826   3982   1477   2002       C  
ATOM    999  C   ASN A 156      13.609  -2.568 101.848  1.00163.18           C  
ANISOU  999  C   ASN A 156    21583  21217  19202   3837   1220   2130       C  
ATOM   1000  O   ASN A 156      13.661  -3.760 101.553  1.00118.94           O  
ANISOU 1000  O   ASN A 156    15721  15791  13680   3441   1039   2091       O  
ATOM   1001  CB  ASN A 156      12.916  -1.835 104.133  1.00149.45           C  
ANISOU 1001  CB  ASN A 156    20055  19369  17360   4373   1757   2181       C  
ATOM   1002  N   LYS A 160      13.902  -8.207 103.988  1.00114.73           N  
ANISOU 1002  N   LYS A 160    14757  15538  13297   2245    987   1842       N  
ATOM   1003  CA  LYS A 160      14.429  -7.879 105.311  1.00113.80           C  
ANISOU 1003  CA  LYS A 160    14971  15146  13122   2377   1206   1723       C  
ATOM   1004  C   LYS A 160      15.532  -8.859 105.740  1.00115.01           C  
ANISOU 1004  C   LYS A 160    15367  15068  13263   2013   1115   1517       C  
ATOM   1005  O   LYS A 160      15.774  -9.851 105.046  1.00113.24           O  
ANISOU 1005  O   LYS A 160    15040  14908  13077   1682    909   1478       O  
ATOM   1006  CB  LYS A 160      13.294  -7.827 106.349  1.00119.14           C  
ANISOU 1006  CB  LYS A 160    15416  16058  13792   2603   1466   1878       C  
ATOM   1007  N   ILE A 161      16.214  -8.560 106.872  1.00110.92           N  
ANISOU 1007  N   ILE A 161    15194  14274  12676   2088   1265   1391       N  
ATOM   1008  CA  ILE A 161      17.289  -9.384 107.451  1.00108.09           C  
ANISOU 1008  CA  ILE A 161    15079  13700  12291   1804   1198   1211       C  
ATOM   1009  C   ILE A 161      16.684 -10.693 107.987  1.00112.05           C  
ANISOU 1009  C   ILE A 161    15350  14403  12822   1575   1217   1260       C  
ATOM   1010  O   ILE A 161      17.222 -11.776 107.742  1.00109.76           O  
ANISOU 1010  O   ILE A 161    15084  14074  12544   1261   1061   1176       O  
ATOM   1011  CB  ILE A 161      18.089  -8.602 108.546  1.00110.64           C  
ANISOU 1011  CB  ILE A 161    15833  13697  12509   1948   1341   1084       C  
ATOM   1012  CG1 ILE A 161      18.591  -7.237 108.015  1.00111.11           C  
ANISOU 1012  CG1 ILE A 161    16152  13550  12516   2155   1335   1051       C  
ATOM   1013  CG2 ILE A 161      19.255  -9.445 109.102  1.00108.87           C  
ANISOU 1013  CG2 ILE A 161    15830  13282  12252   1661   1240    916       C  
ATOM   1014  CD1 ILE A 161      19.094  -6.264 109.069  1.00119.52           C  
ANISOU 1014  CD1 ILE A 161    17651  14317  13445   2331   1505    965       C  
ATOM   1015  N   PHE A 162      15.551 -10.572 108.697  1.00111.02           N  
ANISOU 1015  N   PHE A 162    15007  14487  12689   1745   1423   1404       N  
ATOM   1016  CA  PHE A 162      14.804 -11.682 109.279  1.00111.95           C  
ANISOU 1016  CA  PHE A 162    14886  14828  12821   1542   1481   1482       C  
ATOM   1017  C   PHE A 162      13.575 -11.911 108.399  1.00119.39           C  
ANISOU 1017  C   PHE A 162    15343  16185  13837   1498   1416   1689       C  
ATOM   1018  O   PHE A 162      12.723 -11.023 108.294  1.00121.58           O  
ANISOU 1018  O   PHE A 162    15406  16661  14129   1819   1544   1848       O  
ATOM   1019  CB  PHE A 162      14.407 -11.360 110.738  1.00115.09           C  
ANISOU 1019  CB  PHE A 162    15383  15196  13149   1756   1777   1510       C  
ATOM   1020  CG  PHE A 162      15.519 -10.768 111.576  1.00114.47           C  
ANISOU 1020  CG  PHE A 162    15800  14721  12972   1867   1849   1331       C  
ATOM   1021  CD1 PHE A 162      16.467 -11.583 112.181  1.00114.95           C  
ANISOU 1021  CD1 PHE A 162    16119  14572  12986   1611   1772   1179       C  
ATOM   1022  CD2 PHE A 162      15.619  -9.395 111.759  1.00117.15           C  
ANISOU 1022  CD2 PHE A 162    16366  14897  13249   2220   1983   1324       C  
ATOM   1023  CE1 PHE A 162      17.504 -11.035 112.943  1.00114.34           C  
ANISOU 1023  CE1 PHE A 162    16474  14164  12807   1685   1808   1028       C  
ATOM   1024  CE2 PHE A 162      16.657  -8.849 112.518  1.00118.48           C  
ANISOU 1024  CE2 PHE A 162    17012  14702  13304   2265   2024   1160       C  
ATOM   1025  CZ  PHE A 162      17.590  -9.673 113.109  1.00114.29           C  
ANISOU 1025  CZ  PHE A 162    16688  14003  12733   1988   1928   1017       C  
ATOM   1026  N   SER A 163      13.521 -13.071 107.713  1.00116.31           N  
ANISOU 1026  N   SER A 163    14800  15916  13476   1108   1205   1691       N  
ATOM   1027  CA  SER A 163      12.426 -13.419 106.804  1.00119.01           C  
ANISOU 1027  CA  SER A 163    14695  16658  13867    972   1087   1882       C  
ATOM   1028  C   SER A 163      11.574 -14.605 107.317  1.00126.44           C  
ANISOU 1028  C   SER A 163    15376  17867  14799    654   1124   1989       C  
ATOM   1029  O   SER A 163      11.808 -15.748 106.908  1.00125.21           O  
ANISOU 1029  O   SER A 163    15274  17681  14621    245    943   1929       O  
ATOM   1030  CB  SER A 163      12.952 -13.671 105.392  1.00120.45           C  
ANISOU 1030  CB  SER A 163    14923  16779  14062    764    794   1820       C  
ATOM   1031  OG  SER A 163      13.559 -12.512 104.845  1.00126.76           O  
ANISOU 1031  OG  SER A 163    15904  17392  14868   1055    773   1763       O  
ATOM   1032  N   PRO A 164      10.574 -14.363 108.206  1.00127.02           N  
ANISOU 1032  N   PRO A 164    15184  18203  14874    834   1370   2152       N  
ATOM   1033  CA  PRO A 164       9.752 -15.478 108.706  1.00133.89           C  
ANISOU 1033  CA  PRO A 164    15800  19346  15728    503   1417   2266       C  
ATOM   1034  C   PRO A 164       8.507 -15.723 107.852  1.00170.98           C  
ANISOU 1034  C   PRO A 164    19949  24551  20463    331   1295   2510       C  
ATOM   1035  O   PRO A 164       8.551 -16.478 106.880  1.00131.01           O  
ANISOU 1035  O   PRO A 164    14835  19558  15385    -97   1043   2505       O  
ATOM   1036  CB  PRO A 164       9.389 -15.035 110.131  1.00136.53           C  
ANISOU 1036  CB  PRO A 164    16147  19697  16031    803   1766   2316       C  
ATOM   1037  CG  PRO A 164       9.604 -13.526 110.157  1.00139.17           C  
ANISOU 1037  CG  PRO A 164    16607  19897  16374   1339   1898   2305       C  
ATOM   1038  CD  PRO A 164      10.150 -13.090 108.821  1.00131.77           C  
ANISOU 1038  CD  PRO A 164    15733  18855  15477   1346   1635   2245       C  
ATOM   1039  N   PRO A 176      19.110 -19.040  88.728  1.00121.64           N  
ANISOU 1039  N   PRO A 176    17424  15657  13137  -1763  -1744   1011       N  
ATOM   1040  CA  PRO A 176      19.511 -19.835  89.899  1.00120.17           C  
ANISOU 1040  CA  PRO A 176    17348  15324  12987  -1792  -1593    919       C  
ATOM   1041  C   PRO A 176      20.999 -20.207  89.879  1.00120.50           C  
ANISOU 1041  C   PRO A 176    17778  15021  12987  -1666  -1457    738       C  
ATOM   1042  O   PRO A 176      21.786 -19.629  90.637  1.00118.02           O  
ANISOU 1042  O   PRO A 176    17434  14614  12793  -1392  -1293    678       O  
ATOM   1043  CB  PRO A 176      18.568 -21.051  89.850  1.00124.65           C  
ANISOU 1043  CB  PRO A 176    17943  15993  13426  -2214  -1733    976       C  
ATOM   1044  CG  PRO A 176      17.988 -21.066  88.442  1.00131.53           C  
ANISOU 1044  CG  PRO A 176    18837  16990  14150  -2438  -1970   1054       C  
ATOM   1045  CD  PRO A 176      18.499 -19.876  87.679  1.00125.81           C  
ANISOU 1045  CD  PRO A 176    18083  16248  13472  -2136  -1965   1052       C  
ATOM   1046  N   LEU A 177      21.382 -21.163  89.006  1.00116.32           N  
ANISOU 1046  N   LEU A 177    17614  14311  12271  -1866  -1526    659       N  
ATOM   1047  CA  LEU A 177      22.758 -21.617  88.806  1.00113.73           C  
ANISOU 1047  CA  LEU A 177    17663  13681  11869  -1742  -1398    508       C  
ATOM   1048  C   LEU A 177      23.311 -20.970  87.536  1.00114.57           C  
ANISOU 1048  C   LEU A 177    17885  13738  11907  -1643  -1436    488       C  
ATOM   1049  O   LEU A 177      24.443 -21.248  87.132  1.00112.69           O  
ANISOU 1049  O   LEU A 177    17943  13284  11590  -1533  -1332    381       O  
ATOM   1050  CB  LEU A 177      22.823 -23.158  88.714  1.00115.27           C  
ANISOU 1050  CB  LEU A 177    18248  13677  11873  -2000  -1414    437       C  
ATOM   1051  CG  LEU A 177      22.626 -23.940  90.017  1.00119.96           C  
ANISOU 1051  CG  LEU A 177    18838  14237  12505  -2077  -1335    429       C  
ATOM   1052  CD1 LEU A 177      22.182 -25.362  89.731  1.00122.55           C  
ANISOU 1052  CD1 LEU A 177    19532  14423  12610  -2441  -1419    406       C  
ATOM   1053  CD2 LEU A 177      23.889 -23.926  90.881  1.00119.89           C  
ANISOU 1053  CD2 LEU A 177    18912  14053  12588  -1758  -1125    333       C  
ATOM   1054  N   ALA A 178      22.515 -20.055  86.939  1.00110.99           N  
ANISOU 1054  N   ALA A 178    17184  13502  11487  -1657  -1572    603       N  
ATOM   1055  CA  ALA A 178      22.848 -19.289  85.736  1.00110.51           C  
ANISOU 1055  CA  ALA A 178    17199  13428  11363  -1571  -1627    612       C  
ATOM   1056  C   ALA A 178      24.074 -18.380  85.964  1.00110.48           C  
ANISOU 1056  C   ALA A 178    17206  13305  11467  -1241  -1439    541       C  
ATOM   1057  O   ALA A 178      24.495 -17.661  85.051  1.00110.40           O  
ANISOU 1057  O   ALA A 178    17269  13267  11413  -1147  -1448    544       O  
ATOM   1058  CB  ALA A 178      21.643 -18.466  85.291  1.00112.88           C  
ANISOU 1058  CB  ALA A 178    17185  14012  11693  -1617  -1807    776       C  
ATOM   1059  N   PHE A 179      24.651 -18.443  87.187  1.00103.02           N  
ANISOU 1059  N   PHE A 179    16201  12295  10647  -1092  -1276    484       N  
ATOM   1060  CA  PHE A 179      25.847 -17.718  87.597  1.00 99.45           C  
ANISOU 1060  CA  PHE A 179    15751  11747  10290   -831  -1105    419       C  
ATOM   1061  C   PHE A 179      26.891 -18.668  88.179  1.00 99.95           C  
ANISOU 1061  C   PHE A 179    16016  11636  10326   -786   -964    309       C  
ATOM   1062  O   PHE A 179      28.083 -18.442  87.992  1.00 98.63           O  
ANISOU 1062  O   PHE A 179    15956  11370  10149   -633   -845    247       O  
ATOM   1063  CB  PHE A 179      25.515 -16.594  88.591  1.00100.04           C  
ANISOU 1063  CB  PHE A 179    15522  11945  10544   -661  -1056    482       C  
ATOM   1064  CG  PHE A 179      26.676 -15.659  88.829  1.00 99.60           C  
ANISOU 1064  CG  PHE A 179    15482  11804  10558   -446   -917    431       C  
ATOM   1065  CD1 PHE A 179      27.056 -14.734  87.862  1.00102.59           C  
ANISOU 1065  CD1 PHE A 179    15911  12168  10901   -375   -927    450       C  
ATOM   1066  CD2 PHE A 179      27.409 -15.722  90.006  1.00 99.99           C  
ANISOU 1066  CD2 PHE A 179    15507  11792  10691   -341   -786    371       C  
ATOM   1067  CE1 PHE A 179      28.142 -13.883  88.074  1.00102.17           C  
ANISOU 1067  CE1 PHE A 179    15879  12044  10895   -227   -803    410       C  
ATOM   1068  CE2 PHE A 179      28.497 -14.872  90.216  1.00101.67           C  
ANISOU 1068  CE2 PHE A 179    15729  11950  10950   -193   -679    334       C  
ATOM   1069  CZ  PHE A 179      28.855 -13.958  89.249  1.00 99.99           C  
ANISOU 1069  CZ  PHE A 179    15564  11727  10702   -150   -686    354       C  
ATOM   1070  N   GLY A 180      26.437 -19.707  88.878  1.00 95.28           N  
ANISOU 1070  N   GLY A 180    15467  11021   9714   -915   -976    298       N  
ATOM   1071  CA  GLY A 180      27.310 -20.705  89.489  1.00 93.94           C  
ANISOU 1071  CA  GLY A 180    15510  10680   9501   -860   -851    210       C  
ATOM   1072  C   GLY A 180      28.107 -21.480  88.463  1.00 96.84           C  
ANISOU 1072  C   GLY A 180    16242  10867   9687   -862   -810    137       C  
ATOM   1073  O   GLY A 180      29.337 -21.374  88.416  1.00 95.07           O  
ANISOU 1073  O   GLY A 180    16096  10563   9463   -653   -670     84       O  
ATOM   1074  N   LEU A 181      27.395 -22.231  87.608  1.00 94.67           N  
ANISOU 1074  N   LEU A 181    16190  10541   9242  -1106   -932    143       N  
ATOM   1075  CA  LEU A 181      27.987 -23.032  86.537  1.00 95.47           C  
ANISOU 1075  CA  LEU A 181    16706  10443   9124  -1134   -898     75       C  
ATOM   1076  C   LEU A 181      28.516 -22.131  85.428  1.00 97.31           C  
ANISOU 1076  C   LEU A 181    16931  10708   9335  -1021   -884     79       C  
ATOM   1077  O   LEU A 181      29.711 -22.181  85.131  1.00 96.86           O  
ANISOU 1077  O   LEU A 181    17020  10546   9235   -814   -722     23       O  
ATOM   1078  CB  LEU A 181      26.966 -24.042  85.962  1.00 98.23           C  
ANISOU 1078  CB  LEU A 181    17322  10727   9273  -1484  -1059     85       C  
ATOM   1079  CG  LEU A 181      26.569 -25.216  86.866  1.00104.48           C  
ANISOU 1079  CG  LEU A 181    18273  11415  10010  -1642  -1054     66       C  
ATOM   1080  CD1 LEU A 181      25.096 -25.555  86.708  1.00106.77           C  
ANISOU 1080  CD1 LEU A 181    18510  11830  10229  -2044  -1272    145       C  
ATOM   1081  CD2 LEU A 181      27.445 -26.444  86.611  1.00108.61           C  
ANISOU 1081  CD2 LEU A 181    19324  11625  10319  -1578   -921    -33       C  
ATOM   1082  N   ARG A 182      27.628 -21.275  84.856  1.00 92.18           N  
ANISOU 1082  N   ARG A 182    16089  10221   8714  -1142  -1045    159       N  
ATOM   1083  CA  ARG A 182      27.881 -20.363  83.732  1.00 90.73           C  
ANISOU 1083  CA  ARG A 182    15907  10075   8490  -1081  -1070    183       C  
ATOM   1084  C   ARG A 182      28.973 -19.306  83.956  1.00 89.52           C  
ANISOU 1084  C   ARG A 182    15593   9948   8473   -804   -908    171       C  
ATOM   1085  O   ARG A 182      29.541 -18.831  82.970  1.00 89.32           O  
ANISOU 1085  O   ARG A 182    15682   9888   8367   -741   -866    163       O  
ATOM   1086  CB  ARG A 182      26.586 -19.690  83.301  1.00 92.32           C  
ANISOU 1086  CB  ARG A 182    15895  10470   8711  -1245  -1288    295       C  
ATOM   1087  N   CYS A 183      29.275 -18.940  85.217  1.00 82.08           N  
ANISOU 1087  N   CYS A 183    14407   9065   7715   -665   -821    172       N  
ATOM   1088  CA  CYS A 183      30.295 -17.929  85.484  1.00 79.48           C  
ANISOU 1088  CA  CYS A 183    13931   8770   7499   -457   -688    167       C  
ATOM   1089  C   CYS A 183      31.328 -18.343  86.533  1.00 79.47           C  
ANISOU 1089  C   CYS A 183    13902   8725   7566   -302   -529    114       C  
ATOM   1090  O   CYS A 183      32.496 -18.524  86.180  1.00 78.96           O  
ANISOU 1090  O   CYS A 183    13953   8606   7441   -177   -392     76       O  
ATOM   1091  CB  CYS A 183      29.654 -16.591  85.838  1.00 79.16           C  
ANISOU 1091  CB  CYS A 183    13605   8868   7602   -430   -760    245       C  
ATOM   1092  SG  CYS A 183      30.845 -15.284  86.229  1.00 81.71           S  
ANISOU 1092  SG  CYS A 183    13795   9212   8037   -240   -615    241       S  
ATOM   1093  N   GLU A 184      30.910 -18.425  87.821  1.00 73.06           N  
ANISOU 1093  N   GLU A 184    12918   7962   6879   -300   -544    124       N  
ATOM   1094  CA  GLU A 184      31.765 -18.745  88.968  1.00 70.90           C  
ANISOU 1094  CA  GLU A 184    12591   7670   6677   -163   -425     90       C  
ATOM   1095  C   GLU A 184      32.732 -19.882  88.687  1.00 73.01           C  
ANISOU 1095  C   GLU A 184    13110   7815   6816    -70   -310     35       C  
ATOM   1096  O   GLU A 184      33.937 -19.646  88.717  1.00 72.34           O  
ANISOU 1096  O   GLU A 184    12986   7758   6743     97   -185     26       O  
ATOM   1097  CB  GLU A 184      30.949 -18.997  90.244  1.00 71.73           C  
ANISOU 1097  CB  GLU A 184    12567   7811   6878   -219   -473    107       C  
ATOM   1098  N   GLU A 185      32.214 -21.070  88.322  1.00 68.82           N  
ANISOU 1098  N   GLU A 185    12850   7155   6142   -181   -348      7       N  
ATOM   1099  CA  GLU A 185      33.008 -22.256  88.001  1.00 69.10           C  
ANISOU 1099  CA  GLU A 185    13207   7030   6019    -73   -227    -43       C  
ATOM   1100  C   GLU A 185      34.135 -21.975  86.993  1.00 71.24           C  
ANISOU 1100  C   GLU A 185    13561   7299   6210     90    -97    -53       C  
ATOM   1101  O   GLU A 185      35.301 -22.249  87.289  1.00 70.62           O  
ANISOU 1101  O   GLU A 185    13474   7229   6130    318     60    -57       O  
ATOM   1102  CB  GLU A 185      32.096 -23.379  87.482  1.00 72.31           C  
ANISOU 1102  CB  GLU A 185    13954   7275   6245   -285   -315    -70       C  
ATOM   1103  N   VAL A 186      33.778 -21.384  85.831  1.00 66.55           N  
ANISOU 1103  N   VAL A 186    13017   6718   5550    -22   -164    -42       N  
ATOM   1104  CA  VAL A 186      34.665 -21.051  84.705  1.00 65.80           C  
ANISOU 1104  CA  VAL A 186    13025   6619   5357     87    -49    -45       C  
ATOM   1105  C   VAL A 186      35.803 -20.124  85.105  1.00 66.06           C  
ANISOU 1105  C   VAL A 186    12766   6811   5523    265     75    -11       C  
ATOM   1106  O   VAL A 186      36.958 -20.401  84.784  1.00 65.36           O  
ANISOU 1106  O   VAL A 186    12742   6730   5363    451    251    -11       O  
ATOM   1107  CB  VAL A 186      33.893 -20.483  83.488  1.00 70.20           C  
ANISOU 1107  CB  VAL A 186    13674   7174   5827    -98   -179    -27       C  
ATOM   1108  CG1 VAL A 186      34.614 -20.809  82.186  1.00 71.70           C  
ANISOU 1108  CG1 VAL A 186    14172   7260   5811    -21    -52    -54       C  
ATOM   1109  CG2 VAL A 186      32.453 -20.987  83.445  1.00 70.70           C  
ANISOU 1109  CG2 VAL A 186    13847   7185   5832   -355   -383    -24       C  
ATOM   1110  N   VAL A 187      35.466 -19.024  85.794  1.00 60.92           N  
ANISOU 1110  N   VAL A 187    11805   6291   5051    202    -13     27       N  
ATOM   1111  CA  VAL A 187      36.424 -18.017  86.253  1.00 59.85           C  
ANISOU 1111  CA  VAL A 187    11403   6304   5033    298     69     62       C  
ATOM   1112  C   VAL A 187      37.275 -18.586  87.401  1.00 63.85           C  
ANISOU 1112  C   VAL A 187    11800   6861   5599    457    164     60       C  
ATOM   1113  O   VAL A 187      38.462 -18.272  87.486  1.00 64.28           O  
ANISOU 1113  O   VAL A 187    11712   7037   5673    578    282     92       O  
ATOM   1114  CB  VAL A 187      35.741 -16.653  86.582  1.00 62.24           C  
ANISOU 1114  CB  VAL A 187    11492   6688   5469    178    -51    100       C  
ATOM   1115  CG1 VAL A 187      36.739 -15.630  87.125  1.00 61.46           C  
ANISOU 1115  CG1 VAL A 187    11171   6717   5466    230     26    132       C  
ATOM   1116  CG2 VAL A 187      35.011 -16.082  85.362  1.00 62.50           C  
ANISOU 1116  CG2 VAL A 187    11636   6686   5426     61   -140    121       C  
ATOM   1117  N   LYS A 188      36.685 -19.458  88.241  1.00 59.81           N  
ANISOU 1117  N   LYS A 188    11356   6268   5100    449    111     35       N  
ATOM   1118  CA  LYS A 188      37.387 -20.095  89.359  1.00 59.64           C  
ANISOU 1118  CA  LYS A 188    11264   6278   5117    606    184     39       C  
ATOM   1119  C   LYS A 188      38.488 -21.003  88.806  1.00 65.49           C  
ANISOU 1119  C   LYS A 188    12172   6988   5721    829    357     41       C  
ATOM   1120  O   LYS A 188      39.637 -20.893  89.233  1.00 64.56           O  
ANISOU 1120  O   LYS A 188    11873   7017   5639   1002    461     86       O  
ATOM   1121  CB  LYS A 188      36.398 -20.897  90.227  1.00 61.48           C  
ANISOU 1121  CB  LYS A 188    11592   6402   5366    528     94     13       C  
ATOM   1122  CG  LYS A 188      36.689 -20.893  91.724  1.00 61.66           C  
ANISOU 1122  CG  LYS A 188    11435   6497   5496    609     98     31       C  
ATOM   1123  CD  LYS A 188      35.400 -20.825  92.538  1.00 63.06           C  
ANISOU 1123  CD  LYS A 188    11566   6640   5753    442    -25     23       C  
ATOM   1124  CE  LYS A 188      34.848 -22.174  92.937  1.00 73.75           C  
ANISOU 1124  CE  LYS A 188    13163   7839   7018    409    -35     -3       C  
ATOM   1125  NZ  LYS A 188      33.675 -22.052  93.848  1.00 80.62           N  
ANISOU 1125  NZ  LYS A 188    13938   8720   7975    249   -134      7       N  
ATOM   1126  N   THR A 189      38.137 -21.849  87.810  1.00 64.56           N  
ANISOU 1126  N   THR A 189    12404   6693   5432    822    389      2       N  
ATOM   1127  CA  THR A 189      39.041 -22.778  87.122  1.00 67.18           C  
ANISOU 1127  CA  THR A 189    12987   6948   5592   1053    576     -1       C  
ATOM   1128  C   THR A 189      40.137 -21.992  86.406  1.00 73.74           C  
ANISOU 1128  C   THR A 189    13636   7957   6426   1166    708     49       C  
ATOM   1129  O   THR A 189      41.293 -22.417  86.399  1.00 74.97           O  
ANISOU 1129  O   THR A 189    13755   8199   6531   1429    887     93       O  
ATOM   1130  CB  THR A 189      38.235 -23.677  86.176  1.00 76.23           C  
ANISOU 1130  CB  THR A 189    14589   7841   6535    948    552    -62       C  
ATOM   1131  OG1 THR A 189      37.243 -24.363  86.941  1.00 76.44           O  
ANISOU 1131  OG1 THR A 189    14742   7736   6567    795    420    -94       O  
ATOM   1132  CG2 THR A 189      39.102 -24.685  85.425  1.00 76.44           C  
ANISOU 1132  CG2 THR A 189    14961   7736   6347   1210    767    -73       C  
ATOM   1133  N   LEU A 190      39.768 -20.831  85.829  1.00 70.40           N  
ANISOU 1133  N   LEU A 190    13089   7602   6059    971    622     55       N  
ATOM   1134  CA  LEU A 190      40.679 -19.918  85.147  1.00 70.76           C  
ANISOU 1134  CA  LEU A 190    12963   7813   6108   1007    728    106       C  
ATOM   1135  C   LEU A 190      41.748 -19.438  86.142  1.00 74.07           C  
ANISOU 1135  C   LEU A 190    13005   8477   6663   1112    787    176       C  
ATOM   1136  O   LEU A 190      42.934 -19.574  85.857  1.00 74.83           O  
ANISOU 1136  O   LEU A 190    13003   8720   6708   1295    963    234       O  
ATOM   1137  CB  LEU A 190      39.878 -18.743  84.573  1.00 69.86           C  
ANISOU 1137  CB  LEU A 190    12810   7696   6038    757    588    102       C  
ATOM   1138  CG  LEU A 190      40.414 -18.081  83.314  1.00 76.24           C  
ANISOU 1138  CG  LEU A 190    13638   8567   6763    744    690    134       C  
ATOM   1139  CD1 LEU A 190      40.070 -18.889  82.075  1.00 78.20           C  
ANISOU 1139  CD1 LEU A 190    14277   8641   6793    785    762     95       C  
ATOM   1140  CD2 LEU A 190      39.808 -16.709  83.150  1.00 78.53           C  
ANISOU 1140  CD2 LEU A 190    13821   8883   7135    523    542    151       C  
ATOM   1141  N   LEU A 191      41.329 -18.979  87.341  1.00 69.40           N  
ANISOU 1141  N   LEU A 191    12213   7933   6224   1005    645    176       N  
ATOM   1142  CA  LEU A 191      42.228 -18.530  88.411  1.00 69.41           C  
ANISOU 1142  CA  LEU A 191    11881   8155   6338   1056    657    238       C  
ATOM   1143  C   LEU A 191      43.071 -19.686  88.965  1.00 74.99           C  
ANISOU 1143  C   LEU A 191    12577   8919   6995   1337    775    275       C  
ATOM   1144  O   LEU A 191      44.275 -19.523  89.195  1.00 76.16           O  
ANISOU 1144  O   LEU A 191    12471   9307   7159   1465    871    359       O  
ATOM   1145  CB  LEU A 191      41.422 -17.908  89.568  1.00 67.71           C  
ANISOU 1145  CB  LEU A 191    11541   7923   6263    881    479    216       C  
ATOM   1146  CG  LEU A 191      40.782 -16.539  89.354  1.00 71.80           C  
ANISOU 1146  CG  LEU A 191    11994   8436   6851    648    371    210       C  
ATOM   1147  CD1 LEU A 191      39.766 -16.259  90.436  1.00 70.49           C  
ANISOU 1147  CD1 LEU A 191    11799   8197   6788    538    224    180       C  
ATOM   1148  CD2 LEU A 191      41.827 -15.420  89.329  1.00 75.32           C  
ANISOU 1148  CD2 LEU A 191    12207   9082   7328    580    417    274       C  
ATOM   1149  N   ALA A 192      42.424 -20.847  89.189  1.00 70.75           N  
ANISOU 1149  N   ALA A 192    12319   8171   6391   1424    761    221       N  
ATOM   1150  CA  ALA A 192      43.029 -22.048  89.751  1.00 71.40           C  
ANISOU 1150  CA  ALA A 192    12481   8242   6407   1706    863    250       C  
ATOM   1151  C   ALA A 192      44.099 -22.676  88.879  1.00 76.89           C  
ANISOU 1151  C   ALA A 192    13270   8990   6956   2003   1091    302       C  
ATOM   1152  O   ALA A 192      45.085 -23.174  89.412  1.00 78.30           O  
ANISOU 1152  O   ALA A 192    13312   9318   7119   2277   1198    382       O  
ATOM   1153  CB  ALA A 192      41.953 -23.073  90.061  1.00 71.73           C  
ANISOU 1153  CB  ALA A 192    12864   8003   6388   1670    789    175       C  
ATOM   1154  N   THR A 193      43.912 -22.680  87.557  1.00 73.67           N  
ANISOU 1154  N   THR A 193    13099   8464   6427   1971   1173    264       N  
ATOM   1155  CA  THR A 193      44.861 -23.336  86.665  1.00 76.11           C  
ANISOU 1155  CA  THR A 193    13558   8791   6568   2274   1420    308       C  
ATOM   1156  C   THR A 193      45.759 -22.385  85.876  1.00 80.20           C  
ANISOU 1156  C   THR A 193    13805   9567   7099   2271   1540    382       C  
ATOM   1157  O   THR A 193      46.746 -22.848  85.298  1.00 83.09           O  
ANISOU 1157  O   THR A 193    14195  10029   7345   2561   1774    449       O  
ATOM   1158  CB  THR A 193      44.141 -24.316  85.720  1.00 87.92           C  
ANISOU 1158  CB  THR A 193    15612   9938   7857   2288   1471    216       C  
ATOM   1159  OG1 THR A 193      42.825 -24.596  86.196  1.00 86.31           O  
ANISOU 1159  OG1 THR A 193    15612   9505   7678   2043   1263    129       O  
ATOM   1160  CG2 THR A 193      44.903 -25.620  85.555  1.00 91.55           C  
ANISOU 1160  CG2 THR A 193    16363  10299   8125   2696   1709    245       C  
ATOM   1161  N   LEU A 194      45.431 -21.079  85.820  1.00 73.52           N  
ANISOU 1161  N   LEU A 194    12729   8824   6380   1957   1399    377       N  
ATOM   1162  CA  LEU A 194      46.229 -20.130  85.035  1.00 73.51           C  
ANISOU 1162  CA  LEU A 194    12511   9045   6375   1905   1508    448       C  
ATOM   1163  C   LEU A 194      46.968 -19.091  85.877  1.00 76.64           C  
ANISOU 1163  C   LEU A 194    12424   9768   6929   1783   1446    540       C  
ATOM   1164  O   LEU A 194      48.112 -18.759  85.553  1.00 77.69           O  
ANISOU 1164  O   LEU A 194    12299  10178   7040   1866   1599    646       O  
ATOM   1165  CB  LEU A 194      45.373 -19.457  83.952  1.00 72.22           C  
ANISOU 1165  CB  LEU A 194    12571   8709   6161   1648   1437    378       C  
ATOM   1166  CG  LEU A 194      45.203 -20.185  82.613  1.00 77.84           C  
ANISOU 1166  CG  LEU A 194    13710   9211   6656   1764   1581    331       C  
ATOM   1167  CD1 LEU A 194      44.351 -21.431  82.735  1.00 77.72           C  
ANISOU 1167  CD1 LEU A 194    14103   8890   6539   1830   1524    241       C  
ATOM   1168  CD2 LEU A 194      44.503 -19.311  81.648  1.00 79.13           C  
ANISOU 1168  CD2 LEU A 194    14001   9281   6783   1497   1493    293       C  
ATOM   1169  N   LEU A 195      46.336 -18.590  86.949  1.00 71.53           N  
ANISOU 1169  N   LEU A 195    11661   9095   6424   1579   1230    505       N  
ATOM   1170  CA  LEU A 195      46.957 -17.596  87.821  1.00 71.77           C  
ANISOU 1170  CA  LEU A 195    11294   9396   6579   1424   1147    581       C  
ATOM   1171  C   LEU A 195      47.712 -18.181  89.009  1.00 79.13           C  
ANISOU 1171  C   LEU A 195    11989  10524   7554   1614   1145    657       C  
ATOM   1172  O   LEU A 195      48.789 -17.681  89.340  1.00 80.54           O  
ANISOU 1172  O   LEU A 195    11807  11032   7764   1599   1177    772       O  
ATOM   1173  CB  LEU A 195      45.936 -16.570  88.292  1.00 69.20           C  
ANISOU 1173  CB  LEU A 195    10990   8944   6360   1099    932    513       C  
ATOM   1174  CG  LEU A 195      46.055 -15.217  87.642  1.00 73.93           C  
ANISOU 1174  CG  LEU A 195    11507   9616   6966    845    922    537       C  
ATOM   1175  CD1 LEU A 195      45.493 -15.242  86.223  1.00 74.56           C  
ANISOU 1175  CD1 LEU A 195    11874   9515   6939    839    995    491       C  
ATOM   1176  CD2 LEU A 195      45.350 -14.172  88.471  1.00 74.41           C  
ANISOU 1176  CD2 LEU A 195    11537   9604   7133    578    726    500       C  
ATOM   1177  N   HIS A 196      47.154 -19.227  89.659  1.00 76.35           N  
ANISOU 1177  N   HIS A 196    11834   9983   7192   1774   1100    604       N  
ATOM   1178  CA  HIS A 196      47.787 -19.866  90.818  1.00 77.80           C  
ANISOU 1178  CA  HIS A 196    11839  10320   7400   1979   1088    677       C  
ATOM   1179  C   HIS A 196      47.867 -21.418  90.694  1.00 85.44           C  
ANISOU 1179  C   HIS A 196    13087  11133   8243   2361   1230    674       C  
ATOM   1180  O   HIS A 196      47.437 -22.125  91.619  1.00 84.27           O  
ANISOU 1180  O   HIS A 196    13070  10845   8105   2437   1147    642       O  
ATOM   1181  CB  HIS A 196      47.082 -19.429  92.120  1.00 76.25           C  
ANISOU 1181  CB  HIS A 196    11586  10064   7323   1760    861    630       C  
ATOM   1182  CG  HIS A 196      46.898 -17.948  92.254  1.00 78.10           C  
ANISOU 1182  CG  HIS A 196    11646  10379   7649   1402    732    620       C  
ATOM   1183  ND1 HIS A 196      47.951 -17.116  92.592  1.00 81.05           N  
ANISOU 1183  ND1 HIS A 196    11661  11079   8053   1291    717    726       N  
ATOM   1184  CD2 HIS A 196      45.785 -17.199  92.082  1.00 77.46           C  
ANISOU 1184  CD2 HIS A 196    11724  10090   7617   1144    618    525       C  
ATOM   1185  CE1 HIS A 196      47.445 -15.894  92.619  1.00 78.94           C  
ANISOU 1185  CE1 HIS A 196    11400  10752   7842    963    600    680       C  
ATOM   1186  NE2 HIS A 196      46.145 -15.895  92.324  1.00 77.14           N  
ANISOU 1186  NE2 HIS A 196    11472  10207   7630    892    544    564       N  
ATOM   1187  N   PRO A 197      48.436 -21.988  89.593  1.00 85.89           N  
ANISOU 1187  N   PRO A 197    13270  11200   8165   2617   1458    711       N  
ATOM   1188  CA  PRO A 197      48.499 -23.457  89.492  1.00 88.07           C  
ANISOU 1188  CA  PRO A 197    13884  11286   8294   2993   1604    706       C  
ATOM   1189  C   PRO A 197      49.654 -24.097  90.265  1.00 96.33           C  
ANISOU 1189  C   PRO A 197    14684  12596   9320   3372   1705    853       C  
ATOM   1190  O   PRO A 197      49.805 -25.319  90.235  1.00 97.39           O  
ANISOU 1190  O   PRO A 197    15109  12578   9317   3736   1849    867       O  
ATOM   1191  CB  PRO A 197      48.597 -23.695  87.986  1.00 91.09           C  
ANISOU 1191  CB  PRO A 197    14543  11546   8521   3093   1808    678       C  
ATOM   1192  CG  PRO A 197      49.292 -22.503  87.464  1.00 95.49           C  
ANISOU 1192  CG  PRO A 197    14723  12415   9143   2936   1849    754       C  
ATOM   1193  CD  PRO A 197      49.030 -21.353  88.396  1.00 88.71           C  
ANISOU 1193  CD  PRO A 197    13514  11717   8473   2587   1609    760       C  
ATOM   1194  N   ASP A 198      50.464 -23.269  90.953  1.00 95.29           N  
ANISOU 1194  N   ASP A 198    14039  12858   9309   3284   1625    969       N  
ATOM   1195  CA  ASP A 198      51.605 -23.703  91.757  1.00 98.76           C  
ANISOU 1195  CA  ASP A 198    14148  13632   9744   3601   1676   1137       C  
ATOM   1196  C   ASP A 198      51.263 -23.742  93.251  1.00102.83           C  
ANISOU 1196  C   ASP A 198    14582  14136  10351   3496   1442   1129       C  
ATOM   1197  O   ASP A 198      51.649 -24.686  93.945  1.00104.03           O  
ANISOU 1197  O   ASP A 198    14761  14320  10448   3829   1474   1205       O  
ATOM   1198  CB  ASP A 198      52.823 -22.803  91.494  1.00102.86           C  
ANISOU 1198  CB  ASP A 198    14130  14646  10306   3557   1744   1297       C  
ATOM   1199  CG  ASP A 198      53.826 -23.418  90.542  1.00118.62           C  
ANISOU 1199  CG  ASP A 198    16078  16824  12168   3980   2057   1421       C  
ATOM   1200  OD1 ASP A 198      53.890 -22.969  89.377  1.00119.80           O  
ANISOU 1200  OD1 ASP A 198    16256  16986  12277   3881   2194   1404       O  
ATOM   1201  OD2 ASP A 198      54.546 -24.356  90.961  1.00127.83           O  
ANISOU 1201  OD2 ASP A 198    17186  18122  13260   4429   2176   1543       O  
ATOM   1202  N   GLU A 199      50.536 -22.720  93.735  1.00 97.75           N  
ANISOU 1202  N   GLU A 199    13870  13438   9833   3053   1221   1041       N  
ATOM   1203  CA  GLU A 199      50.125 -22.597  95.132  1.00 96.70           C  
ANISOU 1203  CA  GLU A 199    13682  13277   9781   2904   1000   1020       C  
ATOM   1204  C   GLU A 199      48.934 -23.499  95.444  1.00100.26           C  
ANISOU 1204  C   GLU A 199    14601  13298  10193   2944    959    889       C  
ATOM   1205  O   GLU A 199      48.134 -23.795  94.551  1.00 99.17           O  
ANISOU 1205  O   GLU A 199    14819  12861  10002   2905   1030    780       O  
ATOM   1206  CB  GLU A 199      49.773 -21.134  95.454  1.00 95.94           C  
ANISOU 1206  CB  GLU A 199    13387  13259   9809   2432    811    974       C  
ATOM   1207  N   THR A 200      48.811 -23.924  96.714  1.00 97.28           N  
ANISOU 1207  N   THR A 200    14229  12900   9832   2994    838    907       N  
ATOM   1208  CA  THR A 200      47.680 -24.732  97.170  1.00 95.98           C  
ANISOU 1208  CA  THR A 200    14484  12352   9633   2984    787    796       C  
ATOM   1209  C   THR A 200      46.523 -23.768  97.393  1.00 96.89           C  
ANISOU 1209  C   THR A 200    14630  12322   9861   2546    620    673       C  
ATOM   1210  O   THR A 200      46.681 -22.764  98.096  1.00 95.13           O  
ANISOU 1210  O   THR A 200    14124  12284   9735   2325    481    696       O  
ATOM   1211  CB  THR A 200      48.029 -25.569  98.410  1.00107.39           C  
ANISOU 1211  CB  THR A 200    15939  13831  11034   3224    740    874       C  
ATOM   1212  OG1 THR A 200      48.619 -24.729  99.402  1.00109.29           O  
ANISOU 1212  OG1 THR A 200    15769  14392  11366   3082    581    957       O  
ATOM   1213  CG2 THR A 200      48.956 -26.737  98.088  1.00109.07           C  
ANISOU 1213  CG2 THR A 200    16238  14100  11104   3727    936    989       C  
ATOM   1214  N   ASN A 201      45.387 -24.036  96.738  1.00 92.89           N  
ANISOU 1214  N   ASN A 201    14468  11498   9327   2421    638    552       N  
ATOM   1215  CA  ASN A 201      44.208 -23.168  96.777  1.00 90.47           C  
ANISOU 1215  CA  ASN A 201    14196  11060   9117   2050    504    449       C  
ATOM   1216  C   ASN A 201      42.959 -23.881  97.304  1.00 93.93           C  
ANISOU 1216  C   ASN A 201    14950  11202   9537   1960    437    364       C  
ATOM   1217  O   ASN A 201      42.939 -25.111  97.394  1.00 94.84           O  
ANISOU 1217  O   ASN A 201    15334  11158   9543   2164    505    368       O  
ATOM   1218  CB  ASN A 201      43.936 -22.590  95.374  1.00 90.76           C  
ANISOU 1218  CB  ASN A 201    14288  11050   9147   1921    563    402       C  
ATOM   1219  CG  ASN A 201      45.171 -22.322  94.540  1.00112.42           C  
ANISOU 1219  CG  ASN A 201    16826  14034  11853   2075    698    488       C  
ATOM   1220  OD1 ASN A 201      46.101 -21.622  94.958  1.00107.76           O  
ANISOU 1220  OD1 ASN A 201    15880  13743  11322   2059    674    578       O  
ATOM   1221  ND2 ASN A 201      45.206 -22.884  93.342  1.00103.57           N  
ANISOU 1221  ND2 ASN A 201    15936  12796  10619   2212    847    468       N  
ATOM   1222  N   CYS A 202      41.917 -23.098  97.647  1.00 88.88           N  
ANISOU 1222  N   CYS A 202    14285  10492   8993   1659    313    297       N  
ATOM   1223  CA  CYS A 202      40.638 -23.615  98.127  1.00 88.09           C  
ANISOU 1223  CA  CYS A 202    14424  10157   8888   1523    249    229       C  
ATOM   1224  C   CYS A 202      39.492 -23.005  97.332  1.00 90.53           C  
ANISOU 1224  C   CYS A 202    14795  10362   9240   1265    199    160       C  
ATOM   1225  O   CYS A 202      39.246 -21.798  97.420  1.00 88.69           O  
ANISOU 1225  O   CYS A 202    14359  10229   9111   1094    127    154       O  
ATOM   1226  CB  CYS A 202      40.472 -23.388  99.627  1.00 87.97           C  
ANISOU 1226  CB  CYS A 202    14293  10194   8938   1463    151    246       C  
ATOM   1227  SG  CYS A 202      38.899 -23.993 100.300  1.00 91.06           S  
ANISOU 1227  SG  CYS A 202    14942  10333   9322   1286     95    180       S  
ATOM   1228  N   LEU A 203      38.804 -23.850  96.545  1.00 87.66           N  
ANISOU 1228  N   LEU A 203    14736   9795   8777   1239    235    114       N  
ATOM   1229  CA  LEU A 203      37.679 -23.465  95.690  1.00 86.67           C  
ANISOU 1229  CA  LEU A 203    14693   9578   8660   1002    175     64       C  
ATOM   1230  C   LEU A 203      36.401 -23.221  96.490  1.00 90.00           C  
ANISOU 1230  C   LEU A 203    15077   9957   9162    782     64     44       C  
ATOM   1231  O   LEU A 203      35.789 -22.160  96.352  1.00 88.40           O  
ANISOU 1231  O   LEU A 203    14700   9832   9055    627     -7     42       O  
ATOM   1232  CB  LEU A 203      37.417 -24.537  94.623  1.00 88.12           C  
ANISOU 1232  CB  LEU A 203    15244   9558   8677   1023    236     28       C  
ATOM   1233  CG  LEU A 203      38.516 -24.767  93.603  1.00 94.31           C  
ANISOU 1233  CG  LEU A 203    16111  10364   9359   1238    372     44       C  
ATOM   1234  CD1 LEU A 203      39.227 -26.086  93.862  1.00 96.36           C  
ANISOU 1234  CD1 LEU A 203    16627  10508   9477   1521    499     64       C  
ATOM   1235  CD2 LEU A 203      37.953 -24.739  92.197  1.00 97.50           C  
ANISOU 1235  CD2 LEU A 203    16721  10654   9669   1092    364      0       C  
ATOM   1236  N   ASP A 204      35.995 -24.207  97.316  1.00 87.87           N  
ANISOU 1236  N   ASP A 204    14983   9562   8841    782     61     38       N  
ATOM   1237  CA  ASP A 204      34.770 -24.148  98.111  1.00 87.36           C  
ANISOU 1237  CA  ASP A 204    14897   9463   8833    581    -17     30       C  
ATOM   1238  C   ASP A 204      34.989 -23.851  99.595  1.00 90.10           C  
ANISOU 1238  C   ASP A 204    15093   9885   9254    637    -29     54       C  
ATOM   1239  O   ASP A 204      35.628 -24.627 100.313  1.00 90.17           O  
ANISOU 1239  O   ASP A 204    15208   9851   9202    795     12     72       O  
ATOM   1240  CB  ASP A 204      33.939 -25.427  97.925  1.00 90.89           C  
ANISOU 1240  CB  ASP A 204    15674   9708   9151    458    -20      8       C  
ATOM   1241  CG  ASP A 204      32.821 -25.310  96.902  1.00105.87           C  
ANISOU 1241  CG  ASP A 204    17627  11577  11023    211    -92     -8       C  
ATOM   1242  OD1 ASP A 204      33.096 -24.852  95.764  1.00107.11           O  
ANISOU 1242  OD1 ASP A 204    17769  11766  11162    231    -91    -19       O  
ATOM   1243  OD2 ASP A 204      31.685 -25.725  97.217  1.00113.51           O  
ANISOU 1243  OD2 ASP A 204    18657  12498  11974    -10   -152     -2       O  
ATOM   1244  N   TYR A 205      34.428 -22.712 100.037  1.00 85.25           N  
ANISOU 1244  N   TYR A 205    14255   9377   8759    517    -84     59       N  
ATOM   1245  CA  TYR A 205      34.443 -22.220 101.414  1.00 84.23           C  
ANISOU 1245  CA  TYR A 205    14000   9311   8694    524   -101     75       C  
ATOM   1246  C   TYR A 205      33.039 -22.282 101.985  1.00 86.64           C  
ANISOU 1246  C   TYR A 205    14325   9568   9027    353   -121     75       C  
ATOM   1247  O   TYR A 205      32.059 -22.102 101.256  1.00 86.45           O  
ANISOU 1247  O   TYR A 205    14282   9543   9021    213   -147     75       O  
ATOM   1248  CB  TYR A 205      34.941 -20.766 101.472  1.00 84.78           C  
ANISOU 1248  CB  TYR A 205    13835   9527   8852    526   -128     84       C  
ATOM   1249  CG  TYR A 205      36.446 -20.645 101.457  1.00 87.41           C  
ANISOU 1249  CG  TYR A 205    14084   9967   9161    676   -114    109       C  
ATOM   1250  CD1 TYR A 205      37.178 -20.668 102.639  1.00 89.80           C  
ANISOU 1250  CD1 TYR A 205    14330  10338   9450    755   -133    138       C  
ATOM   1251  CD2 TYR A 205      37.143 -20.513 100.259  1.00 88.71           C  
ANISOU 1251  CD2 TYR A 205    14211  10188   9307    733    -81    116       C  
ATOM   1252  CE1 TYR A 205      38.568 -20.573 102.630  1.00 91.65           C  
ANISOU 1252  CE1 TYR A 205    14439  10723   9659    883   -133    184       C  
ATOM   1253  CE2 TYR A 205      38.532 -20.405 100.238  1.00 90.39           C  
ANISOU 1253  CE2 TYR A 205    14300  10545   9497    868    -57    160       C  
ATOM   1254  CZ  TYR A 205      39.242 -20.442 101.427  1.00 97.32           C  
ANISOU 1254  CZ  TYR A 205    15089  11519  10368    941    -89    200       C  
ATOM   1255  OH  TYR A 205      40.614 -20.358 101.421  1.00 97.58           O  
ANISOU 1255  OH  TYR A 205    14957  11745  10375   1067    -77    266       O  
ATOM   1256  N   GLY A 206      32.953 -22.497 103.289  1.00 81.91           N  
ANISOU 1256  N   GLY A 206    13745   8951   8425    367   -109     86       N  
ATOM   1257  CA  GLY A 206      31.673 -22.539 103.978  1.00 81.10           C  
ANISOU 1257  CA  GLY A 206    13641   8829   8345    220   -101     99       C  
ATOM   1258  C   GLY A 206      31.135 -21.169 104.329  1.00 82.32           C  
ANISOU 1258  C   GLY A 206    13587   9090   8599    183   -104    110       C  
ATOM   1259  O   GLY A 206      31.516 -20.164 103.721  1.00 81.54           O  
ANISOU 1259  O   GLY A 206    13367   9062   8553    217   -126    105       O  
ATOM   1260  N   PHE A 207      30.213 -21.130 105.292  1.00 77.15           N  
ANISOU 1260  N   PHE A 207    12917   8438   7958    116    -66    132       N  
ATOM   1261  CA  PHE A 207      29.603 -19.889 105.737  1.00 75.68           C  
ANISOU 1261  CA  PHE A 207    12578   8332   7844    116    -36    151       C  
ATOM   1262  C   PHE A 207      30.348 -19.392 106.966  1.00 77.66           C  
ANISOU 1262  C   PHE A 207    12868   8566   8074    208    -17    133       C  
ATOM   1263  O   PHE A 207      30.409 -20.101 107.978  1.00 77.92           O  
ANISOU 1263  O   PHE A 207    13015   8544   8048    213     10    136       O  
ATOM   1264  CB  PHE A 207      28.105 -20.098 106.017  1.00 78.28           C  
ANISOU 1264  CB  PHE A 207    12849   8703   8191     -1     13    201       C  
ATOM   1265  CG  PHE A 207      27.319 -18.829 106.229  1.00 79.94           C  
ANISOU 1265  CG  PHE A 207    12892   9009   8471     40     63    239       C  
ATOM   1266  CD1 PHE A 207      27.114 -17.935 105.183  1.00 83.01           C  
ANISOU 1266  CD1 PHE A 207    13157   9467   8917     68     27    255       C  
ATOM   1267  CD2 PHE A 207      26.754 -18.542 107.465  1.00 82.46           C  
ANISOU 1267  CD2 PHE A 207    13206   9340   8785     72    160    264       C  
ATOM   1268  CE1 PHE A 207      26.390 -16.759 105.383  1.00 84.39           C  
ANISOU 1268  CE1 PHE A 207    13212   9712   9140    150     87    299       C  
ATOM   1269  CE2 PHE A 207      26.019 -17.371 107.660  1.00 85.77           C  
ANISOU 1269  CE2 PHE A 207    13504   9833   9251    155    234    304       C  
ATOM   1270  CZ  PHE A 207      25.843 -16.489 106.619  1.00 83.94           C  
ANISOU 1270  CZ  PHE A 207    13158   9662   9075    204    196    324       C  
ATOM   1271  N   MET A 208      30.957 -18.194 106.863  1.00 71.88           N  
ANISOU 1271  N   MET A 208    12067   7872   7370    263    -39    117       N  
ATOM   1272  CA  MET A 208      31.729 -17.603 107.961  1.00 70.68           C  
ANISOU 1272  CA  MET A 208    11967   7712   7176    309    -47    101       C  
ATOM   1273  C   MET A 208      30.957 -16.554 108.756  1.00 71.80           C  
ANISOU 1273  C   MET A 208    12121   7835   7322    309     23    106       C  
ATOM   1274  O   MET A 208      30.967 -15.370 108.405  1.00 70.97           O  
ANISOU 1274  O   MET A 208    11986   7738   7240    320     25    100       O  
ATOM   1275  CB  MET A 208      33.063 -17.028 107.471  1.00 72.69           C  
ANISOU 1275  CB  MET A 208    12177   8019   7422    334   -121     87       C  
ATOM   1276  CG  MET A 208      34.118 -18.058 107.218  1.00 76.28           C  
ANISOU 1276  CG  MET A 208    12645   8502   7835    395   -167     95       C  
ATOM   1277  SD  MET A 208      35.146 -17.542 105.833  1.00 80.01           S  
ANISOU 1277  SD  MET A 208    12994   9071   8334    412   -209     98       S  
ATOM   1278  CE  MET A 208      34.118 -18.048 104.459  1.00 76.24           C  
ANISOU 1278  CE  MET A 208    12526   8541   7903    381   -172     91       C  
ATOM   1279  N   GLN A 209      30.308 -16.993 109.841  1.00 66.76           N  
ANISOU 1279  N   GLN A 209    11559   7160   6646    306     93    119       N  
ATOM   1280  CA  GLN A 209      29.571 -16.113 110.740  1.00 66.23           C  
ANISOU 1280  CA  GLN A 209    11540   7066   6560    337    192    127       C  
ATOM   1281  C   GLN A 209      30.594 -15.363 111.590  1.00 68.39           C  
ANISOU 1281  C   GLN A 209    11953   7286   6747    348    150     89       C  
ATOM   1282  O   GLN A 209      31.646 -15.916 111.911  1.00 67.41           O  
ANISOU 1282  O   GLN A 209    11875   7168   6570    328     57     75       O  
ATOM   1283  CB  GLN A 209      28.639 -16.926 111.649  1.00 68.34           C  
ANISOU 1283  CB  GLN A 209    11851   7319   6794    319    289    159       C  
ATOM   1284  CG  GLN A 209      27.469 -17.579 110.927  1.00 81.06           C  
ANISOU 1284  CG  GLN A 209    13320   9006   8471    256    330    213       C  
ATOM   1285  CD  GLN A 209      26.534 -18.321 111.854  1.00 98.72           C  
ANISOU 1285  CD  GLN A 209    15590  11251  10670    205    440    257       C  
ATOM   1286  OE1 GLN A 209      25.324 -18.086 111.867  1.00 93.68           O  
ANISOU 1286  OE1 GLN A 209    14817  10707  10070    197    542    321       O  
ATOM   1287  NE2 GLN A 209      27.061 -19.266 112.619  1.00 90.46           N  
ANISOU 1287  NE2 GLN A 209    14712  10120   9540    171    424    238       N  
ATOM   1288  N   SER A 210      30.298 -14.109 111.943  1.00 64.57           N  
ANISOU 1288  N   SER A 210    11548   6752   6234    380    214     79       N  
ATOM   1289  CA  SER A 210      31.199 -13.302 112.756  1.00 64.53           C  
ANISOU 1289  CA  SER A 210    11719   6679   6119    344    165     41       C  
ATOM   1290  C   SER A 210      31.195 -13.794 114.220  1.00 69.69           C  
ANISOU 1290  C   SER A 210    12537   7278   6663    340    197     35       C  
ATOM   1291  O   SER A 210      30.148 -13.752 114.876  1.00 69.61           O  
ANISOU 1291  O   SER A 210    12599   7218   6630    401    342     50       O  
ATOM   1292  CB  SER A 210      30.836 -11.824 112.647  1.00 67.77           C  
ANISOU 1292  CB  SER A 210    12235   7010   6503    378    235     29       C  
ATOM   1293  OG  SER A 210      31.615 -11.003 113.499  1.00 75.24           O  
ANISOU 1293  OG  SER A 210    13413   7864   7311    305    192    -11       O  
ATOM   1294  N   PRO A 211      32.341 -14.310 114.738  1.00 67.14           N  
ANISOU 1294  N   PRO A 211    12264   6981   6267    281     67     26       N  
ATOM   1295  CA  PRO A 211      32.366 -14.780 116.135  1.00 67.95           C  
ANISOU 1295  CA  PRO A 211    12545   7027   6246    277     83     26       C  
ATOM   1296  C   PRO A 211      32.271 -13.647 117.159  1.00 74.11           C  
ANISOU 1296  C   PRO A 211    13575   7694   6891    249    134     -7       C  
ATOM   1297  O   PRO A 211      31.939 -13.903 118.318  1.00 75.65           O  
ANISOU 1297  O   PRO A 211    13947   7818   6979    264    200     -7       O  
ATOM   1298  CB  PRO A 211      33.712 -15.495 116.238  1.00 69.61           C  
ANISOU 1298  CB  PRO A 211    12716   7322   6411    241    -92     41       C  
ATOM   1299  CG  PRO A 211      34.576 -14.793 115.260  1.00 73.89           C  
ANISOU 1299  CG  PRO A 211    13123   7950   7001    187   -196     35       C  
ATOM   1300  CD  PRO A 211      33.669 -14.460 114.103  1.00 68.47           C  
ANISOU 1300  CD  PRO A 211    12319   7249   6447    228    -94     29       C  
ATOM   1301  N   GLN A 212      32.565 -12.403 116.732  1.00 70.27           N  
ANISOU 1301  N   GLN A 212    13138   7173   6389    203    109    -34       N  
ATOM   1302  CA  GLN A 212      32.544 -11.210 117.577  1.00 71.06           C  
ANISOU 1302  CA  GLN A 212    13538   7129   6334    163    155    -73       C  
ATOM   1303  C   GLN A 212      31.163 -10.576 117.727  1.00 74.93           C  
ANISOU 1303  C   GLN A 212    14139   7503   6826    313    387    -71       C  
ATOM   1304  O   GLN A 212      30.910  -9.944 118.750  1.00 76.40           O  
ANISOU 1304  O   GLN A 212    14626   7546   6857    331    480    -98       O  
ATOM   1305  CB  GLN A 212      33.564 -10.165 117.083  1.00 72.66           C  
ANISOU 1305  CB  GLN A 212    13794   7327   6486     16     19    -98       C  
ATOM   1306  CG  GLN A 212      35.008 -10.680 117.000  1.00 86.15           C  
ANISOU 1306  CG  GLN A 212    15368   9194   8172   -134   -207    -79       C  
ATOM   1307  CD  GLN A 212      35.765 -10.743 118.308  1.00107.12           C  
ANISOU 1307  CD  GLN A 212    18218  11841  10639   -254   -325    -83       C  
ATOM   1308  OE1 GLN A 212      35.205 -10.882 119.408  1.00102.34           O  
ANISOU 1308  OE1 GLN A 212    17843  11116   9925   -208   -236   -101       O  
ATOM   1309  NE2 GLN A 212      37.083 -10.681 118.203  1.00101.93           N  
ANISOU 1309  NE2 GLN A 212    17457  11338   9934   -412   -533    -55       N  
ATOM   1310  N   ASN A 213      30.270 -10.744 116.737  1.00 70.07           N  
ANISOU 1310  N   ASN A 213    13292   6960   6372    429    483    -31       N  
ATOM   1311  CA  ASN A 213      28.944 -10.127 116.795  1.00 70.68           C  
ANISOU 1311  CA  ASN A 213    13415   6980   6461    605    704     -1       C  
ATOM   1312  C   ASN A 213      27.779 -11.071 116.463  1.00 73.59           C  
ANISOU 1312  C   ASN A 213    13510   7486   6965    700    817     70       C  
ATOM   1313  O   ASN A 213      26.725 -10.975 117.096  1.00 73.58           O  
ANISOU 1313  O   ASN A 213    13551   7474   6933    827   1013    111       O  
ATOM   1314  CB  ASN A 213      28.892  -8.863 115.913  1.00 71.81           C  
ANISOU 1314  CB  ASN A 213    13603   7061   6621    658    722     -5       C  
ATOM   1315  CG  ASN A 213      29.328  -9.060 114.472  1.00 86.51           C  
ANISOU 1315  CG  ASN A 213    15201   9042   8628    595    584      9       C  
ATOM   1316  OD1 ASN A 213      28.636  -9.684 113.662  1.00 75.45           O  
ANISOU 1316  OD1 ASN A 213    13529   7769   7370    662    611     61       O  
ATOM   1317  ND2 ASN A 213      30.479  -8.510 114.113  1.00 76.77           N  
ANISOU 1317  ND2 ASN A 213    14049   7775   7347    448    435    -32       N  
ATOM   1318  N   GLY A 214      27.971 -11.946 115.473  1.00 69.08           N  
ANISOU 1318  N   GLY A 214    12674   7045   6527    630    699     91       N  
ATOM   1319  CA  GLY A 214      26.953 -12.885 115.006  1.00 68.62           C  
ANISOU 1319  CA  GLY A 214    12365   7122   6586    654    766    158       C  
ATOM   1320  C   GLY A 214      25.852 -12.222 114.198  1.00 73.16           C  
ANISOU 1320  C   GLY A 214    12774   7775   7249    783    877    224       C  
ATOM   1321  O   GLY A 214      24.788 -12.815 113.997  1.00 73.76           O  
ANISOU 1321  O   GLY A 214    12645   7984   7395    807    964    301       O  
ATOM   1322  N   ILE A 215      26.099 -10.979 113.733  1.00 69.37           N  
ANISOU 1322  N   ILE A 215    12387   7219   6752    861    871    205       N  
ATOM   1323  CA  ILE A 215      25.156 -10.174 112.950  1.00 69.99           C  
ANISOU 1323  CA  ILE A 215    12345   7354   6894   1024    968    274       C  
ATOM   1324  C   ILE A 215      25.637 -10.032 111.493  1.00 73.37           C  
ANISOU 1324  C   ILE A 215    12631   7832   7415    960    810    270       C  
ATOM   1325  O   ILE A 215      24.923  -9.482 110.648  1.00 73.20           O  
ANISOU 1325  O   ILE A 215    12474   7882   7455   1078    849    338       O  
ATOM   1326  CB  ILE A 215      24.834  -8.810 113.642  1.00 74.84           C  
ANISOU 1326  CB  ILE A 215    13238   7812   7386   1216   1138    273       C  
ATOM   1327  CG1 ILE A 215      25.951  -7.773 113.458  1.00 74.91           C  
ANISOU 1327  CG1 ILE A 215    13524   7634   7303   1153   1036    192       C  
ATOM   1328  CG2 ILE A 215      24.482  -8.982 115.123  1.00 76.87           C  
ANISOU 1328  CG2 ILE A 215    13683   7999   7523   1266   1295    265       C  
ATOM   1329  CD1 ILE A 215      25.476  -6.523 112.895  1.00 82.61           C  
ANISOU 1329  CD1 ILE A 215    14585   8540   8264   1338   1126    232       C  
ATOM   1330  N   PHE A 216      26.859 -10.545 111.218  1.00 69.31           N  
ANISOU 1330  N   PHE A 216    12141   7293   6899    786    638    202       N  
ATOM   1331  CA  PHE A 216      27.512 -10.571 109.908  1.00 67.98           C  
ANISOU 1331  CA  PHE A 216    11859   7170   6800    703    491    189       C  
ATOM   1332  C   PHE A 216      27.945 -11.991 109.566  1.00 71.91           C  
ANISOU 1332  C   PHE A 216    12213   7759   7352    574    380    178       C  
ATOM   1333  O   PHE A 216      28.337 -12.759 110.452  1.00 71.11           O  
ANISOU 1333  O   PHE A 216    12181   7637   7202    517    369    152       O  
ATOM   1334  CB  PHE A 216      28.736  -9.644 109.864  1.00 69.30           C  
ANISOU 1334  CB  PHE A 216    12226   7219   6887    631    408    125       C  
ATOM   1335  CG  PHE A 216      28.466  -8.185 110.131  1.00 72.21           C  
ANISOU 1335  CG  PHE A 216    12824   7444   7169    737    508    124       C  
ATOM   1336  CD1 PHE A 216      27.658  -7.442 109.279  1.00 75.96           C  
ANISOU 1336  CD1 PHE A 216    13245   7926   7690    885    576    184       C  
ATOM   1337  CD2 PHE A 216      29.063  -7.537 111.208  1.00 75.24           C  
ANISOU 1337  CD2 PHE A 216    13511   7672   7404    686    524     68       C  
ATOM   1338  CE1 PHE A 216      27.430  -6.081 109.515  1.00 78.54           C  
ANISOU 1338  CE1 PHE A 216    13838   8088   7915   1013    682    188       C  
ATOM   1339  CE2 PHE A 216      28.836  -6.177 111.442  1.00 79.45           C  
ANISOU 1339  CE2 PHE A 216    14332   8029   7826    778    624     62       C  
ATOM   1340  CZ  PHE A 216      28.034  -5.454 110.586  1.00 78.22           C  
ANISOU 1340  CZ  PHE A 216    14139   7863   7717    955    711    121       C  
ATOM   1341  N   GLY A 217      27.878 -12.316 108.280  1.00 68.86           N  
ANISOU 1341  N   GLY A 217    11663   7455   7044    538    304    200       N  
ATOM   1342  CA  GLY A 217      28.255 -13.621 107.757  1.00 68.08           C  
ANISOU 1342  CA  GLY A 217    11474   7415   6977    432    211    190       C  
ATOM   1343  C   GLY A 217      28.566 -13.568 106.280  1.00 71.57           C  
ANISOU 1343  C   GLY A 217    11823   7902   7469    398    120    193       C  
ATOM   1344  O   GLY A 217      27.751 -13.082 105.496  1.00 71.31           O  
ANISOU 1344  O   GLY A 217    11688   7924   7481    437    134    243       O  
ATOM   1345  N   VAL A 218      29.754 -14.048 105.887  1.00 67.77           N  
ANISOU 1345  N   VAL A 218    11371   7409   6968    340     31    150       N  
ATOM   1346  CA  VAL A 218      30.158 -14.056 104.477  1.00 67.13           C  
ANISOU 1346  CA  VAL A 218    11227   7365   6916    310    -38    150       C  
ATOM   1347  C   VAL A 218      30.473 -15.476 103.978  1.00 71.15           C  
ANISOU 1347  C   VAL A 218    11727   7893   7415    260    -86    139       C  
ATOM   1348  O   VAL A 218      30.383 -16.455 104.728  1.00 71.33           O  
ANISOU 1348  O   VAL A 218    11801   7892   7408    246    -70    135       O  
ATOM   1349  CB  VAL A 218      31.314 -13.051 104.152  1.00 70.69           C  
ANISOU 1349  CB  VAL A 218    11726   7794   7340    301    -77    122       C  
ATOM   1350  CG1 VAL A 218      30.958 -11.628 104.558  1.00 71.20           C  
ANISOU 1350  CG1 VAL A 218    11876   7794   7384    342    -25    129       C  
ATOM   1351  CG2 VAL A 218      32.647 -13.476 104.765  1.00 70.30           C  
ANISOU 1351  CG2 VAL A 218    11715   7756   7238    267   -123     90       C  
ATOM   1352  N   SER A 219      30.836 -15.561 102.698  1.00 66.95           N  
ANISOU 1352  N   SER A 219    11165   7383   6889    240   -134    137       N  
ATOM   1353  CA  SER A 219      31.313 -16.752 102.019  1.00 66.53           C  
ANISOU 1353  CA  SER A 219    11158   7320   6800    218   -166    122       C  
ATOM   1354  C   SER A 219      32.365 -16.269 101.033  1.00 70.60           C  
ANISOU 1354  C   SER A 219    11659   7861   7304    242   -191    108       C  
ATOM   1355  O   SER A 219      32.210 -15.183 100.455  1.00 70.70           O  
ANISOU 1355  O   SER A 219    11625   7894   7343    230   -200    121       O  
ATOM   1356  CB  SER A 219      30.187 -17.457 101.278  1.00 69.96           C  
ANISOU 1356  CB  SER A 219    11588   7761   7234    133   -186    148       C  
ATOM   1357  OG  SER A 219      30.678 -18.638 100.664  1.00 77.85           O  
ANISOU 1357  OG  SER A 219    12705   8707   8166    111   -206    125       O  
ATOM   1358  N   LEU A 220      33.443 -17.047 100.855  1.00 66.28           N  
ANISOU 1358  N   LEU A 220    11157   7318   6710    290   -191     93       N  
ATOM   1359  CA  LEU A 220      34.500 -16.662  99.923  1.00 65.29           C  
ANISOU 1359  CA  LEU A 220    10995   7245   6565    318   -192     93       C  
ATOM   1360  C   LEU A 220      34.401 -17.431  98.611  1.00 68.59           C  
ANISOU 1360  C   LEU A 220    11490   7632   6940    323   -185     88       C  
ATOM   1361  O   LEU A 220      34.296 -18.662  98.617  1.00 67.84           O  
ANISOU 1361  O   LEU A 220    11514   7474   6790    353   -169     77       O  
ATOM   1362  CB  LEU A 220      35.901 -16.758 100.558  1.00 65.28           C  
ANISOU 1362  CB  LEU A 220    10949   7320   6534    387   -187    101       C  
ATOM   1363  CG  LEU A 220      36.129 -16.020 101.894  1.00 68.94           C  
ANISOU 1363  CG  LEU A 220    11375   7811   7008    352   -213    104       C  
ATOM   1364  CD1 LEU A 220      37.579 -16.055 102.280  1.00 69.35           C  
ANISOU 1364  CD1 LEU A 220    11344   7985   7018    390   -237    131       C  
ATOM   1365  CD2 LEU A 220      35.667 -14.569 101.839  1.00 70.65           C  
ANISOU 1365  CD2 LEU A 220    11582   8006   7257    261   -222     99       C  
ATOM   1366  N   ASP A 221      34.381 -16.686  97.489  1.00 65.69           N  
ANISOU 1366  N   ASP A 221    11095   7288   6578    284   -195     95       N  
ATOM   1367  CA  ASP A 221      34.280 -17.225  96.127  1.00 66.26           C  
ANISOU 1367  CA  ASP A 221    11262   7326   6588    272   -193     90       C  
ATOM   1368  C   ASP A 221      35.481 -18.127  95.818  1.00 69.96           C  
ANISOU 1368  C   ASP A 221    11804   7797   6979    389   -125     80       C  
ATOM   1369  O   ASP A 221      35.295 -19.249  95.355  1.00 70.29           O  
ANISOU 1369  O   ASP A 221    12017   7750   6940    411   -105     63       O  
ATOM   1370  CB  ASP A 221      34.123 -16.090  95.088  1.00 68.51           C  
ANISOU 1370  CB  ASP A 221    11504   7642   6885    218   -216    108       C  
ATOM   1371  CG  ASP A 221      32.926 -15.154  95.290  1.00 84.32           C  
ANISOU 1371  CG  ASP A 221    13440   9647   8951    158   -270    136       C  
ATOM   1372  OD1 ASP A 221      32.251 -15.258  96.345  1.00 86.62           O  
ANISOU 1372  OD1 ASP A 221    13693   9932   9286    154   -277    142       O  
ATOM   1373  OD2 ASP A 221      32.680 -14.301  94.406  1.00 89.80           O  
ANISOU 1373  OD2 ASP A 221    14126  10351   9642    134   -293    161       O  
ATOM   1374  N   PHE A 222      36.698 -17.664  96.166  1.00 65.84           N  
ANISOU 1374  N   PHE A 222    11162   7382   6471    465    -87    100       N  
ATOM   1375  CA  PHE A 222      37.970 -18.376  95.992  1.00 66.02           C  
ANISOU 1375  CA  PHE A 222    11186   7468   6429    620     -9    120       C  
ATOM   1376  C   PHE A 222      39.056 -17.670  96.802  1.00 70.38           C  
ANISOU 1376  C   PHE A 222    11534   8189   7020    641    -13    162       C  
ATOM   1377  O   PHE A 222      39.007 -16.450  96.965  1.00 69.92           O  
ANISOU 1377  O   PHE A 222    11375   8181   7011    512    -58    167       O  
ATOM   1378  CB  PHE A 222      38.364 -18.377  94.499  1.00 68.00           C  
ANISOU 1378  CB  PHE A 222    11500   7725   6612    649     56    123       C  
ATOM   1379  CG  PHE A 222      39.664 -19.035  94.094  1.00 70.26           C  
ANISOU 1379  CG  PHE A 222    11780   8097   6820    841    173    158       C  
ATOM   1380  CD1 PHE A 222      39.712 -20.395  93.800  1.00 74.15           C  
ANISOU 1380  CD1 PHE A 222    12494   8472   7206    997    247    144       C  
ATOM   1381  CD2 PHE A 222      40.815 -18.279  93.906  1.00 72.13           C  
ANISOU 1381  CD2 PHE A 222    11806   8528   7071    865    220    213       C  
ATOM   1382  CE1 PHE A 222      40.902 -20.996  93.378  1.00 76.44           C  
ANISOU 1382  CE1 PHE A 222    12789   8843   7411   1227    383    189       C  
ATOM   1383  CE2 PHE A 222      42.005 -18.879  93.489  1.00 76.55           C  
ANISOU 1383  CE2 PHE A 222    12320   9208   7557   1067    346    266       C  
ATOM   1384  CZ  PHE A 222      42.041 -20.234  93.225  1.00 75.88           C  
ANISOU 1384  CZ  PHE A 222    12453   9007   7371   1273    435    255       C  
ATOM   1385  N   ALA A 223      40.043 -18.432  97.289  1.00 67.55           N  
ANISOU 1385  N   ALA A 223    11130   7917   6619    802     29    200       N  
ATOM   1386  CA  ALA A 223      41.221 -17.903  97.980  1.00 67.91           C  
ANISOU 1386  CA  ALA A 223    10954   8172   6678    818     12    261       C  
ATOM   1387  C   ALA A 223      42.424 -18.755  97.600  1.00 74.00           C  
ANISOU 1387  C   ALA A 223    11659   9079   7378   1046    109    327       C  
ATOM   1388  O   ALA A 223      42.335 -19.989  97.575  1.00 74.06           O  
ANISOU 1388  O   ALA A 223    11832   8984   7324   1234    167    323       O  
ATOM   1389  CB  ALA A 223      41.018 -17.874  99.481  1.00 68.13           C  
ANISOU 1389  CB  ALA A 223    10958   8194   6732    780    -74    260       C  
ATOM   1390  N   ALA A 224      43.520 -18.095  97.223  1.00 72.25           N  
ANISOU 1390  N   ALA A 224    11216   9083   7153   1033    141    395       N  
ATOM   1391  CA  ALA A 224      44.726 -18.778  96.774  1.00 74.66           C  
ANISOU 1391  CA  ALA A 224    11405   9572   7391   1271    257    482       C  
ATOM   1392  C   ALA A 224      45.877 -18.615  97.751  1.00 81.15           C  
ANISOU 1392  C   ALA A 224    11936  10683   8215   1316    206    588       C  
ATOM   1393  O   ALA A 224      45.906 -17.636  98.501  1.00 79.67           O  
ANISOU 1393  O   ALA A 224    11621  10576   8073   1085     81    592       O  
ATOM   1394  CB  ALA A 224      45.123 -18.273  95.400  1.00 76.05           C  
ANISOU 1394  CB  ALA A 224    11532   9823   7541   1235    359    499       C  
ATOM   1395  N   ASN A 225      46.828 -19.587  97.733  1.00 81.29           N  
ANISOU 1395  N   ASN A 225    11864  10856   8166   1622    303    682       N  
ATOM   1396  CA  ASN A 225      48.022 -19.649  98.585  1.00 83.77           C  
ANISOU 1396  CA  ASN A 225    11870  11497   8463   1730    260    817       C  
ATOM   1397  C   ASN A 225      47.630 -19.715 100.087  1.00 88.16           C  
ANISOU 1397  C   ASN A 225    12465  11994   9039   1656     95    799       C  
ATOM   1398  O   ASN A 225      47.994 -18.847 100.887  1.00 87.80           O  
ANISOU 1398  O   ASN A 225    12217  12128   9017   1441    -43    840       O  
ATOM   1399  CB  ASN A 225      49.008 -18.510  98.234  1.00 85.52           C  
ANISOU 1399  CB  ASN A 225    11736  12054   8702   1537    248    909       C  
ATOM   1400  CG  ASN A 225      50.339 -18.578  98.929  1.00113.23           C  
ANISOU 1400  CG  ASN A 225    14869  15970  12183   1624    198   1075       C  
ATOM   1401  OD1 ASN A 225      51.036 -19.600  98.917  1.00109.73           O  
ANISOU 1401  OD1 ASN A 225    14339  15668  11683   1986    290   1177       O  
ATOM   1402  ND2 ASN A 225      50.723 -17.474  99.546  1.00107.23           N  
ANISOU 1402  ND2 ASN A 225    13889  15407  11446   1291     48   1114       N  
ATOM   1403  N   VAL A 226      46.844 -20.757 100.439  1.00 84.93           N  
ANISOU 1403  N   VAL A 226    12356  11313   8602   1812    114    735       N  
ATOM   1404  CA  VAL A 226      46.331 -21.020 101.797  1.00 84.25           C  
ANISOU 1404  CA  VAL A 226    12377  11118   8518   1770    -10    709       C  
ATOM   1405  C   VAL A 226      47.073 -22.179 102.480  1.00 90.84           C  
ANISOU 1405  C   VAL A 226    13196  12051   9268   2105      6    814       C  
ATOM   1406  O   VAL A 226      47.640 -23.033 101.795  1.00 92.49           O  
ANISOU 1406  O   VAL A 226    13428  12303   9412   2416    148    877       O  
ATOM   1407  CB  VAL A 226      44.783 -21.209 101.862  1.00 85.61           C  
ANISOU 1407  CB  VAL A 226    12888  10921   8717   1639    -20    570       C  
ATOM   1408  CG1 VAL A 226      44.053 -19.881 101.700  1.00 83.56           C  
ANISOU 1408  CG1 VAL A 226    12602  10607   8541   1308    -88    492       C  
ATOM   1409  CG2 VAL A 226      44.284 -22.237 100.846  1.00 85.38           C  
ANISOU 1409  CG2 VAL A 226    13137  10670   8635   1808    118    522       C  
ATOM   1410  N   LYS A 227      47.063 -22.204 103.828  1.00 87.45           N  
ANISOU 1410  N   LYS A 227    12753  11647   8826   2058   -131    837       N  
ATOM   1411  CA  LYS A 227      47.713 -23.241 104.631  1.00 89.36           C  
ANISOU 1411  CA  LYS A 227    12993  11979   8980   2364   -144    945       C  
ATOM   1412  C   LYS A 227      46.681 -24.075 105.418  1.00 92.88           C  
ANISOU 1412  C   LYS A 227    13817  12089   9385   2402   -159    867       C  
ATOM   1413  O   LYS A 227      45.580 -23.589 105.692  1.00 90.40           O  
ANISOU 1413  O   LYS A 227    13658  11565   9123   2128   -211    750       O  
ATOM   1414  CB  LYS A 227      48.762 -22.614 105.564  1.00 93.28           C  
ANISOU 1414  CB  LYS A 227    13125  12851   9465   2290   -305   1074       C  
ATOM   1415  N   THR A 228      47.027 -25.339 105.753  1.00 91.51           N  
ANISOU 1415  N   THR A 228    13799  11863   9106   2752    -99    940       N  
ATOM   1416  CA  THR A 228      46.161 -26.259 106.509  1.00 90.66           C  
ANISOU 1416  CA  THR A 228    14076  11440   8933   2803    -99    885       C  
ATOM   1417  C   THR A 228      46.874 -26.849 107.735  1.00 95.53           C  
ANISOU 1417  C   THR A 228    14659  12185   9454   3031   -185   1011       C  
ATOM   1418  O   THR A 228      47.947 -27.443 107.602  1.00 97.70           O  
ANISOU 1418  O   THR A 228    14811  12656   9655   3386   -135   1151       O  
ATOM   1419  CB  THR A 228      45.547 -27.349 105.605  1.00101.15           C  
ANISOU 1419  CB  THR A 228    15794  12445  10192   2964     73    820       C  
ATOM   1420  OG1 THR A 228      46.584 -28.037 104.901  1.00104.59           O  
ANISOU 1420  OG1 THR A 228    16186  13007  10547   3347    206    925       O  
ATOM   1421  CG2 THR A 228      44.511 -26.800 104.626  1.00 97.47           C  
ANISOU 1421  CG2 THR A 228    15425  11801   9808   2667    111    681       C  
ATOM   1422  N   ASP A 229      46.264 -26.685 108.923  1.00 90.54           N  
ANISOU 1422  N   ASP A 229    14139  11446   8814   2841   -307    971       N  
ATOM   1423  CA  ASP A 229      46.765 -27.156 110.222  1.00 91.86           C  
ANISOU 1423  CA  ASP A 229    14315  11705   8882   2995   -418   1077       C  
ATOM   1424  C   ASP A 229      46.755 -28.691 110.405  1.00 97.77           C  
ANISOU 1424  C   ASP A 229    15426  12231   9491   3364   -315   1127       C  
ATOM   1425  O   ASP A 229      46.009 -29.392 109.716  1.00 96.83           O  
ANISOU 1425  O   ASP A 229    15649  11795   9349   3397   -170   1038       O  
ATOM   1426  CB  ASP A 229      45.993 -26.484 111.348  1.00 90.76           C  
ANISOU 1426  CB  ASP A 229    14244  11476   8762   2660   -553   1000       C  
ATOM   1427  N   THR A 230      47.594 -29.195 111.352  1.00 96.83           N  
ANISOU 1427  N   THR A 230    15247  12279   9264   3630   -399   1276       N  
ATOM   1428  CA  THR A 230      47.789 -30.607 111.732  1.00118.96           C  
ANISOU 1428  CA  THR A 230    18385  14907  11906   4029   -324   1361       C  
ATOM   1429  C   THR A 230      48.032 -31.549 110.556  1.00136.80           C  
ANISOU 1429  C   THR A 230    20849  17026  14103   4379   -107   1379       C  
ATOM   1430  O   THR A 230      49.069 -31.463 109.904  1.00 96.12           O  
ANISOU 1430  O   THR A 230    15400  12166   8957   4642    -51   1492       O  
ATOM   1431  CB  THR A 230      46.628 -31.104 112.583  1.00118.37           C  
ANISOU 1431  CB  THR A 230    18751  14456  11769   3859   -337   1263       C  
ATOM   1432  N   GLY A 232      43.325 -30.595 111.547  1.00112.46           N  
ANISOU 1432  N   GLY A 232    18522  13010  11199   3013   -178    853       N  
ATOM   1433  CA  GLY A 232      43.431 -29.201 111.958  1.00110.81           C  
ANISOU 1433  CA  GLY A 232    17931  13058  11113   2756   -312    835       C  
ATOM   1434  C   GLY A 232      42.733 -28.204 111.050  1.00112.19           C  
ANISOU 1434  C   GLY A 232    17962  13228  11436   2456   -281    719       C  
ATOM   1435  O   GLY A 232      42.630 -27.024 111.405  1.00110.53           O  
ANISOU 1435  O   GLY A 232    17512  13169  11315   2218   -376    689       O  
ATOM   1436  N   ARG A 233      42.264 -28.671 109.856  1.00107.96           N  
ANISOU 1436  N   ARG A 233    17601  12510  10908   2470   -152    657       N  
ATOM   1437  CA  ARG A 233      41.532 -27.909 108.821  1.00105.47           C  
ANISOU 1437  CA  ARG A 233    17199  12162  10712   2219   -114    555       C  
ATOM   1438  C   ARG A 233      42.320 -26.702 108.231  1.00106.84           C  
ANISOU 1438  C   ARG A 233    16969  12636  10991   2184   -161    579       C  
ATOM   1439  O   ARG A 233      43.525 -26.602 108.439  1.00107.79           O  
ANISOU 1439  O   ARG A 233    16875  12999  11081   2390   -195    685       O  
ATOM   1440  CB  ARG A 233      40.141 -27.475 109.336  1.00104.81           C  
ANISOU 1440  CB  ARG A 233    17205  11930  10689   1882   -141    461       C  
ATOM   1441  N   LEU A 234      41.637 -25.818 107.468  1.00100.25           N  
ANISOU 1441  N   LEU A 234    16033  11791  10266   1925   -157    493       N  
ATOM   1442  CA  LEU A 234      42.228 -24.640 106.824  1.00 99.05           C  
ANISOU 1442  CA  LEU A 234    15555  11877  10204   1843   -190    505       C  
ATOM   1443  C   LEU A 234      42.419 -23.453 107.779  1.00101.15           C  
ANISOU 1443  C   LEU A 234    15603  12313  10518   1644   -323    515       C  
ATOM   1444  O   LEU A 234      41.719 -23.354 108.792  1.00100.13           O  
ANISOU 1444  O   LEU A 234    15594  12076  10375   1523   -373    482       O  
ATOM   1445  CB  LEU A 234      41.387 -24.219 105.609  1.00 97.52           C  
ANISOU 1445  CB  LEU A 234    15400  11571  10082   1677   -125    416       C  
ATOM   1446  N   GLN A 235      43.370 -22.552 107.440  1.00 96.96           N  
ANISOU 1446  N   GLN A 235    14774  12039  10026   1595   -371    562       N  
ATOM   1447  CA  GLN A 235      43.725 -21.352 108.206  1.00 96.19           C  
ANISOU 1447  CA  GLN A 235    14490  12111   9948   1374   -503    576       C  
ATOM   1448  C   GLN A 235      44.126 -20.222 107.270  1.00 98.95           C  
ANISOU 1448  C   GLN A 235    14623  12612  10363   1217   -502    573       C  
ATOM   1449  O   GLN A 235      44.862 -20.460 106.310  1.00 99.37           O  
ANISOU 1449  O   GLN A 235    14533  12803  10419   1357   -434    628       O  
ATOM   1450  CB  GLN A 235      44.885 -21.655 109.167  1.00 99.83           C  
ANISOU 1450  CB  GLN A 235    14802  12807  10320   1498   -616    699       C  
ATOM   1451  N   PHE A 236      43.661 -18.990 107.550  1.00 94.29           N  
ANISOU 1451  N   PHE A 236    14031  11987   9809    937   -565    513       N  
ATOM   1452  CA  PHE A 236      43.968 -17.821 106.711  1.00 93.71           C  
ANISOU 1452  CA  PHE A 236    13808  12015   9781    748   -568    503       C  
ATOM   1453  C   PHE A 236      45.307 -17.168 107.047  1.00 98.68           C  
ANISOU 1453  C   PHE A 236    14173  12960  10360    639   -683    604       C  
ATOM   1454  O   PHE A 236      45.528 -16.756 108.187  1.00 99.01           O  
ANISOU 1454  O   PHE A 236    14224  13054  10340    495   -811    620       O  
ATOM   1455  CB  PHE A 236      42.834 -16.776 106.752  1.00 93.70           C  
ANISOU 1455  CB  PHE A 236    13973  11805   9823    520   -567    399       C  
ATOM   1456  CG  PHE A 236      41.515 -17.207 106.158  1.00 93.06           C  
ANISOU 1456  CG  PHE A 236    14077  11479   9803    577   -460    318       C  
ATOM   1457  CD1 PHE A 236      41.350 -17.296 104.781  1.00 95.04           C  
ANISOU 1457  CD1 PHE A 236    14304  11706  10100    621   -376    304       C  
ATOM   1458  CD2 PHE A 236      40.424 -17.481 106.974  1.00 94.08           C  
ANISOU 1458  CD2 PHE A 236    14397  11416   9931    561   -447    265       C  
ATOM   1459  CE1 PHE A 236      40.130 -17.692 104.235  1.00 94.71           C  
ANISOU 1459  CE1 PHE A 236    14423  11464  10098    637   -306    241       C  
ATOM   1460  CE2 PHE A 236      39.200 -17.871 106.427  1.00 95.46           C  
ANISOU 1460  CE2 PHE A 236    14703  11412  10157    579   -363    210       C  
ATOM   1461  CZ  PHE A 236      39.061 -17.973 105.062  1.00 93.09           C  
ANISOU 1461  CZ  PHE A 236    14372  11101   9898    608   -305    200       C  
ATOM   1462  N   ASP A 237      46.190 -17.053 106.042  1.00 95.56           N  
ANISOU 1462  N   ASP A 237    13545  12784   9978    688   -638    678       N  
ATOM   1463  CA  ASP A 237      47.506 -16.443 106.209  1.00 97.23           C  
ANISOU 1463  CA  ASP A 237    13450  13351  10141    561   -740    797       C  
ATOM   1464  C   ASP A 237      47.575 -15.062 105.552  1.00 99.07           C  
ANISOU 1464  C   ASP A 237    13636  13614  10393    241   -752    767       C  
ATOM   1465  O   ASP A 237      47.148 -14.913 104.409  1.00 97.31           O  
ANISOU 1465  O   ASP A 237    13467  13278  10228    258   -631    717       O  
ATOM   1466  CB  ASP A 237      48.629 -17.370 105.694  1.00101.44           C  
ANISOU 1466  CB  ASP A 237    13714  14175  10655    856   -674    936       C  
ATOM   1467  CG  ASP A 237      48.551 -17.764 104.228  1.00113.15           C  
ANISOU 1467  CG  ASP A 237    15205  15602  12187   1029   -485    918       C  
ATOM   1468  OD1 ASP A 237      49.597 -17.707 103.543  1.00116.10           O  
ANISOU 1468  OD1 ASP A 237    15296  16269  12546   1098   -428   1030       O  
ATOM   1469  OD2 ASP A 237      47.449 -18.157 103.772  1.00116.99           O  
ANISOU 1469  OD2 ASP A 237    15977  15762  12711   1094   -392    801       O  
ATOM   1470  N   PRO A 238      48.155 -14.048 106.239  1.00 95.78           N  
ANISOU 1470  N   PRO A 238    13137  13347   9907    -66   -904    805       N  
ATOM   1471  CA  PRO A 238      48.242 -12.694 105.651  1.00 94.99           C  
ANISOU 1471  CA  PRO A 238    13045  13247   9798   -396   -914    781       C  
ATOM   1472  C   PRO A 238      49.048 -12.571 104.346  1.00 97.84           C  
ANISOU 1472  C   PRO A 238    13145  13842  10187   -390   -819    862       C  
ATOM   1473  O   PRO A 238      49.120 -11.477 103.774  1.00 98.13           O  
ANISOU 1473  O   PRO A 238    13205  13872  10207   -668   -818    848       O  
ATOM   1474  CB  PRO A 238      48.852 -11.866 106.784  1.00 98.70           C  
ANISOU 1474  CB  PRO A 238    13490  13857  10152   -717  -1110    825       C  
ATOM   1475  CG  PRO A 238      48.514 -12.624 108.027  1.00103.30           C  
ANISOU 1475  CG  PRO A 238    14197  14353  10701   -564  -1183    809       C  
ATOM   1476  CD  PRO A 238      48.680 -14.052 107.617  1.00 98.88           C  
ANISOU 1476  CD  PRO A 238    13484  13882  10204   -157  -1080    867       C  
ATOM   1477  N   ASN A 239      49.610 -13.691 103.855  1.00 92.86           N  
ANISOU 1477  N   ASN A 239    12306  13393   9585    -62   -721    947       N  
ATOM   1478  CA  ASN A 239      50.368 -13.752 102.603  1.00 93.00           C  
ANISOU 1478  CA  ASN A 239    12082  13634   9618     13   -592   1031       C  
ATOM   1479  C   ASN A 239      49.531 -14.379 101.451  1.00 91.94           C  
ANISOU 1479  C   ASN A 239    12149  13235   9548    264   -400    941       C  
ATOM   1480  O   ASN A 239      50.089 -14.834 100.450  1.00 91.61           O  
ANISOU 1480  O   ASN A 239    11957  13344   9508    448   -259   1008       O  
ATOM   1481  CB  ASN A 239      51.682 -14.509 102.829  1.00 97.13           C  
ANISOU 1481  CB  ASN A 239    12215  14589  10099    215   -605   1215       C  
ATOM   1482  N   CYS A 240      48.188 -14.369 101.595  1.00 84.87           N  
ANISOU 1482  N   CYS A 240    11595  11957   8693    256   -397    796       N  
ATOM   1483  CA  CYS A 240      47.245 -14.945 100.629  1.00 82.45           C  
ANISOU 1483  CA  CYS A 240    11509  11386   8433    437   -257    706       C  
ATOM   1484  C   CYS A 240      46.445 -13.891  99.840  1.00 82.63           C  
ANISOU 1484  C   CYS A 240    11704  11207   8486    215   -234    618       C  
ATOM   1485  O   CYS A 240      46.461 -12.709 100.186  1.00 82.56           O  
ANISOU 1485  O   CYS A 240    11708  11200   8461    -70   -321    608       O  
ATOM   1486  CB  CYS A 240      46.323 -15.956 101.312  1.00 81.60           C  
ANISOU 1486  CB  CYS A 240    11628  11038   8339    630   -262    636       C  
ATOM   1487  SG  CYS A 240      44.862 -15.228 102.106  1.00 83.32           S  
ANISOU 1487  SG  CYS A 240    12123  10944   8591    411   -356    509       S  
ATOM   1488  N   LYS A 241      45.740 -14.339  98.781  1.00 75.92           N  
ANISOU 1488  N   LYS A 241    11014  10170   7661    350   -121    557       N  
ATOM   1489  CA  LYS A 241      44.912 -13.499  97.920  1.00 73.26           C  
ANISOU 1489  CA  LYS A 241    10849   9641   7347    200    -96    485       C  
ATOM   1490  C   LYS A 241      43.494 -14.064  97.839  1.00 72.70           C  
ANISOU 1490  C   LYS A 241    11030   9281   7313    304    -86    390       C  
ATOM   1491  O   LYS A 241      43.306 -15.195  97.388  1.00 72.28           O  
ANISOU 1491  O   LYS A 241    11045   9171   7247    511    -13    380       O  
ATOM   1492  CB  LYS A 241      45.544 -13.343  96.523  1.00 76.46           C  
ANISOU 1492  CB  LYS A 241    11170  10159   7723    213     21    531       C  
ATOM   1493  N   VAL A 242      42.507 -13.291  98.319  1.00 66.03           N  
ANISOU 1493  N   VAL A 242    10329   8259   6499    160   -154    328       N  
ATOM   1494  CA  VAL A 242      41.090 -13.669  98.326  1.00 63.35           C  
ANISOU 1494  CA  VAL A 242    10183   7689   6198    219   -155    256       C  
ATOM   1495  C   VAL A 242      40.403 -13.034  97.120  1.00 66.30           C  
ANISOU 1495  C   VAL A 242    10657   7954   6581    153   -125    231       C  
ATOM   1496  O   VAL A 242      40.451 -11.813  96.966  1.00 66.13           O  
ANISOU 1496  O   VAL A 242    10650   7925   6552      0   -147    238       O  
ATOM   1497  CB  VAL A 242      40.417 -13.287  99.670  1.00 65.93           C  
ANISOU 1497  CB  VAL A 242    10585   7920   6544    147   -230    224       C  
ATOM   1498  CG1 VAL A 242      38.905 -13.480  99.622  1.00 64.29           C  
ANISOU 1498  CG1 VAL A 242    10533   7515   6379    182   -221    170       C  
ATOM   1499  CG2 VAL A 242      41.025 -14.068 100.830  1.00 66.27           C  
ANISOU 1499  CG2 VAL A 242    10556   8060   6565    227   -268    251       C  
ATOM   1500  N   TYR A 243      39.766 -13.861  96.271  1.00 62.43           N  
ANISOU 1500  N   TYR A 243    10264   7370   6087    258    -83    206       N  
ATOM   1501  CA  TYR A 243      39.093 -13.408  95.050  1.00 61.98           C  
ANISOU 1501  CA  TYR A 243    10306   7223   6021    210    -69    193       C  
ATOM   1502  C   TYR A 243      37.573 -13.386  95.121  1.00 65.53           C  
ANISOU 1502  C   TYR A 243    10871   7519   6507    194   -121    159       C  
ATOM   1503  O   TYR A 243      36.946 -14.289  95.680  1.00 63.99           O  
ANISOU 1503  O   TYR A 243    10717   7269   6328    251   -138    138       O  
ATOM   1504  CB  TYR A 243      39.545 -14.233  93.835  1.00 63.47           C  
ANISOU 1504  CB  TYR A 243    10530   7439   6146    311     13    202       C  
ATOM   1505  CG  TYR A 243      40.993 -14.005  93.461  1.00 66.30           C  
ANISOU 1505  CG  TYR A 243    10744   7983   6464    325     91    258       C  
ATOM   1506  CD1 TYR A 243      41.353 -12.999  92.572  1.00 68.71           C  
ANISOU 1506  CD1 TYR A 243    11033   8333   6741    208    121    284       C  
ATOM   1507  CD2 TYR A 243      42.007 -14.794  93.999  1.00 68.06           C  
ANISOU 1507  CD2 TYR A 243    10839   8353   6668    461    139    298       C  
ATOM   1508  CE1 TYR A 243      42.687 -12.781  92.227  1.00 71.10           C  
ANISOU 1508  CE1 TYR A 243    11174   8838   7001    197    203    350       C  
ATOM   1509  CE2 TYR A 243      43.345 -14.583  93.665  1.00 70.42           C  
ANISOU 1509  CE2 TYR A 243    10951   8876   6929    481    216    374       C  
ATOM   1510  CZ  TYR A 243      43.680 -13.578  92.772  1.00 77.70           C  
ANISOU 1510  CZ  TYR A 243    11841   9856   7827    335    252    400       C  
ATOM   1511  OH  TYR A 243      44.994 -13.365  92.424  1.00 79.03           O  
ANISOU 1511  OH  TYR A 243    11800  10273   7953    329    338    488       O  
ATOM   1512  N   SER A 244      36.993 -12.340  94.517  1.00 63.39           N  
ANISOU 1512  N   SER A 244    10652   7192   6240    117   -144    167       N  
ATOM   1513  CA  SER A 244      35.553 -12.138  94.374  1.00 63.35           C  
ANISOU 1513  CA  SER A 244    10716   7089   6264    115   -193    165       C  
ATOM   1514  C   SER A 244      35.242 -12.406  92.895  1.00 67.89           C  
ANISOU 1514  C   SER A 244    11364   7643   6787    113   -198    174       C  
ATOM   1515  O   SER A 244      35.578 -11.596  92.022  1.00 67.85           O  
ANISOU 1515  O   SER A 244    11395   7640   6744     71   -185    196       O  
ATOM   1516  CB  SER A 244      35.158 -10.716  94.776  1.00 67.13           C  
ANISOU 1516  CB  SER A 244    11224   7518   6765     70   -211    183       C  
ATOM   1517  OG  SER A 244      33.756 -10.505  94.713  1.00 74.82           O  
ANISOU 1517  OG  SER A 244    12224   8433   7769    113   -247    203       O  
ATOM   1518  N   ILE A 245      34.687 -13.590  92.613  1.00 64.60           N  
ANISOU 1518  N   ILE A 245    11000   7198   6348    140   -216    158       N  
ATOM   1519  CA  ILE A 245      34.376 -13.994  91.250  1.00 65.23           C  
ANISOU 1519  CA  ILE A 245    11191   7245   6350    117   -234    161       C  
ATOM   1520  C   ILE A 245      33.014 -13.462  90.815  1.00 70.32           C  
ANISOU 1520  C   ILE A 245    11843   7870   7007     62   -330    198       C  
ATOM   1521  O   ILE A 245      31.967 -13.859  91.344  1.00 69.83           O  
ANISOU 1521  O   ILE A 245    11741   7810   6982     41   -390    210       O  
ATOM   1522  CB  ILE A 245      34.544 -15.512  91.046  1.00 68.73           C  
ANISOU 1522  CB  ILE A 245    11746   7647   6722    153   -205    126       C  
ATOM   1523  CG1 ILE A 245      36.026 -15.888  91.120  1.00 69.63           C  
ANISOU 1523  CG1 ILE A 245    11843   7811   6802    261    -91    116       C  
ATOM   1524  CG2 ILE A 245      33.949 -15.950  89.713  1.00 70.64           C  
ANISOU 1524  CG2 ILE A 245    12153   7829   6859     93   -247    125       C  
ATOM   1525  CD1 ILE A 245      36.279 -17.231  91.634  1.00 79.49           C  
ANISOU 1525  CD1 ILE A 245    13174   9017   8010    353    -49     92       C  
ATOM   1526  N   LYS A 246      33.062 -12.523  89.863  1.00 67.81           N  
ANISOU 1526  N   LYS A 246    11566   7548   6652     42   -342    229       N  
ATOM   1527  CA  LYS A 246      31.926 -11.853  89.231  1.00 68.60           C  
ANISOU 1527  CA  LYS A 246    11676   7646   6744     22   -434    287       C  
ATOM   1528  C   LYS A 246      32.296 -11.782  87.759  1.00 75.86           C  
ANISOU 1528  C   LYS A 246    12729   8543   7551    -16   -438    295       C  
ATOM   1529  O   LYS A 246      33.481 -11.893  87.460  1.00 75.92           O  
ANISOU 1529  O   LYS A 246    12788   8545   7515    -11   -341    263       O  
ATOM   1530  CB  LYS A 246      31.749 -10.423  89.792  1.00 70.15           C  
ANISOU 1530  CB  LYS A 246    11825   7830   6999     71   -421    326       C  
ATOM   1531  CG  LYS A 246      31.487 -10.332  91.301  1.00 77.67           C  
ANISOU 1531  CG  LYS A 246    12681   8788   8042    119   -395    316       C  
ATOM   1532  CD  LYS A 246      30.042 -10.658  91.689  1.00 84.59           C  
ANISOU 1532  CD  LYS A 246    13463   9714   8964    151   -460    362       C  
ATOM   1533  CE  LYS A 246      29.932 -11.143  93.113  1.00 92.42           C  
ANISOU 1533  CE  LYS A 246    14379  10715  10022    173   -418    334       C  
ATOM   1534  NZ  LYS A 246      30.392 -12.555  93.270  1.00 99.36           N  
ANISOU 1534  NZ  LYS A 246    15272  11597  10883    109   -412    278       N  
ATOM   1535  N   CYS A 247      31.321 -11.643  86.833  1.00 74.47           N  
ANISOU 1535  N   CYS A 247    12603   8372   7319    -54   -546    346       N  
ATOM   1536  CA  CYS A 247      31.655 -11.542  85.405  1.00 75.60           C  
ANISOU 1536  CA  CYS A 247    12907   8484   7335    -95   -552    354       C  
ATOM   1537  C   CYS A 247      30.576 -10.836  84.589  1.00 77.93           C  
ANISOU 1537  C   CYS A 247    13224   8800   7585   -108   -684    440       C  
ATOM   1538  O   CYS A 247      29.391 -10.920  84.915  1.00 77.76           O  
ANISOU 1538  O   CYS A 247    13088   8848   7608   -109   -796    494       O  
ATOM   1539  CB  CYS A 247      32.049 -12.888  84.797  1.00 77.25           C  
ANISOU 1539  CB  CYS A 247    13262   8654   7434   -146   -528    298       C  
ATOM   1540  SG  CYS A 247      30.689 -14.059  84.611  1.00 82.54           S  
ANISOU 1540  SG  CYS A 247    13979   9333   8048   -265   -687    307       S  
ATOM   1541  N   ARG A 248      31.010 -10.112  83.544  1.00 73.11           N  
ANISOU 1541  N   ARG A 248    12749   8147   6883   -112   -665    464       N  
ATOM   1542  CA  ARG A 248      30.145  -9.305  82.686  1.00 73.18           C  
ANISOU 1542  CA  ARG A 248    12809   8168   6830   -100   -783    557       C  
ATOM   1543  C   ARG A 248      29.826  -9.981  81.354  1.00 76.83           C  
ANISOU 1543  C   ARG A 248    13428   8631   7133   -201   -883    567       C  
ATOM   1544  O   ARG A 248      30.660  -9.977  80.449  1.00 76.80           O  
ANISOU 1544  O   ARG A 248    13609   8558   7014   -236   -807    534       O  
ATOM   1545  CB  ARG A 248      30.769  -7.917  82.424  1.00 71.88           C  
ANISOU 1545  CB  ARG A 248    12737   7931   6644    -48   -701    588       C  
ATOM   1546  CG  ARG A 248      31.322  -7.203  83.644  1.00 73.76           C  
ANISOU 1546  CG  ARG A 248    12895   8137   6994      5   -593    566       C  
ATOM   1547  CD  ARG A 248      30.436  -6.055  84.058  1.00 75.56           C  
ANISOU 1547  CD  ARG A 248    13103   8342   7265    124   -642    649       C  
ATOM   1548  NE  ARG A 248      29.384  -6.492  84.973  1.00 75.90           N  
ANISOU 1548  NE  ARG A 248    12957   8473   7410    198   -707    672       N  
ATOM   1549  CZ  ARG A 248      29.496  -6.511  86.298  1.00 80.86           C  
ANISOU 1549  CZ  ARG A 248    13483   9097   8142    239   -638    633       C  
ATOM   1550  NH1 ARG A 248      30.615  -6.102  86.883  1.00 75.58           N  
ANISOU 1550  NH1 ARG A 248    12879   8349   7490    201   -521    572       N  
ATOM   1551  NH2 ARG A 248      28.484  -6.907  87.047  1.00 49.90           N  
ANISOU 1551  NH2 ARG A 248     9394   5267   4300    303   -687    665       N  
ATOM   1552  N   PHE A 249      28.601 -10.503  81.216  1.00 72.75           N  
ANISOU 1552  N   PHE A 249    12843   8202   6597   -260  -1055    621       N  
ATOM   1553  CA  PHE A 249      28.130 -11.119  79.983  1.00 73.42           C  
ANISOU 1553  CA  PHE A 249    13091   8296   6510   -394  -1192    641       C  
ATOM   1554  C   PHE A 249      27.568 -10.066  79.020  1.00 78.18           C  
ANISOU 1554  C   PHE A 249    13744   8933   7029   -356  -1310    754       C  
ATOM   1555  O   PHE A 249      26.948 -10.436  78.024  1.00 80.53           O  
ANISOU 1555  O   PHE A 249    14153   9268   7177   -472  -1468    799       O  
ATOM   1556  CB  PHE A 249      27.086 -12.211  80.256  1.00 75.95           C  
ANISOU 1556  CB  PHE A 249    13320   8713   6823   -531  -1342    657       C  
ATOM   1557  CG  PHE A 249      27.522 -13.408  81.067  1.00 76.80           C  
ANISOU 1557  CG  PHE A 249    13450   8764   6968   -590  -1248    552       C  
ATOM   1558  CD1 PHE A 249      28.210 -14.459  80.472  1.00 80.50           C  
ANISOU 1558  CD1 PHE A 249    14196   9103   7288   -679  -1186    459       C  
ATOM   1559  CD2 PHE A 249      27.153 -13.535  82.402  1.00 77.80           C  
ANISOU 1559  CD2 PHE A 249    13346   8959   7254   -549  -1224    556       C  
ATOM   1560  CE1 PHE A 249      28.564 -15.593  81.211  1.00 80.79           C  
ANISOU 1560  CE1 PHE A 249    14285   9071   7339   -707  -1101    374       C  
ATOM   1561  CE2 PHE A 249      27.498 -14.673  83.138  1.00 79.75           C  
ANISOU 1561  CE2 PHE A 249    13638   9145   7518   -604  -1150    469       C  
ATOM   1562  CZ  PHE A 249      28.206 -15.691  82.540  1.00 78.34           C  
ANISOU 1562  CZ  PHE A 249    13742   8831   7194   -676  -1091    381       C  
ATOM   1563  N   LYS A 250      27.768  -8.752  79.314  1.00 72.88           N  
ANISOU 1563  N   LYS A 250    13019   8237   6433   -200  -1240    805       N  
ATOM   1564  CA  LYS A 250      27.349  -7.630  78.449  1.00 73.00           C  
ANISOU 1564  CA  LYS A 250    13123   8252   6363   -123  -1326    919       C  
ATOM   1565  C   LYS A 250      28.193  -7.708  77.179  1.00 75.03           C  
ANISOU 1565  C   LYS A 250    13672   8397   6439   -217  -1280    877       C  
ATOM   1566  O   LYS A 250      27.694  -7.496  76.076  1.00 76.35           O  
ANISOU 1566  O   LYS A 250    13971   8582   6458   -252  -1418    953       O  
ATOM   1567  CB  LYS A 250      27.658  -6.269  79.105  1.00 74.78           C  
ANISOU 1567  CB  LYS A 250    13327   8404   6683     51  -1207    953       C  
ATOM   1568  CG  LYS A 250      26.868  -5.881  80.341  1.00 89.04           C  
ANISOU 1568  CG  LYS A 250    14898  10286   8647    198  -1210   1004       C  
ATOM   1569  CD  LYS A 250      27.256  -4.457  80.740  1.00 98.05           C  
ANISOU 1569  CD  LYS A 250    16143  11296   9814    351  -1090   1033       C  
ATOM   1570  CE  LYS A 250      26.665  -3.982  82.042  1.00108.28           C  
ANISOU 1570  CE  LYS A 250    17276  12620  11247    519  -1044   1068       C  
ATOM   1571  NZ  LYS A 250      27.024  -2.564  82.305  1.00114.55           N  
ANISOU 1571  NZ  LYS A 250    18260  13244  12019    654   -933   1097       N  
ATOM   1572  N   TYR A 251      29.488  -8.026  77.367  1.00 68.80           N  
ANISOU 1572  N   TYR A 251    12971   7510   5658   -251  -1080    764       N  
ATOM   1573  CA  TYR A 251      30.528  -8.146  76.354  1.00 68.35           C  
ANISOU 1573  CA  TYR A 251    13166   7356   5448   -317   -963    714       C  
ATOM   1574  C   TYR A 251      30.592  -9.539  75.672  1.00 71.92           C  
ANISOU 1574  C   TYR A 251    13778   7790   5758   -437   -989    645       C  
ATOM   1575  O   TYR A 251      31.519  -9.791  74.892  1.00 71.78           O  
ANISOU 1575  O   TYR A 251    13978   7691   5603   -468   -855    595       O  
ATOM   1576  CB  TYR A 251      31.886  -7.744  76.966  1.00 67.74           C  
ANISOU 1576  CB  TYR A 251    13060   7228   5452   -281   -727    651       C  
ATOM   1577  CG  TYR A 251      31.941  -6.300  77.418  1.00 68.60           C  
ANISOU 1577  CG  TYR A 251    13125   7303   5638   -208   -694    714       C  
ATOM   1578  CD1 TYR A 251      32.230  -5.278  76.518  1.00 71.61           C  
ANISOU 1578  CD1 TYR A 251    13706   7603   5898   -217   -666    774       C  
ATOM   1579  CD2 TYR A 251      31.696  -5.953  78.743  1.00 68.03           C  
ANISOU 1579  CD2 TYR A 251    12856   7257   5736   -134   -685    713       C  
ATOM   1580  CE1 TYR A 251      32.275  -3.945  76.926  1.00 71.72           C  
ANISOU 1580  CE1 TYR A 251    13748   7548   5955   -159   -630    831       C  
ATOM   1581  CE2 TYR A 251      31.739  -4.623  79.164  1.00 68.81           C  
ANISOU 1581  CE2 TYR A 251    12982   7287   5874    -68   -647    765       C  
ATOM   1582  CZ  TYR A 251      32.030  -3.622  78.252  1.00 73.92           C  
ANISOU 1582  CZ  TYR A 251    13854   7839   6395    -84   -620    824       C  
ATOM   1583  OH  TYR A 251      32.073  -2.311  78.656  1.00 69.47           O  
ANISOU 1583  OH  TYR A 251    13380   7172   5843    -28   -577    874       O  
ATOM   1584  N   THR A 252      29.600 -10.429  75.942  1.00 67.87           N  
ANISOU 1584  N   THR A 252    13182   7348   5256   -512  -1152    648       N  
ATOM   1585  CA  THR A 252      29.545 -11.747  75.311  1.00 68.21           C  
ANISOU 1585  CA  THR A 252    13440   7343   5135   -654  -1195    584       C  
ATOM   1586  C   THR A 252      29.186 -11.501  73.864  1.00 73.44           C  
ANISOU 1586  C   THR A 252    14352   7979   5574   -743  -1325    642       C  
ATOM   1587  O   THR A 252      28.056 -11.117  73.562  1.00 74.46           O  
ANISOU 1587  O   THR A 252    14402   8214   5676   -791  -1556    750       O  
ATOM   1588  CB  THR A 252      28.602 -12.716  76.054  1.00 75.53           C  
ANISOU 1588  CB  THR A 252    14226   8346   6125   -753  -1330    576       C  
ATOM   1589  OG1 THR A 252      29.125 -12.962  77.358  1.00 74.80           O  
ANISOU 1589  OG1 THR A 252    13956   8249   6215   -657  -1174    511       O  
ATOM   1590  CG2 THR A 252      28.447 -14.052  75.335  1.00 74.57           C  
ANISOU 1590  CG2 THR A 252    14397   8144   5794   -938  -1396    514       C  
ATOM   1591  N   PHE A 253      30.194 -11.621  72.995  1.00 70.09           N  
ANISOU 1591  N   PHE A 253    14210   7429   4991   -741  -1164    585       N  
ATOM   1592  CA  PHE A 253      30.087 -11.404  71.555  1.00 71.88           C  
ANISOU 1592  CA  PHE A 253    14740   7596   4974   -818  -1240    624       C  
ATOM   1593  C   PHE A 253      30.084 -12.735  70.790  1.00 78.46           C  
ANISOU 1593  C   PHE A 253    15914   8328   5570   -969  -1265    547       C  
ATOM   1594  O   PHE A 253      30.328 -13.789  71.376  1.00 76.74           O  
ANISOU 1594  O   PHE A 253    15715   8064   5379   -986  -1184    457       O  
ATOM   1595  CB  PHE A 253      31.244 -10.501  71.063  1.00 73.04           C  
ANISOU 1595  CB  PHE A 253    14997   7668   5085   -716  -1014    624       C  
ATOM   1596  CG  PHE A 253      32.626 -11.084  71.255  1.00 73.23           C  
ANISOU 1596  CG  PHE A 253    15094   7622   5108   -652   -716    518       C  
ATOM   1597  CD1 PHE A 253      33.208 -11.876  70.274  1.00 77.10           C  
ANISOU 1597  CD1 PHE A 253    15927   8004   5365   -687   -598    456       C  
ATOM   1598  CD2 PHE A 253      33.341 -10.848  72.418  1.00 73.25           C  
ANISOU 1598  CD2 PHE A 253    14827   7677   5328   -546   -550    489       C  
ATOM   1599  CE1 PHE A 253      34.466 -12.438  70.466  1.00 77.39           C  
ANISOU 1599  CE1 PHE A 253    16003   8004   5398   -582   -307    379       C  
ATOM   1600  CE2 PHE A 253      34.603 -11.405  72.604  1.00 75.45           C  
ANISOU 1600  CE2 PHE A 253    15128   7936   5603   -470   -287    416       C  
ATOM   1601  CZ  PHE A 253      35.150 -12.204  71.631  1.00 74.69           C  
ANISOU 1601  CZ  PHE A 253    15344   7749   5285   -471   -161    367       C  
ATOM   1602  N   ALA A 254      29.837 -12.666  69.470  1.00 78.54           N  
ANISOU 1602  N   ALA A 254    16233   8282   5326  -1072  -1371    582       N  
ATOM   1603  CA  ALA A 254      29.871 -13.803  68.555  1.00 80.81           C  
ANISOU 1603  CA  ALA A 254    16939   8435   5329  -1225  -1390    510       C  
ATOM   1604  C   ALA A 254      30.939 -13.512  67.493  1.00 86.74           C  
ANISOU 1604  C   ALA A 254    18018   9051   5888  -1150  -1168    480       C  
ATOM   1605  O   ALA A 254      31.072 -12.359  67.063  1.00 86.31           O  
ANISOU 1605  O   ALA A 254    17916   9033   5845  -1085  -1157    559       O  
ATOM   1606  CB  ALA A 254      28.511 -13.996  67.906  1.00 83.71           C  
ANISOU 1606  CB  ALA A 254    17396   8878   5534  -1455  -1750    593       C  
ATOM   1607  N   LYS A 255      31.721 -14.543  67.104  1.00 85.03           N  
ANISOU 1607  N   LYS A 255    18142   8675   5491  -1144   -969    370       N  
ATOM   1608  CA  LYS A 255      32.792 -14.440  66.104  1.00 86.55           C  
ANISOU 1608  CA  LYS A 255    18661   8745   5480  -1058   -713    338       C  
ATOM   1609  C   LYS A 255      32.196 -14.207  64.700  1.00 94.03           C  
ANISOU 1609  C   LYS A 255    19970   9628   6128  -1219   -900    391       C  
ATOM   1610  O   LYS A 255      32.093 -15.142  63.900  1.00 95.48           O  
ANISOU 1610  O   LYS A 255    20596   9662   6020  -1338   -923    330       O  
ATOM   1611  CB  LYS A 255      33.684 -15.700  66.129  1.00 89.68           C  
ANISOU 1611  CB  LYS A 255    19324   8993   5757   -965   -441    217       C  
ATOM   1612  CG  LYS A 255      34.729 -15.744  67.235  1.00 97.83           C  
ANISOU 1612  CG  LYS A 255    20037  10098   7037   -737   -157    185       C  
ATOM   1613  CD  LYS A 255      35.673 -16.923  67.014  1.00107.85           C  
ANISOU 1613  CD  LYS A 255    21612  11221   8144   -598    123     88       C  
ATOM   1614  CE  LYS A 255      37.082 -16.635  67.471  1.00116.06           C  
ANISOU 1614  CE  LYS A 255    22426  12355   9316   -341    479     94       C  
ATOM   1615  NZ  LYS A 255      38.033 -17.679  67.006  1.00127.15           N  
ANISOU 1615  NZ  LYS A 255    24184  13623  10505   -158    783     25       N  
ATOM   1616  N   MET A 256      31.768 -12.957  64.430  1.00 92.12           N  
ANISOU 1616  N   MET A 256    19565   9490   5946  -1222  -1042    507       N  
ATOM   1617  CA  MET A 256      31.150 -12.524  63.171  1.00 95.58           C  
ANISOU 1617  CA  MET A 256    20289   9902   6126  -1353  -1251    588       C  
ATOM   1618  C   MET A 256      31.728 -11.167  62.730  1.00101.93           C  
ANISOU 1618  C   MET A 256    21061  10717   6950  -1235  -1124    669       C  
ATOM   1619  O   MET A 256      31.720 -10.228  63.530  1.00 99.78           O  
ANISOU 1619  O   MET A 256    20424  10554   6935  -1127  -1123    735       O  
ATOM   1620  CB  MET A 256      29.618 -12.439  63.322  1.00 98.60           C  
ANISOU 1620  CB  MET A 256    20495  10431   6537  -1515  -1673    688       C  
ATOM   1621  CG  MET A 256      28.947 -13.789  63.462  1.00103.34           C  
ANISOU 1621  CG  MET A 256    21212  11010   7042  -1716  -1834    621       C  
ATOM   1622  SD  MET A 256      27.383 -13.677  64.350  1.00107.51           S  
ANISOU 1622  SD  MET A 256    21285  11805   7760  -1850  -2239    747       S  
ATOM   1623  CE  MET A 256      26.999 -15.408  64.546  1.00105.28           C  
ANISOU 1623  CE  MET A 256    21233  11437   7334  -2116  -2329    636       C  
ATOM   1624  N   GLU A 257      32.226 -11.067  61.461  1.00102.21           N  
ANISOU 1624  N   GLU A 257    21518  10624   6692  -1264  -1010    665       N  
ATOM   1625  CA  GLU A 257      32.840  -9.863  60.867  1.00103.28           C  
ANISOU 1625  CA  GLU A 257    21730  10738   6776  -1190   -865    739       C  
ATOM   1626  C   GLU A 257      32.105  -8.568  61.254  1.00108.13           C  
ANISOU 1626  C   GLU A 257    22052  11468   7564  -1152  -1079    878       C  
ATOM   1627  O   GLU A 257      32.745  -7.585  61.641  1.00106.58           O  
ANISOU 1627  O   GLU A 257    21691  11286   7517  -1045   -900    915       O  
ATOM   1628  CB  GLU A 257      32.932  -9.989  59.330  1.00107.88           C  
ANISOU 1628  CB  GLU A 257    22851  11179   6962  -1292   -871    745       C  
ATOM   1629  CG  GLU A 257      34.174 -10.708  58.811  1.00120.05           C  
ANISOU 1629  CG  GLU A 257    24700  12586   8328  -1222   -472    643       C  
ATOM   1630  CD  GLU A 257      34.196 -11.088  57.334  1.00136.47           C  
ANISOU 1630  CD  GLU A 257    27371  14499   9982  -1326   -466    626       C  
ATOM   1631  OE1 GLU A 257      33.825 -10.247  56.481  1.00121.03           O  
ANISOU 1631  OE1 GLU A 257    25594  12528   7862  -1404   -629    726       O  
ATOM   1632  OE2 GLU A 257      34.628 -12.224  57.029  1.00127.03           O  
ANISOU 1632  OE2 GLU A 257    26490  13175   8602  -1313   -283    515       O  
ATOM   1633  N   CYS A 258      30.756  -8.610  61.200  1.00106.72           N  
ANISOU 1633  N   CYS A 258    21805  11380   7364  -1240  -1458    959       N  
ATOM   1634  CA  CYS A 258      29.823  -7.522  61.505  1.00106.67           C  
ANISOU 1634  CA  CYS A 258    21540  11499   7492  -1171  -1698   1111       C  
ATOM   1635  C   CYS A 258      29.897  -7.016  62.954  1.00106.78           C  
ANISOU 1635  C   CYS A 258    21093  11608   7870  -1021  -1615   1115       C  
ATOM   1636  O   CYS A 258      30.053  -5.811  63.158  1.00105.59           O  
ANISOU 1636  O   CYS A 258    20851  11449   7819   -897  -1549   1194       O  
ATOM   1637  CB  CYS A 258      28.396  -7.921  61.129  1.00109.15           C  
ANISOU 1637  CB  CYS A 258    21858  11933   7679  -1303  -2113   1205       C  
ATOM   1638  SG  CYS A 258      27.787  -9.413  61.965  1.00112.42           S  
ANISOU 1638  SG  CYS A 258    22073  12451   8190  -1457  -2263   1119       S  
ATOM   1639  N   ASP A 259      29.749  -7.932  63.940  1.00101.33           N  
ANISOU 1639  N   ASP A 259    20156  10990   7354  -1042  -1624   1034       N  
ATOM   1640  CA  ASP A 259      29.726  -7.689  65.393  1.00 98.43           C  
ANISOU 1640  CA  ASP A 259    19364  10718   7318   -922  -1565   1024       C  
ATOM   1641  C   ASP A 259      30.677  -6.563  65.870  1.00100.10           C  
ANISOU 1641  C   ASP A 259    19477  10877   7679   -780  -1311   1032       C  
ATOM   1642  O   ASP A 259      31.863  -6.581  65.520  1.00 99.54           O  
ANISOU 1642  O   ASP A 259    19578  10710   7534   -789  -1043    965       O  
ATOM   1643  CB  ASP A 259      29.993  -8.997  66.155  1.00 98.83           C  
ANISOU 1643  CB  ASP A 259    19315  10774   7462   -976  -1473    889       C  
ATOM   1644  CG  ASP A 259      29.501  -9.018  67.585  1.00104.58           C  
ANISOU 1644  CG  ASP A 259    19621  11629   8485   -905  -1526    894       C  
ATOM   1645  OD1 ASP A 259      28.599  -9.828  67.887  1.00105.07           O  
ANISOU 1645  OD1 ASP A 259    19578  11782   8561  -1007  -1729    898       O  
ATOM   1646  OD2 ASP A 259      30.063  -8.273  68.418  1.00107.54           O  
ANISOU 1646  OD2 ASP A 259    19790  12008   9064   -769  -1352    888       O  
ATOM   1647  N   PRO A 260      30.168  -5.555  66.621  1.00 95.17           N  
ANISOU 1647  N   PRO A 260    18600  10318   7243   -656  -1390   1124       N  
ATOM   1648  CA  PRO A 260      31.044  -4.449  67.053  1.00 93.78           C  
ANISOU 1648  CA  PRO A 260    18393  10066   7173   -566  -1166   1133       C  
ATOM   1649  C   PRO A 260      32.035  -4.838  68.148  1.00 94.97           C  
ANISOU 1649  C   PRO A 260    18334  10229   7520   -559   -921   1016       C  
ATOM   1650  O   PRO A 260      33.185  -4.396  68.095  1.00 94.70           O  
ANISOU 1650  O   PRO A 260    18375  10133   7473   -581   -677    984       O  
ATOM   1651  CB  PRO A 260      30.063  -3.361  67.519  1.00 95.76           C  
ANISOU 1651  CB  PRO A 260    18494  10361   7529   -421  -1341   1269       C  
ATOM   1652  CG  PRO A 260      28.681  -3.882  67.211  1.00101.58           C  
ANISOU 1652  CG  PRO A 260    19156  11236   8204   -428  -1662   1351       C  
ATOM   1653  CD  PRO A 260      28.789  -5.363  67.110  1.00 96.80           C  
ANISOU 1653  CD  PRO A 260    18554  10670   7554   -590  -1671   1232       C  
ATOM   1654  N   ILE A 261      31.595  -5.666  69.127  1.00 88.91           N  
ANISOU 1654  N   ILE A 261    17301   9557   6923   -542   -991    962       N  
ATOM   1655  CA  ILE A 261      32.426  -6.144  70.239  1.00 86.26           C  
ANISOU 1655  CA  ILE A 261    16752   9249   6772   -523   -795    859       C  
ATOM   1656  C   ILE A 261      33.536  -7.047  69.691  1.00 88.74           C  
ANISOU 1656  C   ILE A 261    17236   9519   6961   -582   -580    761       C  
ATOM   1657  O   ILE A 261      34.691  -6.888  70.095  1.00 87.78           O  
ANISOU 1657  O   ILE A 261    17039   9405   6909   -562   -339    720       O  
ATOM   1658  CB  ILE A 261      31.594  -6.844  71.363  1.00 88.29           C  
ANISOU 1658  CB  ILE A 261    16724   9609   7213   -492   -931    833       C  
ATOM   1659  CG1 ILE A 261      30.325  -6.061  71.730  1.00 89.37           C  
ANISOU 1659  CG1 ILE A 261    16700   9817   7438   -407  -1151    952       C  
ATOM   1660  CG2 ILE A 261      32.432  -7.135  72.615  1.00 86.68           C  
ANISOU 1660  CG2 ILE A 261    16299   9431   7206   -452   -740    745       C  
ATOM   1661  CD1 ILE A 261      29.058  -6.752  71.324  1.00100.89           C  
ANISOU 1661  CD1 ILE A 261    18135  11380   8818   -469  -1422   1006       C  
ATOM   1662  N   TYR A 262      33.190  -7.966  68.748  1.00 85.05           N  
ANISOU 1662  N   TYR A 262    17012   9012   6289   -655   -665    734       N  
ATOM   1663  CA  TYR A 262      34.150  -8.884  68.119  1.00 84.60           C  
ANISOU 1663  CA  TYR A 262    17185   8889   6069   -677   -453    646       C  
ATOM   1664  C   TYR A 262      35.248  -8.128  67.389  1.00 88.91           C  
ANISOU 1664  C   TYR A 262    17882   9393   6508   -666   -213    671       C  
ATOM   1665  O   TYR A 262      36.416  -8.517  67.479  1.00 88.33           O  
ANISOU 1665  O   TYR A 262    17786   9338   6438   -619     61    615       O  
ATOM   1666  CB  TYR A 262      33.460  -9.896  67.185  1.00 86.50           C  
ANISOU 1666  CB  TYR A 262    17739   9059   6066   -779   -612    620       C  
ATOM   1667  CG  TYR A 262      34.411 -10.878  66.528  1.00 87.99           C  
ANISOU 1667  CG  TYR A 262    18225   9148   6061   -768   -372    525       C  
ATOM   1668  CD1 TYR A 262      35.310 -11.624  67.286  1.00 88.81           C  
ANISOU 1668  CD1 TYR A 262    18203   9267   6274   -662   -139    441       C  
ATOM   1669  CD2 TYR A 262      34.398 -11.078  65.153  1.00 90.49           C  
ANISOU 1669  CD2 TYR A 262    18964   9351   6066   -844   -376    527       C  
ATOM   1670  CE1 TYR A 262      36.188 -12.524  66.689  1.00 90.47           C  
ANISOU 1670  CE1 TYR A 262    18693   9387   6295   -597    106    368       C  
ATOM   1671  CE2 TYR A 262      35.255 -11.995  64.547  1.00 92.35           C  
ANISOU 1671  CE2 TYR A 262    19508   9479   6102   -802   -129    442       C  
ATOM   1672  CZ  TYR A 262      36.154 -12.710  65.319  1.00 97.61           C  
ANISOU 1672  CZ  TYR A 262    20035  10165   6886   -663    119    365       C  
ATOM   1673  OH  TYR A 262      37.017 -13.602  64.735  1.00 99.25           O  
ANISOU 1673  OH  TYR A 262    20548  10270   6890   -568    388    295       O  
ATOM   1674  N   ALA A 263      34.873  -7.034  66.701  1.00 86.38           N  
ANISOU 1674  N   ALA A 263    17700   9031   6091   -704   -313    767       N  
ATOM   1675  CA  ALA A 263      35.797  -6.165  65.979  1.00 87.48           C  
ANISOU 1675  CA  ALA A 263    18006   9122   6112   -728   -108    811       C  
ATOM   1676  C   ALA A 263      36.810  -5.559  66.949  1.00 89.68           C  
ANISOU 1676  C   ALA A 263    18010   9473   6593   -706    110    807       C  
ATOM   1677  O   ALA A 263      38.012  -5.606  66.681  1.00 90.10           O  
ANISOU 1677  O   ALA A 263    18088   9558   6587   -724    384    788       O  
ATOM   1678  CB  ALA A 263      35.029  -5.064  65.261  1.00 89.59           C  
ANISOU 1678  CB  ALA A 263    18455   9320   6264   -758   -298    927       C  
ATOM   1679  N   ALA A 264      36.329  -5.046  68.096  1.00 84.28           N  
ANISOU 1679  N   ALA A 264    17058   8830   6133   -672    -10    828       N  
ATOM   1680  CA  ALA A 264      37.176  -4.448  69.121  1.00 83.10           C  
ANISOU 1680  CA  ALA A 264    16663   8745   6166   -683    151    824       C  
ATOM   1681  C   ALA A 264      38.075  -5.486  69.786  1.00 85.83           C  
ANISOU 1681  C   ALA A 264    16793   9207   6613   -646    335    737       C  
ATOM   1682  O   ALA A 264      39.243  -5.187  70.038  1.00 85.90           O  
ANISOU 1682  O   ALA A 264    16685   9297   6655   -688    558    743       O  
ATOM   1683  CB  ALA A 264      36.325  -3.740  70.161  1.00 82.61           C  
ANISOU 1683  CB  ALA A 264    16424   8675   6289   -637    -29    861       C  
ATOM   1684  N   TYR A 265      37.535  -6.703  70.052  1.00 81.03           N  
ANISOU 1684  N   TYR A 265    16138   8612   6037   -574    240    667       N  
ATOM   1685  CA  TYR A 265      38.261  -7.810  70.683  1.00 79.75           C  
ANISOU 1685  CA  TYR A 265    15815   8535   5953   -498    396    589       C  
ATOM   1686  C   TYR A 265      39.392  -8.304  69.799  1.00 84.35           C  
ANISOU 1686  C   TYR A 265    16552   9137   6360   -470    668    574       C  
ATOM   1687  O   TYR A 265      40.463  -8.604  70.325  1.00 84.24           O  
ANISOU 1687  O   TYR A 265    16335   9248   6424   -410    883    563       O  
ATOM   1688  CB  TYR A 265      37.316  -8.972  71.064  1.00 80.15           C  
ANISOU 1688  CB  TYR A 265    15866   8554   6034   -451    224    524       C  
ATOM   1689  CG  TYR A 265      38.017 -10.272  71.419  1.00 81.75           C  
ANISOU 1689  CG  TYR A 265    16032   8790   6240   -351    394    444       C  
ATOM   1690  CD1 TYR A 265      38.713 -10.409  72.617  1.00 82.43           C  
ANISOU 1690  CD1 TYR A 265    15808   8992   6518   -277    509    426       C  
ATOM   1691  CD2 TYR A 265      37.990 -11.361  70.553  1.00 84.08           C  
ANISOU 1691  CD2 TYR A 265    16634   8989   6323   -323    440    392       C  
ATOM   1692  CE1 TYR A 265      39.369 -11.596  72.942  1.00 83.74           C  
ANISOU 1692  CE1 TYR A 265    15949   9190   6677   -147    668    368       C  
ATOM   1693  CE2 TYR A 265      38.615 -12.564  70.881  1.00 85.36           C  
ANISOU 1693  CE2 TYR A 265    16812   9152   6469   -195    609    324       C  
ATOM   1694  CZ  TYR A 265      39.308 -12.677  72.075  1.00 92.90           C  
ANISOU 1694  CZ  TYR A 265    17434  10236   7627    -92    725    317       C  
ATOM   1695  OH  TYR A 265      39.932 -13.862  72.395  1.00 95.68           O  
ANISOU 1695  OH  TYR A 265    17811  10591   7953     71    895    265       O  
ATOM   1696  N   GLN A 266      39.156  -8.402  68.470  1.00 81.07           N  
ANISOU 1696  N   GLN A 266    16492   8613   5699   -502    662    584       N  
ATOM   1697  CA  GLN A 266      40.161  -8.853  67.508  1.00 82.34           C  
ANISOU 1697  CA  GLN A 266    16855   8775   5654   -457    939    575       C  
ATOM   1698  C   GLN A 266      41.368  -7.936  67.531  1.00 86.00           C  
ANISOU 1698  C   GLN A 266    17154   9368   6154   -501   1181    645       C  
ATOM   1699  O   GLN A 266      42.497  -8.425  67.497  1.00 86.85           O  
ANISOU 1699  O   GLN A 266    17163   9598   6238   -413   1458    642       O  
ATOM   1700  CB  GLN A 266      39.583  -8.932  66.098  1.00 85.62           C  
ANISOU 1700  CB  GLN A 266    17709   9035   5788   -516    857    583       C  
ATOM   1701  CG  GLN A 266      38.902 -10.255  65.798  1.00103.49           C  
ANISOU 1701  CG  GLN A 266    20218  11186   7917   -479    744    501       C  
ATOM   1702  CD  GLN A 266      38.662 -10.429  64.318  1.00124.90           C  
ANISOU 1702  CD  GLN A 266    23403  13754  10300   -539    736    504       C  
ATOM   1703  OE1 GLN A 266      39.389 -11.154  63.629  1.00122.69           O  
ANISOU 1703  OE1 GLN A 266    23379  13418   9820   -458    976    460       O  
ATOM   1704  NE2 GLN A 266      37.652  -9.748  63.789  1.00115.50           N  
ANISOU 1704  NE2 GLN A 266    22351  12503   9032   -666    465    564       N  
ATOM   1705  N   ARG A 267      41.128  -6.612  67.637  1.00 81.57           N  
ANISOU 1705  N   ARG A 267    16555   8789   5648   -636   1076    716       N  
ATOM   1706  CA  ARG A 267      42.166  -5.583  67.724  1.00 82.29           C  
ANISOU 1706  CA  ARG A 267    16513   8987   5767   -750   1265    791       C  
ATOM   1707  C   ARG A 267      43.007  -5.806  68.983  1.00 83.44           C  
ANISOU 1707  C   ARG A 267    16245   9332   6126   -722   1382    781       C  
ATOM   1708  O   ARG A 267      44.233  -5.753  68.910  1.00 83.77           O  
ANISOU 1708  O   ARG A 267    16139   9545   6144   -748   1641    825       O  
ATOM   1709  CB  ARG A 267      41.543  -4.174  67.723  1.00 85.61           C  
ANISOU 1709  CB  ARG A 267    17032   9296   6201   -890   1088    860       C  
ATOM   1710  CG  ARG A 267      41.063  -3.696  66.347  1.00107.12           C  
ANISOU 1710  CG  ARG A 267    20164  11860   8679   -939   1028    909       C  
ATOM   1711  CD  ARG A 267      40.355  -2.349  66.418  1.00127.22           C  
ANISOU 1711  CD  ARG A 267    22820  14279  11238  -1023    840    985       C  
ATOM   1712  NE  ARG A 267      38.917  -2.483  66.680  1.00142.49           N  
ANISOU 1712  NE  ARG A 267    24785  16124  13230   -922    526    977       N  
ATOM   1713  CZ  ARG A 267      38.073  -1.462  66.811  1.00159.32           C  
ANISOU 1713  CZ  ARG A 267    26994  18153  15388   -916    334   1048       C  
ATOM   1714  NH1 ARG A 267      36.786  -1.683  67.044  1.00146.22           N  
ANISOU 1714  NH1 ARG A 267    25311  16467  13781   -805     64   1056       N  
ATOM   1715  NH2 ARG A 267      38.511  -0.212  66.712  1.00148.49           N  
ANISOU 1715  NH2 ARG A 267    25732  16709  13979  -1019    418   1121       N  
ATOM   1716  N   LEU A 268      42.337  -6.117  70.115  1.00 77.57           N  
ANISOU 1716  N   LEU A 268    15310   8583   5579   -664   1193    730       N  
ATOM   1717  CA  LEU A 268      42.940  -6.413  71.418  1.00 75.89           C  
ANISOU 1717  CA  LEU A 268    14724   8540   5572   -626   1248    713       C  
ATOM   1718  C   LEU A 268      43.718  -7.734  71.394  1.00 80.65           C  
ANISOU 1718  C   LEU A 268    15233   9267   6142   -444   1454    677       C  
ATOM   1719  O   LEU A 268      44.793  -7.813  71.980  1.00 80.68           O  
ANISOU 1719  O   LEU A 268    14947   9483   6223   -425   1629    715       O  
ATOM   1720  CB  LEU A 268      41.847  -6.431  72.516  1.00 73.28           C  
ANISOU 1720  CB  LEU A 268    14286   8132   5424   -597    983    667       C  
ATOM   1721  CG  LEU A 268      42.235  -6.830  73.952  1.00 76.16           C  
ANISOU 1721  CG  LEU A 268    14305   8635   5996   -545    988    637       C  
ATOM   1722  CD1 LEU A 268      43.134  -5.797  74.606  1.00 76.57           C  
ANISOU 1722  CD1 LEU A 268    14139   8824   6132   -701   1071    698       C  
ATOM   1723  CD2 LEU A 268      41.005  -7.015  74.802  1.00 76.53           C  
ANISOU 1723  CD2 LEU A 268    14319   8581   6178   -500    740    589       C  
ATOM   1724  N   TYR A 269      43.181  -8.760  70.719  1.00 78.06           N  
ANISOU 1724  N   TYR A 269    15166   8809   5685   -313   1430    615       N  
ATOM   1725  CA  TYR A 269      43.795 -10.084  70.632  1.00 79.39           C  
ANISOU 1725  CA  TYR A 269    15347   9032   5784   -104   1626    574       C  
ATOM   1726  C   TYR A 269      45.139 -10.073  69.903  1.00 86.56           C  
ANISOU 1726  C   TYR A 269    16236  10097   6555    -44   1966    641       C  
ATOM   1727  O   TYR A 269      46.052 -10.799  70.306  1.00 86.88           O  
ANISOU 1727  O   TYR A 269    16071  10309   6629    134   2174    656       O  
ATOM   1728  CB  TYR A 269      42.820 -11.089  69.998  1.00 80.93           C  
ANISOU 1728  CB  TYR A 269    15918   9006   5824    -30   1506    491       C  
ATOM   1729  CG  TYR A 269      43.277 -12.531  70.058  1.00 84.05           C  
ANISOU 1729  CG  TYR A 269    16394   9396   6147    198   1678    435       C  
ATOM   1730  CD1 TYR A 269      43.152 -13.276  71.227  1.00 84.69           C  
ANISOU 1730  CD1 TYR A 269    16275   9512   6393    304   1615    392       C  
ATOM   1731  CD2 TYR A 269      43.776 -13.171  68.928  1.00 87.65           C  
ANISOU 1731  CD2 TYR A 269    17174   9784   6346    320   1906    425       C  
ATOM   1732  CE1 TYR A 269      43.547 -14.613  71.280  1.00 86.74           C  
ANISOU 1732  CE1 TYR A 269    16659   9734   6565    535   1776    345       C  
ATOM   1733  CE2 TYR A 269      44.179 -14.505  68.970  1.00 90.04           C  
ANISOU 1733  CE2 TYR A 269    17611  10046   6555    563   2081    375       C  
ATOM   1734  CZ  TYR A 269      44.064 -15.223  70.149  1.00 96.25           C  
ANISOU 1734  CZ  TYR A 269    18199  10862   7510    674   2014    337       C  
ATOM   1735  OH  TYR A 269      44.459 -16.541  70.192  1.00 99.03           O  
ANISOU 1735  OH  TYR A 269    18727  11147   7751    933   2193    294       O  
ATOM   1736  N   GLU A 270      45.267  -9.240  68.854  1.00 85.16           N  
ANISOU 1736  N   GLU A 270    16259   9876   6221   -182   2030    694       N  
ATOM   1737  CA  GLU A 270      46.501  -9.157  68.075  1.00 88.11           C  
ANISOU 1737  CA  GLU A 270    16622  10409   6447   -146   2368    770       C  
ATOM   1738  C   GLU A 270      47.328  -7.886  68.376  1.00 93.24           C  
ANISOU 1738  C   GLU A 270    16969  11270   7187   -364   2451    881       C  
ATOM   1739  O   GLU A 270      48.368  -7.666  67.746  1.00 95.58           O  
ANISOU 1739  O   GLU A 270    17200  11744   7372   -380   2734    966       O  
ATOM   1740  CB  GLU A 270      46.227  -9.339  66.572  1.00 91.50           C  
ANISOU 1740  CB  GLU A 270    17531  10651   6584   -131   2446    756       C  
ATOM   1741  CG  GLU A 270      45.531 -10.652  66.210  1.00104.53           C  
ANISOU 1741  CG  GLU A 270    19524  12094   8098     51   2387    650       C  
ATOM   1742  CD  GLU A 270      46.217 -11.989  66.465  1.00131.73           C  
ANISOU 1742  CD  GLU A 270    22934  15607  11509    344   2623    615       C  
ATOM   1743  OE1 GLU A 270      47.387 -12.008  66.915  1.00132.78           O  
ANISOU 1743  OE1 GLU A 270    22716  16007  11729    462   2875    688       O  
ATOM   1744  OE2 GLU A 270      45.575 -13.030  66.194  1.00124.20           O  
ANISOU 1744  OE2 GLU A 270    22323  14442  10426    454   2554    522       O  
ATOM   1745  N   ALA A 271      46.887  -7.085  69.372  1.00 87.87           N  
ANISOU 1745  N   ALA A 271    16109  10578   6699   -535   2216    882       N  
ATOM   1746  CA  ALA A 271      47.564  -5.879  69.869  1.00 88.32           C  
ANISOU 1746  CA  ALA A 271    15911  10800   6846   -783   2245    974       C  
ATOM   1747  C   ALA A 271      47.038  -5.531  71.290  1.00 90.03           C  
ANISOU 1747  C   ALA A 271    15908  11003   7298   -856   1995    939       C  
ATOM   1748  O   ALA A 271      46.260  -4.582  71.446  1.00 88.51           O  
ANISOU 1748  O   ALA A 271    15862  10632   7134  -1011   1791    933       O  
ATOM   1749  CB  ALA A 271      47.376  -4.708  68.905  1.00 90.25           C  
ANISOU 1749  CB  ALA A 271    16449  10907   6935  -1009   2237   1029       C  
ATOM   1750  N   PRO A 272      47.429  -6.300  72.340  1.00 85.75           N  
ANISOU 1750  N   PRO A 272    15037  10636   6909   -723   2014    920       N  
ATOM   1751  CA  PRO A 272      46.907  -6.016  73.689  1.00 83.21           C  
ANISOU 1751  CA  PRO A 272    14538  10287   6790   -784   1784    883       C  
ATOM   1752  C   PRO A 272      47.555  -4.820  74.366  1.00 88.13           C  
ANISOU 1752  C   PRO A 272    14950  11051   7483  -1067   1775    961       C  
ATOM   1753  O   PRO A 272      48.775  -4.775  74.535  1.00 89.81           O  
ANISOU 1753  O   PRO A 272    14874  11554   7696  -1143   1955   1046       O  
ATOM   1754  CB  PRO A 272      47.133  -7.327  74.458  1.00 84.22           C  
ANISOU 1754  CB  PRO A 272    14441  10539   7019   -532   1821    840       C  
ATOM   1755  CG  PRO A 272      47.780  -8.272  73.484  1.00 90.89           C  
ANISOU 1755  CG  PRO A 272    15366  11463   7705   -322   2081    857       C  
ATOM   1756  CD  PRO A 272      48.325  -7.470  72.360  1.00 88.66           C  
ANISOU 1756  CD  PRO A 272    15205  11220   7260   -483   2245    937       C  
ATOM   1757  N   GLY A 273      46.721  -3.862  74.745  1.00 83.48           N  
ANISOU 1757  N   GLY A 273    14520  10259   6939  -1223   1567    939       N  
ATOM   1758  CA  GLY A 273      47.161  -2.643  75.406  1.00 83.91           C  
ANISOU 1758  CA  GLY A 273    14486  10365   7031  -1519   1527    998       C  
ATOM   1759  C   GLY A 273      46.030  -1.804  75.953  1.00 86.01           C  
ANISOU 1759  C   GLY A 273    14972  10356   7351  -1585   1290    953       C  
ATOM   1760  O   GLY A 273      44.856  -2.056  75.656  1.00 83.79           O  
ANISOU 1760  O   GLY A 273    14903   9861   7072  -1411   1155    894       O  
ATOM   1761  N   LYS A 274      46.403  -0.793  76.766  1.00 83.34           N  
ANISOU 1761  N   LYS A 274    14586  10036   7045  -1843   1244    991       N  
ATOM   1762  CA  LYS A 274      45.548   0.195  77.432  1.00 82.08           C  
ANISOU 1762  CA  LYS A 274    14646   9624   6916  -1930   1059    966       C  
ATOM   1763  C   LYS A 274      44.496   0.748  76.462  1.00 85.75           C  
ANISOU 1763  C   LYS A 274    15516   9795   7270  -1849    985    965       C  
ATOM   1764  O   LYS A 274      43.305   0.732  76.781  1.00 83.34           O  
ANISOU 1764  O   LYS A 274    15333   9304   7028  -1673    818    918       O  
ATOM   1765  CB  LYS A 274      46.432   1.345  77.953  1.00 86.63           C  
ANISOU 1765  CB  LYS A 274    15219  10257   7440  -2300   1093   1033       C  
ATOM   1766  CG  LYS A 274      45.977   1.982  79.257  1.00102.76           C  
ANISOU 1766  CG  LYS A 274    17323  12160   9562  -2383    930    995       C  
ATOM   1767  CD  LYS A 274      46.685   1.378  80.474  1.00116.19           C  
ANISOU 1767  CD  LYS A 274    18626  14126  11395  -2416    913    980       C  
ATOM   1768  CE  LYS A 274      48.064   1.931  80.756  1.00130.84           C  
ANISOU 1768  CE  LYS A 274    20301  16225  13186  -2798    992   1068       C  
ATOM   1769  NZ  LYS A 274      48.673   1.277  81.946  1.00139.28           N  
ANISOU 1769  NZ  LYS A 274    20972  17567  14380  -2798    948   1064       N  
ATOM   1770  N   LEU A 275      44.948   1.183  75.261  1.00 84.51           N  
ANISOU 1770  N   LEU A 275    15546   9622   6942  -1969   1114   1030       N  
ATOM   1771  CA  LEU A 275      44.123   1.746  74.190  1.00 84.95           C  
ANISOU 1771  CA  LEU A 275    15998   9425   6854  -1916   1061   1054       C  
ATOM   1772  C   LEU A 275      43.184   0.724  73.558  1.00 85.48           C  
ANISOU 1772  C   LEU A 275    16113   9439   6924  -1619    981   1002       C  
ATOM   1773  O   LEU A 275      42.038   1.063  73.261  1.00 84.25           O  
ANISOU 1773  O   LEU A 275    16204   9074   6733  -1500    822   1004       O  
ATOM   1774  CB  LEU A 275      44.994   2.428  73.117  1.00 88.23           C  
ANISOU 1774  CB  LEU A 275    16585   9865   7072  -2149   1242   1142       C  
ATOM   1775  CG  LEU A 275      45.652   3.752  73.539  1.00 95.47           C  
ANISOU 1775  CG  LEU A 275    17617  10735   7921  -2503   1281   1209       C  
ATOM   1776  CD1 LEU A 275      47.113   3.542  73.948  1.00 97.47           C  
ANISOU 1776  CD1 LEU A 275    17502  11332   8202  -2749   1452   1255       C  
ATOM   1777  CD2 LEU A 275      45.545   4.800  72.441  1.00 99.74           C  
ANISOU 1777  CD2 LEU A 275    18598  11057   8244  -2640   1325   1283       C  
ATOM   1778  N   ALA A 276      43.655  -0.523  73.365  1.00 80.72           N  
ANISOU 1778  N   ALA A 276    15288   9029   6352  -1499   1087    966       N  
ATOM   1779  CA  ALA A 276      42.843  -1.598  72.786  1.00 79.11           C  
ANISOU 1779  CA  ALA A 276    15158   8774   6126  -1258   1017    910       C  
ATOM   1780  C   ALA A 276      41.696  -1.987  73.710  1.00 79.65           C  
ANISOU 1780  C   ALA A 276    15153   8761   6350  -1099    795    847       C  
ATOM   1781  O   ALA A 276      40.619  -2.329  73.223  1.00 78.53           O  
ANISOU 1781  O   ALA A 276    15171   8501   6167   -967    651    829       O  
ATOM   1782  CB  ALA A 276      43.706  -2.805  72.480  1.00 80.34           C  
ANISOU 1782  CB  ALA A 276    15130   9133   6264  -1164   1209    886       C  
ATOM   1783  N   LEU A 277      41.929  -1.910  75.041  1.00 74.60           N  
ANISOU 1783  N   LEU A 277    14269   8197   5877  -1131    764    824       N  
ATOM   1784  CA  LEU A 277      40.933  -2.194  76.075  1.00 72.11           C  
ANISOU 1784  CA  LEU A 277    13860   7823   5717   -998    581    772       C  
ATOM   1785  C   LEU A 277      39.813  -1.156  76.040  1.00 74.97           C  
ANISOU 1785  C   LEU A 277    14460   7972   6054   -978    418    809       C  
ATOM   1786  O   LEU A 277      38.652  -1.522  76.231  1.00 73.92           O  
ANISOU 1786  O   LEU A 277    14330   7776   5979   -815    258    790       O  
ATOM   1787  CB  LEU A 277      41.568  -2.200  77.480  1.00 71.35           C  
ANISOU 1787  CB  LEU A 277    13486   7853   5773  -1064    606    749       C  
ATOM   1788  CG  LEU A 277      41.562  -3.506  78.310  1.00 74.41           C  
ANISOU 1788  CG  LEU A 277    13601   8377   6295   -914    595    682       C  
ATOM   1789  CD1 LEU A 277      41.617  -3.193  79.783  1.00 73.40           C  
ANISOU 1789  CD1 LEU A 277    13297   8282   6309   -963    530    664       C  
ATOM   1790  CD2 LEU A 277      40.335  -4.375  78.045  1.00 75.78           C  
ANISOU 1790  CD2 LEU A 277    13851   8456   6485   -719    465    633       C  
ATOM   1791  N   LYS A 278      40.168   0.137  75.804  1.00 71.30           N  
ANISOU 1791  N   LYS A 278    14197   7402   5491  -1142    467    873       N  
ATOM   1792  CA  LYS A 278      39.240   1.270  75.716  1.00 70.97           C  
ANISOU 1792  CA  LYS A 278    14436   7136   5393  -1104    346    926       C  
ATOM   1793  C   LYS A 278      38.225   1.023  74.597  1.00 75.27           C  
ANISOU 1793  C   LYS A 278    15161   7599   5837   -940    232    960       C  
ATOM   1794  O   LYS A 278      37.024   1.215  74.800  1.00 73.64           O  
ANISOU 1794  O   LYS A 278    15013   7301   5667   -770     67    985       O  
ATOM   1795  CB  LYS A 278      40.015   2.586  75.504  1.00 74.65           C  
ANISOU 1795  CB  LYS A 278    15138   7497   5730  -1344    453    990       C  
ATOM   1796  CG  LYS A 278      39.165   3.859  75.505  1.00 78.53           C  
ANISOU 1796  CG  LYS A 278    15974   7720   6143  -1292    355   1050       C  
ATOM   1797  CD  LYS A 278      39.594   4.801  74.382  1.00 84.49           C  
ANISOU 1797  CD  LYS A 278    17083   8339   6681  -1454    441   1132       C  
ATOM   1798  CE  LYS A 278      38.650   5.961  74.178  1.00 87.29           C  
ANISOU 1798  CE  LYS A 278    17829   8410   6928  -1335    342   1207       C  
ATOM   1799  NZ  LYS A 278      39.026   6.768  72.987  1.00 91.82           N  
ANISOU 1799  NZ  LYS A 278    18767   8846   7274  -1473    419   1290       N  
ATOM   1800  N   ASP A 279      38.707   0.549  73.439  1.00 74.22           N  
ANISOU 1800  N   ASP A 279    15103   7522   5574   -987    320    965       N  
ATOM   1801  CA  ASP A 279      37.850   0.218  72.307  1.00 75.85           C  
ANISOU 1801  CA  ASP A 279    15496   7669   5655   -870    208    994       C  
ATOM   1802  C   ASP A 279      36.924  -0.946  72.686  1.00 79.67           C  
ANISOU 1802  C   ASP A 279    15787   8231   6252   -704     52    939       C  
ATOM   1803  O   ASP A 279      35.727  -0.879  72.402  1.00 80.14           O  
ANISOU 1803  O   ASP A 279    15927   8234   6288   -583   -141    983       O  
ATOM   1804  CB  ASP A 279      38.690  -0.125  71.057  1.00 79.62           C  
ANISOU 1804  CB  ASP A 279    16112   8189   5952   -970    369   1001       C  
ATOM   1805  CG  ASP A 279      39.473   1.029  70.438  1.00 92.09           C  
ANISOU 1805  CG  ASP A 279    17926   9686   7378  -1155    514   1075       C  
ATOM   1806  OD1 ASP A 279      39.551   2.112  71.071  1.00 92.89           O  
ANISOU 1806  OD1 ASP A 279    18086   9694   7515  -1243    508   1113       O  
ATOM   1807  OD2 ASP A 279      40.031   0.841  69.332  1.00 98.60           O  
ANISOU 1807  OD2 ASP A 279    18902  10530   8032  -1222    643   1095       O  
ATOM   1808  N   PHE A 280      37.466  -1.979  73.375  1.00 74.99           N  
ANISOU 1808  N   PHE A 280    14936   7779   5778   -703    132    855       N  
ATOM   1809  CA  PHE A 280      36.690  -3.134  73.825  1.00 73.51           C  
ANISOU 1809  CA  PHE A 280    14583   7657   5692   -582      5    797       C  
ATOM   1810  C   PHE A 280      35.571  -2.719  74.783  1.00 77.83           C  
ANISOU 1810  C   PHE A 280    15020   8172   6380   -480   -169    821       C  
ATOM   1811  O   PHE A 280      34.422  -3.111  74.585  1.00 77.94           O  
ANISOU 1811  O   PHE A 280    15025   8194   6395   -386   -347    840       O  
ATOM   1812  CB  PHE A 280      37.587  -4.219  74.457  1.00 74.04           C  
ANISOU 1812  CB  PHE A 280    14423   7859   5851   -586    147    713       C  
ATOM   1813  CG  PHE A 280      36.819  -5.383  75.053  1.00 73.96           C  
ANISOU 1813  CG  PHE A 280    14267   7891   5941   -482     26    653       C  
ATOM   1814  CD1 PHE A 280      36.248  -6.353  74.237  1.00 77.26           C  
ANISOU 1814  CD1 PHE A 280    14819   8289   6246   -450    -52    629       C  
ATOM   1815  CD2 PHE A 280      36.652  -5.496  76.428  1.00 74.22           C  
ANISOU 1815  CD2 PHE A 280    14063   7975   6163   -440    -13    622       C  
ATOM   1816  CE1 PHE A 280      35.519  -7.410  74.787  1.00 77.07           C  
ANISOU 1816  CE1 PHE A 280    14689   8295   6297   -398   -168    579       C  
ATOM   1817  CE2 PHE A 280      35.925  -6.555  76.976  1.00 75.71           C  
ANISOU 1817  CE2 PHE A 280    14134   8198   6433   -365   -118    574       C  
ATOM   1818  CZ  PHE A 280      35.372  -7.507  76.153  1.00 74.38           C  
ANISOU 1818  CZ  PHE A 280    14098   8011   6153   -354   -194    554       C  
ATOM   1819  N   PHE A 281      35.903  -1.922  75.805  1.00 73.89           N  
ANISOU 1819  N   PHE A 281    14444   7647   5986   -507   -115    825       N  
ATOM   1820  CA  PHE A 281      34.926  -1.470  76.782  1.00 73.00           C  
ANISOU 1820  CA  PHE A 281    14251   7493   5995   -389   -238    848       C  
ATOM   1821  C   PHE A 281      33.875  -0.527  76.218  1.00 78.99           C  
ANISOU 1821  C   PHE A 281    15212   8135   6665   -275   -369    952       C  
ATOM   1822  O   PHE A 281      32.711  -0.645  76.595  1.00 79.07           O  
ANISOU 1822  O   PHE A 281    15122   8175   6746   -118   -515    988       O  
ATOM   1823  CB  PHE A 281      35.608  -0.858  78.000  1.00 74.09           C  
ANISOU 1823  CB  PHE A 281    14307   7610   6232   -460   -138    820       C  
ATOM   1824  CG  PHE A 281      36.052  -1.869  79.022  1.00 73.80           C  
ANISOU 1824  CG  PHE A 281    13988   7713   6341   -472    -95    734       C  
ATOM   1825  CD1 PHE A 281      35.121  -2.561  79.789  1.00 75.44           C  
ANISOU 1825  CD1 PHE A 281    14023   7967   6672   -338   -205    707       C  
ATOM   1826  CD2 PHE A 281      37.401  -2.095  79.258  1.00 75.94           C  
ANISOU 1826  CD2 PHE A 281    14154   8080   6618   -615     57    695       C  
ATOM   1827  CE1 PHE A 281      35.531  -3.478  80.755  1.00 75.10           C  
ANISOU 1827  CE1 PHE A 281    13752   8034   6749   -345   -164    633       C  
ATOM   1828  CE2 PHE A 281      37.810  -3.002  80.235  1.00 77.57           C  
ANISOU 1828  CE2 PHE A 281    14105   8418   6949   -599     89    631       C  
ATOM   1829  CZ  PHE A 281      36.872  -3.685  80.977  1.00 74.32           C  
ANISOU 1829  CZ  PHE A 281    13568   8018   6652   -462    -22    596       C  
ATOM   1830  N   TYR A 282      34.258   0.387  75.314  1.00 77.03           N  
ANISOU 1830  N   TYR A 282    15242   7769   6257   -343   -316   1012       N  
ATOM   1831  CA  TYR A 282      33.287   1.321  74.750  1.00 78.75           C  
ANISOU 1831  CA  TYR A 282    15681   7867   6372   -205   -439   1126       C  
ATOM   1832  C   TYR A 282      32.622   0.780  73.467  1.00 82.67           C  
ANISOU 1832  C   TYR A 282    16259   8416   6736   -164   -576   1176       C  
ATOM   1833  O   TYR A 282      32.045   1.554  72.697  1.00 84.24           O  
ANISOU 1833  O   TYR A 282    16689   8523   6797    -82   -663   1283       O  
ATOM   1834  CB  TYR A 282      33.896   2.730  74.565  1.00 82.34           C  
ANISOU 1834  CB  TYR A 282    16449   8127   6710   -287   -327   1180       C  
ATOM   1835  CG  TYR A 282      34.314   3.398  75.862  1.00 84.81           C  
ANISOU 1835  CG  TYR A 282    16741   8362   7123   -331   -235   1145       C  
ATOM   1836  CD1 TYR A 282      33.433   3.489  76.938  1.00 86.69           C  
ANISOU 1836  CD1 TYR A 282    16855   8593   7491   -141   -312   1150       C  
ATOM   1837  CD2 TYR A 282      35.577   3.961  76.006  1.00 86.33           C  
ANISOU 1837  CD2 TYR A 282    17050   8493   7261   -582    -70   1116       C  
ATOM   1838  CE1 TYR A 282      33.823   4.069  78.146  1.00 87.93           C  
ANISOU 1838  CE1 TYR A 282    17032   8661   7716   -191   -227   1110       C  
ATOM   1839  CE2 TYR A 282      35.973   4.560  77.204  1.00 87.31           C  
ANISOU 1839  CE2 TYR A 282    17181   8543   7451   -664     -6   1084       C  
ATOM   1840  CZ  TYR A 282      35.091   4.611  78.274  1.00 93.95           C  
ANISOU 1840  CZ  TYR A 282    17933   9352   8412   -464    -85   1075       C  
ATOM   1841  OH  TYR A 282      35.456   5.207  79.457  1.00 93.11           O  
ANISOU 1841  OH  TYR A 282    17880   9153   8346   -548    -23   1039       O  
ATOM   1842  N   SER A 283      32.646  -0.556  73.275  1.00 77.29           N  
ANISOU 1842  N   SER A 283    15411   7874   6082   -214   -608   1104       N  
ATOM   1843  CA  SER A 283      32.016  -1.213  72.126  1.00 77.74           C  
ANISOU 1843  CA  SER A 283    15560   7981   5998   -214   -754   1137       C  
ATOM   1844  C   SER A 283      30.522  -1.518  72.381  1.00 81.83           C  
ANISOU 1844  C   SER A 283    15909   8605   6577    -70  -1000   1208       C  
ATOM   1845  O   SER A 283      29.823  -1.998  71.481  1.00 82.39           O  
ANISOU 1845  O   SER A 283    16043   8738   6523    -82  -1173   1260       O  
ATOM   1846  CB  SER A 283      32.788  -2.466  71.723  1.00 79.82           C  
ANISOU 1846  CB  SER A 283    15800   8309   6218   -344   -657   1029       C  
ATOM   1847  OG  SER A 283      32.582  -3.528  72.636  1.00 86.23           O  
ANISOU 1847  OG  SER A 283    16346   9228   7188   -327   -683    951       O  
ATOM   1848  N   ILE A 284      30.040  -1.222  73.610  1.00 77.52           N  
ANISOU 1848  N   ILE A 284    15148   8094   6213     55  -1014   1220       N  
ATOM   1849  CA  ILE A 284      28.643  -1.397  74.024  1.00 77.74           C  
ANISOU 1849  CA  ILE A 284    14962   8255   6319    209  -1213   1306       C  
ATOM   1850  C   ILE A 284      28.059  -0.080  74.558  1.00 82.48           C  
ANISOU 1850  C   ILE A 284    15594   8785   6960    436  -1220   1420       C  
ATOM   1851  O   ILE A 284      28.807   0.834  74.916  1.00 81.08           O  
ANISOU 1851  O   ILE A 284    15587   8436   6781    441  -1058   1398       O  
ATOM   1852  CB  ILE A 284      28.403  -2.597  74.993  1.00 79.12           C  
ANISOU 1852  CB  ILE A 284    14828   8576   6660    165  -1234   1221       C  
ATOM   1853  CG1 ILE A 284      29.178  -2.437  76.316  1.00 77.37           C  
ANISOU 1853  CG1 ILE A 284    14495   8297   6605    173  -1046   1127       C  
ATOM   1854  CG2 ILE A 284      28.686  -3.944  74.310  1.00 79.73           C  
ANISOU 1854  CG2 ILE A 284    14932   8710   6651    -23  -1269   1136       C  
ATOM   1855  CD1 ILE A 284      28.576  -3.123  77.467  1.00 80.77           C  
ANISOU 1855  CD1 ILE A 284    14633   8852   7204    217  -1086   1097       C  
ATOM   1856  N   SER A 285      26.720  -0.005  74.607  1.00 81.40           N  
ANISOU 1856  N   SER A 285    15296   8787   6844    620  -1405   1549       N  
ATOM   1857  CA  SER A 285      25.947   1.157  75.049  1.00 83.16           C  
ANISOU 1857  CA  SER A 285    15535   8973   7088    908  -1423   1686       C  
ATOM   1858  C   SER A 285      26.009   1.449  76.563  1.00 85.60           C  
ANISOU 1858  C   SER A 285    15708   9240   7574   1022  -1281   1637       C  
ATOM   1859  O   SER A 285      25.858   2.611  76.941  1.00 86.73           O  
ANISOU 1859  O   SER A 285    16015   9240   7699   1230  -1207   1710       O  
ATOM   1860  CB  SER A 285      24.496   1.045  74.585  1.00 89.76           C  
ANISOU 1860  CB  SER A 285    16189  10031   7886   1078  -1668   1861       C  
ATOM   1861  OG  SER A 285      24.004  -0.285  74.647  1.00 99.48           O  
ANISOU 1861  OG  SER A 285    17112  11500   9187    933  -1802   1828       O  
ATOM   1862  N   LYS A 286      26.205   0.425  77.422  1.00 79.41           N  
ANISOU 1862  N   LYS A 286    14668   8562   6941    897  -1241   1519       N  
ATOM   1863  CA  LYS A 286      26.288   0.621  78.882  1.00 77.98           C  
ANISOU 1863  CA  LYS A 286    14368   8345   6915    983  -1110   1464       C  
ATOM   1864  C   LYS A 286      27.617   0.021  79.439  1.00 78.18           C  
ANISOU 1864  C   LYS A 286    14396   8301   7008    736   -959   1284       C  
ATOM   1865  O   LYS A 286      27.613  -1.091  79.979  1.00 76.27           O  
ANISOU 1865  O   LYS A 286    13915   8191   6872    642   -974   1206       O  
ATOM   1866  CB  LYS A 286      25.037   0.048  79.579  1.00 81.45           C  
ANISOU 1866  CB  LYS A 286    14451   9019   7479   1128  -1217   1535       C  
ATOM   1867  CG  LYS A 286      23.726   0.747  79.207  1.00101.85           C  
ANISOU 1867  CG  LYS A 286    16981  11705  10012   1427  -1338   1739       C  
ATOM   1868  CD  LYS A 286      22.536   0.087  79.888  1.00113.75           C  
ANISOU 1868  CD  LYS A 286    18079  13501  11640   1527  -1441   1820       C  
ATOM   1869  CE  LYS A 286      21.254   0.856  79.696  1.00127.26           C  
ANISOU 1869  CE  LYS A 286    19686  15349  13318   1877  -1528   2043       C  
ATOM   1870  NZ  LYS A 286      20.147   0.267  80.494  1.00136.68           N  
ANISOU 1870  NZ  LYS A 286    20446  16847  14638   1972  -1591   2130       N  
ATOM   1871  N   PRO A 287      28.764   0.740  79.306  1.00 73.74           N  
ANISOU 1871  N   PRO A 287    14098   7546   6373    622   -817   1229       N  
ATOM   1872  CA  PRO A 287      30.060   0.144  79.672  1.00 71.74           C  
ANISOU 1872  CA  PRO A 287    13809   7284   6167    387   -689   1086       C  
ATOM   1873  C   PRO A 287      30.365  -0.082  81.147  1.00 74.99           C  
ANISOU 1873  C   PRO A 287    14056   7709   6727    375   -601   1002       C  
ATOM   1874  O   PRO A 287      29.863   0.617  82.033  1.00 75.31           O  
ANISOU 1874  O   PRO A 287    14112   7684   6817    529   -578   1037       O  
ATOM   1875  CB  PRO A 287      31.085   1.110  79.067  1.00 74.24           C  
ANISOU 1875  CB  PRO A 287    14438   7422   6347    261   -574   1087       C  
ATOM   1876  CG  PRO A 287      30.332   1.912  78.087  1.00 80.84           C  
ANISOU 1876  CG  PRO A 287    15492   8177   7045    405   -664   1216       C  
ATOM   1877  CD  PRO A 287      28.966   2.045  78.655  1.00 76.99           C  
ANISOU 1877  CD  PRO A 287    14857   7762   6635    676   -775   1307       C  
ATOM   1878  N   ALA A 288      31.256  -1.066  81.380  1.00 69.95           N  
ANISOU 1878  N   ALA A 288    13286   7149   6142    198   -539    893       N  
ATOM   1879  CA  ALA A 288      31.764  -1.454  82.687  1.00 68.22           C  
ANISOU 1879  CA  ALA A 288    12912   6961   6047    148   -460    806       C  
ATOM   1880  C   ALA A 288      32.716  -0.381  83.242  1.00 73.45           C  
ANISOU 1880  C   ALA A 288    13752   7480   6674     48   -337    784       C  
ATOM   1881  O   ALA A 288      32.836  -0.260  84.464  1.00 73.99           O  
ANISOU 1881  O   ALA A 288    13764   7527   6821     54   -295    743       O  
ATOM   1882  CB  ALA A 288      32.460  -2.805  82.607  1.00 67.49           C  
ANISOU 1882  CB  ALA A 288    12652   6997   5995     20   -435    717       C  
ATOM   1883  N   VAL A 289      33.366   0.412  82.363  1.00 69.88           N  
ANISOU 1883  N   VAL A 289    13538   6926   6089    -64   -285    815       N  
ATOM   1884  CA  VAL A 289      34.263   1.490  82.796  1.00 70.19           C  
ANISOU 1884  CA  VAL A 289    13783   6823   6063   -216   -180    805       C  
ATOM   1885  C   VAL A 289      33.529   2.833  82.782  1.00 76.02           C  
ANISOU 1885  C   VAL A 289    14832   7342   6709    -73   -192    888       C  
ATOM   1886  O   VAL A 289      32.621   3.027  81.976  1.00 77.00           O  
ANISOU 1886  O   VAL A 289    15037   7440   6779    106   -269    972       O  
ATOM   1887  CB  VAL A 289      35.630   1.536  82.067  1.00 74.51           C  
ANISOU 1887  CB  VAL A 289    14388   7405   6518   -476    -83    788       C  
ATOM   1888  CG1 VAL A 289      36.387   0.231  82.259  1.00 72.88           C  
ANISOU 1888  CG1 VAL A 289    13875   7414   6400   -560    -47    715       C  
ATOM   1889  CG2 VAL A 289      35.478   1.865  80.581  1.00 75.75           C  
ANISOU 1889  CG2 VAL A 289    14749   7502   6531   -470    -96    857       C  
ATOM   1890  N   GLU A 290      33.912   3.740  83.689  1.00 73.19           N  
ANISOU 1890  N   GLU A 290    14665   6826   6318   -145   -119    870       N  
ATOM   1891  CA  GLU A 290      33.298   5.054  83.853  1.00 75.02           C  
ANISOU 1891  CA  GLU A 290    15259   6805   6442      6   -100    941       C  
ATOM   1892  C   GLU A 290      34.384   6.116  84.079  1.00 81.12           C  
ANISOU 1892  C   GLU A 290    16368   7378   7074   -272     -1    921       C  
ATOM   1893  O   GLU A 290      35.370   5.838  84.763  1.00 80.03           O  
ANISOU 1893  O   GLU A 290    16115   7320   6974   -529     40    844       O  
ATOM   1894  CB  GLU A 290      32.345   5.008  85.061  1.00 75.98           C  
ANISOU 1894  CB  GLU A 290    15296   6912   6663    259   -111    939       C  
ATOM   1895  CG  GLU A 290      31.319   6.129  85.118  1.00 89.39           C  
ANISOU 1895  CG  GLU A 290    17311   8391   8263    555    -94   1040       C  
ATOM   1896  CD  GLU A 290      30.575   6.286  86.433  1.00112.10           C  
ANISOU 1896  CD  GLU A 290    20169  11219  11204    789    -52   1036       C  
ATOM   1897  OE1 GLU A 290      30.249   5.258  87.071  1.00105.37           O  
ANISOU 1897  OE1 GLU A 290    18950  10577  10511    834    -87    992       O  
ATOM   1898  OE2 GLU A 290      30.285   7.446  86.809  1.00108.74           O  
ANISOU 1898  OE2 GLU A 290    20128  10533  10655    940     27   1081       O  
ATOM   1899  N   TYR A 291      34.210   7.328  83.511  1.00 80.32           N  
ANISOU 1899  N   TYR A 291    16692   7025   6800   -235     30    998       N  
ATOM   1900  CA  TYR A 291      35.175   8.405  83.729  1.00 82.19           C  
ANISOU 1900  CA  TYR A 291    17310   7044   6876   -533    120    985       C  
ATOM   1901  C   TYR A 291      34.745   9.296  84.896  1.00 88.91           C  
ANISOU 1901  C   TYR A 291    18482   7635   7665   -416    163    978       C  
ATOM   1902  O   TYR A 291      33.566   9.632  85.030  1.00 89.80           O  
ANISOU 1902  O   TYR A 291    18724   7627   7771    -38    154   1041       O  
ATOM   1903  CB  TYR A 291      35.467   9.223  82.454  1.00 85.17           C  
ANISOU 1903  CB  TYR A 291    18028   7269   7063   -642    151   1064       C  
ATOM   1904  CG  TYR A 291      36.505  10.313  82.654  1.00 88.93           C  
ANISOU 1904  CG  TYR A 291    18909   7524   7355  -1009    242   1057       C  
ATOM   1905  CD1 TYR A 291      37.866  10.023  82.620  1.00 90.55           C  
ANISOU 1905  CD1 TYR A 291    18957   7897   7551  -1439    287   1013       C  
ATOM   1906  CD2 TYR A 291      36.125  11.630  82.905  1.00 92.36           C  
ANISOU 1906  CD2 TYR A 291    19892   7589   7610   -932    287   1102       C  
ATOM   1907  CE1 TYR A 291      38.824  11.015  82.834  1.00 93.62           C  
ANISOU 1907  CE1 TYR A 291    19696   8114   7761  -1831    357   1018       C  
ATOM   1908  CE2 TYR A 291      37.074  12.629  83.128  1.00 95.57           C  
ANISOU 1908  CE2 TYR A 291    20715   7773   7824  -1318    363   1092       C  
ATOM   1909  CZ  TYR A 291      38.424  12.319  83.083  1.00102.46           C  
ANISOU 1909  CZ  TYR A 291    21396   8841   8694  -1792    388   1052       C  
ATOM   1910  OH  TYR A 291      39.363  13.302  83.295  1.00104.84           O  
ANISOU 1910  OH  TYR A 291    22092   8950   8792  -2225    449   1055       O  
ATOM   1911  N   VAL A 292      35.712   9.654  85.750  1.00 86.04           N  
ANISOU 1911  N   VAL A 292    18242   7202   7247   -742    212    908       N  
ATOM   1912  CA  VAL A 292      35.519  10.518  86.906  1.00 87.32           C  
ANISOU 1912  CA  VAL A 292    18773   7094   7312   -717    263    882       C  
ATOM   1913  C   VAL A 292      36.597  11.603  86.850  1.00 94.63           C  
ANISOU 1913  C   VAL A 292    20160   7785   8008  -1142    320    880       C  
ATOM   1914  O   VAL A 292      37.767  11.276  86.640  1.00 93.74           O  
ANISOU 1914  O   VAL A 292    19860   7859   7899  -1543    311    854       O  
ATOM   1915  CB  VAL A 292      35.532   9.688  88.212  1.00 89.13           C  
ANISOU 1915  CB  VAL A 292    18667   7500   7701   -723    238    791       C  
ATOM   1916  CG1 VAL A 292      35.681  10.570  89.443  1.00 90.69           C  
ANISOU 1916  CG1 VAL A 292    19274   7424   7760   -828    293    746       C  
ATOM   1917  CG2 VAL A 292      34.273   8.845  88.324  1.00 87.15           C  
ANISOU 1917  CG2 VAL A 292    18070   7410   7633   -289    198    810       C  
ATOM   1918  N   GLY A 293      36.174  12.866  86.997  1.00 94.81           N  
ANISOU 1918  N   GLY A 293    20784   7413   7828  -1041    385    919       N  
ATOM   1919  CA  GLY A 293      37.009  14.067  86.930  1.00 98.20           C  
ANISOU 1919  CA  GLY A 293    21782   7538   7993  -1425    444    929       C  
ATOM   1920  C   GLY A 293      38.224  14.118  87.837  1.00103.68           C  
ANISOU 1920  C   GLY A 293    22474   8291   8630  -1965    431    850       C  
ATOM   1921  O   GLY A 293      39.203  13.403  87.602  1.00102.58           O  
ANISOU 1921  O   GLY A 293    21917   8478   8579  -2295    390    834       O  
ATOM   1922  N   LEU A 294      38.197  15.005  88.848  1.00102.58           N  
ANISOU 1922  N   LEU A 294    22829   7832   8316  -2064    468    811       N  
ATOM   1923  CA  LEU A 294      39.294  15.122  89.820  1.00103.55           C  
ANISOU 1923  CA  LEU A 294    23007   7989   8349  -2595    432    741       C  
ATOM   1924  C   LEU A 294      38.871  14.389  91.120  1.00106.42           C  
ANISOU 1924  C   LEU A 294    23040   8516   8879  -2437    387    658       C  
ATOM   1925  O   LEU A 294      38.937  14.957  92.216  1.00107.42           O  
ANISOU 1925  O   LEU A 294    23438   8500   8876  -2687    373    598       O  
ATOM   1926  CB  LEU A 294      39.625  16.605  90.086  1.00107.53           C  
ANISOU 1926  CB  LEU A 294    24344   8004   8510  -2861    494    747       C  
ATOM   1927  CG  LEU A 294      40.137  17.436  88.914  1.00114.71           C  
ANISOU 1927  CG  LEU A 294    25645   8731   9209  -3150    538    826       C  
ATOM   1928  CD1 LEU A 294      39.977  18.910  89.199  1.00119.02           C  
ANISOU 1928  CD1 LEU A 294    27104   8710   9408  -3261    616    832       C  
ATOM   1929  CD2 LEU A 294      41.596  17.133  88.608  1.00117.43           C  
ANISOU 1929  CD2 LEU A 294    25650   9411   9557  -3779    481    833       C  
ATOM   1930  N   GLY A 295      38.430  13.133  90.958  1.00100.19           N  
ANISOU 1930  N   GLY A 295    21685   8023   8358  -2052    358    658       N  
ATOM   1931  CA  GLY A 295      37.859  12.297  92.009  1.00 97.90           C  
ANISOU 1931  CA  GLY A 295    21052   7896   8248  -1809    328    595       C  
ATOM   1932  C   GLY A 295      36.399  12.674  92.207  1.00103.36           C  
ANISOU 1932  C   GLY A 295    21996   8342   8934  -1253    407    623       C  
ATOM   1933  O   GLY A 295      35.785  12.304  93.210  1.00101.76           O  
ANISOU 1933  O   GLY A 295    21662   8176   8826  -1012    419    581       O  
ATOM   1934  N   LYS A 296      35.837  13.390  91.193  1.00102.93           N  
ANISOU 1934  N   LYS A 296    22280   8060   8769  -1030    465    711       N  
ATOM   1935  CA  LYS A 296      34.515  14.018  91.020  1.00104.46           C  
ANISOU 1935  CA  LYS A 296    22792   7995   8902   -490    553    786       C  
ATOM   1936  C   LYS A 296      33.246  13.173  91.310  1.00107.39           C  
ANISOU 1936  C   LYS A 296    22735   8573   9493     39    555    813       C  
ATOM   1937  O   LYS A 296      32.147  13.682  91.056  1.00109.17           O  
ANISOU 1937  O   LYS A 296    23201   8619   9660    496    632    900       O  
ATOM   1938  CB  LYS A 296      34.404  14.582  89.592  1.00107.95           C  
ANISOU 1938  CB  LYS A 296    23445   8325   9246   -407    563    892       C  
ATOM   1939  CG  LYS A 296      34.709  16.065  89.497  1.00125.07           C  
ANISOU 1939  CG  LYS A 296    26411  10018  11089   -571    651    920       C  
ATOM   1940  CD  LYS A 296      33.562  16.822  88.826  1.00136.05           C  
ANISOU 1940  CD  LYS A 296    28166  11155  12372    -62    723   1047       C  
ATOM   1941  CE  LYS A 296      33.736  18.329  88.894  1.00145.21           C  
ANISOU 1941  CE  LYS A 296    30217  11771  13184   -134    837   1073       C  
ATOM   1942  NZ  LYS A 296      32.567  19.057  88.331  1.00150.86           N  
ANISOU 1942  NZ  LYS A 296    31281  12245  13793    438    916   1211       N  
ATOM   1943  N   LEU A 297      33.377  11.931  91.854  1.00100.54           N  
ANISOU 1943  N   LEU A 297    21271   8072   8858    -16    479    752       N  
ATOM   1944  CA  LEU A 297      32.282  11.004  92.243  1.00 98.19           C  
ANISOU 1944  CA  LEU A 297    20533   8005   8771    394    473    769       C  
ATOM   1945  C   LEU A 297      31.690  10.177  91.088  1.00100.58           C  
ANISOU 1945  C   LEU A 297    20374   8598   9245    602    392    847       C  
ATOM   1946  O   LEU A 297      31.259  10.752  90.083  1.00101.18           O  
ANISOU 1946  O   LEU A 297    20638   8570   9237    767    396    944       O  
ATOM   1947  CB  LEU A 297      31.134  11.714  93.013  1.00100.12           C  
ANISOU 1947  CB  LEU A 297    21111   8002   8929    842    602    814       C  
ATOM   1948  CG  LEU A 297      31.074  11.653  94.550  1.00104.59           C  
ANISOU 1948  CG  LEU A 297    21790   8478   9470    844    674    728       C  
ATOM   1949  CD1 LEU A 297      30.188  10.527  95.034  1.00102.67           C  
ANISOU 1949  CD1 LEU A 297    21017   8538   9454   1151    670    740       C  
ATOM   1950  CD2 LEU A 297      32.453  11.719  95.222  1.00106.33           C  
ANISOU 1950  CD2 LEU A 297    22162   8642   9598    288    623    608       C  
ATOM   1951  N   PRO A 298      31.605   8.825  91.245  1.00 94.95           N  
ANISOU 1951  N   PRO A 298    19086   8236   8753    598    315    808       N  
ATOM   1952  CA  PRO A 298      31.028   7.987  90.182  1.00 93.51           C  
ANISOU 1952  CA  PRO A 298    18494   8323   8712    760    226    876       C  
ATOM   1953  C   PRO A 298      29.539   7.689  90.422  1.00 98.52           C  
ANISOU 1953  C   PRO A 298    18920   9065   9447   1219    235    960       C  
ATOM   1954  O   PRO A 298      28.875   8.428  91.149  1.00100.15           O  
ANISOU 1954  O   PRO A 298    19393   9083   9578   1486    340    995       O  
ATOM   1955  CB  PRO A 298      31.892   6.718  90.252  1.00 92.32           C  
ANISOU 1955  CB  PRO A 298    17908   8460   8710    456    149    783       C  
ATOM   1956  CG  PRO A 298      32.424   6.685  91.689  1.00 96.40           C  
ANISOU 1956  CG  PRO A 298    18479   8925   9225    292    192    686       C  
ATOM   1957  CD  PRO A 298      32.055   7.980  92.369  1.00 94.57           C  
ANISOU 1957  CD  PRO A 298    18767   8347   8818    428    297    705       C  
ATOM   1958  N   SER A 299      29.020   6.611  89.815  1.00 94.00           N  
ANISOU 1958  N   SER A 299    17885   8799   9031   1301    132    997       N  
ATOM   1959  CA  SER A 299      27.634   6.166  89.965  1.00 94.33           C  
ANISOU 1959  CA  SER A 299    17634   9025   9181   1671    114   1091       C  
ATOM   1960  C   SER A 299      27.553   4.632  90.069  1.00 96.72           C  
ANISOU 1960  C   SER A 299    17415   9661   9673   1550     16   1042       C  
ATOM   1961  O   SER A 299      28.508   3.936  89.708  1.00 94.40           O  
ANISOU 1961  O   SER A 299    16996   9456   9416   1239    -48    958       O  
ATOM   1962  CB  SER A 299      26.772   6.695  88.825  1.00 99.58           C  
ANISOU 1962  CB  SER A 299    18363   9694   9778   1950     66   1247       C  
ATOM   1963  OG  SER A 299      27.336   6.380  87.563  1.00108.53           O  
ANISOU 1963  OG  SER A 299    19447  10899  10891   1721    -44   1244       O  
ATOM   1964  N   GLU A 300      26.415   4.108  90.564  1.00 94.35           N  
ANISOU 1964  N   GLU A 300    16823   9545   9481   1802     14   1103       N  
ATOM   1965  CA  GLU A 300      26.187   2.669  90.742  1.00 92.63           C  
ANISOU 1965  CA  GLU A 300    16148   9623   9425   1705    -71   1070       C  
ATOM   1966  C   GLU A 300      26.023   1.899  89.409  1.00 96.55           C  
ANISOU 1966  C   GLU A 300    16409  10322   9953   1615   -229   1118       C  
ATOM   1967  O   GLU A 300      25.446   0.807  89.386  1.00 95.20           O  
ANISOU 1967  O   GLU A 300    15887  10399   9887   1604   -314   1138       O  
ATOM   1968  CB  GLU A 300      25.000   2.431  91.691  1.00 94.90           C  
ANISOU 1968  CB  GLU A 300    16223  10041   9792   1988    -12   1141       C  
ATOM   1969  N   SER A 301      26.568   2.466  88.312  1.00 94.29           N  
ANISOU 1969  N   SER A 301    16354   9917   9556   1527   -264   1134       N  
ATOM   1970  CA  SER A 301      26.557   1.924  86.952  1.00 94.14           C  
ANISOU 1970  CA  SER A 301    16217  10033   9518   1427   -401   1173       C  
ATOM   1971  C   SER A 301      27.240   0.556  86.902  1.00 95.02           C  
ANISOU 1971  C   SER A 301    16089  10299   9717   1143   -455   1058       C  
ATOM   1972  O   SER A 301      26.564  -0.449  86.667  1.00 94.42           O  
ANISOU 1972  O   SER A 301    15728  10437   9710   1147   -558   1087       O  
ATOM   1973  CB  SER A 301      27.238   2.897  85.992  1.00 99.56           C  
ANISOU 1973  CB  SER A 301    17264  10513  10051   1354   -385   1190       C  
ATOM   1974  OG  SER A 301      28.553   3.206  86.428  1.00108.92           O  
ANISOU 1974  OG  SER A 301    18655  11533  11197   1093   -288   1069       O  
ATOM   1975  N   ASP A 302      28.563   0.512  87.157  1.00 89.31           N  
ANISOU 1975  N   ASP A 302    15482   9472   8978    901   -383    937       N  
ATOM   1976  CA  ASP A 302      29.314  -0.736  87.164  1.00 86.54           C  
ANISOU 1976  CA  ASP A 302    14933   9254   8697    675   -407    836       C  
ATOM   1977  C   ASP A 302      30.445  -0.741  88.194  1.00 86.78           C  
ANISOU 1977  C   ASP A 302    15004   9216   8753    509   -310    726       C  
ATOM   1978  O   ASP A 302      30.538   0.175  89.009  1.00 86.93           O  
ANISOU 1978  O   ASP A 302    15206   9084   8739    550   -234    721       O  
ATOM   1979  CB  ASP A 302      29.802  -1.114  85.759  1.00 88.51           C  
ANISOU 1979  CB  ASP A 302    15214   9545   8872    534   -466    837       C  
ATOM   1980  CG  ASP A 302      29.624  -2.593  85.450  1.00 97.32           C  
ANISOU 1980  CG  ASP A 302    16088  10845  10045    455   -547    801       C  
ATOM   1981  OD1 ASP A 302      29.952  -3.429  86.325  1.00 95.34           O  
ANISOU 1981  OD1 ASP A 302    15683  10658   9884    389   -514    722       O  
ATOM   1982  OD2 ASP A 302      29.157  -2.915  84.332  1.00104.92           O  
ANISOU 1982  OD2 ASP A 302    17047  11872  10944    453   -647    853       O  
ATOM   1983  N   TYR A 303      31.262  -1.801  88.188  1.00 80.11           N  
ANISOU 1983  N   TYR A 303    13998   8485   7954    333   -315    646       N  
ATOM   1984  CA  TYR A 303      32.327  -2.033  89.153  1.00 78.21           C  
ANISOU 1984  CA  TYR A 303    13725   8245   7746    181   -249    558       C  
ATOM   1985  C   TYR A 303      33.643  -1.324  88.831  1.00 78.87           C  
ANISOU 1985  C   TYR A 303    13979   8254   7735    -27   -189    537       C  
ATOM   1986  O   TYR A 303      34.417  -1.072  89.753  1.00 78.08           O  
ANISOU 1986  O   TYR A 303    13913   8125   7630   -152   -144    492       O  
ATOM   1987  CB  TYR A 303      32.523  -3.553  89.349  1.00 78.56           C  
ANISOU 1987  CB  TYR A 303    13513   8458   7879    134   -277    501       C  
ATOM   1988  CG  TYR A 303      33.672  -4.224  88.618  1.00 80.13           C  
ANISOU 1988  CG  TYR A 303    13662   8739   8047    -19   -255    460       C  
ATOM   1989  CD1 TYR A 303      34.870  -4.503  89.271  1.00 82.05           C  
ANISOU 1989  CD1 TYR A 303    13833   9038   8304   -144   -196    406       C  
ATOM   1990  CD2 TYR A 303      33.517  -4.691  87.315  1.00 80.67           C  
ANISOU 1990  CD2 TYR A 303    13738   8850   8063    -19   -292    484       C  
ATOM   1991  CE1 TYR A 303      35.914  -5.158  88.624  1.00 83.04           C  
ANISOU 1991  CE1 TYR A 303    13883   9268   8399   -237   -153    387       C  
ATOM   1992  CE2 TYR A 303      34.550  -5.364  86.661  1.00 81.33           C  
ANISOU 1992  CE2 TYR A 303    13792   9006   8106   -122   -242    450       C  
ATOM   1993  CZ  TYR A 303      35.750  -5.586  87.319  1.00 89.53           C  
ANISOU 1993  CZ  TYR A 303    14741  10110   9166   -214   -163    406       C  
ATOM   1994  OH  TYR A 303      36.788  -6.237  86.696  1.00 91.56           O  
ANISOU 1994  OH  TYR A 303    14946  10465   9379   -273    -90    390       O  
ATOM   1995  N   LEU A 304      33.918  -1.040  87.547  1.00 73.38           N  
ANISOU 1995  N   LEU A 304    13385   7541   6953    -86   -193    575       N  
ATOM   1996  CA  LEU A 304      35.162  -0.376  87.167  1.00 72.64           C  
ANISOU 1996  CA  LEU A 304    13438   7401   6761   -309   -125    569       C  
ATOM   1997  C   LEU A 304      34.999   1.108  86.913  1.00 76.32           C  
ANISOU 1997  C   LEU A 304    14248   7648   7102   -317    -99    625       C  
ATOM   1998  O   LEU A 304      33.922   1.563  86.521  1.00 76.25           O  
ANISOU 1998  O   LEU A 304    14364   7541   7068   -110   -137    688       O  
ATOM   1999  CB  LEU A 304      35.844  -1.066  85.985  1.00 72.30           C  
ANISOU 1999  CB  LEU A 304    13303   7485   6684   -407   -106    569       C  
ATOM   2000  CG  LEU A 304      36.632  -2.324  86.315  1.00 75.44           C  
ANISOU 2000  CG  LEU A 304    13432   8073   7157   -463    -79    510       C  
ATOM   2001  CD1 LEU A 304      37.056  -3.035  85.058  1.00 75.70           C  
ANISOU 2001  CD1 LEU A 304    13421   8201   7140   -479    -49    516       C  
ATOM   2002  CD2 LEU A 304      37.851  -2.021  87.177  1.00 78.36           C  
ANISOU 2002  CD2 LEU A 304    13748   8503   7525   -657    -17    487       C  
ATOM   2003  N   VAL A 305      36.082   1.864  87.157  1.00 72.98           N  
ANISOU 2003  N   VAL A 305    13985   7155   6591   -562    -37    611       N  
ATOM   2004  CA  VAL A 305      36.133   3.317  87.014  1.00 74.53           C  
ANISOU 2004  CA  VAL A 305    14576   7107   6636   -634      2    656       C  
ATOM   2005  C   VAL A 305      37.578   3.791  86.681  1.00 78.88           C  
ANISOU 2005  C   VAL A 305    15218   7677   7077   -999     63    654       C  
ATOM   2006  O   VAL A 305      38.539   3.217  87.194  1.00 77.88           O  
ANISOU 2006  O   VAL A 305    14863   7728   6999  -1191     75    612       O  
ATOM   2007  CB  VAL A 305      35.494   3.992  88.268  1.00 78.98           C  
ANISOU 2007  CB  VAL A 305    15331   7487   7191   -506     11    643       C  
ATOM   2008  CG1 VAL A 305      36.468   4.135  89.440  1.00 78.98           C  
ANISOU 2008  CG1 VAL A 305    15347   7488   7174   -760     35    577       C  
ATOM   2009  CG2 VAL A 305      34.838   5.315  87.921  1.00 80.89           C  
ANISOU 2009  CG2 VAL A 305    16001   7446   7290   -372     41    714       C  
ATOM   2010  N   ALA A 306      37.725   4.790  85.783  1.00 76.74           N  
ANISOU 2010  N   ALA A 306    15257   7247   6653  -1092    100    714       N  
ATOM   2011  CA  ALA A 306      39.033   5.319  85.375  1.00 78.12           C  
ANISOU 2011  CA  ALA A 306    15534   7444   6705  -1460    166    733       C  
ATOM   2012  C   ALA A 306      39.101   6.837  85.510  1.00 85.21           C  
ANISOU 2012  C   ALA A 306    16931   8032   7413  -1617    200    767       C  
ATOM   2013  O   ALA A 306      38.139   7.525  85.167  1.00 85.51           O  
ANISOU 2013  O   ALA A 306    17285   7829   7377  -1392    195    812       O  
ATOM   2014  CB  ALA A 306      39.358   4.893  83.960  1.00 78.85           C  
ANISOU 2014  CB  ALA A 306    15528   7663   6767  -1482    202    774       C  
ATOM   2015  N   TYR A 307      40.224   7.355  86.045  1.00 84.22           N  
ANISOU 2015  N   TYR A 307    16888   7916   7198  -2003    231    756       N  
ATOM   2016  CA  TYR A 307      40.412   8.785  86.313  1.00 87.42           C  
ANISOU 2016  CA  TYR A 307    17815   8006   7394  -2224    261    779       C  
ATOM   2017  C   TYR A 307      41.350   9.474  85.327  1.00 95.73           C  
ANISOU 2017  C   TYR A 307    19058   9039   8276  -2581    326    843       C  
ATOM   2018  O   TYR A 307      41.427  10.706  85.323  1.00 97.77           O  
ANISOU 2018  O   TYR A 307    19822   8994   8331  -2762    358    873       O  
ATOM   2019  CB  TYR A 307      40.884   9.024  87.766  1.00 89.12           C  
ANISOU 2019  CB  TYR A 307    18091   8186   7583  -2441    230    721       C  
ATOM   2020  CG  TYR A 307      40.142   8.234  88.826  1.00 88.50           C  
ANISOU 2020  CG  TYR A 307    17772   8180   7674  -2143    178    655       C  
ATOM   2021  CD1 TYR A 307      38.895   8.646  89.288  1.00 90.47           C  
ANISOU 2021  CD1 TYR A 307    18292   8168   7915  -1793    184    645       C  
ATOM   2022  CD2 TYR A 307      40.713   7.109  89.411  1.00 87.51           C  
ANISOU 2022  CD2 TYR A 307    17164   8384   7702  -2210    134    614       C  
ATOM   2023  CE1 TYR A 307      38.216   7.932  90.277  1.00 89.44           C  
ANISOU 2023  CE1 TYR A 307    17938   8114   7932  -1537    152    593       C  
ATOM   2024  CE2 TYR A 307      40.044   6.386  90.396  1.00 86.67           C  
ANISOU 2024  CE2 TYR A 307    16864   8330   7737  -1957     91    557       C  
ATOM   2025  CZ  TYR A 307      38.796   6.803  90.829  1.00 95.19           C  
ANISOU 2025  CZ  TYR A 307    18205   9154   8809  -1636    102    545       C  
ATOM   2026  OH  TYR A 307      38.140   6.087  91.804  1.00 96.89           O  
ANISOU 2026  OH  TYR A 307    18221   9436   9156  -1404     75    497       O  
ATOM   2027  N   ASP A 308      42.063   8.685  84.499  1.00 93.43           N  
ANISOU 2027  N   ASP A 308    18393   9056   8050  -2679    361    868       N  
ATOM   2028  CA  ASP A 308      43.000   9.188  83.487  1.00 96.15           C  
ANISOU 2028  CA  ASP A 308    18854   9438   8242  -3011    446    940       C  
ATOM   2029  C   ASP A 308      42.256   9.743  82.273  1.00100.76           C  
ANISOU 2029  C   ASP A 308    19788   9779   8716  -2809    477    996       C  
ATOM   2030  O   ASP A 308      41.198   9.222  81.914  1.00 98.45           O  
ANISOU 2030  O   ASP A 308    19416   9467   8524  -2401    430    988       O  
ATOM   2031  CB  ASP A 308      43.981   8.085  83.055  1.00 97.79           C  
ANISOU 2031  CB  ASP A 308    18531  10074   8552  -3129    500    955       C  
ATOM   2032  CG  ASP A 308      44.848   7.551  84.181  1.00111.87           C  
ANISOU 2032  CG  ASP A 308    19919  12150  10438  -3314    466    924       C  
ATOM   2033  OD1 ASP A 308      44.298   6.885  85.095  1.00111.02           O  
ANISOU 2033  OD1 ASP A 308    19629  12073  10479  -3065    388    856       O  
ATOM   2034  OD2 ASP A 308      46.081   7.763  84.131  1.00120.39           O  
ANISOU 2034  OD2 ASP A 308    20837  13458  11448  -3700    519    980       O  
ATOM   2035  N   GLN A 309      42.828  10.781  81.633  1.00100.45           N  
ANISOU 2035  N   GLN A 309    20127   9577   8463  -3117    549   1063       N  
ATOM   2036  CA  GLN A 309      42.272  11.476  80.466  1.00101.81           C  
ANISOU 2036  CA  GLN A 309    20704   9498   8482  -2994    585   1134       C  
ATOM   2037  C   GLN A 309      41.791  10.554  79.333  1.00103.97           C  
ANISOU 2037  C   GLN A 309    20717   9941   8846  -2692    583   1154       C  
ATOM   2038  O   GLN A 309      40.641  10.681  78.912  1.00103.30           O  
ANISOU 2038  O   GLN A 309    20832   9673   8745  -2336    526   1182       O  
ATOM   2039  CB  GLN A 309      43.270  12.519  79.919  1.00106.61           C  
ANISOU 2039  CB  GLN A 309    21659   9999   8851  -3476    683   1204       C  
ATOM   2040  CG  GLN A 309      42.621  13.828  79.454  1.00124.51           C  
ANISOU 2040  CG  GLN A 309    24619  11806  10883  -3425    702   1265       C  
ATOM   2041  CD  GLN A 309      41.739  13.670  78.236  1.00145.06           C  
ANISOU 2041  CD  GLN A 309    27311  14331  13473  -3037    692   1320       C  
ATOM   2042  OE1 GLN A 309      42.203  13.361  77.132  1.00142.31           O  
ANISOU 2042  OE1 GLN A 309    26844  14141  13086  -3131    755   1367       O  
ATOM   2043  NE2 GLN A 309      40.439  13.857  78.419  1.00135.95           N  
ANISOU 2043  NE2 GLN A 309    26345  12960  12351  -2582    612   1323       N  
ATOM   2044  N   GLU A 310      42.653   9.624  78.865  1.00 99.68           N  
ANISOU 2044  N   GLU A 310    19740   9751   8382  -2825    645   1149       N  
ATOM   2045  CA  GLU A 310      42.396   8.687  77.757  1.00 98.45           C  
ANISOU 2045  CA  GLU A 310    19369   9761   8277  -2599    663   1162       C  
ATOM   2046  C   GLU A 310      41.067   7.895  77.842  1.00100.32           C  
ANISOU 2046  C   GLU A 310    19472   9984   8660  -2137    537   1121       C  
ATOM   2047  O   GLU A 310      40.627   7.351  76.827  1.00 98.64           O  
ANISOU 2047  O   GLU A 310    19219   9823   8438  -1949    522   1142       O  
ATOM   2048  CB  GLU A 310      43.585   7.720  77.566  1.00 99.55           C  
ANISOU 2048  CB  GLU A 310    19046  10291   8489  -2784    769   1154       C  
ATOM   2049  CG  GLU A 310      43.899   6.830  78.761  1.00108.20           C  
ANISOU 2049  CG  GLU A 310    19698  11635   9780  -2758    729   1084       C  
ATOM   2050  CD  GLU A 310      45.313   6.896  79.308  1.00127.94           C  
ANISOU 2050  CD  GLU A 310    21967  14382  12265  -3159    809   1110       C  
ATOM   2051  OE1 GLU A 310      45.900   5.816  79.549  1.00116.84           O  
ANISOU 2051  OE1 GLU A 310    20101  13310  10983  -3126    850   1095       O  
ATOM   2052  OE2 GLU A 310      45.821   8.019  79.534  1.00123.67           O  
ANISOU 2052  OE2 GLU A 310    21709  13703  11576  -3506    826   1153       O  
ATOM   2053  N   TRP A 311      40.432   7.846  79.027  1.00 97.26           N  
ANISOU 2053  N   TRP A 311    19032   9531   8391  -1975    447   1070       N  
ATOM   2054  CA  TRP A 311      39.180   7.110  79.231  1.00 95.83           C  
ANISOU 2054  CA  TRP A 311    18690   9368   8353  -1572    330   1041       C  
ATOM   2055  C   TRP A 311      37.918   7.990  79.197  1.00102.69           C  
ANISOU 2055  C   TRP A 311    19926   9943   9148  -1295    254   1098       C  
ATOM   2056  O   TRP A 311      36.840   7.519  79.573  1.00100.92           O  
ANISOU 2056  O   TRP A 311    19559   9743   9042   -975    157   1089       O  
ATOM   2057  CB  TRP A 311      39.239   6.279  80.522  1.00 92.45           C  
ANISOU 2057  CB  TRP A 311    17898   9112   8117  -1533    293    956       C  
ATOM   2058  CG  TRP A 311      40.323   5.241  80.533  1.00 92.47           C  
ANISOU 2058  CG  TRP A 311    17500   9429   8205  -1704    357    916       C  
ATOM   2059  CD1 TRP A 311      41.610   5.408  80.949  1.00 96.41           C  
ANISOU 2059  CD1 TRP A 311    17890  10063   8677  -2040    439    914       C  
ATOM   2060  CD2 TRP A 311      40.201   3.865  80.148  1.00 90.52           C  
ANISOU 2060  CD2 TRP A 311    16915   9407   8071  -1535    346    882       C  
ATOM   2061  NE1 TRP A 311      42.312   4.236  80.801  1.00 94.87           N  
ANISOU 2061  NE1 TRP A 311    17290  10180   8577  -2050    492    893       N  
ATOM   2062  CE2 TRP A 311      41.468   3.265  80.331  1.00 94.45           C  
ANISOU 2062  CE2 TRP A 311    17118  10162   8605  -1738    443    865       C  
ATOM   2063  CE3 TRP A 311      39.145   3.079  79.655  1.00 90.46           C  
ANISOU 2063  CE3 TRP A 311    16837   9412   8122  -1241    259    873       C  
ATOM   2064  CZ2 TRP A 311      41.709   1.918  80.038  1.00 92.51           C  
ANISOU 2064  CZ2 TRP A 311    16555  10149   8447  -1616    478    833       C  
ATOM   2065  CZ3 TRP A 311      39.382   1.741  79.376  1.00 90.75           C  
ANISOU 2065  CZ3 TRP A 311    16578   9666   8236  -1173    279    831       C  
ATOM   2066  CH2 TRP A 311      40.653   1.176  79.557  1.00 91.49           C  
ANISOU 2066  CH2 TRP A 311    16425   9978   8357  -1340    398    809       C  
ATOM   2067  N   GLU A 312      38.037   9.246  78.720  1.00103.36           N  
ANISOU 2067  N   GLU A 312    20480   9762   9029  -1406    303   1168       N  
ATOM   2068  CA  GLU A 312      36.901  10.164  78.630  1.00105.44           C  
ANISOU 2068  CA  GLU A 312    21136   9732   9193  -1112    251   1242       C  
ATOM   2069  C   GLU A 312      35.943   9.702  77.533  1.00110.94           C  
ANISOU 2069  C   GLU A 312    21759  10499   9896   -798    154   1310       C  
ATOM   2070  O   GLU A 312      36.356   9.540  76.380  1.00110.68           O  
ANISOU 2070  O   GLU A 312    21746  10534   9774   -914    175   1341       O  
ATOM   2071  CB  GLU A 312      37.373  11.610  78.376  1.00109.99           C  
ANISOU 2071  CB  GLU A 312    22285   9983   9524  -1332    338   1301       C  
ATOM   2072  CG  GLU A 312      36.295  12.665  78.599  1.00122.14           C  
ANISOU 2072  CG  GLU A 312    24284  11176  10947  -1010    312   1373       C  
ATOM   2073  CD  GLU A 312      36.407  13.933  77.770  1.00142.79           C  
ANISOU 2073  CD  GLU A 312    27505  13459  13288  -1100    374   1470       C  
ATOM   2074  OE1 GLU A 312      37.546  14.384  77.508  1.00136.86           O  
ANISOU 2074  OE1 GLU A 312    26927  12667  12408  -1543    466   1461       O  
ATOM   2075  OE2 GLU A 312      35.349  14.502  77.417  1.00136.98           O  
ANISOU 2075  OE2 GLU A 312    27075  12511  12460   -725    332   1565       O  
ATOM   2076  N   ALA A 313      34.676   9.445  77.912  1.00108.88           N  
ANISOU 2076  N   ALA A 313    21393  10245   9733   -414     47   1337       N  
ATOM   2077  CA  ALA A 313      33.627   9.014  76.981  1.00109.65           C  
ANISOU 2077  CA  ALA A 313    21387  10439   9835   -115    -82   1417       C  
ATOM   2078  C   ALA A 313      32.231   9.493  77.393  1.00115.39           C  
ANISOU 2078  C   ALA A 313    22199  11065  10578    308   -166   1507       C  
ATOM   2079  O   ALA A 313      31.899   9.494  78.589  1.00114.12           O  
ANISOU 2079  O   ALA A 313    21942  10891  10528    423   -145   1467       O  
ATOM   2080  CB  ALA A 313      33.642   7.502  76.809  1.00108.02           C  
ANISOU 2080  CB  ALA A 313    20690  10560   9795   -139   -148   1347       C  
ATOM   2081  N   CYS A 314      31.424   9.906  76.380  1.00113.83           N  
ANISOU 2081  N   CYS A 314    22181  10811  10259    549   -257   1640       N  
ATOM   2082  CA  CYS A 314      30.052  10.406  76.518  1.00142.13           C  
ANISOU 2082  CA  CYS A 314    25829  14342  13831    998   -344   1769       C  
ATOM   2083  C   CYS A 314      29.251  10.122  75.249  1.00156.46           C  
ANISOU 2083  C   CYS A 314    27577  16295  15576   1188   -510   1897       C  
ATOM   2084  O   CYS A 314      28.194   9.498  75.310  1.00111.78           O  
ANISOU 2084  O   CYS A 314    21587  10862  10024   1450   -651   1962       O  
ATOM   2085  CB  CYS A 314      30.042  11.894  76.862  1.00145.05           C  
ANISOU 2085  CB  CYS A 314    26743  14336  14033   1122   -231   1833       C  
ATOM   2086  SG  CYS A 314      30.063  12.250  78.641  1.00148.31           S  
ANISOU 2086  SG  CYS A 314    27181  14624  14548   1180   -110   1745       S  
ATOM   2087  N   LEU A 324      26.185  10.206 102.496  1.00117.68           N  
ANISOU 2087  N   LEU A 324    23303  10154  11258   2689   1498    652       N  
ATOM   2088  CA  LEU A 324      27.598  10.377 102.823  1.00117.12           C  
ANISOU 2088  CA  LEU A 324    23565   9888  11048   2141   1383    508       C  
ATOM   2089  C   LEU A 324      28.467  10.503 101.563  1.00119.95           C  
ANISOU 2089  C   LEU A 324    23874  10277  11426   1811   1210    511       C  
ATOM   2090  O   LEU A 324      28.638   9.538 100.809  1.00116.99           O  
ANISOU 2090  O   LEU A 324    22930  10249  11272   1701   1063    532       O  
ATOM   2091  CB  LEU A 324      28.084   9.231 103.698  1.00115.35           C  
ANISOU 2091  CB  LEU A 324    22990   9894  10944   1839   1283    404       C  
ATOM   2092  N   HIS A 325      28.999  11.720 101.342  1.00118.15           N  
ANISOU 2092  N   HIS A 325    24281   9667  10942   1649   1240    490       N  
ATOM   2093  CA  HIS A 325      29.852  12.098 100.211  1.00116.96           C  
ANISOU 2093  CA  HIS A 325    24215   9476  10748   1318   1112    497       C  
ATOM   2094  C   HIS A 325      31.333  11.951 100.586  1.00117.53           C  
ANISOU 2094  C   HIS A 325    24347   9556  10753    679    963    374       C  
ATOM   2095  O   HIS A 325      32.128  11.483  99.770  1.00115.07           O  
ANISOU 2095  O   HIS A 325    23733   9451  10536    350    814    371       O  
ATOM   2096  CB  HIS A 325      29.550  13.553  99.829  1.00121.57           C  
ANISOU 2096  CB  HIS A 325    25507   9618  11065   1517   1246    560       C  
ATOM   2097  CG  HIS A 325      29.816  13.889  98.397  1.00125.06           C  
ANISOU 2097  CG  HIS A 325    25924  10079  11516   1445   1162    636       C  
ATOM   2098  ND1 HIS A 325      28.857  13.686  97.424  1.00126.26           N  
ANISOU 2098  ND1 HIS A 325    25702  10443  11828   1856   1161    767       N  
ATOM   2099  CD2 HIS A 325      30.905  14.457  97.827  1.00127.66           C  
ANISOU 2099  CD2 HIS A 325    26577  10235  11692   1005   1083    606       C  
ATOM   2100  CE1 HIS A 325      29.395  14.120  96.297  1.00126.01           C  
ANISOU 2100  CE1 HIS A 325    25798  10345  11734   1671   1084    805       C  
ATOM   2101  NE2 HIS A 325      30.629  14.585  96.489  1.00127.17           N  
ANISOU 2101  NE2 HIS A 325    26354  10267  11700   1159   1043    712       N  
ATOM   2102  N   ASN A 326      31.688  12.357 101.830  1.00114.07           N  
ANISOU 2102  N   ASN A 326    24299   8904  10138    514   1009    284       N  
ATOM   2103  CA  ASN A 326      33.041  12.336 102.401  1.00112.95           C  
ANISOU 2103  CA  ASN A 326    24268   8760   9889    -87    867    180       C  
ATOM   2104  C   ASN A 326      33.655  10.944 102.446  1.00110.48           C  
ANISOU 2104  C   ASN A 326    23225   8918   9834   -324    695    147       C  
ATOM   2105  O   ASN A 326      34.844  10.800 102.150  1.00109.33           O  
ANISOU 2105  O   ASN A 326    22949   8911   9682   -799    542    120       O  
ATOM   2106  CB  ASN A 326      33.049  12.952 103.800  1.00116.42           C  
ANISOU 2106  CB  ASN A 326    25291   8870  10073   -140    959    100       C  
ATOM   2107  CG  ASN A 326      32.497  14.349 103.845  1.00143.88           C  
ANISOU 2107  CG  ASN A 326    29575  11837  13257    105   1150    127       C  
ATOM   2108  OD1 ASN A 326      31.292  14.559 104.015  1.00140.12           O  
ANISOU 2108  OD1 ASN A 326    29203  11247  12788    680   1344    190       O  
ATOM   2109  ND2 ASN A 326      33.366  15.331 103.680  1.00138.26           N  
ANISOU 2109  ND2 ASN A 326    29445  10814  12272   -322   1104     92       N  
ATOM   2110  N   LEU A 327      32.851   9.925 102.813  1.00102.96           N  
ANISOU 2110  N   LEU A 327    21810   8213   9098      8    729    159       N  
ATOM   2111  CA  LEU A 327      33.293   8.534 102.903  1.00 98.84           C  
ANISOU 2111  CA  LEU A 327    20633   8109   8813   -148    588    133       C  
ATOM   2112  C   LEU A 327      33.737   8.016 101.532  1.00 99.26           C  
ANISOU 2112  C   LEU A 327    20255   8428   9033   -273    473    181       C  
ATOM   2113  O   LEU A 327      34.718   7.272 101.455  1.00 97.20           O  
ANISOU 2113  O   LEU A 327    19640   8430   8863   -596    334    150       O  
ATOM   2114  CB  LEU A 327      32.181   7.652 103.491  1.00 97.39           C  
ANISOU 2114  CB  LEU A 327    20110   8092   8802    257    673    151       C  
ATOM   2115  CG  LEU A 327      32.634   6.389 104.226  1.00 99.67           C  
ANISOU 2115  CG  LEU A 327    19956   8678   9235     83    564     95       C  
ATOM   2116  CD1 LEU A 327      31.742   6.109 105.417  1.00 99.86           C  
ANISOU 2116  CD1 LEU A 327    20020   8664   9258    365    690     79       C  
ATOM   2117  CD2 LEU A 327      32.657   5.183 103.292  1.00 99.56           C  
ANISOU 2117  CD2 LEU A 327    19308   9038   9484    103    461    135       C  
ATOM   2118  N   ILE A 328      33.031   8.436 100.456  1.00 94.89           N  
ANISOU 2118  N   ILE A 328    19746   7806   8501     -2    537    264       N  
ATOM   2119  CA  ILE A 328      33.343   8.071  99.067  1.00 92.36           C  
ANISOU 2119  CA  ILE A 328    19097   7691   8304    -82    448    316       C  
ATOM   2120  C   ILE A 328      34.711   8.658  98.688  1.00 95.35           C  
ANISOU 2120  C   ILE A 328    19694   7999   8536   -578    366    288       C  
ATOM   2121  O   ILE A 328      35.532   7.948  98.113  1.00 93.05           O  
ANISOU 2121  O   ILE A 328    19014   7986   8356   -828    259    287       O  
ATOM   2122  CB  ILE A 328      32.212   8.486  98.066  1.00 96.09           C  
ANISOU 2122  CB  ILE A 328    19636   8077   8794    337    532    422       C  
ATOM   2123  CG1 ILE A 328      30.782   8.076  98.550  1.00 96.53           C  
ANISOU 2123  CG1 ILE A 328    19510   8206   8963    831    632    472       C  
ATOM   2124  CG2 ILE A 328      32.486   7.982  96.646  1.00 94.74           C  
ANISOU 2124  CG2 ILE A 328    19124   8128   8744    262    434    473       C  
ATOM   2125  CD1 ILE A 328      30.435   6.504  98.713  1.00102.87           C  
ANISOU 2125  CD1 ILE A 328    19639   9415  10032    904    556    469       C  
ATOM   2126  N   ARG A 329      34.963   9.928  99.065  1.00 93.98           N  
ANISOU 2126  N   ARG A 329    20152   7458   8099   -730    423    270       N  
ATOM   2127  CA  ARG A 329      36.219  10.636  98.800  1.00 95.21           C  
ANISOU 2127  CA  ARG A 329    20596   7510   8069  -1246    353    253       C  
ATOM   2128  C   ARG A 329      37.428   9.942  99.438  1.00 97.08           C  
ANISOU 2128  C   ARG A 329    20514   8026   8346  -1692    210    196       C  
ATOM   2129  O   ARG A 329      38.454   9.789  98.771  1.00 96.06           O  
ANISOU 2129  O   ARG A 329    20161   8102   8237  -2043    119    219       O  
ATOM   2130  CB  ARG A 329      36.124  12.106  99.243  1.00 99.24           C  
ANISOU 2130  CB  ARG A 329    21915   7531   8262  -1304    451    238       C  
ATOM   2131  N   GLU A 330      37.292   9.499 100.711  1.00 92.91           N  
ANISOU 2131  N   GLU A 330    19949   7525   7827  -1654    198    135       N  
ATOM   2132  CA  GLU A 330      38.335   8.797 101.470  1.00 91.87           C  
ANISOU 2132  CA  GLU A 330    19518   7662   7726  -2018     56     92       C  
ATOM   2133  C   GLU A 330      38.738   7.485 100.770  1.00 92.33           C  
ANISOU 2133  C   GLU A 330    18862   8171   8049  -2008    -29    126       C  
ATOM   2134  O   GLU A 330      39.930   7.187 100.663  1.00 92.55           O  
ANISOU 2134  O   GLU A 330    18646   8443   8075  -2390   -145    138       O  
ATOM   2135  CB  GLU A 330      37.867   8.526 102.914  1.00 93.21           C  
ANISOU 2135  CB  GLU A 330    19792   7756   7866  -1873     80     28       C  
ATOM   2136  CG  GLU A 330      38.988   8.137 103.868  1.00106.38           C  
ANISOU 2136  CG  GLU A 330    21344   9605   9469  -2299    -77    -13       C  
ATOM   2137  CD  GLU A 330      38.564   7.774 105.283  1.00134.38           C  
ANISOU 2137  CD  GLU A 330    24959  13107  12990  -2161    -63    -73       C  
ATOM   2138  OE1 GLU A 330      38.714   6.589 105.664  1.00123.89           O  
ANISOU 2138  OE1 GLU A 330    23132  12099  11842  -2112   -140    -76       O  
ATOM   2139  OE2 GLU A 330      38.119   8.683 106.023  1.00135.05           O  
ANISOU 2139  OE2 GLU A 330    25633  12823  12857  -2109     31   -117       O  
ATOM   2140  N   CYS A 331      37.745   6.730 100.272  1.00 85.41           N  
ANISOU 2140  N   CYS A 331    17668   7404   7381  -1576     33    149       N  
ATOM   2141  CA  CYS A 331      37.947   5.464  99.569  1.00 82.07           C  
ANISOU 2141  CA  CYS A 331    16640   7352   7189  -1513    -25    176       C  
ATOM   2142  C   CYS A 331      38.638   5.630  98.209  1.00 84.33           C  
ANISOU 2142  C   CYS A 331    16816   7745   7478  -1698    -48    231       C  
ATOM   2143  O   CYS A 331      39.503   4.819  97.875  1.00 82.64           O  
ANISOU 2143  O   CYS A 331    16199   7842   7359  -1873   -119    246       O  
ATOM   2144  CB  CYS A 331      36.631   4.707  99.441  1.00 80.42           C  
ANISOU 2144  CB  CYS A 331    16191   7200   7163  -1046     40    188       C  
ATOM   2145  SG  CYS A 331      35.982   4.074 101.007  1.00 83.74           S  
ANISOU 2145  SG  CYS A 331    16600   7600   7619   -844     73    134       S  
ATOM   2146  N   ILE A 332      38.259   6.673  97.430  1.00 81.40           N  
ANISOU 2146  N   ILE A 332    16816   7118   6993  -1643     23    268       N  
ATOM   2147  CA  ILE A 332      38.832   6.968  96.107  1.00 81.34           C  
ANISOU 2147  CA  ILE A 332    16781   7165   6958  -1813     20    325       C  
ATOM   2148  C   ILE A 332      40.346   7.188  96.214  1.00 87.24           C  
ANISOU 2148  C   ILE A 332    17496   8055   7598  -2340    -56    329       C  
ATOM   2149  O   ILE A 332      41.099   6.662  95.392  1.00 86.72           O  
ANISOU 2149  O   ILE A 332    17093   8256   7602  -2488    -80    372       O  
ATOM   2150  CB  ILE A 332      38.084   8.125  95.372  1.00 85.78           C  
ANISOU 2150  CB  ILE A 332    17822   7384   7385  -1645    111    370       C  
ATOM   2151  CG1 ILE A 332      36.612   7.742  95.089  1.00 84.33           C  
ANISOU 2151  CG1 ILE A 332    17535   7170   7335  -1110    169    399       C  
ATOM   2152  CG2 ILE A 332      38.794   8.516  94.056  1.00 87.43           C  
ANISOU 2152  CG2 ILE A 332    18058   7632   7530  -1880    109    429       C  
ATOM   2153  CD1 ILE A 332      35.633   8.910  94.811  1.00 91.23           C  
ANISOU 2153  CD1 ILE A 332    18926   7677   8061   -832    270    448       C  
ATOM   2154  N   LEU A 333      40.780   7.912  97.259  1.00 86.13           N  
ANISOU 2154  N   LEU A 333    17692   7756   7280  -2619    -93    292       N  
ATOM   2155  CA  LEU A 333      42.185   8.202  97.557  1.00 88.22           C  
ANISOU 2155  CA  LEU A 333    17946   8163   7412  -3164   -189    307       C  
ATOM   2156  C   LEU A 333      43.028   6.919  97.684  1.00 91.46           C  
ANISOU 2156  C   LEU A 333    17703   9050   7998  -3252   -278    327       C  
ATOM   2157  O   LEU A 333      44.156   6.876  97.188  1.00 92.26           O  
ANISOU 2157  O   LEU A 333    17575   9407   8074  -3590   -322    388       O  
ATOM   2158  CB  LEU A 333      42.272   9.026  98.865  1.00 90.46           C  
ANISOU 2158  CB  LEU A 333    18716   8178   7475  -3388   -228    251       C  
ATOM   2159  CG  LEU A 333      42.492  10.548  98.776  1.00 98.26           C  
ANISOU 2159  CG  LEU A 333    20394   8779   8161  -3711   -198    256       C  
ATOM   2160  CD1 LEU A 333      43.882  10.889  98.273  1.00100.57           C  
ANISOU 2160  CD1 LEU A 333    20594   9275   8342  -4292   -285    319       C  
ATOM   2161  CD2 LEU A 333      41.396  11.253  97.983  1.00100.26           C  
ANISOU 2161  CD2 LEU A 333    21047   8674   8375  -3342    -51    272       C  
ATOM   2162  N   HIS A 334      42.456   5.874  98.314  1.00 86.22           N  
ANISOU 2162  N   HIS A 334    16749   8507   7504  -2929   -292    287       N  
ATOM   2163  CA  HIS A 334      43.097   4.577  98.560  1.00 85.05           C  
ANISOU 2163  CA  HIS A 334    16030   8768   7517  -2925   -365    304       C  
ATOM   2164  C   HIS A 334      43.135   3.608  97.368  1.00 87.35           C  
ANISOU 2164  C   HIS A 334    15882   9312   7994  -2711   -315    348       C  
ATOM   2165  O   HIS A 334      44.043   2.773  97.292  1.00 86.81           O  
ANISOU 2165  O   HIS A 334    15387   9596   8003  -2807   -358    390       O  
ATOM   2166  CB  HIS A 334      42.432   3.889  99.758  1.00 84.47           C  
ANISOU 2166  CB  HIS A 334    15896   8677   7522  -2677   -391    242       C  
ATOM   2167  CG  HIS A 334      43.049   4.265 101.063  1.00 90.00           C  
ANISOU 2167  CG  HIS A 334    16776   9355   8064  -2988   -496    218       C  
ATOM   2168  ND1 HIS A 334      43.848   3.380 101.762  1.00 91.61           N  
ANISOU 2168  ND1 HIS A 334    16602   9882   8322  -3096   -610    236       N  
ATOM   2169  CD2 HIS A 334      42.998   5.437 101.738  1.00 94.39           C  
ANISOU 2169  CD2 HIS A 334    17875   9596   8391  -3210   -506    182       C  
ATOM   2170  CE1 HIS A 334      44.244   4.031 102.842  1.00 93.39           C  
ANISOU 2170  CE1 HIS A 334    17129  10001   8356  -3399   -702    211       C  
ATOM   2171  NE2 HIS A 334      43.759   5.274 102.871  1.00 95.43           N  
ANISOU 2171  NE2 HIS A 334    17963   9864   8433  -3488   -641    173       N  
ATOM   2172  N   ASN A 335      42.151   3.704  96.460  1.00 82.50           N  
ANISOU 2172  N   ASN A 335    15382   8525   7438  -2411   -224    344       N  
ATOM   2173  CA  ASN A 335      42.020   2.788  95.330  1.00 80.15           C  
ANISOU 2173  CA  ASN A 335    14738   8424   7293  -2196   -179    375       C  
ATOM   2174  C   ASN A 335      42.597   3.281  94.003  1.00 84.14           C  
ANISOU 2174  C   ASN A 335    15273   8969   7728  -2376   -129    439       C  
ATOM   2175  O   ASN A 335      42.839   2.455  93.128  1.00 83.62           O  
ANISOU 2175  O   ASN A 335    14879   9133   7758  -2292    -97    471       O  
ATOM   2176  CB  ASN A 335      40.558   2.379  95.154  1.00 78.31           C  
ANISOU 2176  CB  ASN A 335    14532   8047   7175  -1763   -135    345       C  
ATOM   2177  CG  ASN A 335      40.085   1.466  96.258  1.00 91.09           C  
ANISOU 2177  CG  ASN A 335    15986   9724   8900  -1569   -168    296       C  
ATOM   2178  OD1 ASN A 335      40.319   0.256  96.236  1.00 80.78           O  
ANISOU 2178  OD1 ASN A 335    14315   8653   7724  -1463   -189    293       O  
ATOM   2179  ND2 ASN A 335      39.487   2.041  97.288  1.00 82.34           N  
ANISOU 2179  ND2 ASN A 335    15175   8390   7721  -1523   -163    258       N  
ATOM   2180  N   SER A 336      42.850   4.587  93.852  1.00 81.40           N  
ANISOU 2180  N   SER A 336    15334   8395   7197  -2634   -113    459       N  
ATOM   2181  CA  SER A 336      43.369   5.175  92.609  1.00 81.99           C  
ANISOU 2181  CA  SER A 336    15494   8479   7181  -2832    -56    524       C  
ATOM   2182  C   SER A 336      44.872   4.927  92.306  1.00 87.14           C  
ANISOU 2182  C   SER A 336    15805   9495   7809  -3194    -63    593       C  
ATOM   2183  O   SER A 336      45.395   5.522  91.363  1.00 87.86           O  
ANISOU 2183  O   SER A 336    15991   9589   7802  -3400     -3    654       O  
ATOM   2184  CB  SER A 336      43.078   6.670  92.591  1.00 86.78           C  
ANISOU 2184  CB  SER A 336    16691   8703   7577  -3001    -32    528       C  
ATOM   2185  OG  SER A 336      43.796   7.325  93.622  1.00 96.10           O  
ANISOU 2185  OG  SER A 336    18076   9825   8611  -3366    -99    512       O  
ATOM   2186  N   THR A 337      45.553   4.038  93.055  1.00 84.21           N  
ANISOU 2186  N   THR A 337    15031   9440   7525  -3243   -125    598       N  
ATOM   2187  CA  THR A 337      46.986   3.790  92.835  1.00 86.11           C  
ANISOU 2187  CA  THR A 337    14898  10075   7745  -3552   -130    687       C  
ATOM   2188  C   THR A 337      47.304   2.437  92.165  1.00 88.25           C  
ANISOU 2188  C   THR A 337    14662  10688   8180  -3283    -64    723       C  
ATOM   2189  O   THR A 337      48.065   2.424  91.200  1.00 89.80           O  
ANISOU 2189  O   THR A 337    14665  11108   8348  -3415     19    805       O  
ATOM   2190  CB  THR A 337      47.796   3.972  94.132  1.00 99.88           C  
ANISOU 2190  CB  THR A 337    16569  11969   9413  -3883   -260    701       C  
ATOM   2191  OG1 THR A 337      47.324   5.125  94.849  1.00102.98           O  
ANISOU 2191  OG1 THR A 337    17505  11982   9641  -4072   -313    646       O  
ATOM   2192  CG2 THR A 337      49.305   4.095  93.867  1.00101.56           C  
ANISOU 2192  CG2 THR A 337    16461  12580   9549  -4304   -276    823       C  
ATOM   2193  N   THR A 338      46.778   1.314  92.688  1.00 81.67           N  
ANISOU 2193  N   THR A 338    13634   9899   7499  -2927    -88    668       N  
ATOM   2194  CA  THR A 338      47.083  -0.013  92.140  1.00 80.09           C  
ANISOU 2194  CA  THR A 338    13020   9985   7427  -2666    -21    698       C  
ATOM   2195  C   THR A 338      46.263  -0.307  90.866  1.00 81.34           C  
ANISOU 2195  C   THR A 338    13287   9989   7629  -2387     81    673       C  
ATOM   2196  O   THR A 338      45.029  -0.286  90.901  1.00 78.77           O  
ANISOU 2196  O   THR A 338    13195   9389   7345  -2162     58    601       O  
ATOM   2197  CB  THR A 338      46.959  -1.102  93.223  1.00 88.20           C  
ANISOU 2197  CB  THR A 338    13805  11139   8569  -2449    -92    664       C  
ATOM   2198  OG1 THR A 338      47.590  -0.654  94.425  1.00 89.56           O  
ANISOU 2198  OG1 THR A 338    13959  11401   8670  -2734   -211    684       O  
ATOM   2199  CG2 THR A 338      47.587  -2.422  92.798  1.00 87.05           C  
ANISOU 2199  CG2 THR A 338    13237  11324   8513  -2235    -18    718       C  
ATOM   2200  N   GLU A 339      46.968  -0.591  89.748  1.00 78.79           N  
ANISOU 2200  N   GLU A 339    12784   9865   7286  -2404    195    741       N  
ATOM   2201  CA  GLU A 339      46.370  -0.888  88.435  1.00 77.62           C  
ANISOU 2201  CA  GLU A 339    12743   9603   7147  -2181    292    728       C  
ATOM   2202  C   GLU A 339      45.746  -2.287  88.332  1.00 78.09           C  
ANISOU 2202  C   GLU A 339    12649   9693   7331  -1791    307    677       C  
ATOM   2203  O   GLU A 339      46.188  -3.222  89.004  1.00 77.16           O  
ANISOU 2203  O   GLU A 339    12251   9780   7287  -1687    296    681       O  
ATOM   2204  CB  GLU A 339      47.389  -0.682  87.293  1.00 81.22           C  
ANISOU 2204  CB  GLU A 339    13090  10257   7511  -2353    426    822       C  
ATOM   2205  CG  GLU A 339      47.418   0.727  86.722  1.00 93.36           C  
ANISOU 2205  CG  GLU A 339    14967  11604   8902  -2649    443    854       C  
ATOM   2206  CD  GLU A 339      48.290   0.941  85.494  1.00117.35           C  
ANISOU 2206  CD  GLU A 339    17934  14812  11841  -2805    594    947       C  
ATOM   2207  OE1 GLU A 339      49.395   0.355  85.427  1.00112.72           O  
ANISOU 2207  OE1 GLU A 339    16962  14595  11272  -2845    680   1022       O  
ATOM   2208  OE2 GLU A 339      47.886   1.738  84.616  1.00113.36           O  
ANISOU 2208  OE2 GLU A 339    17765  14077  11229  -2885    632    954       O  
ATOM   2209  N   SER A 340      44.727  -2.423  87.464  1.00 72.68           N  
ANISOU 2209  N   SER A 340    12164   8800   6651  -1590    326    637       N  
ATOM   2210  CA  SER A 340      44.049  -3.691  87.210  1.00 70.28           C  
ANISOU 2210  CA  SER A 340    11785   8488   6431  -1270    332    588       C  
ATOM   2211  C   SER A 340      44.906  -4.565  86.308  1.00 75.39           C  
ANISOU 2211  C   SER A 340    12238   9356   7050  -1184    470    632       C  
ATOM   2212  O   SER A 340      45.540  -4.071  85.368  1.00 76.36           O  
ANISOU 2212  O   SER A 340    12393   9542   7077  -1314    571    690       O  
ATOM   2213  CB  SER A 340      42.683  -3.468  86.566  1.00 71.40           C  
ANISOU 2213  CB  SER A 340    12204   8362   6564  -1130    285    549       C  
ATOM   2214  OG  SER A 340      41.647  -3.401  87.531  1.00 75.00           O  
ANISOU 2214  OG  SER A 340    12734   8666   7097  -1024    176    496       O  
ATOM   2215  N   ASP A 341      44.911  -5.869  86.600  1.00 71.43           N  
ANISOU 2215  N   ASP A 341    11563   8958   6619   -953    487    606       N  
ATOM   2216  CA  ASP A 341      45.658  -6.876  85.861  1.00 72.19           C  
ANISOU 2216  CA  ASP A 341    11506   9241   6682   -795    635    642       C  
ATOM   2217  C   ASP A 341      44.752  -7.471  84.777  1.00 73.54           C  
ANISOU 2217  C   ASP A 341    11911   9221   6812   -608    661    589       C  
ATOM   2218  O   ASP A 341      43.711  -8.046  85.104  1.00 71.45           O  
ANISOU 2218  O   ASP A 341    11748   8796   6603   -469    564    519       O  
ATOM   2219  CB  ASP A 341      46.140  -7.956  86.840  1.00 74.44           C  
ANISOU 2219  CB  ASP A 341    11536   9706   7041   -630    634    647       C  
ATOM   2220  CG  ASP A 341      47.470  -8.582  86.491  1.00 91.98           C  
ANISOU 2220  CG  ASP A 341    13492  12236   9220   -534    801    738       C  
ATOM   2221  OD1 ASP A 341      47.897  -8.467  85.310  1.00 94.17           O  
ANISOU 2221  OD1 ASP A 341    13811  12562   9405   -535    946    779       O  
ATOM   2222  OD2 ASP A 341      48.064  -9.234  87.377  1.00100.51           O  
ANISOU 2222  OD2 ASP A 341    14327  13514  10349   -431    795    774       O  
ATOM   2223  N   VAL A 342      45.122  -7.299  83.492  1.00 70.14           N  
ANISOU 2223  N   VAL A 342    11573   8808   6270   -632    786    627       N  
ATOM   2224  CA  VAL A 342      44.317  -7.764  82.354  1.00 69.15           C  
ANISOU 2224  CA  VAL A 342    11703   8504   6068   -499    802    585       C  
ATOM   2225  C   VAL A 342      44.945  -8.968  81.651  1.00 74.77           C  
ANISOU 2225  C   VAL A 342    12378   9326   6705   -293    974    594       C  
ATOM   2226  O   VAL A 342      46.080  -8.876  81.181  1.00 77.35           O  
ANISOU 2226  O   VAL A 342    12567   9856   6966   -315   1147    669       O  
ATOM   2227  CB  VAL A 342      43.999  -6.618  81.362  1.00 73.21           C  
ANISOU 2227  CB  VAL A 342    12451   8883   6481   -664    795    612       C  
ATOM   2228  CG1 VAL A 342      43.015  -7.074  80.290  1.00 72.52           C  
ANISOU 2228  CG1 VAL A 342    12636   8608   6312   -542    760    571       C  
ATOM   2229  CG2 VAL A 342      43.459  -5.399  82.094  1.00 72.25           C  
ANISOU 2229  CG2 VAL A 342    12402   8637   6411   -838    653    613       C  
ATOM   2230  N   TYR A 343      44.179 -10.074  81.534  1.00 69.19           N  
ANISOU 2230  N   TYR A 343    11820   8479   5990    -99    935    523       N  
ATOM   2231  CA  TYR A 343      44.614 -11.325  80.912  1.00 69.35           C  
ANISOU 2231  CA  TYR A 343    11902   8533   5914    127   1094    515       C  
ATOM   2232  C   TYR A 343      43.882 -11.640  79.605  1.00 72.92           C  
ANISOU 2232  C   TYR A 343    12708   8781   6218    162   1101    471       C  
ATOM   2233  O   TYR A 343      42.693 -11.958  79.630  1.00 71.68           O  
ANISOU 2233  O   TYR A 343    12735   8432   6068    162    939    405       O  
ATOM   2234  CB  TYR A 343      44.457 -12.489  81.903  1.00 69.27           C  
ANISOU 2234  CB  TYR A 343    11818   8521   5981    313   1056    472       C  
ATOM   2235  CG  TYR A 343      45.228 -12.301  83.190  1.00 70.92           C  
ANISOU 2235  CG  TYR A 343    11687   8946   6313    299   1045    522       C  
ATOM   2236  CD1 TYR A 343      46.578 -12.629  83.271  1.00 75.14           C  
ANISOU 2236  CD1 TYR A 343    11973   9753   6823    416   1222    609       C  
ATOM   2237  CD2 TYR A 343      44.609 -11.799  84.329  1.00 69.71           C  
ANISOU 2237  CD2 TYR A 343    11457   8741   6287    175    860    493       C  
ATOM   2238  CE1 TYR A 343      47.294 -12.463  84.455  1.00 75.89           C  
ANISOU 2238  CE1 TYR A 343    11741  10076   7018    385   1186    669       C  
ATOM   2239  CE2 TYR A 343      45.318 -11.617  85.517  1.00 70.65           C  
ANISOU 2239  CE2 TYR A 343    11296   9053   6496    140    834    538       C  
ATOM   2240  CZ  TYR A 343      46.663 -11.947  85.573  1.00 78.31           C  
ANISOU 2240  CZ  TYR A 343    12010  10304   7439    232    984    628       C  
ATOM   2241  OH  TYR A 343      47.370 -11.786  86.737  1.00 77.22           O  
ANISOU 2241  OH  TYR A 343    11580  10384   7375    184    935    686       O  
ATOM   2242  N   VAL A 344      44.595 -11.563  78.468  1.00 70.46           N  
ANISOU 2242  N   VAL A 344    12485   8526   5760    182   1287    515       N  
ATOM   2243  CA  VAL A 344      44.062 -11.894  77.144  1.00 70.95           C  
ANISOU 2243  CA  VAL A 344    12909   8405   5644    214   1314    479       C  
ATOM   2244  C   VAL A 344      44.244 -13.407  76.968  1.00 75.37           C  
ANISOU 2244  C   VAL A 344    13611   8918   6109    468   1439    435       C  
ATOM   2245  O   VAL A 344      45.378 -13.884  76.917  1.00 76.50           O  
ANISOU 2245  O   VAL A 344    13624   9231   6211    644   1668    484       O  
ATOM   2246  CB  VAL A 344      44.755 -11.076  76.015  1.00 77.18           C  
ANISOU 2246  CB  VAL A 344    13764   9263   6300    115   1474    549       C  
ATOM   2247  CG1 VAL A 344      44.391 -11.607  74.626  1.00 78.35           C  
ANISOU 2247  CG1 VAL A 344    14302   9239   6227    187   1545    515       C  
ATOM   2248  CG2 VAL A 344      44.424  -9.589  76.123  1.00 76.33           C  
ANISOU 2248  CG2 VAL A 344    13623   9129   6251   -142   1336    586       C  
ATOM   2249  N   LEU A 345      43.134 -14.158  76.914  1.00 71.19           N  
ANISOU 2249  N   LEU A 345    13348   8167   5535    488   1289    352       N  
ATOM   2250  CA  LEU A 345      43.173 -15.618  76.783  1.00 72.09           C  
ANISOU 2250  CA  LEU A 345    13682   8174   5533    701   1386    298       C  
ATOM   2251  C   LEU A 345      43.254 -16.048  75.336  1.00 78.74           C  
ANISOU 2251  C   LEU A 345    14916   8882   6120    758   1523    279       C  
ATOM   2252  O   LEU A 345      42.619 -15.421  74.483  1.00 78.53           O  
ANISOU 2252  O   LEU A 345    15084   8747   6006    582   1410    271       O  
ATOM   2253  CB  LEU A 345      41.960 -16.276  77.466  1.00 70.50           C  
ANISOU 2253  CB  LEU A 345    13593   7803   5392    652   1158    222       C  
ATOM   2254  CG  LEU A 345      41.750 -15.941  78.950  1.00 73.11           C  
ANISOU 2254  CG  LEU A 345    13588   8232   5957    607   1019    231       C  
ATOM   2255  CD1 LEU A 345      40.332 -16.230  79.382  1.00 71.92           C  
ANISOU 2255  CD1 LEU A 345    13552   7921   5852    486    775    172       C  
ATOM   2256  CD2 LEU A 345      42.731 -16.676  79.833  1.00 75.36           C  
ANISOU 2256  CD2 LEU A 345    13684   8651   6299    829   1171    253       C  
ATOM   2257  N   THR A 346      44.039 -17.120  75.058  1.00 77.66           N  
ANISOU 2257  N   THR A 346    14917   8744   5847   1024   1771    277       N  
ATOM   2258  CA  THR A 346      44.236 -17.698  73.713  1.00 79.93           C  
ANISOU 2258  CA  THR A 346    15631   8883   5855   1130   1954    254       C  
ATOM   2259  C   THR A 346      42.913 -18.248  73.175  1.00 84.92           C  
ANISOU 2259  C   THR A 346    16714   9210   6340    982   1738    156       C  
ATOM   2260  O   THR A 346      42.082 -18.701  73.966  1.00 83.07           O  
ANISOU 2260  O   THR A 346    16480   8884   6200    910   1533    106       O  
ATOM   2261  CB  THR A 346      45.291 -18.829  73.730  1.00 85.02           C  
ANISOU 2261  CB  THR A 346    16347   9570   6388   1498   2265    272       C  
ATOM   2262  OG1 THR A 346      44.948 -19.802  74.711  1.00 83.41           O  
ANISOU 2262  OG1 THR A 346    16181   9265   6245   1610   2180    221       O  
ATOM   2263  CG2 THR A 346      46.698 -18.339  73.972  1.00 82.37           C  
ANISOU 2263  CG2 THR A 346    15570   9582   6144   1654   2510    395       C  
ATOM   2264  N   ASP A 347      42.710 -18.220  71.849  1.00 84.41           N  
ANISOU 2264  N   ASP A 347    17032   9002   6037    914   1777    138       N  
ATOM   2265  CA  ASP A 347      41.475 -18.756  71.284  1.00 85.11           C  
ANISOU 2265  CA  ASP A 347    17554   8824   5957    738   1553     57       C  
ATOM   2266  C   ASP A 347      41.555 -20.269  71.052  1.00 92.26           C  
ANISOU 2266  C   ASP A 347    18917   9505   6634    913   1687    -18       C  
ATOM   2267  O   ASP A 347      42.440 -20.719  70.317  1.00 94.20           O  
ANISOU 2267  O   ASP A 347    19410   9707   6674   1133   1983    -13       O  
ATOM   2268  CB  ASP A 347      41.026 -18.012  70.026  1.00 87.79           C  
ANISOU 2268  CB  ASP A 347    18120   9098   6138    538   1461     73       C  
ATOM   2269  CG  ASP A 347      39.522 -18.038  69.901  1.00 96.99           C  
ANISOU 2269  CG  ASP A 347    19471  10116   7266    267   1099     32       C  
ATOM   2270  OD1 ASP A 347      38.985 -19.070  69.451  1.00 98.03           O  
ANISOU 2270  OD1 ASP A 347    20038  10033   7177    225   1045    -38       O  
ATOM   2271  OD2 ASP A 347      38.874 -17.066  70.350  1.00102.95           O  
ANISOU 2271  OD2 ASP A 347    19924  10978   8215    102    869     77       O  
ATOM   2272  N   PRO A 348      40.644 -21.064  71.678  1.00 89.19           N  
ANISOU 2272  N   PRO A 348    18661   8965   6263    820   1484    -83       N  
ATOM   2273  CA  PRO A 348      40.695 -22.530  71.521  1.00 91.55           C  
ANISOU 2273  CA  PRO A 348    19451   9009   6325    967   1605   -158       C  
ATOM   2274  C   PRO A 348      40.489 -23.031  70.098  1.00 99.42           C  
ANISOU 2274  C   PRO A 348    21073   9751   6950    908   1662   -212       C  
ATOM   2275  O   PRO A 348      40.885 -24.150  69.787  1.00101.54           O  
ANISOU 2275  O   PRO A 348    21796   9807   6977   1109   1868   -264       O  
ATOM   2276  CB  PRO A 348      39.595 -23.026  72.463  1.00 91.74           C  
ANISOU 2276  CB  PRO A 348    19456   8944   6457    772   1320   -204       C  
ATOM   2277  CG  PRO A 348      38.678 -21.883  72.616  1.00 93.80           C  
ANISOU 2277  CG  PRO A 348    19373   9355   6914    475   1018   -164       C  
ATOM   2278  CD  PRO A 348      39.552 -20.672  72.591  1.00 88.39           C  
ANISOU 2278  CD  PRO A 348    18278   8918   6390    583   1157    -84       C  
ATOM   2279  N   GLN A 349      39.887 -22.198  69.234  1.00 96.86           N  
ANISOU 2279  N   GLN A 349    20801   9438   6562    648   1486   -197       N  
ATOM   2280  CA  GLN A 349      39.664 -22.502  67.822  1.00 99.96           C  
ANISOU 2280  CA  GLN A 349    21777   9610   6594    554   1511   -239       C  
ATOM   2281  C   GLN A 349      41.004 -22.437  67.075  1.00107.75           C  
ANISOU 2281  C   GLN A 349    22873  10633   7433    869   1924   -207       C  
ATOM   2282  O   GLN A 349      41.164 -23.093  66.043  1.00110.85           O  
ANISOU 2282  O   GLN A 349    23841  10795   7480    936   2081   -257       O  
ATOM   2283  CB  GLN A 349      38.687 -21.483  67.223  1.00100.32           C  
ANISOU 2283  CB  GLN A 349    21757   9712   6647    210   1194   -204       C  
ATOM   2284  CG  GLN A 349      37.882 -22.000  66.042  1.00118.94           C  
ANISOU 2284  CG  GLN A 349    24737  11815   8640    -26   1038   -260       C  
ATOM   2285  CD  GLN A 349      36.970 -20.940  65.473  1.00140.22           C  
ANISOU 2285  CD  GLN A 349    27320  14605  11351   -328    720   -201       C  
ATOM   2286  OE1 GLN A 349      36.281 -20.206  66.197  1.00132.08           O  
ANISOU 2286  OE1 GLN A 349    25837  13756  10591   -470    464   -144       O  
ATOM   2287  NE2 GLN A 349      36.924 -20.858  64.151  1.00138.43           N  
ANISOU 2287  NE2 GLN A 349    27531  14251  10814   -417    733   -206       N  
ATOM   2288  N   ASP A 350      41.958 -21.641  67.609  1.00103.69           N  
ANISOU 2288  N   ASP A 350    21811  10418   7169   1049   2102   -118       N  
ATOM   2289  CA  ASP A 350      43.290 -21.417  67.040  1.00105.72           C  
ANISOU 2289  CA  ASP A 350    22020  10808   7342   1333   2497    -53       C  
ATOM   2290  C   ASP A 350      44.403 -22.192  67.754  1.00109.68           C  
ANISOU 2290  C   ASP A 350    22363  11410   7901   1743   2818    -23       C  
ATOM   2291  O   ASP A 350      45.428 -22.479  67.135  1.00112.07           O  
ANISOU 2291  O   ASP A 350    22789  11755   8036   2042   3189     19       O  
ATOM   2292  CB  ASP A 350      43.626 -19.905  67.032  1.00106.30           C  
ANISOU 2292  CB  ASP A 350    21591  11175   7624   1208   2474     48       C  
ATOM   2293  CG  ASP A 350      42.752 -19.023  66.145  1.00116.35           C  
ANISOU 2293  CG  ASP A 350    23018  12374   8817    872   2216     48       C  
ATOM   2294  OD1 ASP A 350      42.371 -17.918  66.599  1.00114.42           O  
ANISOU 2294  OD1 ASP A 350    22375  12286   8811    676   1998     99       O  
ATOM   2295  OD2 ASP A 350      42.496 -19.411  64.977  1.00124.01           O  
ANISOU 2295  OD2 ASP A 350    24523  13130   9467    821   2246      4       O  
ATOM   2296  N   THR A 351      44.218 -22.512  69.046  1.00103.82           N  
ANISOU 2296  N   THR A 351    21338  10721   7386   1776   2688    -31       N  
ATOM   2297  CA  THR A 351      45.237 -23.199  69.852  1.00104.48           C  
ANISOU 2297  CA  THR A 351    21222  10929   7546   2171   2955     16       C  
ATOM   2298  C   THR A 351      44.860 -24.653  70.219  1.00107.90           C  
ANISOU 2298  C   THR A 351    22118  11055   7823   2320   2960    -72       C  
ATOM   2299  O   THR A 351      45.344 -25.181  71.225  1.00107.11           O  
ANISOU 2299  O   THR A 351    21809  11042   7846   2582   3059    -38       O  
ATOM   2300  CB  THR A 351      45.589 -22.355  71.090  1.00112.97           C  
ANISOU 2300  CB  THR A 351    21568  12355   9000   2139   2858    102       C  
ATOM   2301  OG1 THR A 351      44.413 -22.172  71.881  1.00110.55           O  
ANISOU 2301  OG1 THR A 351    21162  11971   8869   1831   2476     45       O  
ATOM   2302  CG2 THR A 351      46.214 -21.003  70.726  1.00112.03           C  
ANISOU 2302  CG2 THR A 351    21031  12540   8994   2044   2936    204       C  
ATOM   2303  N   ARG A 352      44.039 -25.303  69.369  1.00105.10           N  
ANISOU 2303  N   ARG A 352    22423  10340   7173   2151   2860   -177       N  
ATOM   2304  CA  ARG A 352      43.566 -26.688  69.499  1.00106.25           C  
ANISOU 2304  CA  ARG A 352    23152  10125   7096   2210   2848   -273       C  
ATOM   2305  C   ARG A 352      42.941 -27.003  70.886  1.00106.72           C  
ANISOU 2305  C   ARG A 352    22964  10192   7394   2094   2595   -292       C  
ATOM   2306  O   ARG A 352      43.279 -28.010  71.517  1.00107.83           O  
ANISOU 2306  O   ARG A 352    23277  10208   7484   2360   2731   -305       O  
ATOM   2307  CB  ARG A 352      44.673 -27.697  69.117  1.00110.13           C  
ANISOU 2307  CB  ARG A 352    24028  10489   7327   2719   3297   -261       C  
ATOM   2308  N   GLY A 353      42.033 -26.133  71.327  1.00 98.95           N  
ANISOU 2308  N   GLY A 353    21601   9347   6650   1713   2241   -288       N  
ATOM   2309  CA  GLY A 353      41.290 -26.287  72.575  1.00 96.13           C  
ANISOU 2309  CA  GLY A 353    20994   9012   6519   1544   1977   -303       C  
ATOM   2310  C   GLY A 353      41.934 -25.790  73.859  1.00 97.22           C  
ANISOU 2310  C   GLY A 353    20473   9464   7002   1725   2019   -220       C  
ATOM   2311  O   GLY A 353      41.240 -25.647  74.872  1.00 94.33           O  
ANISOU 2311  O   GLY A 353    19837   9155   6850   1541   1777   -225       O  
ATOM   2312  N   GLN A 354      43.257 -25.529  73.842  1.00 93.89           N  
ANISOU 2312  N   GLN A 354    19785   9262   6627   2074   2324   -137       N  
ATOM   2313  CA  GLN A 354      43.994 -25.077  75.023  1.00 91.27           C  
ANISOU 2313  CA  GLN A 354    18833   9254   6592   2246   2373    -45       C  
ATOM   2314  C   GLN A 354      43.902 -23.564  75.261  1.00 90.10           C  
ANISOU 2314  C   GLN A 354    18119   9403   6713   1990   2201     14       C  
ATOM   2315  O   GLN A 354      44.505 -22.775  74.530  1.00 89.96           O  
ANISOU 2315  O   GLN A 354    17959   9546   6677   1996   2329     70       O  
ATOM   2316  CB  GLN A 354      45.457 -25.558  74.985  1.00 95.38           C  
ANISOU 2316  CB  GLN A 354    19290   9916   7033   2733   2767     41       C  
ATOM   2317  N   ILE A 355      43.129 -23.176  76.292  1.00 82.46           N  
ANISOU 2317  N   ILE A 355    16861   8490   5979   1768   1922      2       N  
ATOM   2318  CA  ILE A 355      42.956 -21.790  76.730  1.00 79.16           C  
ANISOU 2318  CA  ILE A 355    15946   8317   5817   1543   1752     53       C  
ATOM   2319  C   ILE A 355      44.039 -21.498  77.778  1.00 82.29           C  
ANISOU 2319  C   ILE A 355    15842   9010   6413   1748   1875    144       C  
ATOM   2320  O   ILE A 355      44.133 -22.188  78.794  1.00 81.43           O  
ANISOU 2320  O   ILE A 355    15667   8898   6374   1894   1870    143       O  
ATOM   2321  CB  ILE A 355      41.517 -21.488  77.251  1.00 79.42           C  
ANISOU 2321  CB  ILE A 355    15945   8258   5973   1206   1400      2       C  
ATOM   2322  CG1 ILE A 355      40.451 -21.791  76.174  1.00 80.65           C  
ANISOU 2322  CG1 ILE A 355    16573   8158   5911    986   1257    -68       C  
ATOM   2323  CG2 ILE A 355      41.394 -20.036  77.766  1.00 77.15           C  
ANISOU 2323  CG2 ILE A 355    15188   8198   5927   1023   1258     60       C  
ATOM   2324  CD1 ILE A 355      39.072 -22.116  76.731  1.00 87.04           C  
ANISOU 2324  CD1 ILE A 355    17433   8856   6784    721    952   -114       C  
ATOM   2325  N   SER A 356      44.879 -20.503  77.490  1.00 79.23           N  
ANISOU 2325  N   SER A 356    15127   8883   6096   1746   1987    229       N  
ATOM   2326  CA  SER A 356      45.983 -20.056  78.338  1.00 79.27           C  
ANISOU 2326  CA  SER A 356    14625   9224   6271   1876   2093    336       C  
ATOM   2327  C   SER A 356      46.211 -18.547  78.150  1.00 82.15           C  
ANISOU 2327  C   SER A 356    14658   9802   6752   1624   2037    399       C  
ATOM   2328  O   SER A 356      45.598 -17.943  77.263  1.00 81.58           O  
ANISOU 2328  O   SER A 356    14784   9607   6607   1415   1960    364       O  
ATOM   2329  CB  SER A 356      47.252 -20.867  78.060  1.00 86.62           C  
ANISOU 2329  CB  SER A 356    15567  10277   7068   2280   2431    411       C  
ATOM   2330  OG  SER A 356      47.503 -21.083  76.678  1.00 98.57           O  
ANISOU 2330  OG  SER A 356    17420  11688   8344   2376   2643    404       O  
ATOM   2331  N   ILE A 357      47.056 -17.931  78.998  1.00 78.10           N  
ANISOU 2331  N   ILE A 357    13669   9599   6405   1624   2062    494       N  
ATOM   2332  CA  ILE A 357      47.350 -16.499  78.900  1.00 77.37           C  
ANISOU 2332  CA  ILE A 357    13290   9700   6406   1360   2015    558       C  
ATOM   2333  C   ILE A 357      48.159 -16.219  77.617  1.00 84.20           C  
ANISOU 2333  C   ILE A 357    14217  10667   7109   1405   2266    623       C  
ATOM   2334  O   ILE A 357      49.332 -16.598  77.538  1.00 86.89           O  
ANISOU 2334  O   ILE A 357    14364  11249   7399   1641   2519    721       O  
ATOM   2335  CB  ILE A 357      48.069 -15.957  80.178  1.00 79.87           C  
ANISOU 2335  CB  ILE A 357    13111  10321   6915   1307   1962    644       C  
ATOM   2336  CG1 ILE A 357      47.374 -16.405  81.497  1.00 78.20           C  
ANISOU 2336  CG1 ILE A 357    12859  10010   6841   1313   1750    584       C  
ATOM   2337  CG2 ILE A 357      48.268 -14.434  80.128  1.00 79.91           C  
ANISOU 2337  CG2 ILE A 357    12892  10475   6995    977   1888    700       C  
ATOM   2338  CD1 ILE A 357      45.941 -15.896  81.777  1.00 84.31           C  
ANISOU 2338  CD1 ILE A 357    13803  10535   7696   1052   1474    484       C  
ATOM   2339  N   LYS A 358      47.517 -15.596  76.607  1.00 79.55           N  
ANISOU 2339  N   LYS A 358    13899   9902   6425   1199   2203    580       N  
ATOM   2340  CA  LYS A 358      48.180 -15.220  75.357  1.00 81.45           C  
ANISOU 2340  CA  LYS A 358    14233  10214   6499   1199   2427    638       C  
ATOM   2341  C   LYS A 358      49.074 -14.036  75.672  1.00 85.33           C  
ANISOU 2341  C   LYS A 358    14289  11028   7103   1016   2473    757       C  
ATOM   2342  O   LYS A 358      50.253 -14.038  75.314  1.00 87.76           O  
ANISOU 2342  O   LYS A 358    14390  11606   7349   1135   2737    867       O  
ATOM   2343  CB  LYS A 358      47.158 -14.825  74.273  1.00 83.42           C  
ANISOU 2343  CB  LYS A 358    14900  10179   6616   1003   2302    563       C  
ATOM   2344  CG  LYS A 358      47.742 -14.793  72.860  1.00100.00           C  
ANISOU 2344  CG  LYS A 358    17237  12276   8481   1070   2560    600       C  
ATOM   2345  CD  LYS A 358      47.028 -13.780  71.967  1.00108.71           C  
ANISOU 2345  CD  LYS A 358    18552  13242   9510    781   2428    589       C  
ATOM   2346  CE  LYS A 358      47.491 -13.840  70.531  1.00120.78           C  
ANISOU 2346  CE  LYS A 358    20386  14726  10778    845   2673    614       C  
ATOM   2347  NZ  LYS A 358      48.806 -13.174  70.332  1.00131.26           N  
ANISOU 2347  NZ  LYS A 358    21399  16373  12102    858   2953    745       N  
ATOM   2348  N   ALA A 359      48.503 -13.033  76.360  1.00 79.14           N  
ANISOU 2348  N   ALA A 359    13374  10221   6475    723   2219    741       N  
ATOM   2349  CA  ALA A 359      49.181 -11.811  76.771  1.00 79.41           C  
ANISOU 2349  CA  ALA A 359    13061  10505   6607    472   2207    838       C  
ATOM   2350  C   ALA A 359      48.566 -11.268  78.052  1.00 81.13           C  
ANISOU 2350  C   ALA A 359    13126  10682   7015    291   1931    801       C  
ATOM   2351  O   ALA A 359      47.364 -11.419  78.277  1.00 78.67           O  
ANISOU 2351  O   ALA A 359    13038  10106   6745    272   1727    701       O  
ATOM   2352  CB  ALA A 359      49.096 -10.772  75.669  1.00 80.88           C  
ANISOU 2352  CB  ALA A 359    13434  10619   6678    238   2240    863       C  
ATOM   2353  N   ARG A 360      49.395 -10.629  78.885  1.00 78.39           N  
ANISOU 2353  N   ARG A 360    12401  10613   6771    148   1927    891       N  
ATOM   2354  CA  ARG A 360      48.996 -10.049  80.164  1.00 76.23           C  
ANISOU 2354  CA  ARG A 360    11982  10326   6656    -34   1692    867       C  
ATOM   2355  C   ARG A 360      49.592  -8.643  80.287  1.00 81.84           C  
ANISOU 2355  C   ARG A 360    12523  11196   7376   -385   1672    953       C  
ATOM   2356  O   ARG A 360      50.791  -8.460  80.051  1.00 84.54           O  
ANISOU 2356  O   ARG A 360    12599  11850   7671   -439   1845   1072       O  
ATOM   2357  CB  ARG A 360      49.420 -10.993  81.307  1.00 75.40           C  
ANISOU 2357  CB  ARG A 360    11616  10383   6651    178   1681    881       C  
ATOM   2358  CG  ARG A 360      49.662 -10.370  82.668  1.00 84.72           C  
ANISOU 2358  CG  ARG A 360    12514  11712   7965    -18   1517    914       C  
ATOM   2359  CD  ARG A 360      50.775 -11.133  83.361  1.00 98.43           C  
ANISOU 2359  CD  ARG A 360    13870  13798   9733    168   1619   1016       C  
ATOM   2360  NE  ARG A 360      50.607 -11.182  84.815  1.00106.85           N  
ANISOU 2360  NE  ARG A 360    14783  14894  10923    134   1427    998       N  
ATOM   2361  CZ  ARG A 360      51.103 -10.286  85.665  1.00117.59           C  
ANISOU 2361  CZ  ARG A 360    15901  16439  12339   -148   1308   1059       C  
ATOM   2362  NH1 ARG A 360      50.911 -10.424  86.970  1.00 98.13           N  
ANISOU 2362  NH1 ARG A 360    13341  13979   9966   -154   1139   1035       N  
ATOM   2363  NH2 ARG A 360      51.793  -9.242  85.215  1.00105.04           N  
ANISOU 2363  NH2 ARG A 360    14191  15022  10696   -446   1355   1145       N  
ATOM   2364  N   PHE A 361      48.750  -7.651  80.619  1.00 76.70           N  
ANISOU 2364  N   PHE A 361    12041  10331   6770   -623   1472    900       N  
ATOM   2365  CA  PHE A 361      49.176  -6.254  80.751  1.00 77.78           C  
ANISOU 2365  CA  PHE A 361    12125  10538   6889   -984   1434    967       C  
ATOM   2366  C   PHE A 361      48.476  -5.511  81.911  1.00 80.87           C  
ANISOU 2366  C   PHE A 361    12577  10771   7381  -1159   1198    913       C  
ATOM   2367  O   PHE A 361      47.608  -6.088  82.578  1.00 78.83           O  
ANISOU 2367  O   PHE A 361    12376  10361   7214   -989   1069    827       O  
ATOM   2368  CB  PHE A 361      49.014  -5.510  79.408  1.00 80.42           C  
ANISOU 2368  CB  PHE A 361    12747  10730   7080  -1115   1518    984       C  
ATOM   2369  CG  PHE A 361      47.588  -5.307  78.950  1.00 79.74           C  
ANISOU 2369  CG  PHE A 361    13059  10268   6972  -1063   1373    887       C  
ATOM   2370  CD1 PHE A 361      46.923  -4.112  79.202  1.00 81.93           C  
ANISOU 2370  CD1 PHE A 361    13536  10339   7254  -1278   1217    873       C  
ATOM   2371  CD2 PHE A 361      46.917  -6.301  78.253  1.00 80.87           C  
ANISOU 2371  CD2 PHE A 361    13389  10268   7071   -802   1394    822       C  
ATOM   2372  CE1 PHE A 361      45.604  -3.925  78.783  1.00 81.10           C  
ANISOU 2372  CE1 PHE A 361    13757   9930   7127  -1198   1083    808       C  
ATOM   2373  CE2 PHE A 361      45.599  -6.112  77.832  1.00 82.08           C  
ANISOU 2373  CE2 PHE A 361    13868  10123   7196   -776   1239    753       C  
ATOM   2374  CZ  PHE A 361      44.956  -4.923  78.093  1.00 79.38           C  
ANISOU 2374  CZ  PHE A 361    13668   9618   6875   -960   1086    755       C  
ATOM   2375  N   LYS A 362      48.865  -4.232  82.148  1.00 78.44           N  
ANISOU 2375  N   LYS A 362    12280  10489   7036  -1505   1155    966       N  
ATOM   2376  CA  LYS A 362      48.302  -3.378  83.206  1.00 76.83           C  
ANISOU 2376  CA  LYS A 362    12190  10114   6886  -1691    959    923       C  
ATOM   2377  C   LYS A 362      47.389  -2.294  82.637  1.00 80.39           C  
ANISOU 2377  C   LYS A 362    13052  10229   7262  -1810    892    888       C  
ATOM   2378  O   LYS A 362      47.742  -1.650  81.642  1.00 81.41           O  
ANISOU 2378  O   LYS A 362    13318  10345   7270  -1958    993    944       O  
ATOM   2379  CB  LYS A 362      49.410  -2.738  84.079  1.00 80.60           C  
ANISOU 2379  CB  LYS A 362    12418  10849   7356  -2011    935   1008       C  
ATOM   2380  CG  LYS A 362      50.294  -3.723  84.848  1.00 91.03           C  
ANISOU 2380  CG  LYS A 362    13307  12524   8757  -1890    959   1059       C  
ATOM   2381  CD  LYS A 362      49.520  -4.559  85.887  1.00 96.55           C  
ANISOU 2381  CD  LYS A 362    14000  13104   9581  -1634    825    964       C  
ATOM   2382  CE  LYS A 362      50.074  -5.956  86.048  1.00103.89           C  
ANISOU 2382  CE  LYS A 362    14629  14279  10566  -1315    917    995       C  
ATOM   2383  NZ  LYS A 362      50.005  -6.749  84.785  1.00108.79           N  
ANISOU 2383  NZ  LYS A 362    15333  14868  11134  -1050   1095    989       N  
ATOM   2384  N   ALA A 363      46.225  -2.085  83.290  1.00 75.14           N  
ANISOU 2384  N   ALA A 363    12583   9303   6663  -1730    730    807       N  
ATOM   2385  CA  ALA A 363      45.235  -1.073  82.910  1.00 74.57           C  
ANISOU 2385  CA  ALA A 363    12896   8909   6527  -1779    652    784       C  
ATOM   2386  C   ALA A 363      44.904  -0.118  84.058  1.00 78.44           C  
ANISOU 2386  C   ALA A 363    13526   9244   7034  -1933    527    763       C  
ATOM   2387  O   ALA A 363      44.723  -0.555  85.202  1.00 76.17           O  
ANISOU 2387  O   ALA A 363    13097   8993   6851  -1857    444    718       O  
ATOM   2388  CB  ALA A 363      43.967  -1.735  82.400  1.00 73.33           C  
ANISOU 2388  CB  ALA A 363    12881   8574   6409  -1475    593    723       C  
ATOM   2389  N   ASN A 364      44.804   1.189  83.747  1.00 76.95           N  
ANISOU 2389  N   ASN A 364    13659   8857   6723  -2143    521    795       N  
ATOM   2390  CA  ASN A 364      44.455   2.204  84.747  1.00 77.24           C  
ANISOU 2390  CA  ASN A 364    13931   8686   6730  -2286    423    774       C  
ATOM   2391  C   ASN A 364      42.946   2.197  85.009  1.00 78.39           C  
ANISOU 2391  C   ASN A 364    14283   8564   6937  -1984    327    715       C  
ATOM   2392  O   ASN A 364      42.248   3.187  84.752  1.00 79.15           O  
ANISOU 2392  O   ASN A 364    14746   8386   6943  -1975    303    728       O  
ATOM   2393  CB  ASN A 364      44.990   3.608  84.388  1.00 81.52           C  
ANISOU 2393  CB  ASN A 364    14779   9103   7093  -2643    463    837       C  
ATOM   2394  CG  ASN A 364      45.398   3.798  82.951  1.00111.26           C  
ANISOU 2394  CG  ASN A 364    18616  12908  10751  -2720    584    904       C  
ATOM   2395  OD1 ASN A 364      44.666   3.462  82.017  1.00105.48           O  
ANISOU 2395  OD1 ASN A 364    17979  12079  10021  -2468    602    895       O  
ATOM   2396  ND2 ASN A 364      46.581   4.354  82.749  1.00108.20           N  
ANISOU 2396  ND2 ASN A 364    18190  12670  10250  -3095    665    979       N  
ATOM   2397  N   LEU A 365      42.453   1.044  85.499  1.00 71.04           N  
ANISOU 2397  N   LEU A 365    13111   7730   6152  -1727    281    661       N  
ATOM   2398  CA  LEU A 365      41.056   0.807  85.840  1.00 68.43           C  
ANISOU 2398  CA  LEU A 365    12870   7229   5901  -1440    194    615       C  
ATOM   2399  C   LEU A 365      41.000   0.420  87.296  1.00 70.86           C  
ANISOU 2399  C   LEU A 365    13028   7587   6309  -1413    135    564       C  
ATOM   2400  O   LEU A 365      41.699  -0.495  87.732  1.00 70.40           O  
ANISOU 2400  O   LEU A 365    12671   7757   6322  -1437    147    550       O  
ATOM   2401  CB  LEU A 365      40.420  -0.269  84.950  1.00 66.96           C  
ANISOU 2401  CB  LEU A 365    12565   7106   5772  -1191    190    604       C  
ATOM   2402  CG  LEU A 365      40.448   0.005  83.455  1.00 72.65           C  
ANISOU 2402  CG  LEU A 365    13446   7782   6378  -1205    242    653       C  
ATOM   2403  CD1 LEU A 365      39.933  -1.182  82.674  1.00 71.80           C  
ANISOU 2403  CD1 LEU A 365    13229   7745   6305   -995    228    633       C  
ATOM   2404  CD2 LEU A 365      39.686   1.267  83.112  1.00 76.14           C  
ANISOU 2404  CD2 LEU A 365    14249   7961   6720  -1198    201    694       C  
ATOM   2405  N   PHE A 366      40.215   1.168  88.061  1.00 66.30           N  
ANISOU 2405  N   PHE A 366    12680   6792   5719  -1361     82    545       N  
ATOM   2406  CA  PHE A 366      40.102   1.005  89.501  1.00 64.68           C  
ANISOU 2406  CA  PHE A 366    12412   6588   5577  -1350     33    497       C  
ATOM   2407  C   PHE A 366      38.683   0.670  89.899  1.00 66.49           C  
ANISOU 2407  C   PHE A 366    12669   6700   5894  -1037    -11    469       C  
ATOM   2408  O   PHE A 366      37.756   0.826  89.103  1.00 65.67           O  
ANISOU 2408  O   PHE A 366    12681   6490   5782   -856    -16    498       O  
ATOM   2409  CB  PHE A 366      40.627   2.266  90.210  1.00 68.10           C  
ANISOU 2409  CB  PHE A 366    13123   6875   5879  -1626     30    504       C  
ATOM   2410  CG  PHE A 366      41.909   2.792  89.604  1.00 71.39           C  
ANISOU 2410  CG  PHE A 366    13547   7397   6180  -1972     75    556       C  
ATOM   2411  CD1 PHE A 366      43.137   2.232  89.938  1.00 75.05           C  
ANISOU 2411  CD1 PHE A 366    13680   8166   6672  -2174     76    574       C  
ATOM   2412  CD2 PHE A 366      41.884   3.806  88.656  1.00 75.03           C  
ANISOU 2412  CD2 PHE A 366    14330   7676   6503  -2085    122    603       C  
ATOM   2413  CE1 PHE A 366      44.320   2.701  89.360  1.00 78.15           C  
ANISOU 2413  CE1 PHE A 366    14033   8703   6958  -2503    127    642       C  
ATOM   2414  CE2 PHE A 366      43.067   4.267  88.071  1.00 80.10           C  
ANISOU 2414  CE2 PHE A 366    14969   8433   7033  -2429    175    661       C  
ATOM   2415  CZ  PHE A 366      44.278   3.718  88.434  1.00 78.77           C  
ANISOU 2415  CZ  PHE A 366    14438   8594   6898  -2643    180    683       C  
ATOM   2416  N   VAL A 367      38.520   0.162  91.117  1.00 62.22           N  
ANISOU 2416  N   VAL A 367    11997   6207   5435   -976    -44    422       N  
ATOM   2417  CA  VAL A 367      37.220  -0.244  91.624  1.00 60.95           C  
ANISOU 2417  CA  VAL A 367    11818   5977   5362   -699    -72    403       C  
ATOM   2418  C   VAL A 367      36.348   0.978  91.983  1.00 66.65           C  
ANISOU 2418  C   VAL A 367    12884   6435   6004   -603    -54    423       C  
ATOM   2419  O   VAL A 367      36.837   1.985  92.511  1.00 68.03           O  
ANISOU 2419  O   VAL A 367    13320   6464   6063   -779    -32    417       O  
ATOM   2420  CB  VAL A 367      37.356  -1.286  92.771  1.00 63.48           C  
ANISOU 2420  CB  VAL A 367    11895   6438   5785   -665    -99    352       C  
ATOM   2421  CG1 VAL A 367      38.195  -0.760  93.927  1.00 64.33           C  
ANISOU 2421  CG1 VAL A 367    12077   6534   5831   -881   -108    327       C  
ATOM   2422  CG2 VAL A 367      36.001  -1.802  93.249  1.00 62.20           C  
ANISOU 2422  CG2 VAL A 367    11690   6231   5713   -402   -116    342       C  
ATOM   2423  N   ASN A 368      35.063   0.885  91.608  1.00 62.78           N  
ANISOU 2423  N   ASN A 368    12404   5891   5559   -324    -63    458       N  
ATOM   2424  CA  ASN A 368      34.012   1.856  91.879  1.00 63.20           C  
ANISOU 2424  CA  ASN A 368    12731   5729   5553   -120    -31    500       C  
ATOM   2425  C   ASN A 368      33.623   1.618  93.348  1.00 66.34           C  
ANISOU 2425  C   ASN A 368    13096   6109   6001    -31    -10    456       C  
ATOM   2426  O   ASN A 368      33.028   0.585  93.694  1.00 64.36           O  
ANISOU 2426  O   ASN A 368    12568   6009   5876    106    -34    446       O  
ATOM   2427  CB  ASN A 368      32.834   1.609  90.932  1.00 60.17           C  
ANISOU 2427  CB  ASN A 368    12260   5389   5214    142    -66    575       C  
ATOM   2428  CG  ASN A 368      31.780   2.676  90.934  1.00 74.25           C  
ANISOU 2428  CG  ASN A 368    14308   6980   6923    398    -27    652       C  
ATOM   2429  OD1 ASN A 368      31.116   2.933  91.940  1.00 64.01           O  
ANISOU 2429  OD1 ASN A 368    13072   5611   5639    573     23    654       O  
ATOM   2430  ND2 ASN A 368      31.556   3.274  89.774  1.00 69.36           N  
ANISOU 2430  ND2 ASN A 368    13844   6290   6222    460    -44    727       N  
ATOM   2431  N   VAL A 369      34.033   2.553  94.214  1.00 63.68           N  
ANISOU 2431  N   VAL A 369    13066   5582   5548   -143     36    428       N  
ATOM   2432  CA  VAL A 369      33.825   2.477  95.660  1.00 62.99           C  
ANISOU 2432  CA  VAL A 369    13018   5447   5468    -98     66    379       C  
ATOM   2433  C   VAL A 369      32.361   2.770  96.063  1.00 68.00           C  
ANISOU 2433  C   VAL A 369    13755   5968   6114    272    140    425       C  
ATOM   2434  O   VAL A 369      32.019   2.640  97.240  1.00 68.22           O  
ANISOU 2434  O   VAL A 369    13826   5951   6142    354    188    393       O  
ATOM   2435  CB  VAL A 369      34.853   3.333  96.447  1.00 67.77           C  
ANISOU 2435  CB  VAL A 369    13928   5902   5919   -400     73    329       C  
ATOM   2436  CG1 VAL A 369      36.282   2.899  96.133  1.00 66.88           C  
ANISOU 2436  CG1 VAL A 369    13617   5983   5811   -752     -1    309       C  
ATOM   2437  CG2 VAL A 369      34.668   4.824  96.187  1.00 70.02           C  
ANISOU 2437  CG2 VAL A 369    14721   5867   6016   -396    140    360       C  
ATOM   2438  N   ARG A 370      31.507   3.150  95.094  1.00 64.88           N  
ANISOU 2438  N   ARG A 370    13382   5549   5722    500    150    512       N  
ATOM   2439  CA  ARG A 370      30.081   3.378  95.317  1.00 65.43           C  
ANISOU 2439  CA  ARG A 370    13467   5581   5813    883    217    590       C  
ATOM   2440  C   ARG A 370      29.321   2.080  95.022  1.00 67.76           C  
ANISOU 2440  C   ARG A 370    13292   6171   6284   1008    150    626       C  
ATOM   2441  O   ARG A 370      28.295   1.818  95.650  1.00 68.27           O  
ANISOU 2441  O   ARG A 370    13228   6304   6408   1254    199    672       O  
ATOM   2442  CB  ARG A 370      29.555   4.498  94.413  1.00 67.10           C  
ANISOU 2442  CB  ARG A 370    13970   5617   5909   1073    253    688       C  
ATOM   2443  CG  ARG A 370      29.686   5.891  94.998  1.00 79.81           C  
ANISOU 2443  CG  ARG A 370    16126   6876   7322   1112    368    683       C  
ATOM   2444  CD  ARG A 370      28.832   6.881  94.229  1.00 92.56           C  
ANISOU 2444  CD  ARG A 370    18002   8329   8835   1432    424    806       C  
ATOM   2445  NE  ARG A 370      27.424   6.830  94.637  1.00102.23           N  
ANISOU 2445  NE  ARG A 370    19111   9620  10114   1881    505    901       N  
ATOM   2446  CZ  ARG A 370      26.417   7.358  93.946  1.00116.75           C  
ANISOU 2446  CZ  ARG A 370    20987  11451  11920   2248    532   1045       C  
ATOM   2447  NH1 ARG A 370      26.642   7.969  92.790  1.00102.25           N  
ANISOU 2447  NH1 ARG A 370    19331   9523   9995   2219    477   1103       N  
ATOM   2448  NH2 ARG A 370      25.174   7.268  94.401  1.00105.46           N  
ANISOU 2448  NH2 ARG A 370    19396  10129  10543   2650    616   1144       N  
ATOM   2449  N   HIS A 371      29.835   1.273  94.067  1.00 62.08           N  
ANISOU 2449  N   HIS A 371    12337   5621   5630    828     47    610       N  
ATOM   2450  CA  HIS A 371      29.250   0.013  93.611  1.00 60.47           C  
ANISOU 2450  CA  HIS A 371    11749   5669   5558    877    -35    635       C  
ATOM   2451  C   HIS A 371      29.246  -1.068  94.678  1.00 63.46           C  
ANISOU 2451  C   HIS A 371    11898   6175   6038    828    -31    571       C  
ATOM   2452  O   HIS A 371      30.189  -1.155  95.466  1.00 62.85           O  
ANISOU 2452  O   HIS A 371    11887   6050   5943    654    -10    486       O  
ATOM   2453  CB  HIS A 371      29.973  -0.490  92.354  1.00 60.44           C  
ANISOU 2453  CB  HIS A 371    11656   5756   5553    686   -122    621       C  
ATOM   2454  CG  HIS A 371      29.303  -1.658  91.700  1.00 62.95           C  
ANISOU 2454  CG  HIS A 371    11671   6287   5960    728   -213    654       C  
ATOM   2455  ND1 HIS A 371      28.190  -1.496  90.895  1.00 65.82           N  
ANISOU 2455  ND1 HIS A 371    11979   6714   6315    905   -271    763       N  
ATOM   2456  CD2 HIS A 371      29.594  -2.975  91.782  1.00 62.94           C  
ANISOU 2456  CD2 HIS A 371    11441   6438   6037    605   -258    597       C  
ATOM   2457  CE1 HIS A 371      27.852  -2.715  90.504  1.00 64.25           C  
ANISOU 2457  CE1 HIS A 371    11524   6705   6184    844   -361    763       C  
ATOM   2458  NE2 HIS A 371      28.667  -3.637  91.016  1.00 62.90           N  
ANISOU 2458  NE2 HIS A 371    11264   6573   6062    672   -347    660       N  
ATOM   2459  N   SER A 372      28.184  -1.912  94.663  1.00 59.62           N  
ANISOU 2459  N   SER A 372    11138   5867   5648    966    -63    624       N  
ATOM   2460  CA  SER A 372      27.926  -3.041  95.563  1.00 57.87           C  
ANISOU 2460  CA  SER A 372    10689   5779   5521    942    -61    586       C  
ATOM   2461  C   SER A 372      29.167  -3.836  95.864  1.00 59.71           C  
ANISOU 2461  C   SER A 372    10883   6035   5771    700    -92    479       C  
ATOM   2462  O   SER A 372      29.509  -3.989  97.033  1.00 58.67           O  
ANISOU 2462  O   SER A 372    10777   5871   5645    661    -46    423       O  
ATOM   2463  CB  SER A 372      26.872  -3.973  94.972  1.00 61.01           C  
ANISOU 2463  CB  SER A 372    10795   6390   5997   1007   -137    662       C  
ATOM   2464  OG  SER A 372      25.591  -3.369  94.954  1.00 73.29           O  
ANISOU 2464  OG  SER A 372    12301   7993   7553   1263    -99    783       O  
ATOM   2465  N   TYR A 373      29.863  -4.294  94.802  1.00 56.00           N  
ANISOU 2465  N   TYR A 373    10363   5620   5295    556   -163    459       N  
ATOM   2466  CA  TYR A 373      31.080  -5.117  94.831  1.00 54.93           C  
ANISOU 2466  CA  TYR A 373    10161   5541   5169    366   -187    381       C  
ATOM   2467  C   TYR A 373      32.083  -4.670  95.874  1.00 57.87           C  
ANISOU 2467  C   TYR A 373    10651   5835   5501    257   -143    322       C  
ATOM   2468  O   TYR A 373      32.601  -5.519  96.602  1.00 57.61           O  
ANISOU 2468  O   TYR A 373    10510   5875   5503    190   -151    274       O  
ATOM   2469  CB  TYR A 373      31.751  -5.184  93.446  1.00 56.68           C  
ANISOU 2469  CB  TYR A 373    10396   5791   5348    263   -228    386       C  
ATOM   2470  CG  TYR A 373      31.009  -5.964  92.378  1.00 59.52           C  
ANISOU 2470  CG  TYR A 373    10639   6249   5728    306   -298    426       C  
ATOM   2471  CD1 TYR A 373      29.699  -6.397  92.579  1.00 61.84           C  
ANISOU 2471  CD1 TYR A 373    10806   6615   6074    420   -336    477       C  
ATOM   2472  CD2 TYR A 373      31.608  -6.251  91.158  1.00 60.76           C  
ANISOU 2472  CD2 TYR A 373    10818   6434   5834    215   -326    421       C  
ATOM   2473  CE1 TYR A 373      29.007  -7.088  91.591  1.00 62.94           C  
ANISOU 2473  CE1 TYR A 373    10849   6856   6210    411   -426    521       C  
ATOM   2474  CE2 TYR A 373      30.918  -6.923  90.154  1.00 62.21           C  
ANISOU 2474  CE2 TYR A 373    10943   6688   6004    230   -403    455       C  
ATOM   2475  CZ  TYR A 373      29.623  -7.354  90.382  1.00 72.40           C  
ANISOU 2475  CZ  TYR A 373    12112   8054   7343    311   -465    504       C  
ATOM   2476  OH  TYR A 373      28.965  -8.082  89.427  1.00 78.88           O  
ANISOU 2476  OH  TYR A 373    12879   8958   8133    275   -564    540       O  
ATOM   2477  N   PHE A 374      32.336  -3.345  95.971  1.00 53.35           N  
ANISOU 2477  N   PHE A 374    10322   5109   4840    232   -104    332       N  
ATOM   2478  CA  PHE A 374      33.260  -2.771  96.943  1.00 52.88           C  
ANISOU 2478  CA  PHE A 374    10421   4962   4707     83    -79    282       C  
ATOM   2479  C   PHE A 374      32.807  -3.125  98.377  1.00 56.51           C  
ANISOU 2479  C   PHE A 374    10864   5412   5196    163    -48    252       C  
ATOM   2480  O   PHE A 374      33.598  -3.670  99.154  1.00 55.16           O  
ANISOU 2480  O   PHE A 374    10622   5308   5029     36    -75    204       O  
ATOM   2481  CB  PHE A 374      33.385  -1.252  96.728  1.00 55.94           C  
ANISOU 2481  CB  PHE A 374    11142   5146   4968     47    -39    305       C  
ATOM   2482  CG  PHE A 374      34.332  -0.560  97.679  1.00 58.08           C  
ANISOU 2482  CG  PHE A 374    11631   5309   5129   -162    -30    258       C  
ATOM   2483  CD1 PHE A 374      35.706  -0.613  97.479  1.00 60.86           C  
ANISOU 2483  CD1 PHE A 374    11933   5752   5438   -445    -81    238       C  
ATOM   2484  CD2 PHE A 374      33.849   0.143  98.777  1.00 60.94           C  
ANISOU 2484  CD2 PHE A 374    12253   5488   5413    -83     31    241       C  
ATOM   2485  CE1 PHE A 374      36.583   0.003  98.371  1.00 62.79           C  
ANISOU 2485  CE1 PHE A 374    12359   5930   5567   -683    -99    206       C  
ATOM   2486  CE2 PHE A 374      34.725   0.767  99.666  1.00 64.76           C  
ANISOU 2486  CE2 PHE A 374    12976   5863   5767   -314     22    195       C  
ATOM   2487  CZ  PHE A 374      36.086   0.699  99.453  1.00 62.99           C  
ANISOU 2487  CZ  PHE A 374    12680   5751   5504   -632    -57    180       C  
ATOM   2488  N   TYR A 375      31.511  -2.890  98.677  1.00 53.60           N  
ANISOU 2488  N   TYR A 375    10530   4986   4848    388     12    293       N  
ATOM   2489  CA  TYR A 375      30.869  -3.165  99.967  1.00 53.64           C  
ANISOU 2489  CA  TYR A 375    10529   4980   4873    503     73    281       C  
ATOM   2490  C   TYR A 375      30.800  -4.685 100.265  1.00 57.03           C  
ANISOU 2490  C   TYR A 375    10671   5590   5407    477     30    260       C  
ATOM   2491  O   TYR A 375      30.934  -5.105 101.421  1.00 55.85           O  
ANISOU 2491  O   TYR A 375    10528   5441   5254    454     52    221       O  
ATOM   2492  CB  TYR A 375      29.477  -2.501 100.013  1.00 55.76           C  
ANISOU 2492  CB  TYR A 375    10870   5182   5135    779    165    358       C  
ATOM   2493  CG  TYR A 375      29.517  -0.992  99.890  1.00 58.74           C  
ANISOU 2493  CG  TYR A 375    11607   5330   5379    841    231    378       C  
ATOM   2494  CD1 TYR A 375      29.551  -0.181 101.020  1.00 61.78           C  
ANISOU 2494  CD1 TYR A 375    12308   5517   5648    879    328    346       C  
ATOM   2495  CD2 TYR A 375      29.522  -0.374  98.644  1.00 60.19           C  
ANISOU 2495  CD2 TYR A 375    11863   5473   5531    856    198    428       C  
ATOM   2496  CE1 TYR A 375      29.592   1.210 100.914  1.00 63.98           C  
ANISOU 2496  CE1 TYR A 375    12989   5545   5776    929    396    361       C  
ATOM   2497  CE2 TYR A 375      29.572   1.014  98.525  1.00 63.12           C  
ANISOU 2497  CE2 TYR A 375    12616   5606   5761    909    263    450       C  
ATOM   2498  CZ  TYR A 375      29.603   1.804  99.662  1.00 71.47           C  
ANISOU 2498  CZ  TYR A 375    14008   6450   6698    946    364    415       C  
ATOM   2499  OH  TYR A 375      29.643   3.175  99.536  1.00 73.83           O  
ANISOU 2499  OH  TYR A 375    14747   6475   6830    995    436    434       O  
ATOM   2500  N   GLN A 376      30.614  -5.497  99.207  1.00 53.71           N  
ANISOU 2500  N   GLN A 376    10043   5303   5059    470    -32    286       N  
ATOM   2501  CA  GLN A 376      30.580  -6.955  99.277  1.00 52.59           C  
ANISOU 2501  CA  GLN A 376     9689   5302   4992    431    -75    268       C  
ATOM   2502  C   GLN A 376      31.955  -7.460  99.711  1.00 55.98           C  
ANISOU 2502  C   GLN A 376    10118   5755   5398    276   -109    203       C  
ATOM   2503  O   GLN A 376      32.037  -8.257 100.644  1.00 55.44           O  
ANISOU 2503  O   GLN A 376     9994   5724   5348    268   -106    175       O  
ATOM   2504  CB  GLN A 376      30.187  -7.548  97.909  1.00 53.86           C  
ANISOU 2504  CB  GLN A 376     9710   5562   5191    432   -139    308       C  
ATOM   2505  CG  GLN A 376      29.999  -9.067  97.906  1.00 75.52           C  
ANISOU 2505  CG  GLN A 376    12295   8416   7984    384   -179    292       C  
ATOM   2506  CD  GLN A 376      30.573  -9.756  96.685  1.00107.34           C  
ANISOU 2506  CD  GLN A 376    16291  12493  11998    298   -242    280       C  
ATOM   2507  OE1 GLN A 376      31.045  -9.125  95.722  1.00106.05           O  
ANISOU 2507  OE1 GLN A 376    16195  12303  11796    269   -256    286       O  
ATOM   2508  NE2 GLN A 376      30.547 -11.084  96.700  1.00102.19           N  
ANISOU 2508  NE2 GLN A 376    15568  11897  11360    255   -270    262       N  
ATOM   2509  N   VAL A 377      33.030  -6.963  99.058  1.00 52.57           N  
ANISOU 2509  N   VAL A 377     9742   5314   4917    158   -138    191       N  
ATOM   2510  CA  VAL A 377      34.416  -7.339  99.356  1.00 52.16           C  
ANISOU 2510  CA  VAL A 377     9646   5336   4838     16   -173    157       C  
ATOM   2511  C   VAL A 377      34.843  -6.762 100.724  1.00 56.89           C  
ANISOU 2511  C   VAL A 377    10375   5869   5371    -60   -169    129       C  
ATOM   2512  O   VAL A 377      35.632  -7.400 101.429  1.00 56.24           O  
ANISOU 2512  O   VAL A 377    10215   5875   5278   -130   -207    110       O  
ATOM   2513  CB  VAL A 377      35.386  -7.005  98.187  1.00 56.22           C  
ANISOU 2513  CB  VAL A 377    10143   5901   5316    -95   -192    171       C  
ATOM   2514  CG1 VAL A 377      36.830  -7.367  98.523  1.00 56.25           C  
ANISOU 2514  CG1 VAL A 377    10052   6032   5289   -229   -219    162       C  
ATOM   2515  CG2 VAL A 377      34.965  -7.737  96.918  1.00 55.52           C  
ANISOU 2515  CG2 VAL A 377     9953   5871   5271    -21   -198    190       C  
ATOM   2516  N   LEU A 378      34.256  -5.597 101.121  1.00 54.06           N  
ANISOU 2516  N   LEU A 378    10234   5351   4955    -24   -120    132       N  
ATOM   2517  CA  LEU A 378      34.496  -4.920 102.407  1.00 54.03           C  
ANISOU 2517  CA  LEU A 378    10437   5235   4855    -93   -106    102       C  
ATOM   2518  C   LEU A 378      34.088  -5.814 103.568  1.00 56.63           C  
ANISOU 2518  C   LEU A 378    10697   5602   5218    -11    -90     81       C  
ATOM   2519  O   LEU A 378      34.885  -6.016 104.479  1.00 56.37           O  
ANISOU 2519  O   LEU A 378    10688   5601   5131   -128   -139     54       O  
ATOM   2520  CB  LEU A 378      33.733  -3.586 102.466  1.00 55.06           C  
ANISOU 2520  CB  LEU A 378    10857   5156   4906     -7    -25    115       C  
ATOM   2521  CG  LEU A 378      34.104  -2.627 103.582  1.00 60.79           C  
ANISOU 2521  CG  LEU A 378    11905   5711   5481   -120     -6     78       C  
ATOM   2522  CD1 LEU A 378      34.291  -1.226 103.043  1.00 62.38           C  
ANISOU 2522  CD1 LEU A 378    12412   5725   5564   -188     22     91       C  
ATOM   2523  CD2 LEU A 378      33.054  -2.635 104.669  1.00 63.19           C  
ANISOU 2523  CD2 LEU A 378    12325   5915   5767     71     93     69       C  
ATOM   2524  N   LEU A 379      32.857  -6.353 103.535  1.00 52.49           N  
ANISOU 2524  N   LEU A 379    10081   5088   4773    175    -29    105       N  
ATOM   2525  CA  LEU A 379      32.372  -7.227 104.594  1.00 51.95           C  
ANISOU 2525  CA  LEU A 379     9953   5053   4731    242      0     94       C  
ATOM   2526  C   LEU A 379      33.201  -8.491 104.671  1.00 55.77           C  
ANISOU 2526  C   LEU A 379    10270   5672   5249    157    -81     76       C  
ATOM   2527  O   LEU A 379      33.544  -8.911 105.774  1.00 55.71           O  
ANISOU 2527  O   LEU A 379    10301   5669   5196    119    -98     53       O  
ATOM   2528  CB  LEU A 379      30.882  -7.550 104.420  1.00 51.87           C  
ANISOU 2528  CB  LEU A 379     9840   5070   4799    423     78    142       C  
ATOM   2529  CG  LEU A 379      30.182  -8.165 105.631  1.00 56.58           C  
ANISOU 2529  CG  LEU A 379    10426   5673   5398    496    149    142       C  
ATOM   2530  CD1 LEU A 379      30.300  -7.281 106.859  1.00 57.84           C  
ANISOU 2530  CD1 LEU A 379    10848   5687   5442    504    215    110       C  
ATOM   2531  CD2 LEU A 379      28.749  -8.427 105.330  1.00 59.01           C  
ANISOU 2531  CD2 LEU A 379    10595   6049   5776    648    226    212       C  
ATOM   2532  N   GLN A 380      33.551  -9.069 103.501  1.00 52.38           N  
ANISOU 2532  N   GLN A 380     9681   5342   4878    142   -126     91       N  
ATOM   2533  CA  GLN A 380      34.369 -10.276 103.377  1.00 52.12           C  
ANISOU 2533  CA  GLN A 380     9509   5429   4866    108   -181     84       C  
ATOM   2534  C   GLN A 380      35.740 -10.038 103.978  1.00 57.44           C  
ANISOU 2534  C   GLN A 380    10199   6158   5467    -12   -242     75       C  
ATOM   2535  O   GLN A 380      36.243 -10.900 104.695  1.00 57.26           O  
ANISOU 2535  O   GLN A 380    10123   6203   5429     -2   -276     74       O  
ATOM   2536  CB  GLN A 380      34.526 -10.688 101.908  1.00 53.20           C  
ANISOU 2536  CB  GLN A 380     9538   5633   5044    115   -198    102       C  
ATOM   2537  CG  GLN A 380      33.356 -11.482 101.355  1.00 69.09           C  
ANISOU 2537  CG  GLN A 380    11493   7643   7114    198   -178    117       C  
ATOM   2538  CD  GLN A 380      33.518 -11.812  99.892  1.00 88.03           C  
ANISOU 2538  CD  GLN A 380    13838  10085   9522    188   -200    130       C  
ATOM   2539  OE1 GLN A 380      32.555 -11.774  99.121  1.00 86.30           O  
ANISOU 2539  OE1 GLN A 380    13605   9857   9328    213   -205    155       O  
ATOM   2540  NE2 GLN A 380      34.728 -12.176  99.476  1.00 77.52           N  
ANISOU 2540  NE2 GLN A 380    12472   8820   8163    158   -214    121       N  
ATOM   2541  N   SER A 381      36.330  -8.854 103.717  1.00 55.10           N  
ANISOU 2541  N   SER A 381     9985   5838   5112   -136   -263     77       N  
ATOM   2542  CA  SER A 381      37.646  -8.504 104.243  1.00 56.21           C  
ANISOU 2542  CA  SER A 381    10125   6064   5170   -306   -340     84       C  
ATOM   2543  C   SER A 381      37.633  -8.378 105.753  1.00 61.80           C  
ANISOU 2543  C   SER A 381    10970   6713   5799   -348   -367     61       C  
ATOM   2544  O   SER A 381      38.612  -8.754 106.402  1.00 62.57           O  
ANISOU 2544  O   SER A 381    10992   6936   5845   -436   -452     78       O  
ATOM   2545  CB  SER A 381      38.195  -7.240 103.585  1.00 60.13           C  
ANISOU 2545  CB  SER A 381    10712   6531   5602   -474   -353     95       C  
ATOM   2546  OG  SER A 381      37.447  -6.072 103.870  1.00 66.55           O  
ANISOU 2546  OG  SER A 381    11794   7134   6356   -485   -304     72       O  
ATOM   2547  N   SER A 382      36.501  -7.895 106.306  1.00 58.39           N  
ANISOU 2547  N   SER A 382    10731   6102   5351   -265   -289     33       N  
ATOM   2548  CA  SER A 382      36.294  -7.689 107.736  1.00 58.79           C  
ANISOU 2548  CA  SER A 382    10972   6055   5309   -283   -282      6       C  
ATOM   2549  C   SER A 382      36.191  -8.994 108.534  1.00 60.25           C  
ANISOU 2549  C   SER A 382    11050   6318   5523   -194   -295      9       C  
ATOM   2550  O   SER A 382      36.712  -9.065 109.651  1.00 60.23           O  
ANISOU 2550  O   SER A 382    11134   6327   5425   -275   -357      1       O  
ATOM   2551  CB  SER A 382      35.078  -6.803 107.979  1.00 63.55           C  
ANISOU 2551  CB  SER A 382    11810   6454   5883   -174   -158    -12       C  
ATOM   2552  OG  SER A 382      35.158  -6.218 109.268  1.00 77.25           O  
ANISOU 2552  OG  SER A 382    13817   8060   7473   -245   -150    -44       O  
ATOM   2553  N   ILE A 383      35.518 -10.017 107.968  1.00 54.57           N  
ANISOU 2553  N   ILE A 383    10172   5644   4918    -45   -245     23       N  
ATOM   2554  CA  ILE A 383      35.363 -11.314 108.627  1.00 53.39           C  
ANISOU 2554  CA  ILE A 383     9957   5541   4787     36   -246     29       C  
ATOM   2555  C   ILE A 383      36.677 -12.101 108.529  1.00 56.88           C  
ANISOU 2555  C   ILE A 383    10252   6144   5217      3   -351     56       C  
ATOM   2556  O   ILE A 383      37.080 -12.696 109.530  1.00 57.34           O  
ANISOU 2556  O   ILE A 383    10332   6238   5218     12   -397     66       O  
ATOM   2557  CB  ILE A 383      34.095 -12.073 108.150  1.00 55.25           C  
ANISOU 2557  CB  ILE A 383    10125   5750   5119    166   -154     39       C  
ATOM   2558  CG1 ILE A 383      32.895 -11.645 109.010  1.00 56.29           C  
ANISOU 2558  CG1 ILE A 383    10391   5770   5228    228    -46     34       C  
ATOM   2559  CG2 ILE A 383      34.261 -13.592 108.183  1.00 54.67           C  
ANISOU 2559  CG2 ILE A 383     9956   5743   5073    218   -177     54       C  
ATOM   2560  CD1 ILE A 383      31.550 -11.786 108.346  1.00 66.08           C  
ANISOU 2560  CD1 ILE A 383    11544   7009   6555    325     45     65       C  
ATOM   2561  N   VAL A 384      37.383 -12.044 107.370  1.00 52.14           N  
ANISOU 2561  N   VAL A 384     9507   5648   4655    -26   -383     78       N  
ATOM   2562  CA  VAL A 384      38.691 -12.706 107.211  1.00 51.90           C  
ANISOU 2562  CA  VAL A 384     9308   5804   4606    -26   -460    124       C  
ATOM   2563  C   VAL A 384      39.633 -12.201 108.324  1.00 56.60           C  
ANISOU 2563  C   VAL A 384     9932   6481   5091   -165   -569    145       C  
ATOM   2564  O   VAL A 384      40.240 -13.020 109.016  1.00 56.90           O  
ANISOU 2564  O   VAL A 384     9901   6629   5089   -110   -631    183       O  
ATOM   2565  CB  VAL A 384      39.299 -12.553 105.783  1.00 55.24           C  
ANISOU 2565  CB  VAL A 384     9581   6333   5073    -39   -451    150       C  
ATOM   2566  CG1 VAL A 384      40.711 -13.137 105.702  1.00 55.90           C  
ANISOU 2566  CG1 VAL A 384     9470   6645   5126    -19   -512    217       C  
ATOM   2567  CG2 VAL A 384      38.406 -13.198 104.731  1.00 53.84           C  
ANISOU 2567  CG2 VAL A 384     9399   6080   4979     88   -367    133       C  
ATOM   2568  N   GLU A 385      39.660 -10.866 108.551  1.00 53.62           N  
ANISOU 2568  N   GLU A 385     9696   6030   4646   -346   -592    121       N  
ATOM   2569  CA  GLU A 385      40.445 -10.199 109.595  1.00 55.27           C  
ANISOU 2569  CA  GLU A 385     9999   6284   4719   -543   -706    132       C  
ATOM   2570  C   GLU A 385      40.135 -10.755 110.997  1.00 59.89           C  
ANISOU 2570  C   GLU A 385    10713   6806   5236   -483   -728    118       C  
ATOM   2571  O   GLU A 385      41.066 -10.982 111.774  1.00 60.44           O  
ANISOU 2571  O   GLU A 385    10730   7020   5214   -564   -855    163       O  
ATOM   2572  CB  GLU A 385      40.220  -8.676 109.553  1.00 57.33           C  
ANISOU 2572  CB  GLU A 385    10497   6386   4901   -731   -692     92       C  
ATOM   2573  N   GLU A 386      38.829 -10.998 111.294  1.00 55.96           N  
ANISOU 2573  N   GLU A 386    10366   6117   4778   -341   -604     70       N  
ATOM   2574  CA  GLU A 386      38.319 -11.552 112.559  1.00 55.99           C  
ANISOU 2574  CA  GLU A 386    10516   6035   4722   -269   -583     55       C  
ATOM   2575  C   GLU A 386      38.809 -12.972 112.774  1.00 59.12           C  
ANISOU 2575  C   GLU A 386    10754   6568   5140   -147   -635    105       C  
ATOM   2576  O   GLU A 386      39.232 -13.301 113.878  1.00 60.29           O  
ANISOU 2576  O   GLU A 386    10974   6749   5184   -169   -715    125       O  
ATOM   2577  CB  GLU A 386      36.781 -11.546 112.594  1.00 56.70           C  
ANISOU 2577  CB  GLU A 386    10734   5939   4870   -137   -414     14       C  
ATOM   2578  CG  GLU A 386      36.165 -10.221 113.013  1.00 72.46           C  
ANISOU 2578  CG  GLU A 386    12992   7756   6785   -196   -338    -29       C  
ATOM   2579  CD  GLU A 386      34.716 -10.283 113.460  1.00 95.41           C  
ANISOU 2579  CD  GLU A 386    16026  10518   9709    -42   -167    -47       C  
ATOM   2580  OE1 GLU A 386      34.043  -9.226 113.448  1.00 95.27           O  
ANISOU 2580  OE1 GLU A 386    16185  10358   9654    -13    -63    -68       O  
ATOM   2581  OE2 GLU A 386      34.258 -11.381 113.853  1.00 84.39           O  
ANISOU 2581  OE2 GLU A 386    14561   9152   8350     53   -128    -31       O  
ATOM   2582  N   TYR A 387      38.746 -13.813 111.723  1.00 53.76           N  
ANISOU 2582  N   TYR A 387     9894   5954   4577    -14   -590    126       N  
ATOM   2583  CA  TYR A 387      39.186 -15.204 111.758  1.00 53.24           C  
ANISOU 2583  CA  TYR A 387     9723   5985   4523    139   -615    176       C  
ATOM   2584  C   TYR A 387      40.699 -15.305 111.853  1.00 57.96           C  
ANISOU 2584  C   TYR A 387    10146   6817   5058    115   -753    253       C  
ATOM   2585  O   TYR A 387      41.220 -16.345 112.262  1.00 58.95           O  
ANISOU 2585  O   TYR A 387    10218   7031   5149    256   -795    310       O  
ATOM   2586  CB  TYR A 387      38.660 -15.957 110.552  1.00 53.57           C  
ANISOU 2586  CB  TYR A 387     9684   5995   4676    270   -518    170       C  
ATOM   2587  CG  TYR A 387      37.232 -16.432 110.695  1.00 55.98           C  
ANISOU 2587  CG  TYR A 387    10123   6124   5021    322   -405    130       C  
ATOM   2588  CD1 TYR A 387      36.928 -17.788 110.709  1.00 58.67           C  
ANISOU 2588  CD1 TYR A 387    10508   6422   5363    441   -365    146       C  
ATOM   2589  CD2 TYR A 387      36.174 -15.526 110.741  1.00 56.61           C  
ANISOU 2589  CD2 TYR A 387    10288   6092   5130    254   -330     88       C  
ATOM   2590  CE1 TYR A 387      35.609 -18.234 110.781  1.00 60.66           C  
ANISOU 2590  CE1 TYR A 387    10861   6542   5647    442   -267    123       C  
ATOM   2591  CE2 TYR A 387      34.851 -15.960 110.827  1.00 57.33           C  
ANISOU 2591  CE2 TYR A 387    10445   6076   5261    297   -223     75       C  
ATOM   2592  CZ  TYR A 387      34.574 -17.315 110.831  1.00 67.59           C  
ANISOU 2592  CZ  TYR A 387    11761   7355   6564    367   -198     93       C  
ATOM   2593  OH  TYR A 387      33.276 -17.754 110.888  1.00 70.51           O  
ANISOU 2593  OH  TYR A 387    12176   7647   6966    362   -101     92       O  
ATOM   2594  N   ILE A 388      41.407 -14.216 111.509  1.00 53.96           N  
ANISOU 2594  N   ILE A 388     9554   6421   4527    -67   -826    265       N  
ATOM   2595  CA  ILE A 388      42.851 -14.157 111.658  1.00 54.83           C  
ANISOU 2595  CA  ILE A 388     9461   6804   4568   -141   -970    357       C  
ATOM   2596  C   ILE A 388      43.141 -13.883 113.151  1.00 61.13           C  
ANISOU 2596  C   ILE A 388    10399   7609   5218   -274  -1100    368       C  
ATOM   2597  O   ILE A 388      43.593 -14.794 113.840  1.00 62.54           O  
ANISOU 2597  O   ILE A 388    10533   7885   5344   -147  -1167    430       O  
ATOM   2598  CB  ILE A 388      43.543 -13.217 110.621  1.00 57.66           C  
ANISOU 2598  CB  ILE A 388     9651   7306   4952   -307   -991    382       C  
ATOM   2599  CG1 ILE A 388      43.505 -13.887 109.220  1.00 56.47           C  
ANISOU 2599  CG1 ILE A 388     9338   7196   4923   -114   -872    396       C  
ATOM   2600  CG2 ILE A 388      44.992 -12.895 111.031  1.00 60.88           C  
ANISOU 2600  CG2 ILE A 388     9854   8022   5257   -474  -1164    487       C  
ATOM   2601  CD1 ILE A 388      44.146 -13.140 108.012  1.00 60.88           C  
ANISOU 2601  CD1 ILE A 388     9731   7889   5514   -239   -856    424       C  
ATOM   2602  N   GLY A 389      42.772 -12.697 113.649  1.00 57.61           N  
ANISOU 2602  N   GLY A 389    10173   7022   4694   -500  -1120    305       N  
ATOM   2603  CA  GLY A 389      42.973 -12.303 115.042  1.00 80.74           C  
ANISOU 2603  CA  GLY A 389    13306   9918   7453   -661  -1238    302       C  
ATOM   2604  C   GLY A 389      41.848 -12.727 115.961  1.00112.49           C  
ANISOU 2604  C   GLY A 389    17595  13701  11446   -531  -1140    240       C  
ATOM   2605  O   GLY A 389      41.848 -13.845 116.480  1.00 80.32           O  
ANISOU 2605  O   GLY A 389    13485   9667   7364   -361  -1153    281       O  
ATOM   2606  N   SER A 399      48.124  -8.691 106.257  1.00 83.80           N  
ANISOU 2606  N   SER A 399    12087  11590   8163  -1484  -1131    674       N  
ATOM   2607  CA  SER A 399      46.730  -8.877 105.850  1.00 80.41           C  
ANISOU 2607  CA  SER A 399    11925  10799   7827  -1260   -991    550       C  
ATOM   2608  C   SER A 399      46.614  -9.375 104.396  1.00 79.38           C  
ANISOU 2608  C   SER A 399    11661  10689   7809  -1048   -836    557       C  
ATOM   2609  O   SER A 399      47.403  -8.943 103.548  1.00 79.74           O  
ANISOU 2609  O   SER A 399    11535  10921   7842  -1179   -813    624       O  
ATOM   2610  CB  SER A 399      45.943  -7.577 106.028  1.00 85.25           C  
ANISOU 2610  CB  SER A 399    12916  11099   8375  -1481   -986    453       C  
ATOM   2611  OG  SER A 399      44.576  -7.707 105.662  1.00 93.57           O  
ANISOU 2611  OG  SER A 399    14191  11846   9515  -1259   -859    356       O  
ATOM   2612  N   PRO A 400      45.619 -10.246 104.079  1.00 71.48           N  
ANISOU 2612  N   PRO A 400    10759   9498   6905   -750   -729    492       N  
ATOM   2613  CA  PRO A 400      45.471 -10.720 102.695  1.00 69.49           C  
ANISOU 2613  CA  PRO A 400    10431   9242   6730   -574   -593    493       C  
ATOM   2614  C   PRO A 400      45.087  -9.616 101.715  1.00 70.46           C  
ANISOU 2614  C   PRO A 400    10691   9228   6853   -742   -539    455       C  
ATOM   2615  O   PRO A 400      44.495  -8.608 102.107  1.00 69.54           O  
ANISOU 2615  O   PRO A 400    10810   8915   6696   -914   -576    398       O  
ATOM   2616  CB  PRO A 400      44.350 -11.765 102.791  1.00 69.31           C  
ANISOU 2616  CB  PRO A 400    10552   9006   6777   -302   -526    422       C  
ATOM   2617  CG  PRO A 400      44.274 -12.138 104.219  1.00 74.40           C  
ANISOU 2617  CG  PRO A 400    11246   9637   7385   -280   -615    418       C  
ATOM   2618  CD  PRO A 400      44.608 -10.874 104.953  1.00 71.47           C  
ANISOU 2618  CD  PRO A 400    10943   9286   6927   -583   -726    421       C  
ATOM   2619  N   LYS A 401      45.461  -9.806 100.442  1.00 65.21           N  
ANISOU 2619  N   LYS A 401     9898   8663   6215   -676   -443    492       N  
ATOM   2620  CA  LYS A 401      45.153  -8.885  99.363  1.00 63.77           C  
ANISOU 2620  CA  LYS A 401     9839   8366   6026   -804   -381    470       C  
ATOM   2621  C   LYS A 401      43.832  -9.348  98.749  1.00 64.63           C  
ANISOU 2621  C   LYS A 401    10129   8221   6205   -592   -304    390       C  
ATOM   2622  O   LYS A 401      43.666 -10.537  98.493  1.00 63.46           O  
ANISOU 2622  O   LYS A 401     9916   8094   6102   -356   -252    387       O  
ATOM   2623  CB  LYS A 401      46.297  -8.869  98.338  1.00 67.37           C  
ANISOU 2623  CB  LYS A 401    10053   9089   6458   -850   -313    564       C  
ATOM   2624  N   TYR A 402      42.870  -8.432  98.576  1.00 60.24           N  
ANISOU 2624  N   TYR A 402     9815   7428   5646   -672   -304    334       N  
ATOM   2625  CA  TYR A 402      41.553  -8.767  98.023  1.00 58.43           C  
ANISOU 2625  CA  TYR A 402     9728   6995   5477   -496   -253    278       C  
ATOM   2626  C   TYR A 402      41.410  -8.235  96.593  1.00 62.33           C  
ANISOU 2626  C   TYR A 402    10284   7441   5957   -527   -192    289       C  
ATOM   2627  O   TYR A 402      41.954  -7.171  96.276  1.00 64.49           O  
ANISOU 2627  O   TYR A 402    10599   7737   6168   -722   -192    319       O  
ATOM   2628  CB  TYR A 402      40.425  -8.258  98.934  1.00 58.94           C  
ANISOU 2628  CB  TYR A 402     9996   6847   5552   -488   -287    223       C  
ATOM   2629  CG  TYR A 402      40.525  -8.752 100.363  1.00 61.07           C  
ANISOU 2629  CG  TYR A 402    10238   7147   5817   -467   -342    211       C  
ATOM   2630  CD1 TYR A 402      39.851  -9.896 100.775  1.00 62.10           C  
ANISOU 2630  CD1 TYR A 402    10343   7248   6005   -278   -328    188       C  
ATOM   2631  CD2 TYR A 402      41.275  -8.061 101.309  1.00 63.25           C  
ANISOU 2631  CD2 TYR A 402    10546   7474   6013   -660   -414    225       C  
ATOM   2632  CE1 TYR A 402      39.953 -10.363 102.087  1.00 63.11           C  
ANISOU 2632  CE1 TYR A 402    10467   7396   6115   -257   -374    181       C  
ATOM   2633  CE2 TYR A 402      41.384  -8.516 102.621  1.00 64.35           C  
ANISOU 2633  CE2 TYR A 402    10678   7642   6130   -645   -475    217       C  
ATOM   2634  CZ  TYR A 402      40.728  -9.672 103.004  1.00 70.19           C  
ANISOU 2634  CZ  TYR A 402    11386   8351   6933   -431   -450    196       C  
ATOM   2635  OH  TYR A 402      40.814 -10.085 104.309  1.00 70.98           O  
ANISOU 2635  OH  TYR A 402    11508   8465   6997   -418   -506    192       O  
ATOM   2636  N   TYR A 403      40.731  -9.002  95.716  1.00 55.26           N  
ANISOU 2636  N   TYR A 403     9411   6485   5102   -355   -144    270       N  
ATOM   2637  CA  TYR A 403      40.570  -8.653  94.303  1.00 53.60           C  
ANISOU 2637  CA  TYR A 403     9269   6231   4864   -364    -91    283       C  
ATOM   2638  C   TYR A 403      39.207  -9.048  93.742  1.00 55.23           C  
ANISOU 2638  C   TYR A 403     9597   6282   5104   -228    -98    249       C  
ATOM   2639  O   TYR A 403      38.608 -10.026  94.200  1.00 53.77           O  
ANISOU 2639  O   TYR A 403     9393   6072   4965   -107   -116    221       O  
ATOM   2640  CB  TYR A 403      41.617  -9.390  93.456  1.00 54.67           C  
ANISOU 2640  CB  TYR A 403     9253   6549   4970   -311    -11    324       C  
ATOM   2641  CG  TYR A 403      43.062  -9.189  93.841  1.00 56.73           C  
ANISOU 2641  CG  TYR A 403     9312   7047   5196   -425      4    388       C  
ATOM   2642  CD1 TYR A 403      43.838  -8.223  93.215  1.00 60.00           C  
ANISOU 2642  CD1 TYR A 403     9698   7553   5547   -620     40    442       C  
ATOM   2643  CD2 TYR A 403      43.691 -10.052  94.732  1.00 57.63           C  
ANISOU 2643  CD2 TYR A 403     9248   7319   5329   -333    -13    412       C  
ATOM   2644  CE1 TYR A 403      45.187  -8.068  93.521  1.00 62.73           C  
ANISOU 2644  CE1 TYR A 403     9813   8166   5854   -752     49    522       C  
ATOM   2645  CE2 TYR A 403      45.037  -9.905  95.052  1.00 60.45           C  
ANISOU 2645  CE2 TYR A 403     9372   7948   5649   -432    -12    496       C  
ATOM   2646  CZ  TYR A 403      45.784  -8.911  94.441  1.00 70.54           C  
ANISOU 2646  CZ  TYR A 403    10593   9342   6870   -654     18    554       C  
ATOM   2647  OH  TYR A 403      47.117  -8.760  94.740  1.00 75.35           O  
ANISOU 2647  OH  TYR A 403    10930  10263   7436   -783     13    655       O  
ATOM   2648  N   ILE A 404      38.769  -8.343  92.677  1.00 51.17           N  
ANISOU 2648  N   ILE A 404     9205   5681   4556   -262    -88    262       N  
ATOM   2649  CA  ILE A 404      37.543  -8.668  91.944  1.00 49.98           C  
ANISOU 2649  CA  ILE A 404     9145   5426   4418   -158   -113    253       C  
ATOM   2650  C   ILE A 404      37.957  -9.252  90.587  1.00 54.12           C  
ANISOU 2650  C   ILE A 404     9680   6000   4883   -134    -62    264       C  
ATOM   2651  O   ILE A 404      38.356  -8.500  89.695  1.00 54.67           O  
ANISOU 2651  O   ILE A 404     9814   6068   4890   -213    -27    294       O  
ATOM   2652  CB  ILE A 404      36.535  -7.479  91.820  1.00 52.87           C  
ANISOU 2652  CB  ILE A 404     9659   5652   4779   -166   -154    272       C  
ATOM   2653  CG1 ILE A 404      36.113  -6.970  93.219  1.00 52.87           C  
ANISOU 2653  CG1 ILE A 404     9683   5587   4819   -157   -175    257       C  
ATOM   2654  CG2 ILE A 404      35.295  -7.881  90.978  1.00 52.46           C  
ANISOU 2654  CG2 ILE A 404     9647   5552   4733    -66   -201    286       C  
ATOM   2655  CD1 ILE A 404      35.519  -5.597  93.246  1.00 59.41           C  
ANISOU 2655  CD1 ILE A 404    10692   6271   5608   -165   -177    283       C  
ATOM   2656  N   ALA A 405      37.901 -10.595  90.455  1.00 50.19           N  
ANISOU 2656  N   ALA A 405     9151   5532   4386    -29    -46    239       N  
ATOM   2657  CA  ALA A 405      38.231 -11.307  89.215  1.00 50.46           C  
ANISOU 2657  CA  ALA A 405     9248   5584   4341     20     16    241       C  
ATOM   2658  C   ALA A 405      36.970 -11.376  88.361  1.00 53.71           C  
ANISOU 2658  C   ALA A 405     9808   5879   4719     20    -59    235       C  
ATOM   2659  O   ALA A 405      35.978 -12.001  88.766  1.00 52.10           O  
ANISOU 2659  O   ALA A 405     9620   5626   4551     50   -133    215       O  
ATOM   2660  CB  ALA A 405      38.752 -12.707  89.515  1.00 51.33           C  
ANISOU 2660  CB  ALA A 405     9316   5748   4439    144     74    219       C  
ATOM   2661  N   THR A 406      37.002 -10.662  87.210  1.00 50.73           N  
ANISOU 2661  N   THR A 406     9532   5476   4269    -33    -48    264       N  
ATOM   2662  CA  THR A 406      35.906 -10.539  86.250  1.00 50.49           C  
ANISOU 2662  CA  THR A 406     9638   5361   4184    -48   -136    280       C  
ATOM   2663  C   THR A 406      36.237 -11.243  84.950  1.00 55.16           C  
ANISOU 2663  C   THR A 406    10374   5938   4646    -41    -86    271       C  
ATOM   2664  O   THR A 406      37.268 -10.973  84.336  1.00 55.42           O  
ANISOU 2664  O   THR A 406    10433   6012   4613    -53     26    286       O  
ATOM   2665  CB  THR A 406      35.497  -9.063  86.070  1.00 57.18           C  
ANISOU 2665  CB  THR A 406    10529   6160   5037    -96   -182    331       C  
ATOM   2666  OG1 THR A 406      35.187  -8.527  87.344  1.00 56.36           O  
ANISOU 2666  OG1 THR A 406    10336   6047   5032    -82   -208    331       O  
ATOM   2667  CG2 THR A 406      34.281  -8.879  85.183  1.00 56.44           C  
ANISOU 2667  CG2 THR A 406    10541   6010   4894    -84   -295    371       C  
ATOM   2668  N   GLY A 407      35.341 -12.131  84.550  1.00 52.02           N  
ANISOU 2668  N   GLY A 407    10079   5486   4200    -37   -167    252       N  
ATOM   2669  CA  GLY A 407      35.460 -12.883  83.314  1.00 53.21           C  
ANISOU 2669  CA  GLY A 407    10434   5585   4197    -43   -137    235       C  
ATOM   2670  C   GLY A 407      34.698 -12.248  82.172  1.00 58.17           C  
ANISOU 2670  C   GLY A 407    11198   6170   4735   -119   -239    279       C  
ATOM   2671  O   GLY A 407      33.606 -11.705  82.362  1.00 57.74           O  
ANISOU 2671  O   GLY A 407    11086   6120   4732   -155   -383    321       O  
ATOM   2672  N   PHE A 408      35.289 -12.293  80.982  1.00 56.03           N  
ANISOU 2672  N   PHE A 408    11104   5868   4318   -127   -157    278       N  
ATOM   2673  CA  PHE A 408      34.693 -11.787  79.753  1.00 57.16           C  
ANISOU 2673  CA  PHE A 408    11422   5962   4336   -198   -246    321       C  
ATOM   2674  C   PHE A 408      34.725 -12.954  78.776  1.00 63.46           C  
ANISOU 2674  C   PHE A 408    12480   6683   4948   -217   -225    278       C  
ATOM   2675  O   PHE A 408      35.745 -13.638  78.651  1.00 63.63           O  
ANISOU 2675  O   PHE A 408    12581   6692   4904   -139    -45    236       O  
ATOM   2676  CB  PHE A 408      35.426 -10.539  79.238  1.00 59.33           C  
ANISOU 2676  CB  PHE A 408    11707   6249   4584   -209   -154    368       C  
ATOM   2677  CG  PHE A 408      35.331  -9.346  80.164  1.00 60.24           C  
ANISOU 2677  CG  PHE A 408    11649   6395   4844   -211   -185    408       C  
ATOM   2678  CD1 PHE A 408      34.374  -8.362  79.960  1.00 63.84           C  
ANISOU 2678  CD1 PHE A 408    12143   6811   5303   -222   -320    474       C  
ATOM   2679  CD2 PHE A 408      36.193  -9.213  81.248  1.00 62.15           C  
ANISOU 2679  CD2 PHE A 408    11713   6701   5199   -193    -79    388       C  
ATOM   2680  CE1 PHE A 408      34.279  -7.264  80.827  1.00 64.42           C  
ANISOU 2680  CE1 PHE A 408    12119   6876   5483   -201   -328    508       C  
ATOM   2681  CE2 PHE A 408      36.092  -8.120  82.119  1.00 64.38           C  
ANISOU 2681  CE2 PHE A 408    11895   6981   5584   -214   -109    417       C  
ATOM   2682  CZ  PHE A 408      35.137  -7.153  81.903  1.00 62.66           C  
ANISOU 2682  CZ  PHE A 408    11759   6691   5359   -211   -222    473       C  
ATOM   2683  N   PHE A 409      33.572 -13.234  78.161  1.00 61.19           N  
ANISOU 2683  N   PHE A 409    12325   6353   4570   -318   -411    295       N  
ATOM   2684  CA  PHE A 409      33.356 -14.389  77.292  1.00 62.10           C  
ANISOU 2684  CA  PHE A 409    12739   6371   4484   -387   -440    251       C  
ATOM   2685  C   PHE A 409      32.961 -14.035  75.858  1.00 67.20           C  
ANISOU 2685  C   PHE A 409    13628   6969   4935   -482   -534    291       C  
ATOM   2686  O   PHE A 409      32.945 -12.861  75.478  1.00 66.67           O  
ANISOU 2686  O   PHE A 409    13504   6941   4885   -472   -553    356       O  
ATOM   2687  CB  PHE A 409      32.258 -15.289  77.915  1.00 63.41           C  
ANISOU 2687  CB  PHE A 409    12876   6536   4681   -490   -612    237       C  
ATOM   2688  CG  PHE A 409      32.544 -15.842  79.291  1.00 62.81           C  
ANISOU 2688  CG  PHE A 409    12621   6481   4762   -410   -533    195       C  
ATOM   2689  CD1 PHE A 409      32.910 -17.171  79.459  1.00 65.98           C  
ANISOU 2689  CD1 PHE A 409    13212   6780   5076   -386   -442    122       C  
ATOM   2690  CD2 PHE A 409      32.399 -15.048  80.420  1.00 62.81           C  
ANISOU 2690  CD2 PHE A 409    12301   6587   4976   -356   -553    231       C  
ATOM   2691  CE1 PHE A 409      33.166 -17.688  80.728  1.00 65.48           C  
ANISOU 2691  CE1 PHE A 409    13002   6732   5145   -305   -377     92       C  
ATOM   2692  CE2 PHE A 409      32.664 -15.562  81.690  1.00 64.70           C  
ANISOU 2692  CE2 PHE A 409    12397   6844   5344   -290   -488    195       C  
ATOM   2693  CZ  PHE A 409      33.040 -16.881  81.836  1.00 63.17           C  
ANISOU 2693  CZ  PHE A 409    12374   6560   5068   -266   -407    128       C  
ATOM   2694  N   ARG A 410      32.648 -15.090  75.076  1.00 65.55           N  
ANISOU 2694  N   ARG A 410    13729   6657   4518   -583   -592    250       N  
ATOM   2695  CA  ARG A 410      32.142 -15.092  73.698  1.00 67.46           C  
ANISOU 2695  CA  ARG A 410    14274   6835   4522   -715   -718    275       C  
ATOM   2696  C   ARG A 410      31.252 -16.326  73.497  1.00 73.67           C  
ANISOU 2696  C   ARG A 410    15280   7551   5159   -900   -891    241       C  
ATOM   2697  O   ARG A 410      31.494 -17.364  74.122  1.00 74.10           O  
ANISOU 2697  O   ARG A 410    15391   7536   5228   -881   -808    168       O  
ATOM   2698  CB  ARG A 410      33.273 -15.054  72.652  1.00 67.06           C  
ANISOU 2698  CB  ARG A 410    14510   6685   4286   -635   -495    242       C  
ATOM   2699  CG  ARG A 410      34.062 -16.346  72.482  1.00 71.55           C  
ANISOU 2699  CG  ARG A 410    15367   7117   4704   -561   -294    146       C  
ATOM   2700  CD  ARG A 410      35.066 -16.232  71.366  1.00 73.59           C  
ANISOU 2700  CD  ARG A 410    15896   7302   4765   -471    -71    134       C  
ATOM   2701  NE  ARG A 410      35.913 -17.418  71.280  1.00 76.51           N  
ANISOU 2701  NE  ARG A 410    16527   7548   4995   -330    168     54       N  
ATOM   2702  CZ  ARG A 410      35.619 -18.498  70.564  1.00 91.41           C  
ANISOU 2702  CZ  ARG A 410    18873   9245   6615   -401    148     -7       C  
ATOM   2703  NH1 ARG A 410      34.486 -18.558  69.873  1.00 76.33           N  
ANISOU 2703  NH1 ARG A 410    17181   7270   4550   -651   -127      4       N  
ATOM   2704  NH2 ARG A 410      36.450 -19.531  70.540  1.00 81.91           N  
ANISOU 2704  NH2 ARG A 410    17926   7915   5282   -221    398    -74       N  
ATOM   2705  N   LYS A 411      30.235 -16.224  72.639  1.00 71.29           N  
ANISOU 2705  N   LYS A 411    15115   7269   4703  -1091  -1136    299       N  
ATOM   2706  CA  LYS A 411      29.341 -17.347  72.378  1.00 73.03           C  
ANISOU 2706  CA  LYS A 411    15558   7438   4753  -1332  -1331    278       C  
ATOM   2707  C   LYS A 411      30.123 -18.503  71.744  1.00 79.18           C  
ANISOU 2707  C   LYS A 411    16830   7977   5277  -1338  -1156    162       C  
ATOM   2708  O   LYS A 411      31.138 -18.265  71.081  1.00 79.29           O  
ANISOU 2708  O   LYS A 411    17033   7899   5192  -1183   -938    129       O  
ATOM   2709  CB  LYS A 411      28.158 -16.919  71.485  1.00 77.36           C  
ANISOU 2709  CB  LYS A 411    16136   8091   5167  -1546  -1646    385       C  
ATOM   2710  CG  LYS A 411      27.091 -16.077  72.194  1.00 86.94           C  
ANISOU 2710  CG  LYS A 411    16876   9553   6602  -1552  -1854    515       C  
ATOM   2711  CD  LYS A 411      25.871 -16.900  72.625  1.00 97.29           C  
ANISOU 2711  CD  LYS A 411    18078  10980   7906  -1803  -2097    555       C  
ATOM   2712  CE  LYS A 411      25.917 -17.294  74.087  1.00106.34           C  
ANISOU 2712  CE  LYS A 411    18956  12161   9288  -1729  -1987    514       C  
ATOM   2713  NZ  LYS A 411      24.728 -18.091  74.490  1.00114.46           N  
ANISOU 2713  NZ  LYS A 411    19869  13319  10303  -1997  -2214    566       N  
ATOM   2714  N   ARG A 412      29.698 -19.750  72.008  1.00 77.04           N  
ANISOU 2714  N   ARG A 412    16773   7602   4897  -1500  -1224    104       N  
ATOM   2715  CA  ARG A 412      30.358 -20.916  71.432  1.00 78.73           C  
ANISOU 2715  CA  ARG A 412    17522   7552   4840  -1491  -1055     -6       C  
ATOM   2716  C   ARG A 412      29.804 -21.102  70.039  1.00 85.69           C  
ANISOU 2716  C   ARG A 412    18832   8336   5389  -1734  -1229      1       C  
ATOM   2717  O   ARG A 412      28.585 -21.112  69.863  1.00 87.10           O  
ANISOU 2717  O   ARG A 412    18971   8614   5510  -2033  -1551     67       O  
ATOM   2718  CB  ARG A 412      30.142 -22.181  72.281  1.00 79.80           C  
ANISOU 2718  CB  ARG A 412    17785   7573   4964  -1571  -1048    -73       C  
ATOM   2719  CG  ARG A 412      30.956 -23.383  71.780  1.00 94.35           C  
ANISOU 2719  CG  ARG A 412    20219   9107   6521  -1487   -820   -187       C  
ATOM   2720  CD  ARG A 412      30.761 -24.631  72.615  1.00108.76           C  
ANISOU 2720  CD  ARG A 412    22238  10782   8306  -1563   -809   -250       C  
ATOM   2721  NE  ARG A 412      31.340 -24.498  73.957  1.00117.84           N  
ANISOU 2721  NE  ARG A 412    22995  12025   9752  -1298   -640   -249       N  
ATOM   2722  CZ  ARG A 412      32.557 -24.916  74.296  1.00130.58           C  
ANISOU 2722  CZ  ARG A 412    24716  13526  11372   -961   -326   -303       C  
ATOM   2723  NH1 ARG A 412      33.338 -25.507  73.400  1.00123.98           N  
ANISOU 2723  NH1 ARG A 412    24371  12473  10263   -815   -115   -363       N  
ATOM   2724  NH2 ARG A 412      33.001 -24.748  75.535  1.00108.86           N  
ANISOU 2724  NH2 ARG A 412    21585  10890   8887   -754   -217   -288       N  
ATOM   2725  N   GLY A 413      30.700 -21.221  69.068  1.00 83.13           N  
ANISOU 2725  N   GLY A 413    18900   7840   4846  -1605  -1017    -54       N  
ATOM   2726  CA  GLY A 413      30.338 -21.415  67.671  1.00 85.60           C  
ANISOU 2726  CA  GLY A 413    19695   8025   4804  -1812  -1144    -59       C  
ATOM   2727  C   GLY A 413      30.314 -22.869  67.262  1.00 91.54           C  
ANISOU 2727  C   GLY A 413    21073   8486   5222  -1964  -1116   -165       C  
ATOM   2728  O   GLY A 413      30.736 -23.741  68.028  1.00 90.47           O  
ANISOU 2728  O   GLY A 413    21028   8224   5125  -1851   -944   -240       O  
ATOM   2729  N   TYR A 414      29.831 -23.135  66.039  1.00 91.34           N  
ANISOU 2729  N   TYR A 414    21520   8339   4846  -2223  -1286   -170       N  
ATOM   2730  CA  TYR A 414      29.758 -24.478  65.459  1.00 94.56           C  
ANISOU 2730  CA  TYR A 414    22639   8427   4861  -2415  -1279   -274       C  
ATOM   2731  C   TYR A 414      31.155 -25.021  65.177  1.00 99.39           C  
ANISOU 2731  C   TYR A 414    23667   8774   5324  -2050   -830   -381       C  
ATOM   2732  O   TYR A 414      31.399 -26.210  65.371  1.00 99.92           O  
ANISOU 2732  O   TYR A 414    24164   8581   5220  -2025   -689   -476       O  
ATOM   2733  CB  TYR A 414      28.927 -24.461  64.169  1.00 99.11           C  
ANISOU 2733  CB  TYR A 414    23601   8965   5090  -2784  -1584   -239       C  
ATOM   2734  CG  TYR A 414      27.450 -24.234  64.400  1.00101.88           C  
ANISOU 2734  CG  TYR A 414    23620   9573   5517  -3187  -2047   -126       C  
ATOM   2735  CD1 TYR A 414      26.564 -25.303  64.474  1.00106.63           C  
ANISOU 2735  CD1 TYR A 414    24519  10084   5912  -3600  -2291   -149       C  
ATOM   2736  CD2 TYR A 414      26.935 -22.949  64.537  1.00101.12           C  
ANISOU 2736  CD2 TYR A 414    22918   9820   5683  -3156  -2237     18       C  
ATOM   2737  CE1 TYR A 414      25.202 -25.100  64.693  1.00108.84           C  
ANISOU 2737  CE1 TYR A 414    24440  10653   6261  -3979  -2714    -22       C  
ATOM   2738  CE2 TYR A 414      25.575 -22.733  64.750  1.00102.99           C  
ANISOU 2738  CE2 TYR A 414    22814  10330   5987  -3483  -2647    146       C  
ATOM   2739  CZ  TYR A 414      24.711 -23.812  64.825  1.00114.04           C  
ANISOU 2739  CZ  TYR A 414    24458  11680   7193  -3900  -2887    131       C  
ATOM   2740  OH  TYR A 414      23.370 -23.600  65.043  1.00117.13           O  
ANISOU 2740  OH  TYR A 414    24460  12391   7653  -4230  -3286    278       O  
ATOM   2741  N   GLN A 415      32.075 -24.135  64.753  1.00 96.47           N  
ANISOU 2741  N   GLN A 415    23149   8482   5024  -1754   -595   -352       N  
ATOM   2742  CA  GLN A 415      33.472 -24.448  64.434  1.00 97.79           C  
ANISOU 2742  CA  GLN A 415    23601   8480   5076  -1368   -144   -419       C  
ATOM   2743  C   GLN A 415      34.399 -24.488  65.677  1.00101.10           C  
ANISOU 2743  C   GLN A 415    23591   9002   5822   -993    145   -422       C  
ATOM   2744  O   GLN A 415      35.612 -24.680  65.539  1.00100.74           O  
ANISOU 2744  O   GLN A 415    23663   8888   5726   -635    529   -449       O  
ATOM   2745  CB  GLN A 415      34.004 -23.484  63.354  1.00 99.47           C  
ANISOU 2745  CB  GLN A 415    23849   8753   5192  -1266    -29   -372       C  
ATOM   2746  CG  GLN A 415      33.409 -23.725  61.971  1.00107.42           C  
ANISOU 2746  CG  GLN A 415    25471   9572   5771  -1557   -211   -393       C  
ATOM   2747  CD  GLN A 415      32.784 -22.477  61.404  1.00120.16           C  
ANISOU 2747  CD  GLN A 415    26810  11404   7443  -1736   -481   -281       C  
ATOM   2748  OE1 GLN A 415      33.476 -21.545  60.987  1.00115.04           O  
ANISOU 2748  OE1 GLN A 415    26007  10849   6852  -1537   -297   -232       O  
ATOM   2749  NE2 GLN A 415      31.458 -22.436  61.359  1.00108.72           N  
ANISOU 2749  NE2 GLN A 415    25297  10045   5964  -2115   -923   -227       N  
ATOM   2750  N   ASP A 416      33.825 -24.327  66.882  1.00 97.40           N  
ANISOU 2750  N   ASP A 416    22630   8709   5670  -1076    -38   -386       N  
ATOM   2751  CA  ASP A 416      34.585 -24.374  68.126  1.00 96.13           C  
ANISOU 2751  CA  ASP A 416    22064   8652   5808   -767    181   -384       C  
ATOM   2752  C   ASP A 416      34.743 -25.808  68.622  1.00105.06           C  
ANISOU 2752  C   ASP A 416    23592   9530   6798   -696    303   -471       C  
ATOM   2753  O   ASP A 416      33.780 -26.581  68.553  1.00105.94           O  
ANISOU 2753  O   ASP A 416    24035   9482   6735  -1017     68   -510       O  
ATOM   2754  CB  ASP A 416      33.970 -23.470  69.199  1.00 94.54           C  
ANISOU 2754  CB  ASP A 416    21177   8745   5999   -862    -44   -303       C  
ATOM   2755  CG  ASP A 416      34.445 -22.036  69.104  1.00103.12           C  
ANISOU 2755  CG  ASP A 416    21807  10075   7300   -730     13   -220       C  
ATOM   2756  OD1 ASP A 416      35.677 -21.817  69.091  1.00103.14           O  
ANISOU 2756  OD1 ASP A 416    21735  10109   7344   -427    333   -219       O  
ATOM   2757  OD2 ASP A 416      33.588 -21.129  69.087  1.00109.30           O  
ANISOU 2757  OD2 ASP A 416    22301  11024   8206   -926   -258   -145       O  
ATOM   2758  N   PRO A 417      35.954 -26.193  69.103  1.00104.46           N  
ANISOU 2758  N   PRO A 417    23500   9416   6775   -281    668   -491       N  
ATOM   2759  CA  PRO A 417      36.152 -27.579  69.566  1.00107.15           C  
ANISOU 2759  CA  PRO A 417    24265   9489   6959   -163    806   -566       C  
ATOM   2760  C   PRO A 417      35.220 -27.972  70.706  1.00112.76           C  
ANISOU 2760  C   PRO A 417    24778  10225   7841   -399    549   -568       C  
ATOM   2761  O   PRO A 417      34.891 -27.134  71.549  1.00109.42           O  
ANISOU 2761  O   PRO A 417    23723  10087   7765   -455    397   -501       O  
ATOM   2762  CB  PRO A 417      37.626 -27.615  69.986  1.00108.58           C  
ANISOU 2762  CB  PRO A 417    24269   9742   7246    362   1221   -543       C  
ATOM   2763  CG  PRO A 417      38.013 -26.194  70.190  1.00109.76           C  
ANISOU 2763  CG  PRO A 417    23732  10258   7714    434   1222   -451       C  
ATOM   2764  CD  PRO A 417      37.195 -25.401  69.229  1.00105.02           C  
ANISOU 2764  CD  PRO A 417    23174   9697   7033     92    968   -434       C  
ATOM   2765  N   VAL A 418      34.760 -29.237  70.693  1.00114.04           N  
ANISOU 2765  N   VAL A 418    25519  10075   7736   -561    499   -644       N  
ATOM   2766  CA  VAL A 418      33.841 -29.784  71.693  1.00114.35           C  
ANISOU 2766  CA  VAL A 418    25478  10096   7875   -827    269   -649       C  
ATOM   2767  C   VAL A 418      34.566 -29.925  73.040  1.00119.95           C  
ANISOU 2767  C   VAL A 418    25817  10897   8861   -471    467   -629       C  
ATOM   2768  O   VAL A 418      34.024 -29.528  74.077  1.00117.06           O  
ANISOU 2768  O   VAL A 418    24952  10738   8787   -595    290   -582       O  
ATOM   2769  CB  VAL A 418      33.166 -31.110  71.241  1.00121.75           C  
ANISOU 2769  CB  VAL A 418    27203  10649   8406  -1144    162   -734       C  
ATOM   2770  CG1 VAL A 418      31.893 -31.370  72.038  1.00120.91           C  
ANISOU 2770  CG1 VAL A 418    26929  10604   8407  -1561   -160   -713       C  
ATOM   2771  CG2 VAL A 418      32.855 -31.103  69.746  1.00124.32           C  
ANISOU 2771  CG2 VAL A 418    28011  10839   8385  -1416     39   -763       C  
ATOM   2772  N   ASN A 419      35.805 -30.457  73.008  1.00120.49           N  
ANISOU 2772  N   ASN A 419    26125  10827   8830    -13    838   -653       N  
ATOM   2773  CA  ASN A 419      36.639 -30.637  74.197  1.00120.02           C  
ANISOU 2773  CA  ASN A 419    25749  10861   8994    374   1047   -621       C  
ATOM   2774  C   ASN A 419      37.698 -29.527  74.285  1.00123.81           C  
ANISOU 2774  C   ASN A 419    25629  11677   9735    714   1236   -541       C  
ATOM   2775  O   ASN A 419      38.610 -29.462  73.451  1.00125.24           O  
ANISOU 2775  O   ASN A 419    25983  11833   9768    996   1504   -535       O  
ATOM   2776  CB  ASN A 419      37.280 -32.040  74.218  1.00124.72           C  
ANISOU 2776  CB  ASN A 419    27000  11094   9296    674   1326   -679       C  
ATOM   2777  CG  ASN A 419      36.303 -33.199  74.257  1.00148.19           C  
ANISOU 2777  CG  ASN A 419    30592  13710  12003    328   1154   -757       C  
ATOM   2778  OD1 ASN A 419      35.314 -33.206  75.006  1.00138.05           O  
ANISOU 2778  OD1 ASN A 419    29092  12495  10865    -22    875   -747       O  
ATOM   2779  ND2 ASN A 419      36.589 -34.229  73.471  1.00144.55           N  
ANISOU 2779  ND2 ASN A 419    30941  12852  11129    425   1336   -831       N  
ATOM   2780  N   CYS A 420      37.538 -28.631  75.279  1.00118.14           N  
ANISOU 2780  N   CYS A 420    24224  11274   9389    658   1091   -476       N  
ATOM   2781  CA  CYS A 420      38.437 -27.503  75.546  1.00116.51           C  
ANISOU 2781  CA  CYS A 420    23414  11402   9451    897   1219   -395       C  
ATOM   2782  C   CYS A 420      39.102 -27.656  76.910  1.00120.55           C  
ANISOU 2782  C   CYS A 420    23556  12055  10193   1175   1331   -351       C  
ATOM   2783  O   CYS A 420      38.490 -28.201  77.830  1.00119.71           O  
ANISOU 2783  O   CYS A 420    23477  11864  10144   1065   1197   -373       O  
ATOM   2784  CB  CYS A 420      37.690 -26.176  75.444  1.00114.27           C  
ANISOU 2784  CB  CYS A 420    22687  11354   9374    588    954   -352       C  
ATOM   2785  SG  CYS A 420      37.102 -25.781  73.780  1.00119.74           S  
ANISOU 2785  SG  CYS A 420    23735  11951   9810    321    839   -373       S  
ATOM   2786  N   THR A 421      40.342 -27.158  77.050  1.00117.60           N  
ANISOU 2786  N   THR A 421    22826  11914   9943   1514   1567   -279       N  
ATOM   2787  CA  THR A 421      41.073 -27.247  78.311  1.00116.80           C  
ANISOU 2787  CA  THR A 421    22341  11988  10050   1784   1665   -220       C  
ATOM   2788  C   THR A 421      41.576 -25.873  78.772  1.00119.94           C  
ANISOU 2788  C   THR A 421    22054  12769  10747   1780   1634   -134       C  
ATOM   2789  O   THR A 421      42.236 -25.156  78.021  1.00119.89           O  
ANISOU 2789  O   THR A 421    21909  12914  10728   1847   1764    -89       O  
ATOM   2790  CB  THR A 421      42.173 -28.331  78.259  1.00126.24           C  
ANISOU 2790  CB  THR A 421    23841  13069  11057   2252   2000   -202       C  
ATOM   2791  OG1 THR A 421      42.769 -28.464  79.549  1.00124.11           O  
ANISOU 2791  OG1 THR A 421    23204  12972  10981   2492   2049   -135       O  
ATOM   2792  CG2 THR A 421      43.246 -28.077  77.190  1.00126.63           C  
ANISOU 2792  CG2 THR A 421    23926  13216  10972   2529   2297   -153       C  
ATOM   2793  N   ILE A 422      41.224 -25.518  80.016  1.00115.66           N  
ANISOU 2793  N   ILE A 422    21125  12364  10455   1674   1461   -113       N  
ATOM   2794  CA  ILE A 422      41.610 -24.289  80.710  1.00113.95           C  
ANISOU 2794  CA  ILE A 422    20301  12476  10520   1638   1402    -39       C  
ATOM   2795  C   ILE A 422      42.896 -24.638  81.482  1.00119.86           C  
ANISOU 2795  C   ILE A 422    20810  13401  11330   2012   1615     38       C  
ATOM   2796  O   ILE A 422      42.835 -25.094  82.629  1.00118.56           O  
ANISOU 2796  O   ILE A 422    20541  13244  11264   2080   1556     46       O  
ATOM   2797  CB  ILE A 422      40.467 -23.791  81.651  1.00114.55           C  
ANISOU 2797  CB  ILE A 422    20150  12577  10798   1334   1106    -59       C  
ATOM   2798  CG1 ILE A 422      39.089 -23.781  80.947  1.00115.07           C  
ANISOU 2798  CG1 ILE A 422    20502  12454  10764    997    888   -122       C  
ATOM   2799  CG2 ILE A 422      40.795 -22.425  82.248  1.00113.19           C  
ANISOU 2799  CG2 ILE A 422    19437  12695  10874   1264   1042      6       C  
ATOM   2800  CD1 ILE A 422      37.896 -23.982  81.900  1.00122.95           C  
ANISOU 2800  CD1 ILE A 422    21444  13398  11872    772    655   -147       C  
ATOM   2801  N   GLY A 423      44.035 -24.488  80.809  1.00119.36           N  
ANISOU 2801  N   GLY A 423    20682  13482  11187   2260   1866    103       N  
ATOM   2802  CA  GLY A 423      45.346 -24.817  81.361  1.00121.16           C  
ANISOU 2802  CA  GLY A 423    20659  13930  11447   2645   2089    204       C  
ATOM   2803  C   GLY A 423      45.577 -26.314  81.425  1.00128.05           C  
ANISOU 2803  C   GLY A 423    21967  14568  12116   2986   2261    186       C  
ATOM   2804  O   GLY A 423      46.268 -26.877  80.569  1.00130.83           O  
ANISOU 2804  O   GLY A 423    22593  14859  12257   3280   2530    209       O  
ATOM   2805  N   GLY A 424      44.973 -26.948  82.431  1.00123.40           N  
ANISOU 2805  N   GLY A 424    21474  13835  11577   2948   2115    147       N  
ATOM   2806  CA  GLY A 424      45.049 -28.385  82.666  1.00125.47           C  
ANISOU 2806  CA  GLY A 424    22193  13830  11648   3234   2240    126       C  
ATOM   2807  C   GLY A 424      43.691 -29.054  82.771  1.00128.84           C  
ANISOU 2807  C   GLY A 424    23091  13883  11977   2935   2039      4       C  
ATOM   2808  O   GLY A 424      43.525 -30.189  82.315  1.00130.75           O  
ANISOU 2808  O   GLY A 424    23934  13791  11953   3053   2150    -52       O  
ATOM   2809  N   ASP A 425      42.712 -28.352  83.377  1.00122.74           N  
ANISOU 2809  N   ASP A 425    22061  13169  11404   2540   1748    -31       N  
ATOM   2810  CA  ASP A 425      41.346 -28.842  83.579  1.00121.94           C  
ANISOU 2810  CA  ASP A 425    22292  12794  11248   2198   1528   -123       C  
ATOM   2811  C   ASP A 425      40.411 -28.419  82.449  1.00125.03           C  
ANISOU 2811  C   ASP A 425    22887  13074  11544   1838   1388   -190       C  
ATOM   2812  O   ASP A 425      40.492 -27.288  81.983  1.00123.34           O  
ANISOU 2812  O   ASP A 425    22353  13069  11443   1733   1349   -162       O  
ATOM   2813  CB  ASP A 425      40.796 -28.381  84.938  1.00121.33           C  
ANISOU 2813  CB  ASP A 425    21814  12858  11426   2009   1312   -106       C  
ATOM   2814  CG  ASP A 425      39.560 -29.132  85.388  1.00133.40           C  
ANISOU 2814  CG  ASP A 425    23670  14127  12888   1730   1134   -176       C  
ATOM   2815  OD1 ASP A 425      38.602 -28.474  85.847  1.00131.69           O  
ANISOU 2815  OD1 ASP A 425    23200  14001  12837   1398    907   -187       O  
ATOM   2816  OD2 ASP A 425      39.550 -30.379  85.281  1.00143.32           O  
ANISOU 2816  OD2 ASP A 425    25450  15091  13915   1843   1232   -212       O  
ATOM   2817  N   ALA A 426      39.501 -29.320  82.049  1.00122.66           N  
ANISOU 2817  N   ALA A 426    23123  12451  11030   1625   1297   -271       N  
ATOM   2818  CA  ALA A 426      38.548 -29.155  80.949  1.00122.79           C  
ANISOU 2818  CA  ALA A 426    23417  12336  10902   1269   1145   -330       C  
ATOM   2819  C   ALA A 426      37.400 -28.160  81.179  1.00124.04           C  
ANISOU 2819  C   ALA A 426    23203  12661  11264    855    835   -322       C  
ATOM   2820  O   ALA A 426      37.018 -27.896  82.323  1.00121.51           O  
ANISOU 2820  O   ALA A 426    22539  12467  11160    774    711   -296       O  
ATOM   2821  CB  ALA A 426      37.979 -30.506  80.572  1.00126.29           C  
ANISOU 2821  CB  ALA A 426    24576  12383  11024   1161   1145   -408       C  
ATOM   2822  N   LEU A 427      36.832 -27.642  80.060  1.00121.21           N  
ANISOU 2822  N   LEU A 427    22943  12297  10815    611    720   -338       N  
ATOM   2823  CA  LEU A 427      35.707 -26.697  80.004  1.00119.34           C  
ANISOU 2823  CA  LEU A 427    22413  12213  10719    246    436   -316       C  
ATOM   2824  C   LEU A 427      34.452 -27.367  79.418  1.00124.94           C  
ANISOU 2824  C   LEU A 427    23542  12718  11210   -135    224   -362       C  
ATOM   2825  O   LEU A 427      34.547 -28.066  78.402  1.00127.34           O  
ANISOU 2825  O   LEU A 427    24382  12787  11216   -158    292   -414       O  
ATOM   2826  CB  LEU A 427      36.076 -25.464  79.158  1.00118.67           C  
ANISOU 2826  CB  LEU A 427    22092  12308  10690    272    458   -277       C  
ATOM   2827  N   ASP A 428      33.280 -27.128  80.055  1.00119.64           N  
ANISOU 2827  N   ASP A 428    22628  12153  10678   -443    -32   -334       N  
ATOM   2828  CA  ASP A 428      31.963 -27.661  79.671  1.00120.65           C  
ANISOU 2828  CA  ASP A 428    23029  12174  10639   -867   -279   -347       C  
ATOM   2829  C   ASP A 428      31.552 -27.222  78.242  1.00125.30           C  
ANISOU 2829  C   ASP A 428    23789  12764  11053  -1067   -406   -341       C  
ATOM   2830  O   ASP A 428      31.700 -26.042  77.920  1.00123.78           O  
ANISOU 2830  O   ASP A 428    23236  12784  11012   -999   -431   -289       O  
ATOM   2831  CB  ASP A 428      30.906 -27.239  80.716  1.00120.51           C  
ANISOU 2831  CB  ASP A 428    22560  12369  10861  -1093   -494   -285       C  
ATOM   2832  CG  ASP A 428      29.485 -27.691  80.439  1.00129.49           C  
ANISOU 2832  CG  ASP A 428    23843  13491  11865  -1559   -771   -265       C  
ATOM   2833  OD1 ASP A 428      29.231 -28.915  80.478  1.00131.73           O  
ANISOU 2833  OD1 ASP A 428    24595  13532  11926  -1734   -781   -315       O  
ATOM   2834  OD2 ASP A 428      28.614 -26.818  80.254  1.00133.41           O  
ANISOU 2834  OD2 ASP A 428    23976  14230  12482  -1750   -979   -188       O  
ATOM   2835  N   PRO A 429      31.048 -28.138  77.368  1.00123.76           N  
ANISOU 2835  N   PRO A 429    24172  12326  10525  -1321   -488   -392       N  
ATOM   2836  CA  PRO A 429      30.682 -27.719  75.998  1.00124.47           C  
ANISOU 2836  CA  PRO A 429    24442  12421  10430  -1512   -619   -382       C  
ATOM   2837  C   PRO A 429      29.403 -26.871  75.877  1.00125.91           C  
ANISOU 2837  C   PRO A 429    24231  12876  10732  -1855   -956   -289       C  
ATOM   2838  O   PRO A 429      29.125 -26.363  74.790  1.00126.26           O  
ANISOU 2838  O   PRO A 429    24347  12969  10657  -1975  -1074   -261       O  
ATOM   2839  CB  PRO A 429      30.576 -29.043  75.235  1.00129.98           C  
ANISOU 2839  CB  PRO A 429    25914  12756  10717  -1687   -603   -467       C  
ATOM   2840  CG  PRO A 429      30.221 -30.044  76.262  1.00135.13           C  
ANISOU 2840  CG  PRO A 429    26701  13278  11364  -1798   -621   -493       C  
ATOM   2841  CD  PRO A 429      30.825 -29.587  77.565  1.00127.70           C  
ANISOU 2841  CD  PRO A 429    25231  12514  10775  -1454   -465   -460       C  
ATOM   2842  N   HIS A 430      28.632 -26.708  76.975  1.00119.70           N  
ANISOU 2842  N   HIS A 430    23033  12275  10172  -1992  -1103   -230       N  
ATOM   2843  CA  HIS A 430      27.406 -25.895  76.979  1.00118.12           C  
ANISOU 2843  CA  HIS A 430    22405  12371  10103  -2262  -1401   -118       C  
ATOM   2844  C   HIS A 430      27.717 -24.434  77.327  1.00115.81           C  
ANISOU 2844  C   HIS A 430    21542  12339  10121  -1989  -1349    -49       C  
ATOM   2845  O   HIS A 430      27.063 -23.531  76.801  1.00115.78           O  
ANISOU 2845  O   HIS A 430    21305  12531  10156  -2092  -1532     39       O  
ATOM   2846  CB  HIS A 430      26.333 -26.461  77.937  1.00119.33           C  
ANISOU 2846  CB  HIS A 430    22398  12615  10326  -2553  -1573    -74       C  
ATOM   2847  CG  HIS A 430      26.204 -27.955  77.926  1.00125.28           C  
ANISOU 2847  CG  HIS A 430    23721  13074  10804  -2788  -1568   -152       C  
ATOM   2848  ND1 HIS A 430      25.841 -28.644  76.779  1.00130.31           N  
ANISOU 2848  ND1 HIS A 430    24911  13518  11081  -3092  -1692   -189       N  
ATOM   2849  CD2 HIS A 430      26.378 -28.842  78.933  1.00126.89           C  
ANISOU 2849  CD2 HIS A 430    24045  13138  11031  -2768  -1458   -196       C  
ATOM   2850  CE1 HIS A 430      25.823 -29.921  77.121  1.00131.62           C  
ANISOU 2850  CE1 HIS A 430    25537  13415  11056  -3246  -1644   -258       C  
ATOM   2851  NE2 HIS A 430      26.137 -30.089  78.408  1.00129.99           N  
ANISOU 2851  NE2 HIS A 430    25086  13231  11073  -3053  -1503   -261       N  
ATOM   2852  N   VAL A 431      28.721 -24.209  78.203  1.00106.87           N  
ANISOU 2852  N   VAL A 431    20214  11203   9188  -1646  -1107    -81       N  
ATOM   2853  CA  VAL A 431      29.156 -22.886  78.650  1.00102.64           C  
ANISOU 2853  CA  VAL A 431    19196  10874   8928  -1397  -1032    -28       C  
ATOM   2854  C   VAL A 431      29.890 -22.098  77.520  1.00102.79           C  
ANISOU 2854  C   VAL A 431    19302  10884   8870  -1248   -939    -27       C  
ATOM   2855  O   VAL A 431      30.411 -22.704  76.577  1.00104.29           O  
ANISOU 2855  O   VAL A 431    19932  10880   8814  -1230   -839    -89       O  
ATOM   2856  CB  VAL A 431      29.975 -22.996  79.971  1.00104.69           C  
ANISOU 2856  CB  VAL A 431    19250  11136   9392  -1133   -829    -59       C  
ATOM   2857  CG1 VAL A 431      31.443 -23.341  79.723  1.00104.63           C  
ANISOU 2857  CG1 VAL A 431    19477  10975   9303   -834   -546   -129       C  
ATOM   2858  CG2 VAL A 431      29.842 -21.737  80.821  1.00102.14           C  
ANISOU 2858  CG2 VAL A 431    18390  11053   9366  -1023   -855     13       C  
ATOM   2859  N   GLU A 432      29.890 -20.746  77.621  1.00 94.24           N  
ANISOU 2859  N   GLU A 432    17828   9999   7981  -1148   -968     46       N  
ATOM   2860  CA  GLU A 432      30.527 -19.813  76.677  1.00 92.08           C  
ANISOU 2860  CA  GLU A 432    17575   9744   7666  -1024   -888     66       C  
ATOM   2861  C   GLU A 432      32.051 -19.842  76.851  1.00 90.11           C  
ANISOU 2861  C   GLU A 432    17365   9425   7448   -733   -576     10       C  
ATOM   2862  O   GLU A 432      32.542 -20.148  77.940  1.00 88.68           O  
ANISOU 2862  O   GLU A 432    17028   9257   7410   -593   -456    -16       O  
ATOM   2863  CB  GLU A 432      30.012 -18.378  76.890  1.00 92.15           C  
ANISOU 2863  CB  GLU A 432    17171   9966   7874  -1004  -1008    169       C  
ATOM   2864  CG  GLU A 432      28.502 -18.216  76.822  1.00104.95           C  
ANISOU 2864  CG  GLU A 432    18652  11726   9497  -1235  -1306    260       C  
ATOM   2865  CD  GLU A 432      27.921 -17.456  78.001  1.00128.88           C  
ANISOU 2865  CD  GLU A 432    21220  14949  12798  -1166  -1365    336       C  
ATOM   2866  OE1 GLU A 432      27.860 -18.032  79.113  1.00122.24           O  
ANISOU 2866  OE1 GLU A 432    20256  14114  12075  -1157  -1317    304       O  
ATOM   2867  OE2 GLU A 432      27.523 -16.283  77.812  1.00124.12           O  
ANISOU 2867  OE2 GLU A 432    20406  14479  12275  -1109  -1449    430       O  
ATOM   2868  N   ILE A 433      32.792 -19.517  75.785  1.00 83.34           N  
ANISOU 2868  N   ILE A 433    16699   8516   6451   -646   -449      3       N  
ATOM   2869  CA  ILE A 433      34.252 -19.529  75.797  1.00 81.16           C  
ANISOU 2869  CA  ILE A 433    16441   8217   6179   -378   -146    -28       C  
ATOM   2870  C   ILE A 433      34.807 -18.283  76.485  1.00 80.41           C  
ANISOU 2870  C   ILE A 433    15900   8315   6337   -255    -78     30       C  
ATOM   2871  O   ILE A 433      34.446 -17.178  76.086  1.00 78.89           O  
ANISOU 2871  O   ILE A 433    15582   8207   6187   -332   -181     90       O  
ATOM   2872  CB  ILE A 433      34.822 -19.731  74.363  1.00 86.10           C  
ANISOU 2872  CB  ILE A 433    17473   8713   6528   -343    -13    -53       C  
ATOM   2873  CG1 ILE A 433      34.511 -21.139  73.843  1.00 88.69           C  
ANISOU 2873  CG1 ILE A 433    18317   8802   6577   -430    -23   -129       C  
ATOM   2874  CG2 ILE A 433      36.326 -19.464  74.292  1.00 86.49           C  
ANISOU 2874  CG2 ILE A 433    17445   8815   6601    -66    306    -48       C  
ATOM   2875  CD1 ILE A 433      33.978 -21.162  72.479  1.00 97.02           C  
ANISOU 2875  CD1 ILE A 433    19752   9748   7362   -627   -149   -132       C  
ATOM   2876  N   PRO A 434      35.700 -18.427  77.496  1.00 75.17           N  
ANISOU 2876  N   PRO A 434    15023   7716   5822    -68     91     19       N  
ATOM   2877  CA  PRO A 434      36.288 -17.227  78.119  1.00 73.01           C  
ANISOU 2877  CA  PRO A 434    14365   7619   5756      8    150     73       C  
ATOM   2878  C   PRO A 434      37.385 -16.629  77.247  1.00 76.86           C  
ANISOU 2878  C   PRO A 434    14892   8152   6158    101    347    101       C  
ATOM   2879  O   PRO A 434      38.183 -17.358  76.652  1.00 77.44           O  
ANISOU 2879  O   PRO A 434    15189   8163   6071    233    541     74       O  
ATOM   2880  CB  PRO A 434      36.814 -17.730  79.467  1.00 73.72           C  
ANISOU 2880  CB  PRO A 434    14246   7766   5998    144    236     56       C  
ATOM   2881  CG  PRO A 434      36.984 -19.197  79.304  1.00 79.85           C  
ANISOU 2881  CG  PRO A 434    15337   8389   6615    228    321     -4       C  
ATOM   2882  CD  PRO A 434      36.251 -19.668  78.078  1.00 77.17           C  
ANISOU 2882  CD  PRO A 434    15401   7883   6038     82    234    -35       C  
ATOM   2883  N   THR A 435      37.405 -15.300  77.154  1.00 72.99           N  
ANISOU 2883  N   THR A 435    14210   7764   5760     34    306    160       N  
ATOM   2884  CA  THR A 435      38.365 -14.573  76.323  1.00 74.11           C  
ANISOU 2884  CA  THR A 435    14373   7961   5823     67    475    201       C  
ATOM   2885  C   THR A 435      39.248 -13.626  77.114  1.00 77.53           C  
ANISOU 2885  C   THR A 435    14462   8566   6430     96    572    253       C  
ATOM   2886  O   THR A 435      40.391 -13.382  76.723  1.00 78.80           O  
ANISOU 2886  O   THR A 435    14579   8823   6540    157    777    288       O  
ATOM   2887  CB  THR A 435      37.633 -13.784  75.234  1.00 82.41           C  
ANISOU 2887  CB  THR A 435    15605   8946   6759    -80    337    236       C  
ATOM   2888  OG1 THR A 435      36.694 -12.886  75.836  1.00 78.96           O  
ANISOU 2888  OG1 THR A 435    14975   8549   6477   -180    125    278       O  
ATOM   2889  CG2 THR A 435      36.962 -14.683  74.205  1.00 83.26           C  
ANISOU 2889  CG2 THR A 435    16099   8897   6639   -141    253    194       C  
ATOM   2890  N   LEU A 436      38.708 -13.061  78.199  1.00 71.84           N  
ANISOU 2890  N   LEU A 436    13507   7891   5896     35    425    264       N  
ATOM   2891  CA  LEU A 436      39.418 -12.077  78.995  1.00 71.00           C  
ANISOU 2891  CA  LEU A 436    13119   7921   5936     12    478    309       C  
ATOM   2892  C   LEU A 436      39.148 -12.238  80.480  1.00 73.23           C  
ANISOU 2892  C   LEU A 436    13179   8248   6398     36    392    289       C  
ATOM   2893  O   LEU A 436      38.086 -12.723  80.870  1.00 72.06           O  
ANISOU 2893  O   LEU A 436    13075   8017   6287     26    244    256       O  
ATOM   2894  CB  LEU A 436      38.980 -10.684  78.524  1.00 71.19           C  
ANISOU 2894  CB  LEU A 436    13181   7913   5956   -126    383    361       C  
ATOM   2895  CG  LEU A 436      39.848  -9.501  78.887  1.00 76.47           C  
ANISOU 2895  CG  LEU A 436    13681   8682   6691   -208    464    415       C  
ATOM   2896  CD1 LEU A 436      40.981  -9.336  77.884  1.00 78.81           C  
ANISOU 2896  CD1 LEU A 436    14025   9062   6859   -222    674    455       C  
ATOM   2897  CD2 LEU A 436      39.014  -8.242  78.945  1.00 78.64           C  
ANISOU 2897  CD2 LEU A 436    14019   8867   6993   -313    316    454       C  
ATOM   2898  N   LEU A 437      40.117 -11.820  81.303  1.00 69.46           N  
ANISOU 2898  N   LEU A 437    12460   7912   6019     48    483    318       N  
ATOM   2899  CA  LEU A 437      40.034 -11.855  82.753  1.00 68.05           C  
ANISOU 2899  CA  LEU A 437    12073   7788   5997     61    415    306       C  
ATOM   2900  C   LEU A 437      40.638 -10.576  83.305  1.00 72.43           C  
ANISOU 2900  C   LEU A 437    12450   8445   6627    -59    426    355       C  
ATOM   2901  O   LEU A 437      41.793 -10.278  83.004  1.00 74.18           O  
ANISOU 2901  O   LEU A 437    12576   8805   6805    -85    565    402       O  
ATOM   2902  CB  LEU A 437      40.770 -13.090  83.303  1.00 68.51           C  
ANISOU 2902  CB  LEU A 437    12048   7923   6060    227    524    287       C  
ATOM   2903  CG  LEU A 437      40.858 -13.229  84.827  1.00 72.49           C  
ANISOU 2903  CG  LEU A 437    12336   8500   6706    253    469    282       C  
ATOM   2904  CD1 LEU A 437      39.507 -13.557  85.437  1.00 71.36           C  
ANISOU 2904  CD1 LEU A 437    12265   8219   6628    226    304    234       C  
ATOM   2905  CD2 LEU A 437      41.862 -14.290  85.213  1.00 76.13           C  
ANISOU 2905  CD2 LEU A 437    12704   9074   7148    441    605    294       C  
ATOM   2906  N   ILE A 438      39.861  -9.812  84.094  1.00 67.14           N  
ANISOU 2906  N   ILE A 438    11749   7710   6050   -139    288    352       N  
ATOM   2907  CA  ILE A 438      40.345  -8.571  84.698  1.00 66.75           C  
ANISOU 2907  CA  ILE A 438    11603   7711   6047   -277    287    390       C  
ATOM   2908  C   ILE A 438      40.332  -8.678  86.211  1.00 69.96           C  
ANISOU 2908  C   ILE A 438    11851   8160   6571   -268    227    370       C  
ATOM   2909  O   ILE A 438      39.269  -8.792  86.824  1.00 68.15           O  
ANISOU 2909  O   ILE A 438    11658   7828   6407   -221    120    338       O  
ATOM   2910  CB  ILE A 438      39.638  -7.309  84.159  1.00 69.83           C  
ANISOU 2910  CB  ILE A 438    12172   7965   6396   -380    215    419       C  
ATOM   2911  CG1 ILE A 438      40.053  -7.077  82.698  1.00 71.60           C  
ANISOU 2911  CG1 ILE A 438    12536   8185   6482   -424    306    455       C  
ATOM   2912  CG2 ILE A 438      39.969  -6.077  85.028  1.00 70.86           C  
ANISOU 2912  CG2 ILE A 438    12269   8090   6565   -523    196    444       C  
ATOM   2913  CD1 ILE A 438      39.226  -6.115  81.940  1.00 80.38           C  
ANISOU 2913  CD1 ILE A 438    13870   9146   7526   -467    225    485       C  
ATOM   2914  N   VAL A 439      41.533  -8.630  86.801  1.00 68.06           N  
ANISOU 2914  N   VAL A 439    11424   8091   6347   -318    299    399       N  
ATOM   2915  CA  VAL A 439      41.754  -8.736  88.242  1.00 67.78           C  
ANISOU 2915  CA  VAL A 439    11232   8125   6398   -327    245    389       C  
ATOM   2916  C   VAL A 439      41.999  -7.334  88.846  1.00 72.03           C  
ANISOU 2916  C   VAL A 439    11781   8650   6936   -541    196    415       C  
ATOM   2917  O   VAL A 439      43.043  -6.720  88.611  1.00 73.05           O  
ANISOU 2917  O   VAL A 439    11830   8915   7011   -701    255    471       O  
ATOM   2918  CB  VAL A 439      42.865  -9.770  88.561  1.00 72.76           C  
ANISOU 2918  CB  VAL A 439    11649   8966   7032   -217    335    416       C  
ATOM   2919  CG1 VAL A 439      43.034  -9.945  90.063  1.00 72.17           C  
ANISOU 2919  CG1 VAL A 439    11434   8954   7035   -214    258    408       C  
ATOM   2920  CG2 VAL A 439      42.569 -11.118  87.901  1.00 72.48           C  
ANISOU 2920  CG2 VAL A 439    11696   8884   6958     -1    401    385       C  
ATOM   2921  N   THR A 440      41.001  -6.836  89.605  1.00 67.33           N  
ANISOU 2921  N   THR A 440    11306   7891   6387   -548     95    379       N  
ATOM   2922  CA  THR A 440      40.976  -5.504  90.208  1.00 67.51           C  
ANISOU 2922  CA  THR A 440    11441   7825   6386   -723     50    390       C  
ATOM   2923  C   THR A 440      41.232  -5.533  91.727  1.00 71.64           C  
ANISOU 2923  C   THR A 440    11871   8397   6952   -774     -7    372       C  
ATOM   2924  O   THR A 440      40.394  -6.054  92.473  1.00 70.40           O  
ANISOU 2924  O   THR A 440    11718   8168   6863   -635    -55    330       O  
ATOM   2925  CB  THR A 440      39.660  -4.797  89.836  1.00 73.66           C  
ANISOU 2925  CB  THR A 440    12462   8373   7154   -663      2    379       C  
ATOM   2926  OG1 THR A 440      39.503  -4.835  88.419  1.00 73.49           O  
ANISOU 2926  OG1 THR A 440    12524   8324   7075   -629     37    404       O  
ATOM   2927  CG2 THR A 440      39.611  -3.355  90.312  1.00 73.53           C  
ANISOU 2927  CG2 THR A 440    12645   8214   7077   -816    -20    393       C  
ATOM   2928  N   PRO A 441      42.356  -4.933  92.208  1.00 68.97           N  
ANISOU 2928  N   PRO A 441    11464   8181   6561   -997     -9    410       N  
ATOM   2929  CA  PRO A 441      42.621  -4.918  93.653  1.00 68.39           C  
ANISOU 2929  CA  PRO A 441    11328   8154   6502  -1071    -82    397       C  
ATOM   2930  C   PRO A 441      41.667  -3.989  94.373  1.00 71.59           C  
ANISOU 2930  C   PRO A 441    12009   8306   6887  -1103   -137    353       C  
ATOM   2931  O   PRO A 441      41.307  -2.937  93.842  1.00 72.69           O  
ANISOU 2931  O   PRO A 441    12387   8273   6959  -1183   -120    360       O  
ATOM   2932  CB  PRO A 441      44.069  -4.412  93.752  1.00 72.20           C  
ANISOU 2932  CB  PRO A 441    11671   8855   6907  -1346    -80    467       C  
ATOM   2933  CG  PRO A 441      44.611  -4.477  92.370  1.00 77.76           C  
ANISOU 2933  CG  PRO A 441    12296   9670   7580  -1352     25    519       C  
ATOM   2934  CD  PRO A 441      43.442  -4.259  91.476  1.00 72.36           C  
ANISOU 2934  CD  PRO A 441    11862   8732   6901  -1217     50    476       C  
ATOM   2935  N   VAL A 442      41.231  -4.405  95.565  1.00 66.44           N  
ANISOU 2935  N   VAL A 442    11343   7620   6281  -1015   -187    312       N  
ATOM   2936  CA  VAL A 442      40.316  -3.644  96.415  1.00 65.74           C  
ANISOU 2936  CA  VAL A 442    11511   7300   6166  -1002   -215    272       C  
ATOM   2937  C   VAL A 442      41.030  -3.319  97.738  1.00 69.65           C  
ANISOU 2937  C   VAL A 442    12032   7837   6595  -1195   -281    265       C  
ATOM   2938  O   VAL A 442      41.581  -4.218  98.384  1.00 68.89           O  
ANISOU 2938  O   VAL A 442    11715   7922   6538  -1174   -322    270       O  
ATOM   2939  CB  VAL A 442      38.932  -4.329  96.627  1.00 68.02           C  
ANISOU 2939  CB  VAL A 442    11809   7484   6550   -723   -204    236       C  
ATOM   2940  CG1 VAL A 442      37.824  -3.291  96.718  1.00 67.94           C  
ANISOU 2940  CG1 VAL A 442    12084   7229   6502   -653   -182    227       C  
ATOM   2941  CG2 VAL A 442      38.615  -5.329  95.515  1.00 66.95           C  
ANISOU 2941  CG2 VAL A 442    11525   7426   6487   -563   -176    247       C  
ATOM   2942  N   TYR A 443      41.064  -2.022  98.095  1.00 66.86           N  
ANISOU 2942  N   TYR A 443    11974   7309   6120  -1392   -295    259       N  
ATOM   2943  CA  TYR A 443      41.700  -1.492  99.301  1.00 67.91           C  
ANISOU 2943  CA  TYR A 443    12222   7439   6144  -1634   -371    250       C  
ATOM   2944  C   TYR A 443      40.656  -0.786 100.155  1.00 71.44           C  
ANISOU 2944  C   TYR A 443    13035   7582   6529  -1548   -350    194       C  
ATOM   2945  O   TYR A 443      39.859  -0.011  99.617  1.00 70.80           O  
ANISOU 2945  O   TYR A 443    13218   7271   6413  -1454   -280    189       O  
ATOM   2946  CB  TYR A 443      42.816  -0.507  98.925  1.00 71.76           C  
ANISOU 2946  CB  TYR A 443    12788   7983   6493  -2009   -402    299       C  
ATOM   2947  CG  TYR A 443      44.034  -1.154  98.302  1.00 74.77           C  
ANISOU 2947  CG  TYR A 443    12774   8720   6914  -2121   -416    373       C  
ATOM   2948  CD1 TYR A 443      45.117  -1.541  99.084  1.00 78.05           C  
ANISOU 2948  CD1 TYR A 443    12945   9412   7300  -2304   -511    419       C  
ATOM   2949  CD2 TYR A 443      44.128  -1.328  96.925  1.00 75.59           C  
ANISOU 2949  CD2 TYR A 443    12756   8896   7067  -2040   -330    410       C  
ATOM   2950  CE1 TYR A 443      46.252  -2.119  98.515  1.00 80.07           C  
ANISOU 2950  CE1 TYR A 443    12810  10027   7587  -2370   -505    509       C  
ATOM   2951  CE2 TYR A 443      45.253  -1.912  96.345  1.00 77.62           C  
ANISOU 2951  CE2 TYR A 443    12658   9486   7349  -2110   -311    486       C  
ATOM   2952  CZ  TYR A 443      46.316  -2.302  97.144  1.00 87.08           C  
ANISOU 2952  CZ  TYR A 443    13587  10974   8526  -2263   -391    541       C  
ATOM   2953  OH  TYR A 443      47.432  -2.871  96.578  1.00 90.01           O  
ANISOU 2953  OH  TYR A 443    13582  11703   8917  -2295   -355    637       O  
ATOM   2954  N   PHE A 444      40.658  -1.047 101.481  1.00 68.60           N  
ANISOU 2954  N   PHE A 444    12702   7221   6142  -1560   -401    161       N  
ATOM   2955  CA  PHE A 444      39.689  -0.451 102.407  1.00 69.21           C  
ANISOU 2955  CA  PHE A 444    13129   7019   6146  -1455   -358    109       C  
ATOM   2956  C   PHE A 444      40.328   0.432 103.472  1.00 77.24           C  
ANISOU 2956  C   PHE A 444    14450   7929   6967  -1760   -428     86       C  
ATOM   2957  O   PHE A 444      41.061  -0.088 104.320  1.00 77.97           O  
ANISOU 2957  O   PHE A 444    14392   8195   7038  -1897   -529     88       O  
ATOM   2958  CB  PHE A 444      38.782  -1.516 103.061  1.00 69.12           C  
ANISOU 2958  CB  PHE A 444    12967   7037   6260  -1153   -325     81       C  
ATOM   2959  CG  PHE A 444      38.239  -2.512 102.072  1.00 69.05           C  
ANISOU 2959  CG  PHE A 444    12662   7151   6423   -910   -282    104       C  
ATOM   2960  CD1 PHE A 444      37.201  -2.168 101.215  1.00 72.11           C  
ANISOU 2960  CD1 PHE A 444    13140   7407   6853   -716   -201    117       C  
ATOM   2961  CD2 PHE A 444      38.814  -3.770 101.944  1.00 70.57           C  
ANISOU 2961  CD2 PHE A 444    12508   7592   6714   -881   -328    120       C  
ATOM   2962  CE1 PHE A 444      36.737  -3.068 100.256  1.00 71.79           C  
ANISOU 2962  CE1 PHE A 444    12849   7483   6944   -541   -184    140       C  
ATOM   2963  CE2 PHE A 444      38.347  -4.672 100.987  1.00 72.21           C  
ANISOU 2963  CE2 PHE A 444    12507   7882   7047   -687   -290    135       C  
ATOM   2964  CZ  PHE A 444      37.311  -4.314 100.151  1.00 70.03           C  
ANISOU 2964  CZ  PHE A 444    12326   7477   6805   -541   -227    142       C  
ATOM   2965  N   PRO A 445      40.044   1.761 103.480  1.00 75.98           N  
ANISOU 2965  N   PRO A 445    14753   7471   6645  -1862   -380     68       N  
ATOM   2966  CA  PRO A 445      40.588   2.614 104.548  1.00 78.54           C  
ANISOU 2966  CA  PRO A 445    15447   7648   6745  -2174   -448     38       C  
ATOM   2967  C   PRO A 445      39.922   2.236 105.872  1.00 82.20           C  
ANISOU 2967  C   PRO A 445    16029   8011   7191  -1993   -426    -17       C  
ATOM   2968  O   PRO A 445      38.704   2.033 105.899  1.00 80.59           O  
ANISOU 2968  O   PRO A 445    15886   7667   7070  -1625   -296    -36       O  
ATOM   2969  CB  PRO A 445      40.223   4.036 104.094  1.00 82.24           C  
ANISOU 2969  CB  PRO A 445    16428   7770   7049  -2239   -362     30       C  
ATOM   2970  CG  PRO A 445      39.785   3.904 102.651  1.00 85.02           C  
ANISOU 2970  CG  PRO A 445    16590   8170   7546  -2033   -285     76       C  
ATOM   2971  CD  PRO A 445      39.187   2.542 102.568  1.00 77.69           C  
ANISOU 2971  CD  PRO A 445    15216   7452   6849  -1691   -264     79       C  
ATOM   2972  N   ARG A 446      40.727   2.054 106.937  1.00 79.94           N  
ANISOU 2972  N   ARG A 446    15731   7839   6806  -2245   -556    -28       N  
ATOM   2973  CA  ARG A 446      40.257   1.629 108.261  1.00 79.62           C  
ANISOU 2973  CA  ARG A 446    15792   7730   6729  -2113   -551    -75       C  
ATOM   2974  C   ARG A 446      39.091   2.464 108.788  1.00 84.15           C  
ANISOU 2974  C   ARG A 446    16883   7909   7183  -1904   -390   -132       C  
ATOM   2975  O   ARG A 446      38.050   1.895 109.123  1.00 82.02           O  
ANISOU 2975  O   ARG A 446    16546   7599   7020  -1545   -273   -147       O  
ATOM   2976  CB  ARG A 446      41.412   1.573 109.274  1.00 81.99           C  
ANISOU 2976  CB  ARG A 446    16094   8181   6878  -2487   -740    -70       C  
ATOM   2977  N   GLY A 447      39.262   3.790 108.803  1.00 83.49           N  
ANISOU 2977  N   GLY A 447    17306   7543   6875  -2119   -372   -153       N  
ATOM   2978  CA  GLY A 447      38.255   4.747 109.260  1.00 85.04           C  
ANISOU 2978  CA  GLY A 447    18071   7328   6911  -1918   -202   -198       C  
ATOM   2979  C   GLY A 447      36.908   4.572 108.587  1.00 87.54           C  
ANISOU 2979  C   GLY A 447    18285   7575   7400  -1417     -9   -173       C  
ATOM   2980  O   GLY A 447      35.877   4.498 109.264  1.00 87.29           O  
ANISOU 2980  O   GLY A 447    18398   7405   7365  -1092    135   -192       O  
ATOM   2981  N   ALA A 448      36.920   4.464 107.244  1.00 82.58           N  
ANISOU 2981  N   ALA A 448    17382   7073   6922  -1359    -11   -119       N  
ATOM   2982  CA  ALA A 448      35.726   4.256 106.423  1.00 80.55           C  
ANISOU 2982  CA  ALA A 448    16964   6808   6833   -927    129    -75       C  
ATOM   2983  C   ALA A 448      35.119   2.873 106.681  1.00 80.44           C  
ANISOU 2983  C   ALA A 448    16474   7048   7040   -670    142    -65       C  
ATOM   2984  O   ALA A 448      33.906   2.765 106.837  1.00 80.29           O  
ANISOU 2984  O   ALA A 448    16468   6959   7078   -309    284    -47       O  
ATOM   2985  CB  ALA A 448      36.067   4.420 104.947  1.00 80.72           C  
ANISOU 2985  CB  ALA A 448    16810   6923   6935   -998     90    -22       C  
ATOM   2986  N   LYS A 449      35.962   1.829 106.762  1.00 73.68           N  
ANISOU 2986  N   LYS A 449    15217   6485   6291   -855     -1    -68       N  
ATOM   2987  CA  LYS A 449      35.527   0.458 107.011  1.00 70.80           C  
ANISOU 2987  CA  LYS A 449    14442   6347   6113   -659     -3    -61       C  
ATOM   2988  C   LYS A 449      34.785   0.373 108.352  1.00 75.09           C  
ANISOU 2988  C   LYS A 449    15184   6761   6587   -497     91    -95       C  
ATOM   2989  O   LYS A 449      33.688  -0.185 108.401  1.00 73.64           O  
ANISOU 2989  O   LYS A 449    14844   6614   6522   -189    202    -72       O  
ATOM   2990  CB  LYS A 449      36.735  -0.486 106.976  1.00 72.06           C  
ANISOU 2990  CB  LYS A 449    14241   6800   6341   -900   -168    -55       C  
ATOM   2991  CG  LYS A 449      36.406  -1.924 106.630  1.00 82.38           C  
ANISOU 2991  CG  LYS A 449    15100   8345   7857   -704   -173    -31       C  
ATOM   2992  CD  LYS A 449      37.690  -2.730 106.531  1.00 94.92           C  
ANISOU 2992  CD  LYS A 449    16381  10202   9482   -909   -318    -13       C  
ATOM   2993  CE  LYS A 449      37.475  -4.207 106.735  1.00107.07           C  
ANISOU 2993  CE  LYS A 449    17589  11925  11166   -734   -327     -3       C  
ATOM   2994  NZ  LYS A 449      38.761  -4.959 106.739  1.00117.58           N  
ANISOU 2994  NZ  LYS A 449    18648  13515  12512   -888   -455     29       N  
ATOM   2995  N   HIS A 450      35.356   0.996 109.412  1.00 73.28           N  
ANISOU 2995  N   HIS A 450    15323   6375   6144   -718     52   -145       N  
ATOM   2996  CA  HIS A 450      34.787   1.055 110.765  1.00 73.54           C  
ANISOU 2996  CA  HIS A 450    15634   6249   6058   -603    145   -185       C  
ATOM   2997  C   HIS A 450      33.447   1.808 110.778  1.00 77.02           C  
ANISOU 2997  C   HIS A 450    16374   6436   6454   -242    377   -172       C  
ATOM   2998  O   HIS A 450      32.482   1.322 111.375  1.00 75.80           O  
ANISOU 2998  O   HIS A 450    16159   6290   6351     37    511   -162       O  
ATOM   2999  CB  HIS A 450      35.784   1.690 111.750  1.00 76.39           C  
ANISOU 2999  CB  HIS A 450    16381   6479   6163   -968     31   -239       C  
ATOM   3000  N   ARG A 451      33.384   2.968 110.081  1.00 74.26           N  
ANISOU 3000  N   ARG A 451    16331   5877   6007   -237    431   -158       N  
ATOM   3001  CA  ARG A 451      32.180   3.797 109.962  1.00 75.30           C  
ANISOU 3001  CA  ARG A 451    16764   5767   6079    135    652   -124       C  
ATOM   3002  C   ARG A 451      31.023   3.036 109.297  1.00 78.62           C  
ANISOU 3002  C   ARG A 451    16727   6399   6745    518    748    -43       C  
ATOM   3003  O   ARG A 451      29.885   3.143 109.756  1.00 79.48           O  
ANISOU 3003  O   ARG A 451    16907   6443   6848    866    936     -8       O  
ATOM   3004  CB  ARG A 451      32.482   5.102 109.209  1.00 75.52           C  
ANISOU 3004  CB  ARG A 451    17190   5547   5957     37    661   -115       C  
ATOM   3005  N   LEU A 452      31.320   2.238 108.246  1.00 73.06           N  
ANISOU 3005  N   LEU A 452    15551   5964   6244    441    619     -8       N  
ATOM   3006  CA  LEU A 452      30.319   1.463 107.510  1.00 71.13           C  
ANISOU 3006  CA  LEU A 452    14869   5938   6217    726    667     70       C  
ATOM   3007  C   LEU A 452      29.767   0.293 108.313  1.00 73.94           C  
ANISOU 3007  C   LEU A 452    14930   6478   6686    836    702     72       C  
ATOM   3008  O   LEU A 452      28.547   0.135 108.388  1.00 73.50           O  
ANISOU 3008  O   LEU A 452    14764   6467   6693   1150    848    138       O  
ATOM   3009  CB  LEU A 452      30.844   1.008 106.143  1.00 69.33           C  
ANISOU 3009  CB  LEU A 452    14305   5905   6133    586    521     97       C  
ATOM   3010  CG  LEU A 452      31.209   2.114 105.145  1.00 75.35           C  
ANISOU 3010  CG  LEU A 452    15325   6505   6799    506    503    116       C  
ATOM   3011  CD1 LEU A 452      32.055   1.570 104.024  1.00 74.06           C  
ANISOU 3011  CD1 LEU A 452    14866   6538   6737    263    345    118       C  
ATOM   3012  CD2 LEU A 452      29.984   2.807 104.583  1.00 79.02           C  
ANISOU 3012  CD2 LEU A 452    15889   6869   7267    873    641    203       C  
ATOM   3013  N   LEU A 453      30.653  -0.496 108.949  1.00 70.41           N  
ANISOU 3013  N   LEU A 453    14367   6138   6246    581    576     12       N  
ATOM   3014  CA  LEU A 453      30.273  -1.638 109.796  1.00 69.78           C  
ANISOU 3014  CA  LEU A 453    14060   6207   6244    644    598      8       C  
ATOM   3015  C   LEU A 453      29.385  -1.188 110.962  1.00 76.60           C  
ANISOU 3015  C   LEU A 453    15215   6902   6986    864    797      8       C  
ATOM   3016  O   LEU A 453      28.567  -1.971 111.448  1.00 75.35           O  
ANISOU 3016  O   LEU A 453    14853   6866   6911   1032    890     43       O  
ATOM   3017  CB  LEU A 453      31.522  -2.337 110.347  1.00 68.79           C  
ANISOU 3017  CB  LEU A 453    13867   6176   6092    339    427    -52       C  
ATOM   3018  CG  LEU A 453      32.211  -3.331 109.434  1.00 70.85           C  
ANISOU 3018  CG  LEU A 453    13731   6681   6508    198    268    -38       C  
ATOM   3019  CD1 LEU A 453      33.696  -3.291 109.649  1.00 71.27           C  
ANISOU 3019  CD1 LEU A 453    13836   6773   6470   -118    100    -77       C  
ATOM   3020  CD2 LEU A 453      31.708  -4.727 109.686  1.00 70.82           C  
ANISOU 3020  CD2 LEU A 453    13410   6859   6639    297    273    -18       C  
ATOM   3021  N   HIS A 454      29.548   0.082 111.392  1.00 76.33           N  
ANISOU 3021  N   HIS A 454    15683   6580   6738    856    871    -28       N  
ATOM   3022  CA  HIS A 454      28.768   0.697 112.457  1.00 78.86           C  
ANISOU 3022  CA  HIS A 454    16377   6690   6899   1085   1086    -31       C  
ATOM   3023  C   HIS A 454      27.343   0.957 111.968  1.00 83.83           C  
ANISOU 3023  C   HIS A 454    16890   7349   7611   1512   1294     75       C  
ATOM   3024  O   HIS A 454      26.392   0.508 112.608  1.00 83.52           O  
ANISOU 3024  O   HIS A 454    16725   7397   7611   1749   1454    122       O  
ATOM   3025  CB  HIS A 454      29.440   1.991 112.941  1.00 82.22           C  
ANISOU 3025  CB  HIS A 454    17422   6772   7044    924   1091   -102       C  
ATOM   3026  CG  HIS A 454      28.817   2.566 114.173  1.00 88.32           C  
ANISOU 3026  CG  HIS A 454    18656   7294   7608   1124   1308   -125       C  
ATOM   3027  ND1 HIS A 454      28.173   3.793 114.151  1.00 92.90           N  
ANISOU 3027  ND1 HIS A 454    19697   7580   8020   1390   1514   -102       N  
ATOM   3028  CD2 HIS A 454      28.736   2.051 115.422  1.00 90.47           C  
ANISOU 3028  CD2 HIS A 454    19009   7564   7801   1110   1359   -164       C  
ATOM   3029  CE1 HIS A 454      27.736   3.990 115.384  1.00 94.40           C  
ANISOU 3029  CE1 HIS A 454    20237   7597   8034   1534   1693   -130       C  
ATOM   3030  NE2 HIS A 454      28.048   2.967 116.184  1.00 93.37           N  
ANISOU 3030  NE2 HIS A 454    19889   7637   7950   1365   1606   -169       N  
ATOM   3031  N   GLN A 455      27.204   1.630 110.805  1.00 81.47           N  
ANISOU 3031  N   GLN A 455    16595   7014   7345   1602   1283    127       N  
ATOM   3032  CA  GLN A 455      25.918   1.938 110.174  1.00 82.80           C  
ANISOU 3032  CA  GLN A 455    16622   7247   7593   2009   1446    250       C  
ATOM   3033  C   GLN A 455      25.077   0.673 109.990  1.00 85.64           C  
ANISOU 3033  C   GLN A 455    16399   7962   8177   2124   1449    330       C  
ATOM   3034  O   GLN A 455      23.908   0.656 110.383  1.00 86.96           O  
ANISOU 3034  O   GLN A 455    16478   8203   8360   2448   1646    419       O  
ATOM   3035  CB  GLN A 455      26.128   2.642 108.827  1.00 84.31           C  
ANISOU 3035  CB  GLN A 455    16844   7388   7801   2006   1363    291       C  
ATOM   3036  CG  GLN A 455      26.536   4.100 108.953  1.00104.72           C  
ANISOU 3036  CG  GLN A 455    20064   9587  10137   2005   1433    252       C  
ATOM   3037  CD  GLN A 455      26.760   4.710 107.598  1.00129.65           C  
ANISOU 3037  CD  GLN A 455    23242  12705  13314   1986   1350    298       C  
ATOM   3038  OE1 GLN A 455      25.825   5.179 106.937  1.00127.78           O  
ANISOU 3038  OE1 GLN A 455    22981  12469  13100   2343   1461    411       O  
ATOM   3039  NE2 GLN A 455      28.004   4.693 107.142  1.00123.17           N  
ANISOU 3039  NE2 GLN A 455    22451  11871  12479   1575   1152    225       N  
ATOM   3040  N   ALA A 456      25.699  -0.396 109.449  1.00 79.48           N  
ANISOU 3040  N   ALA A 456    15244   7400   7554   1849   1240    302       N  
ATOM   3041  CA  ALA A 456      25.076  -1.704 109.234  1.00 77.78           C  
ANISOU 3041  CA  ALA A 456    14522   7500   7532   1867   1206    361       C  
ATOM   3042  C   ALA A 456      24.673  -2.363 110.558  1.00 80.95           C  
ANISOU 3042  C   ALA A 456    14904   7944   7909   1900   1320    347       C  
ATOM   3043  O   ALA A 456      23.614  -2.989 110.623  1.00 80.34           O  
ANISOU 3043  O   ALA A 456    14512   8078   7936   2055   1412    438       O  
ATOM   3044  CB  ALA A 456      26.020  -2.616 108.461  1.00 75.97           C  
ANISOU 3044  CB  ALA A 456    14026   7418   7422   1558    970    314       C  
ATOM   3045  N   ALA A 457      25.502  -2.211 111.608  1.00 77.75           N  
ANISOU 3045  N   ALA A 457    14839   7349   7354   1737   1310    242       N  
ATOM   3046  CA  ALA A 457      25.212  -2.787 112.919  1.00 78.51           C  
ANISOU 3046  CA  ALA A 457    14977   7457   7398   1757   1417    223       C  
ATOM   3047  C   ALA A 457      24.012  -2.115 113.574  1.00 86.16           C  
ANISOU 3047  C   ALA A 457    16113   8349   8276   2122   1705    297       C  
ATOM   3048  O   ALA A 457      23.209  -2.805 114.204  1.00 86.11           O  
ANISOU 3048  O   ALA A 457    15909   8493   8316   2239   1836    353       O  
ATOM   3049  CB  ALA A 457      26.428  -2.704 113.821  1.00 79.15           C  
ANISOU 3049  CB  ALA A 457    15393   7360   7320   1485   1312    102       C  
ATOM   3050  N   ASN A 458      23.879  -0.776 113.396  1.00 85.51           N  
ANISOU 3050  N   ASN A 458    16396   8034   8058   2314   1816    308       N  
ATOM   3051  CA  ASN A 458      22.767   0.026 113.917  1.00 88.64           C  
ANISOU 3051  CA  ASN A 458    17004   8331   8344   2728   2116    390       C  
ATOM   3052  C   ASN A 458      21.471  -0.342 113.211  1.00 93.67           C  
ANISOU 3052  C   ASN A 458    17141   9284   9166   3021   2214    558       C  
ATOM   3053  O   ASN A 458      20.416  -0.345 113.844  1.00 95.39           O  
ANISOU 3053  O   ASN A 458    17287   9593   9363   3317   2457    651       O  
ATOM   3054  CB  ASN A 458      23.046   1.523 113.772  1.00 91.48           C  
ANISOU 3054  CB  ASN A 458    17921   8338   8499   2847   2189    360       C  
ATOM   3055  CG  ASN A 458      24.048   2.084 114.758  1.00116.29           C  
ANISOU 3055  CG  ASN A 458    21649  11143  11392   2606   2160    215       C  
ATOM   3056  OD1 ASN A 458      24.311   1.525 115.836  1.00106.53           O  
ANISOU 3056  OD1 ASN A 458    20482   9902  10092   2457   2159    149       O  
ATOM   3057  ND2 ASN A 458      24.605   3.238 114.417  1.00111.95           N  
ANISOU 3057  ND2 ASN A 458    21564  10297  10676   2552   2132    169       N  
ATOM   3058  N   PHE A 459      21.558  -0.670 111.903  1.00 89.07           N  
ANISOU 3058  N   PHE A 459    16202   8888   8754   2922   2024    602       N  
ATOM   3059  CA  PHE A 459      20.428  -1.113 111.084  1.00 89.45           C  
ANISOU 3059  CA  PHE A 459    15738   9273   8978   3119   2050    765       C  
ATOM   3060  C   PHE A 459      19.954  -2.483 111.581  1.00 92.14           C  
ANISOU 3060  C   PHE A 459    15668   9901   9442   2993   2048    798       C  
ATOM   3061  O   PHE A 459      18.748  -2.711 111.674  1.00 93.37           O  
ANISOU 3061  O   PHE A 459    15510  10303   9661   3226   2202    944       O  
ATOM   3062  CB  PHE A 459      20.826  -1.177 109.601  1.00 89.61           C  
ANISOU 3062  CB  PHE A 459    15549   9383   9115   2972   1815    779       C  
ATOM   3063  CG  PHE A 459      19.696  -1.492 108.648  1.00 92.15           C  
ANISOU 3063  CG  PHE A 459    15388  10038   9588   3159   1808    953       C  
ATOM   3064  CD1 PHE A 459      18.804  -0.503 108.248  1.00 98.44           C  
ANISOU 3064  CD1 PHE A 459    16216  10846  10342   3563   1955   1095       C  
ATOM   3065  CD2 PHE A 459      19.546  -2.768 108.119  1.00 92.55           C  
ANISOU 3065  CD2 PHE A 459    14972  10388   9805   2923   1641    981       C  
ATOM   3066  CE1 PHE A 459      17.770  -0.792 107.351  1.00100.49           C  
ANISOU 3066  CE1 PHE A 459    15998  11451  10732   3721   1921   1274       C  
ATOM   3067  CE2 PHE A 459      18.510  -3.056 107.225  1.00 96.58           C  
ANISOU 3067  CE2 PHE A 459    15044  11218  10433   3046   1606   1147       C  
ATOM   3068  CZ  PHE A 459      17.633  -2.065 106.843  1.00 97.63           C  
ANISOU 3068  CZ  PHE A 459    15166  11397  10530   3439   1736   1297       C  
ATOM   3069  N   TRP A 460      20.906  -3.376 111.921  1.00 86.17           N  
ANISOU 3069  N   TRP A 460    14922   9115   8705   2630   1881    672       N  
ATOM   3070  CA  TRP A 460      20.613  -4.697 112.462  1.00 85.43           C  
ANISOU 3070  CA  TRP A 460    14534   9230   8695   2476   1872    685       C  
ATOM   3071  C   TRP A 460      19.969  -4.523 113.835  1.00 92.26           C  
ANISOU 3071  C   TRP A 460    15575  10040   9440   2675   2142    710       C  
ATOM   3072  O   TRP A 460      18.959  -5.168 114.115  1.00 93.17           O  
ANISOU 3072  O   TRP A 460    15373  10404   9625   2759   2267    820       O  
ATOM   3073  CB  TRP A 460      21.894  -5.533 112.580  1.00 81.57           C  
ANISOU 3073  CB  TRP A 460    14104   8671   8218   2094   1644    545       C  
ATOM   3074  CG  TRP A 460      21.640  -6.998 112.791  1.00 81.60           C  
ANISOU 3074  CG  TRP A 460    13791   8890   8323   1914   1590    566       C  
ATOM   3075  CD1 TRP A 460      21.612  -7.972 111.836  1.00 83.06           C  
ANISOU 3075  CD1 TRP A 460    13634   9275   8652   1736   1420    596       C  
ATOM   3076  CD2 TRP A 460      21.347  -7.648 114.035  1.00 82.07           C  
ANISOU 3076  CD2 TRP A 460    13895   8964   8326   1888   1713    561       C  
ATOM   3077  NE1 TRP A 460      21.337  -9.191 112.410  1.00 82.18           N  
ANISOU 3077  NE1 TRP A 460    13369   9286   8571   1591   1428    608       N  
ATOM   3078  CE2 TRP A 460      21.159  -9.020 113.757  1.00 84.76           C  
ANISOU 3078  CE2 TRP A 460    13913   9510   8781   1683   1608    591       C  
ATOM   3079  CE3 TRP A 460      21.233  -7.204 115.363  1.00 85.08           C  
ANISOU 3079  CE3 TRP A 460    14594   9184   8548   2012   1909    533       C  
ATOM   3080  CZ2 TRP A 460      20.868  -9.951 114.754  1.00 84.59           C  
ANISOU 3080  CZ2 TRP A 460    13870   9541   8729   1595   1690    598       C  
ATOM   3081  CZ3 TRP A 460      20.933  -8.126 116.350  1.00 87.06           C  
ANISOU 3081  CZ3 TRP A 460    14803   9503   8773   1935   1993    541       C  
ATOM   3082  CH2 TRP A 460      20.744  -9.480 116.042  1.00 86.55           C  
ANISOU 3082  CH2 TRP A 460    14405   9649   8832   1728   1885    577       C  
ATOM   3083  N   SER A 461      20.545  -3.633 114.676  1.00 89.90           N  
ANISOU 3083  N   SER A 461    15795   9419   8945   2733   2234    613       N  
ATOM   3084  CA  SER A 461      20.064  -3.313 116.024  1.00 92.02           C  
ANISOU 3084  CA  SER A 461    16347   9566   9049   2931   2504    617       C  
ATOM   3085  C   SER A 461      18.634  -2.766 115.994  1.00 98.65           C  
ANISOU 3085  C   SER A 461    17034  10552   9895   3376   2795    790       C  
ATOM   3086  O   SER A 461      17.811  -3.195 116.800  1.00 99.82           O  
ANISOU 3086  O   SER A 461    17055  10842  10028   3511   3007    866       O  
ATOM   3087  CB  SER A 461      20.996  -2.313 116.705  1.00 96.42           C  
ANISOU 3087  CB  SER A 461    17541   9725   9371   2890   2516    481       C  
ATOM   3088  OG  SER A 461      22.328  -2.796 116.785  1.00102.77           O  
ANISOU 3088  OG  SER A 461    18450  10438  10160   2485   2246    344       O  
ATOM   3089  N   ARG A 462      18.336  -1.844 115.054  1.00 96.28           N  
ANISOU 3089  N   ARG A 462    16728  10237   9615   3612   2808    864       N  
ATOM   3090  CA  ARG A 462      17.007  -1.252 114.896  1.00 99.53           C  
ANISOU 3090  CA  ARG A 462    16969  10814  10034   4080   3069   1053       C  
ATOM   3091  C   ARG A 462      15.990  -2.292 114.414  1.00104.19           C  
ANISOU 3091  C   ARG A 462    16867  11886  10836   4070   3050   1219       C  
ATOM   3092  O   ARG A 462      14.923  -2.418 115.020  1.00106.63           O  
ANISOU 3092  O   ARG A 462    16977  12401  11137   4319   3305   1354       O  
ATOM   3093  CB  ARG A 462      17.045  -0.033 113.958  1.00100.32           C  
ANISOU 3093  CB  ARG A 462    17268  10761  10089   4318   3055   1092       C  
ATOM   3094  N   SER A 463      16.334  -3.059 113.357  1.00 98.31           N  
ANISOU 3094  N   SER A 463    15772  11320  10263   3759   2753   1209       N  
ATOM   3095  CA  SER A 463      15.465  -4.095 112.792  1.00 98.13           C  
ANISOU 3095  CA  SER A 463    15128  11736  10423   3660   2681   1354       C  
ATOM   3096  C   SER A 463      15.184  -5.250 113.759  1.00101.51           C  
ANISOU 3096  C   SER A 463    15388  12313  10869   3464   2756   1352       C  
ATOM   3097  O   SER A 463      14.030  -5.651 113.876  1.00103.40           O  
ANISOU 3097  O   SER A 463    15229  12890  11169   3588   2903   1525       O  
ATOM   3098  CB  SER A 463      16.004  -4.608 111.460  1.00 98.88           C  
ANISOU 3098  CB  SER A 463    15002  11916  10653   3351   2347   1317       C  
ATOM   3099  OG  SER A 463      17.349  -5.037 111.582  1.00104.95           O  
ANISOU 3099  OG  SER A 463    16033  12446  11398   2990   2155   1118       O  
ATOM   3100  N   ALA A 464      16.213  -5.753 114.474  1.00 95.51           N  
ANISOU 3100  N   ALA A 464    14930  11317  10044   3170   2663   1173       N  
ATOM   3101  CA  ALA A 464      16.053  -6.844 115.444  1.00 95.30           C  
ANISOU 3101  CA  ALA A 464    14818  11383  10010   2975   2728   1161       C  
ATOM   3102  C   ALA A 464      15.151  -6.457 116.624  1.00102.66           C  
ANISOU 3102  C   ALA A 464    15841  12342  10823   3288   3091   1250       C  
ATOM   3103  O   ALA A 464      14.449  -7.317 117.160  1.00103.48           O  
ANISOU 3103  O   ALA A 464    15684  12676  10957   3211   3203   1335       O  
ATOM   3104  CB  ALA A 464      17.406  -7.310 115.948  1.00 93.23           C  
ANISOU 3104  CB  ALA A 464    14900  10842   9679   2652   2550    961       C  
ATOM   3105  N   LYS A 465      15.169  -5.165 117.013  1.00100.61           N  
ANISOU 3105  N   LYS A 465    15977  11838  10414   3638   3284   1235       N  
ATOM   3106  CA  LYS A 465      14.350  -4.620 118.095  1.00103.56           C  
ANISOU 3106  CA  LYS A 465    16512  12195  10643   4003   3663   1318       C  
ATOM   3107  C   LYS A 465      12.909  -4.388 117.627  1.00110.16           C  
ANISOU 3107  C   LYS A 465    16862  13422  11572   4366   3866   1569       C  
ATOM   3108  O   LYS A 465      11.990  -4.446 118.444  1.00112.79           O  
ANISOU 3108  O   LYS A 465    17072  13929  11852   4591   4170   1693       O  
ATOM   3109  CB  LYS A 465      14.963  -3.322 118.642  1.00106.85           C  
ANISOU 3109  CB  LYS A 465    17606  12161  10831   4227   3787   1198       C  
ATOM   3110  N   ASP A 466      12.713  -4.134 116.318  1.00105.98           N  
ANISOU 3110  N   ASP A 466    16043  13053  11173   4423   3697   1654       N  
ATOM   3111  CA  ASP A 466      11.394  -3.901 115.726  1.00108.98           C  
ANISOU 3111  CA  ASP A 466    15917  13844  11646   4757   3835   1911       C  
ATOM   3112  C   ASP A 466      10.694  -5.216 115.366  1.00112.44           C  
ANISOU 3112  C   ASP A 466    15698  14763  12262   4456   3718   2045       C  
ATOM   3113  O   ASP A 466       9.511  -5.379 115.672  1.00115.51           O  
ANISOU 3113  O   ASP A 466    15691  15524  12675   4657   3947   2253       O  
ATOM   3114  CB  ASP A 466      11.502  -2.984 114.498  1.00110.86           C  
ANISOU 3114  CB  ASP A 466    16176  14028  11919   4955   3698   1951       C  
ATOM   3115  N   THR A 467      11.433  -6.149 114.725  1.00104.89           N  
ANISOU 3115  N   THR A 467    14644  13798  11412   3969   3371   1929       N  
ATOM   3116  CA  THR A 467      10.967  -7.472 114.290  1.00103.94           C  
ANISOU 3116  CA  THR A 467    14005  14053  11434   3590   3202   2017       C  
ATOM   3117  C   THR A 467      10.628  -8.372 115.490  1.00108.22           C  
ANISOU 3117  C   THR A 467    14498  14689  11933   3420   3374   2028       C  
ATOM   3118  O   THR A 467       9.636  -9.102 115.443  1.00109.85           O  
ANISOU 3118  O   THR A 467    14214  15309  12215   3307   3421   2205       O  
ATOM   3119  CB  THR A 467      11.992  -8.096 113.321  1.00106.82           C  
ANISOU 3119  CB  THR A 467    14421  14284  11880   3170   2813   1865       C  
ATOM   3120  OG1 THR A 467      12.300  -7.145 112.300  1.00105.51           O  
ANISOU 3120  OG1 THR A 467    14349  14010  11730   3359   2695   1858       O  
ATOM   3121  CG2 THR A 467      11.501  -9.387 112.678  1.00105.11           C  
ANISOU 3121  CG2 THR A 467    13723  14426  11788   2783   2617   1957       C  
ATOM   3122  N   PHE A 468      11.445  -8.307 116.560  1.00103.08           N  
ANISOU 3122  N   PHE A 468    14356  13661  11148   3384   3463   1847       N  
ATOM   3123  CA  PHE A 468      11.249  -9.087 117.785  1.00103.35           C  
ANISOU 3123  CA  PHE A 468    14442  13718  11110   3237   3632   1838       C  
ATOM   3124  C   PHE A 468      11.052  -8.143 118.985  1.00109.78           C  
ANISOU 3124  C   PHE A 468    15631  14338  11743   3644   4000   1835       C  
ATOM   3125  O   PHE A 468      12.020  -7.825 119.686  1.00107.41           O  
ANISOU 3125  O   PHE A 468    15883  13627  11301   3619   3998   1645       O  
ATOM   3126  CB  PHE A 468      12.417 -10.063 118.007  1.00101.26           C  
ANISOU 3126  CB  PHE A 468    14448  13195  10831   2784   3381   1632       C  
ATOM   3127  CG  PHE A 468      12.735 -10.952 116.828  1.00100.19           C  
ANISOU 3127  CG  PHE A 468    14043  13183  10840   2409   3035   1613       C  
ATOM   3128  CD1 PHE A 468      11.978 -12.088 116.568  1.00104.01           C  
ANISOU 3128  CD1 PHE A 468    14103  14006  11410   2122   2983   1737       C  
ATOM   3129  CD2 PHE A 468      13.803 -10.664 115.989  1.00 99.14           C  
ANISOU 3129  CD2 PHE A 468    14108  12820  10741   2326   2768   1473       C  
ATOM   3130  CE1 PHE A 468      12.277 -12.915 115.484  1.00102.84           C  
ANISOU 3130  CE1 PHE A 468    13773  13936  11364   1770   2669   1712       C  
ATOM   3131  CE2 PHE A 468      14.100 -11.491 114.903  1.00 99.94           C  
ANISOU 3131  CE2 PHE A 468    13995  13020  10956   2001   2472   1454       C  
ATOM   3132  CZ  PHE A 468      13.335 -12.611 114.659  1.00 98.93           C  
ANISOU 3132  CZ  PHE A 468    13489  13201  10898   1729   2424   1569       C  
ATOM   3133  N   PRO A 469       9.805  -7.656 119.213  1.00111.21           N  
ANISOU 3133  N   PRO A 469    15522  14819  11912   4032   4320   2054       N  
ATOM   3134  CA  PRO A 469       9.574  -6.708 120.320  1.00114.28           C  
ANISOU 3134  CA  PRO A 469    16306  15009  12106   4470   4705   2059       C  
ATOM   3135  C   PRO A 469       9.728  -7.286 121.729  1.00119.65           C  
ANISOU 3135  C   PRO A 469    17280  15540  12642   4325   4882   1974       C  
ATOM   3136  O   PRO A 469      10.219  -6.591 122.621  1.00119.97           O  
ANISOU 3136  O   PRO A 469    17905  15194  12483   4506   5038   1845       O  
ATOM   3137  CB  PRO A 469       8.153  -6.201 120.059  1.00120.58           C  
ANISOU 3137  CB  PRO A 469    16615  16246  12953   4910   4986   2347       C  
ATOM   3138  CG  PRO A 469       7.494  -7.295 119.301  1.00124.75           C  
ANISOU 3138  CG  PRO A 469    16448  17270  13680   4571   4792   2503       C  
ATOM   3139  CD  PRO A 469       8.561  -7.913 118.455  1.00115.44           C  
ANISOU 3139  CD  PRO A 469    15366  15899  12598   4104   4347   2317       C  
ATOM   3140  N   TYR A 470       9.305  -8.547 121.923  1.00116.60           N  
ANISOU 3140  N   TYR A 470    16519  15448  12337   3983   4852   2049       N  
ATOM   3141  CA  TYR A 470       9.342  -9.288 123.188  1.00117.03           C  
ANISOU 3141  CA  TYR A 470    16776  15422  12266   3798   5007   1999       C  
ATOM   3142  C   TYR A 470      10.750  -9.525 123.729  1.00118.26           C  
ANISOU 3142  C   TYR A 470    17528  15099  12307   3522   4798   1731       C  
ATOM   3143  O   TYR A 470      10.918  -9.584 124.948  1.00118.86           O  
ANISOU 3143  O   TYR A 470    17983  14976  12202   3539   4986   1664       O  
ATOM   3144  CB  TYR A 470       8.571 -10.617 123.064  1.00119.04           C  
ANISOU 3144  CB  TYR A 470    16475  16110  12645   3440   4973   2150       C  
ATOM   3145  CG  TYR A 470       9.031 -11.485 121.915  1.00117.71           C  
ANISOU 3145  CG  TYR A 470    16051  16024  12649   2996   4547   2102       C  
ATOM   3146  CD1 TYR A 470       8.633 -11.215 120.608  1.00119.95           C  
ANISOU 3146  CD1 TYR A 470    15908  16575  13092   3052   4386   2218       C  
ATOM   3147  CD2 TYR A 470       9.851 -12.587 122.133  1.00115.55           C  
ANISOU 3147  CD2 TYR A 470    15982  15558  12363   2537   4312   1949       C  
ATOM   3148  CE1 TYR A 470       9.078 -11.990 119.542  1.00118.06           C  
ANISOU 3148  CE1 TYR A 470    15489  16384  12986   2650   4004   2166       C  
ATOM   3149  CE2 TYR A 470      10.283 -13.386 121.076  1.00113.80           C  
ANISOU 3149  CE2 TYR A 470    15575  15387  12278   2159   3945   1904       C  
ATOM   3150  CZ  TYR A 470       9.899 -13.077 119.781  1.00121.80           C  
ANISOU 3150  CZ  TYR A 470    16194  16646  13439   2210   3795   2006       C  
ATOM   3151  OH  TYR A 470      10.323 -13.845 118.729  1.00120.72           O  
ANISOU 3151  OH  TYR A 470    15916  16540  13413   1845   3445   1958       O  
ATOM   3152  N   ILE A 471      11.758  -9.651 122.838  1.00111.88           N  
ANISOU 3152  N   ILE A 471    16795  14123  11591   3273   4414   1591       N  
ATOM   3153  CA  ILE A 471      13.154  -9.871 123.239  1.00108.72           C  
ANISOU 3153  CA  ILE A 471    16895  13319  11093   3010   4183   1358       C  
ATOM   3154  C   ILE A 471      13.757  -8.593 123.831  1.00114.06           C  
ANISOU 3154  C   ILE A 471    18168  13601  11570   3291   4299   1234       C  
ATOM   3155  O   ILE A 471      13.841  -7.565 123.149  1.00113.71           O  
ANISOU 3155  O   ILE A 471    18196  13471  11539   3528   4281   1233       O  
ATOM   3156  CB  ILE A 471      14.041 -10.500 122.117  1.00107.81           C  
ANISOU 3156  CB  ILE A 471    16646  13182  11134   2654   3757   1262       C  
ATOM   3157  CG1 ILE A 471      13.437 -11.831 121.608  1.00108.04           C  
ANISOU 3157  CG1 ILE A 471    16171  13560  11318   2340   3651   1376       C  
ATOM   3158  CG2 ILE A 471      15.488 -10.703 122.614  1.00105.38           C  
ANISOU 3158  CG2 ILE A 471    16828  12497  10716   2420   3539   1046       C  
ATOM   3159  CD1 ILE A 471      14.045 -12.438 120.328  1.00113.79           C  
ANISOU 3159  CD1 ILE A 471    16709  14322  12202   2038   3274   1321       C  
ATOM   3160  N   LYS A 472      14.175  -8.675 125.107  1.00111.85           N  
ANISOU 3160  N   LYS A 472    18343  13069  11084   3245   4411   1134       N  
ATOM   3161  CA  LYS A 472      14.804  -7.584 125.843  1.00112.82           C  
ANISOU 3161  CA  LYS A 472    19111  12787  10969   3432   4507   1002       C  
ATOM   3162  C   LYS A 472      16.301  -7.549 125.489  1.00113.42           C  
ANISOU 3162  C   LYS A 472    19482  12579  11032   3128   4114    808       C  
ATOM   3163  O   LYS A 472      17.159  -7.822 126.332  1.00111.79           O  
ANISOU 3163  O   LYS A 472    19662  12141  10674   2915   4009    678       O  
ATOM   3164  CB  LYS A 472      14.567  -7.755 127.356  1.00117.87           C  
ANISOU 3164  CB  LYS A 472    20100  13307  11380   3483   4784    988       C  
ATOM   3165  N   TRP A 473      16.595  -7.220 124.217  1.00108.58           N  
ANISOU 3165  N   TRP A 473    18662  12016  10579   3108   3896    805       N  
ATOM   3166  CA  TRP A 473      17.937  -7.154 123.642  1.00105.43           C  
ANISOU 3166  CA  TRP A 473    18437  11419  10202   2836   3531    654       C  
ATOM   3167  C   TRP A 473      18.905  -6.292 124.455  1.00111.00           C  
ANISOU 3167  C   TRP A 473    19804  11720  10650   2818   3509    498       C  
ATOM   3168  O   TRP A 473      18.568  -5.173 124.850  1.00113.07           O  
ANISOU 3168  O   TRP A 473    20424  11794  10744   3115   3745    502       O  
ATOM   3169  CB  TRP A 473      17.882  -6.624 122.202  1.00103.07           C  
ANISOU 3169  CB  TRP A 473    17874  11217  10072   2919   3397    697       C  
ATOM   3170  CG  TRP A 473      17.158  -7.480 121.203  1.00103.12           C  
ANISOU 3170  CG  TRP A 473    17247  11606  10326   2850   3318    831       C  
ATOM   3171  CD1 TRP A 473      15.936  -7.231 120.648  1.00108.10           C  
ANISOU 3171  CD1 TRP A 473    17494  12517  11063   3119   3492   1008       C  
ATOM   3172  CD2 TRP A 473      17.672  -8.644 120.534  1.00 99.94           C  
ANISOU 3172  CD2 TRP A 473    16553  11338  10082   2486   3020    800       C  
ATOM   3173  NE1 TRP A 473      15.634  -8.192 119.711  1.00106.12           N  
ANISOU 3173  NE1 TRP A 473    16728  12574  11019   2903   3308   1087       N  
ATOM   3174  CE2 TRP A 473      16.682  -9.073 119.620  1.00104.35           C  
ANISOU 3174  CE2 TRP A 473    16578  12246  10824   2519   3027    955       C  
ATOM   3175  CE3 TRP A 473      18.864  -9.384 120.637  1.00 98.27           C  
ANISOU 3175  CE3 TRP A 473    16487  10993   9859   2148   2753    666       C  
ATOM   3176  CZ2 TRP A 473      16.845 -10.211 118.819  1.00101.34           C  
ANISOU 3176  CZ2 TRP A 473    15861  12045  10600   2203   2782    964       C  
ATOM   3177  CZ3 TRP A 473      19.026 -10.505 119.837  1.00 97.46           C  
ANISOU 3177  CZ3 TRP A 473    16041  11070   9920   1886   2532    681       C  
ATOM   3178  CH2 TRP A 473      18.025 -10.909 118.942  1.00 98.62           C  
ANISOU 3178  CH2 TRP A 473    15714  11525  10232   1904   2549    821       C  
ATOM   3179  N   ASP A 474      20.105  -6.831 124.700  1.00106.69           N  
ANISOU 3179  N   ASP A 474    19427  11049  10062   2470   3224    372       N  
ATOM   3180  CA  ASP A 474      21.193  -6.158 125.403  1.00107.55           C  
ANISOU 3180  CA  ASP A 474    20118  10817   9930   2349   3118    226       C  
ATOM   3181  C   ASP A 474      22.331  -5.984 124.390  1.00110.73           C  
ANISOU 3181  C   ASP A 474    20468  11177  10426   2113   2766    147       C  
ATOM   3182  O   ASP A 474      23.125  -6.904 124.169  1.00107.97           O  
ANISOU 3182  O   ASP A 474    19935  10919  10169   1824   2493    107       O  
ATOM   3183  CB  ASP A 474      21.624  -6.961 126.652  1.00109.61           C  
ANISOU 3183  CB  ASP A 474    20602  11007  10038   2147   3084    169       C  
ATOM   3184  CG  ASP A 474      22.865  -6.441 127.359  1.00120.32           C  
ANISOU 3184  CG  ASP A 474    22505  12062  11150   1940   2897     27       C  
ATOM   3185  OD1 ASP A 474      22.958  -5.210 127.573  1.00123.09           O  
ANISOU 3185  OD1 ASP A 474    23301  12158  11310   2063   2997    -25       O  
ATOM   3186  OD2 ASP A 474      23.734  -7.266 127.714  1.00124.33           O  
ANISOU 3186  OD2 ASP A 474    23008  12591  11642   1654   2648    -25       O  
ATOM   3187  N   PHE A 475      22.354  -4.820 123.721  1.00109.46           N  
ANISOU 3187  N   PHE A 475    20455  10891  10245   2260   2792    139       N  
ATOM   3188  CA  PHE A 475      23.338  -4.506 122.684  1.00107.80           C  
ANISOU 3188  CA  PHE A 475    20200  10644  10115   2061   2500     80       C  
ATOM   3189  C   PHE A 475      24.609  -3.843 123.230  1.00114.89           C  
ANISOU 3189  C   PHE A 475    21623  11251  10780   1818   2324    -54       C  
ATOM   3190  O   PHE A 475      25.503  -3.485 122.458  1.00112.53           O  
ANISOU 3190  O   PHE A 475    21327  10913  10515   1627   2090   -103       O  
ATOM   3191  CB  PHE A 475      22.695  -3.682 121.560  1.00109.80           C  
ANISOU 3191  CB  PHE A 475    20304  10937  10478   2318   2596    157       C  
ATOM   3192  CG  PHE A 475      21.622  -4.408 120.777  1.00110.27           C  
ANISOU 3192  CG  PHE A 475    19761  11343  10792   2466   2667    297       C  
ATOM   3193  CD1 PHE A 475      21.854  -5.678 120.256  1.00110.43           C  
ANISOU 3193  CD1 PHE A 475    19343  11606  11008   2219   2457    310       C  
ATOM   3194  CD2 PHE A 475      20.405  -3.797 120.504  1.00114.40           C  
ANISOU 3194  CD2 PHE A 475    20167  11953  11346   2849   2934    424       C  
ATOM   3195  CE1 PHE A 475      20.873  -6.336 119.512  1.00110.92           C  
ANISOU 3195  CE1 PHE A 475    18885  11981  11280   2303   2501    439       C  
ATOM   3196  CE2 PHE A 475      19.429  -4.452 119.748  1.00116.78           C  
ANISOU 3196  CE2 PHE A 475    19887  12611  11873   2945   2967    568       C  
ATOM   3197  CZ  PHE A 475      19.671  -5.715 119.252  1.00112.21           C  
ANISOU 3197  CZ  PHE A 475    18902  12258  11475   2647   2742    569       C  
ATOM   3198  N   SER A 476      24.704  -3.730 124.570  1.00116.59           N  
ANISOU 3198  N   SER A 476    22270  11281  10748   1797   2427   -108       N  
ATOM   3199  CA  SER A 476      25.864  -3.190 125.280  1.00118.75           C  
ANISOU 3199  CA  SER A 476    23062  11296  10761   1526   2251   -227       C  
ATOM   3200  C   SER A 476      27.057  -4.144 125.081  1.00123.68           C  
ANISOU 3200  C   SER A 476    23420  12087  11484   1153   1881   -262       C  
ATOM   3201  O   SER A 476      28.187  -3.685 124.908  1.00123.51           O  
ANISOU 3201  O   SER A 476    23585  11975  11368    883   1635   -329       O  
ATOM   3202  CB  SER A 476      25.551  -3.028 126.766  1.00124.75           C  
ANISOU 3202  CB  SER A 476    24306  11854  11237   1605   2459   -261       C  
ATOM   3203  OG  SER A 476      24.392  -2.237 126.973  1.00135.52           O  
ANISOU 3203  OG  SER A 476    25890  13089  12511   2003   2839   -211       O  
ATOM   3204  N   TYR A 477      26.787  -5.471 125.075  1.00120.46           N  
ANISOU 3204  N   TYR A 477    22577  11933  11261   1145   1851   -205       N  
ATOM   3205  CA  TYR A 477      27.774  -6.529 124.842  1.00118.60           C  
ANISOU 3205  CA  TYR A 477    22051  11876  11135    873   1543   -214       C  
ATOM   3206  C   TYR A 477      28.195  -6.513 123.370  1.00121.44           C  
ANISOU 3206  C   TYR A 477    22044  12380  11717    805   1365   -197       C  
ATOM   3207  O   TYR A 477      29.367  -6.734 123.062  1.00119.80           O  
ANISOU 3207  O   TYR A 477    21761  12235  11524    560   1088   -229       O  
ATOM   3208  CB  TYR A 477      27.186  -7.896 125.212  1.00119.00           C  
ANISOU 3208  CB  TYR A 477    21808  12109  11297    925   1615   -151       C  
ATOM   3209  N   LEU A 478      27.226  -6.229 122.472  1.00118.65           N  
ANISOU 3209  N   LEU A 478    21460  12096  11526   1033   1532   -136       N  
ATOM   3210  CA  LEU A 478      27.399  -6.117 121.022  1.00117.01           C  
ANISOU 3210  CA  LEU A 478    20928  12012  11520   1017   1411   -110       C  
ATOM   3211  C   LEU A 478      28.230  -4.863 120.676  1.00122.40           C  
ANISOU 3211  C   LEU A 478    21924  12506  12077    899   1301   -173       C  
ATOM   3212  O   LEU A 478      28.975  -4.887 119.693  1.00120.30           O  
ANISOU 3212  O   LEU A 478    21455  12331  11921    744   1101   -179       O  
ATOM   3213  CB  LEU A 478      26.006  -6.082 120.344  1.00117.22           C  
ANISOU 3213  CB  LEU A 478    20676  12158  11706   1312   1639    -12       C  
ATOM   3214  CG  LEU A 478      25.918  -5.737 118.851  1.00120.54           C  
ANISOU 3214  CG  LEU A 478    20826  12672  12300   1361   1569     28       C  
ATOM   3215  CD1 LEU A 478      25.022  -6.704 118.123  1.00119.48           C  
ANISOU 3215  CD1 LEU A 478    20195  12811  12392   1453   1609    126       C  
ATOM   3216  CD2 LEU A 478      25.417  -4.312 118.645  1.00124.92           C  
ANISOU 3216  CD2 LEU A 478    21670  13042  12753   1590   1742     41       C  
ATOM   3217  N   SER A 479      28.122  -3.791 121.507  1.00122.08           N  
ANISOU 3217  N   SER A 479    22407  12193  11786    957   1439   -219       N  
ATOM   3218  CA  SER A 479      28.800  -2.496 121.348  1.00123.54           C  
ANISOU 3218  CA  SER A 479    23008  12140  11793    831   1369   -282       C  
ATOM   3219  C   SER A 479      30.317  -2.577 121.084  1.00127.49           C  
ANISOU 3219  C   SER A 479    23480  12696  12266    429   1028   -332       C  
ATOM   3220  O   SER A 479      30.874  -1.632 120.519  1.00127.87           O  
ANISOU 3220  O   SER A 479    23720  12624  12240    291    942   -360       O  
ATOM   3221  CB  SER A 479      28.518  -1.590 122.540  1.00129.72           C  
ANISOU 3221  CB  SER A 479    24417  12605  12266    915   1560   -333       C  
ATOM   3222  OG  SER A 479      29.064  -0.295 122.350  1.00139.53           O  
ANISOU 3222  OG  SER A 479    26117  13583  13314    788   1510   -390       O  
ATOM   3223  N   ALA A 480      30.972  -3.695 121.473  1.00123.23           N  
ANISOU 3223  N   ALA A 480    22694  12348  11778    252    844   -330       N  
ATOM   3224  CA  ALA A 480      32.402  -3.935 121.248  1.00122.45           C  
ANISOU 3224  CA  ALA A 480    22479  12378  11671    -90    527   -349       C  
ATOM   3225  C   ALA A 480      32.720  -4.144 119.750  1.00124.40           C  
ANISOU 3225  C   ALA A 480    22295  12817  12156   -118    415   -309       C  
ATOM   3226  O   ALA A 480      33.795  -3.746 119.293  1.00124.29           O  
ANISOU 3226  O   ALA A 480    22278  12845  12103   -376    214   -321       O  
ATOM   3227  CB  ALA A 480      32.865  -5.137 122.056  1.00122.56           C  
ANISOU 3227  CB  ALA A 480    22333  12551  11681   -182    398   -335       C  
ATOM   3228  N   ASN A 481      31.779  -4.757 118.993  1.00118.87           N  
ANISOU 3228  N   ASN A 481    21238  12241  11685    131    546   -255       N  
ATOM   3229  CA  ASN A 481      31.918  -5.017 117.557  1.00138.82           C  
ANISOU 3229  CA  ASN A 481    23376  14938  14430    137    467   -216       C  
ATOM   3230  C   ASN A 481      30.702  -4.499 116.789  1.00142.06           C  
ANISOU 3230  C   ASN A 481    23742  15293  14940    412    676   -175       C  
ATOM   3231  O   ASN A 481      30.823  -3.595 115.965  1.00 91.52           O  
ANISOU 3231  O   ASN A 481    17440   8804   8527    406    674   -176       O  
ATOM   3232  CB  ASN A 481      32.120  -6.511 117.295  1.00137.35           C  
ANISOU 3232  CB  ASN A 481    22760  15005  14423    129    365   -177       C  
TER    3233      ASN A 481                                                      
ATOM   3234  P     U B   3       5.994  -8.850  70.974  1.00208.46           P  
ANISOU 3234  P     U B   3    26073  25882  27251   2314  -1862  -1251       P  
ATOM   3235  OP1   U B   3       5.891 -10.093  71.772  1.00209.14           O  
ANISOU 3235  OP1   U B   3    26023  25924  27518   2095  -2068  -1139       O  
ATOM   3236  OP2   U B   3       5.025  -7.750  71.183  1.00208.13           O  
ANISOU 3236  OP2   U B   3    26082  25782  27216   2195  -1591  -1356       O  
ATOM   3237  O5'   U B   3       7.471  -8.248  71.125  1.00207.75           O  
ANISOU 3237  O5'   U B   3    26071  26045  26818   2231  -1672  -1116       O  
ATOM   3238  C5'   U B   3       8.545  -8.782  70.349  1.00207.62           C  
ANISOU 3238  C5'   U B   3    26085  26142  26658   2527  -1874  -1053       C  
ATOM   3239  C4'   U B   3       9.285  -7.681  69.601  1.00207.26           C  
ANISOU 3239  C4'   U B   3    26134  26232  26385   2729  -1656  -1013       C  
ATOM   3240  O4'   U B   3       8.334  -6.789  68.971  1.00207.19           O  
ANISOU 3240  O4'   U B   3    26172  26095  26455   2924  -1502  -1180       O  
ATOM   3241  C3'   U B   3      10.160  -6.784  70.461  1.00206.94           C  
ANISOU 3241  C3'   U B   3    26120  26349  26160   2347  -1344   -873       C  
ATOM   3242  O3'   U B   3      11.461  -7.381  70.623  1.00206.90           O  
ANISOU 3242  O3'   U B   3    26118  26518  25978   2311  -1443   -720       O  
ATOM   3243  C2'   U B   3      10.220  -5.491  69.636  1.00206.77           C  
ANISOU 3243  C2'   U B   3    26160  26349  26053   2555  -1105   -890       C  
ATOM   3244  O2'   U B   3      11.258  -5.502  68.672  1.00206.86           O  
ANISOU 3244  O2'   U B   3    26185  26498  25913   2904  -1143   -757       O  
ATOM   3245  C1'   U B   3       8.858  -5.468  68.931  1.00206.72           C  
ANISOU 3245  C1'   U B   3    26178  26153  26213   2836  -1169  -1117       C  
ATOM   3246  N1    U B   3       7.843  -4.484  69.531  1.00206.07           N  
ANISOU 3246  N1    U B   3    26136  25989  26174   2551   -933  -1241       N  
ATOM   3247  C2    U B   3       7.920  -3.119  69.213  1.00205.51           C  
ANISOU 3247  C2    U B   3    26145  25974  25964   2555   -654  -1261       C  
ATOM   3248  O2    U B   3       8.780  -2.634  68.493  1.00205.61           O  
ANISOU 3248  O2    U B   3    26174  26084  25866   2770   -556  -1161       O  
ATOM   3249  N3    U B   3       6.945  -2.334  69.795  1.00204.87           N  
ANISOU 3249  N3    U B   3    26120  25845  25875   2306   -506  -1385       N  
ATOM   3250  C4    U B   3       5.915  -2.755  70.625  1.00204.80           C  
ANISOU 3250  C4    U B   3    26082  25748  25984   2079   -586  -1458       C  
ATOM   3251  O4    U B   3       5.120  -1.934  71.066  1.00204.23           O  
ANISOU 3251  O4    U B   3    26078  25680  25842   1901   -453  -1546       O  
ATOM   3252  C5    U B   3       5.886  -4.176  70.894  1.00205.51           C  
ANISOU 3252  C5    U B   3    26057  25762  26267   2089   -845  -1402       C  
ATOM   3253  C6    U B   3       6.826  -4.968  70.349  1.00206.01           C  
ANISOU 3253  C6    U B   3    26079  25864  26333   2310  -1015  -1313       C  
ATOM   3254  P     C B   4      12.314  -7.170  71.971  1.00206.63           P  
ANISOU 3254  P     C B   4    26082  26591  25837   1845  -1260   -618       P  
ATOM   3255  OP1   C B   4      13.259  -8.304  72.089  1.00206.23           O  
ANISOU 3255  OP1   C B   4    26046  26669  25641   1850  -1480   -553       O  
ATOM   3256  OP2   C B   4      11.375  -6.884  73.082  1.00206.76           O  
ANISOU 3256  OP2   C B   4    26060  26493  26006   1523  -1121   -688       O  
ATOM   3257  O5'   C B   4      13.140  -5.828  71.670  1.00206.68           O  
ANISOU 3257  O5'   C B   4    26120  26692  25717   1858   -994   -508       O  
ATOM   3258  C5'   C B   4      14.299  -5.862  70.829  1.00206.85           C  
ANISOU 3258  C5'   C B   4    26158  26867  25568   2132  -1044   -359       C  
ATOM   3259  C4'   C B   4      14.521  -4.520  70.152  1.00207.39           C  
ANISOU 3259  C4'   C B   4    26217  26946  25636   2280   -800   -269       C  
ATOM   3260  O4'   C B   4      13.244  -3.969  69.760  1.00207.49           O  
ANISOU 3260  O4'   C B   4    26246  26811  25781   2399   -726   -432       O  
ATOM   3261  C3'   C B   4      15.169  -3.460  71.029  1.00207.56           C  
ANISOU 3261  C3'   C B   4    26214  26977  25673   1922   -550   -179       C  
ATOM   3262  O3'   C B   4      16.598  -3.538  70.914  1.00207.86           O  
ANISOU 3262  O3'   C B   4    26230  27163  25583   1944   -545     21       O  
ATOM   3263  C2'   C B   4      14.615  -2.148  70.457  1.00207.90           C  
ANISOU 3263  C2'   C B   4    26251  26946  25797   2039   -346   -192       C  
ATOM   3264  O2'   C B   4      15.420  -1.613  69.424  1.00208.50           O  
ANISOU 3264  O2'   C B   4    26285  27114  25821   2347   -254      4       O  
ATOM   3265  C1'   C B   4      13.250  -2.561  69.900  1.00207.64           C  
ANISOU 3265  C1'   C B   4    26265  26807  25823   2262   -449   -402       C  
ATOM   3266  N1    C B   4      12.059  -2.131  70.747  1.00207.22           N  
ANISOU 3266  N1    C B   4    26242  26629  25864   1965   -379   -581       N  
ATOM   3267  C2    C B   4      11.301  -0.996  70.372  1.00207.06           C  
ANISOU 3267  C2    C B   4    26274  26545  25855   2020   -210   -689       C  
ATOM   3268  O2    C B   4      11.626  -0.344  69.368  1.00207.29           O  
ANISOU 3268  O2    C B   4    26312  26603  25846   2309    -92   -640       O  
ATOM   3269  N3    C B   4      10.223  -0.645  71.134  1.00206.59           N  
ANISOU 3269  N3    C B   4    26257  26413  25826   1775   -179   -837       N  
ATOM   3270  C4    C B   4       9.894  -1.371  72.215  1.00206.45           C  
ANISOU 3270  C4    C B   4    26204  26376  25861   1515   -287   -847       C  
ATOM   3271  N4    C B   4       8.831  -0.984  72.929  1.00206.04           N  
ANISOU 3271  N4    C B   4    26184  26281  25820   1327   -256   -949       N  
ATOM   3272  C5    C B   4      10.641  -2.529  72.607  1.00206.66           C  
ANISOU 3272  C5    C B   4    26168  26446  25908   1463   -432   -744       C  
ATOM   3273  C6    C B   4      11.698  -2.871  71.853  1.00206.92           C  
ANISOU 3273  C6    C B   4    26187  26559  25876   1676   -483   -632       C  
ATOM   3274  P     U B   5      17.541  -3.157  72.157  1.00207.83           P  
ANISOU 3274  P     U B   5    26207  27163  25596   1543   -423     73       P  
ATOM   3275  OP1   U B   5      18.919  -3.613  71.846  1.00207.93           O  
ANISOU 3275  OP1   U B   5    26220  27345  25441   1640   -481    252       O  
ATOM   3276  OP2   U B   5      16.881  -3.625  73.401  1.00207.21           O  
ANISOU 3276  OP2   U B   5    26162  26997  25573   1244   -463   -114       O  
ATOM   3277  O5'   U B   5      17.499  -1.553  72.157  1.00208.35           O  
ANISOU 3277  O5'   U B   5    26208  27130  25824   1468   -193    143       O  
ATOM   3278  C5'   U B   5      18.432  -0.784  71.384  1.00208.97           C  
ANISOU 3278  C5'   U B   5    26208  27266  25923   1637    -74    384       C  
ATOM   3279  C4'   U B   5      18.290   0.698  71.692  1.00209.30           C  
ANISOU 3279  C4'   U B   5    26186  27180  26160   1469    100    414       C  
ATOM   3280  O4'   U B   5      16.911   1.095  71.484  1.00208.88           O  
ANISOU 3280  O4'   U B   5    26189  27046  26130   1522    136    236       O  
ATOM   3281  C3'   U B   5      18.605   1.085  73.131  1.00208.95           C  
ANISOU 3281  C3'   U B   5    26129  27033  26229   1093     92    339       C  
ATOM   3282  O3'   U B   5      19.992   1.377  73.267  1.00209.56           O  
ANISOU 3282  O3'   U B   5    26118  27121  26384   1033    129    532       O  
ATOM   3283  C2'   U B   5      17.735   2.325  73.349  1.00209.12           C  
ANISOU 3283  C2'   U B   5    26145  26934  26378   1000    161    258       C  
ATOM   3284  O2'   U B   5      18.371   3.520  72.936  1.00210.21           O  
ANISOU 3284  O2'   U B   5    26173  27020  26678   1017    264    448       O  
ATOM   3285  C1'   U B   5      16.518   2.044  72.464  1.00208.71           C  
ANISOU 3285  C1'   U B   5    26171  26912  26219   1226    175    140       C  
ATOM   3286  N1    U B   5      15.288   1.528  73.215  1.00207.68           N  
ANISOU 3286  N1    U B   5    26133  26741  26033   1098     81   -102       N  
ATOM   3287  C2    U B   5      14.393   2.437  73.785  1.00207.29           C  
ANISOU 3287  C2    U B   5    26124  26624  26013    945    100   -223       C  
ATOM   3288  O2    U B   5      14.542   3.650  73.746  1.00207.67           O  
ANISOU 3288  O2    U B   5    26147  26633  26126    897    164   -170       O  
ATOM   3289  N3    U B   5      13.304   1.861  74.412  1.00206.49           N  
ANISOU 3289  N3    U B   5    26087  26510  25860    864     19   -391       N  
ATOM   3290  C4    U B   5      13.024   0.502  74.526  1.00206.16           C  
ANISOU 3290  C4    U B   5    26055  26487  25789    900    -77   -447       C  
ATOM   3291  O4    U B   5      12.021   0.134  75.123  1.00205.70           O  
ANISOU 3291  O4    U B   5    26024  26402  25730    819   -133   -559       O  
ATOM   3292  C5    U B   5      13.988  -0.374  73.905  1.00206.47           C  
ANISOU 3292  C5    U B   5    26063  26588  25797   1050   -122   -342       C  
ATOM   3293  C6    U B   5      15.056   0.158  73.288  1.00207.12           C  
ANISOU 3293  C6    U B   5    26100  26714  25883   1150    -43   -177       C  
ATOM   3294  P     U B  13      21.550   4.281  75.303  1.00216.61           P  
ANISOU 3294  P     U B  13    26743  27589  27969    565    153    680       P  
ATOM   3295  OP1   U B  13      22.165   5.164  74.283  1.00218.21           O  
ANISOU 3295  OP1   U B  13    26788  27783  28339    690    264    986       O  
ATOM   3296  OP2   U B  13      22.312   3.914  76.517  1.00216.16           O  
ANISOU 3296  OP2   U B  13    26699  27451  27982    418     66    570       O  
ATOM   3297  O5'   U B  13      20.136   4.886  75.771  1.00216.05           O  
ANISOU 3297  O5'   U B  13    26746  27446  27895    497     92    473       O  
ATOM   3298  C5'   U B  13      19.497   5.922  75.014  1.00216.58           C  
ANISOU 3298  C5'   U B  13    26785  27495  28011    571    153    537       C  
ATOM   3299  C4'   U B  13      18.227   6.426  75.692  1.00215.69           C  
ANISOU 3299  C4'   U B  13    26778  27347  27828    487     53    311       C  
ATOM   3300  O4'   U B  13      17.099   5.610  75.307  1.00214.65           O  
ANISOU 3300  O4'   U B  13    26781  27331  27447    568     96    157       O  
ATOM   3301  C3'   U B  13      18.199   6.372  77.210  1.00215.07           C  
ANISOU 3301  C3'   U B  13    26730  27189  27799    354   -121    157       C  
ATOM   3302  O3'   U B  13      18.952   7.459  77.777  1.00215.80           O  
ANISOU 3302  O3'   U B  13    26708  27118  28168    298   -246    234       O  
ATOM   3303  C2'   U B  13      16.696   6.498  77.484  1.00214.18           C  
ANISOU 3303  C2'   U B  13    26749  27140  27490    353   -176    -29       C  
ATOM   3304  O2'   U B  13      16.246   7.842  77.493  1.00214.44           O  
ANISOU 3304  O2'   U B  13    26785  27126  27566    337   -269    -38       O  
ATOM   3305  C1'   U B  13      16.082   5.741  76.297  1.00213.87           C  
ANISOU 3305  C1'   U B  13    26776  27220  27267    465    -22    -41       C  
ATOM   3306  N1    U B  13      15.539   4.369  76.667  1.00213.22           N  
ANISOU 3306  N1    U B  13    26770  27209  27034    467    -40   -166       N  
ATOM   3307  C2    U B  13      14.216   4.251  77.099  1.00212.49           C  
ANISOU 3307  C2    U B  13    26770  27150  26815    445    -93   -322       C  
ATOM   3308  O2    U B  13      13.440   5.191  77.163  1.00212.22           O  
ANISOU 3308  O2    U B  13    26788  27119  26728    433   -129   -384       O  
ATOM   3309  N3    U B  13      13.830   2.969  77.439  1.00212.06           N  
ANISOU 3309  N3    U B  13    26744  27139  26690    442   -112   -392       N  
ATOM   3310  C4    U B  13      14.616   1.822  77.418  1.00212.13           C  
ANISOU 3310  C4    U B  13    26724  27171  26706    451   -104   -352       C  
ATOM   3311  O4    U B  13      14.130   0.744  77.751  1.00211.69           O  
ANISOU 3311  O4    U B  13    26692  27147  26594    443   -142   -421       O  
ATOM   3312  C5    U B  13      15.980   2.025  76.976  1.00212.73           C  
ANISOU 3312  C5    U B  13    26737  27237  26855    474    -61   -213       C  
ATOM   3313  C6    U B  13      16.386   3.263  76.640  1.00213.38           C  
ANISOU 3313  C6    U B  13    26762  27263  27049    481    -23   -113       C  
ATOM   3314  P     G B  14      19.736   7.280  79.176  1.00215.36           P  
ANISOU 3314  P     G B  14    26620  26929  28279    258   -405    143       P  
ATOM   3315  OP1   G B  14      20.899   8.196  79.160  1.00216.99           O  
ANISOU 3315  OP1   G B  14    26654  26951  28843    239   -474    312       O  
ATOM   3316  OP2   G B  14      19.951   5.830  79.419  1.00214.37           O  
ANISOU 3316  OP2   G B  14    26576  26903  27971    259   -314     49       O  
ATOM   3317  O5'   G B  14      18.681   7.825  80.253  1.00214.02           O  
ANISOU 3317  O5'   G B  14    26533  26738  28048    290   -617    -39       O  
ATOM   3318  C5'   G B  14      17.792   6.936  80.907  1.00212.06           C  
ANISOU 3318  C5'   G B  14    26412  26608  27554    325   -613   -205       C  
ATOM   3319  C4'   G B  14      16.577   7.679  81.424  1.00210.90           C  
ANISOU 3319  C4'   G B  14    26341  26511  27280    381   -781   -293       C  
ATOM   3320  O4'   G B  14      15.398   7.270  80.678  1.00210.04           O  
ANISOU 3320  O4'   G B  14    26336  26566  26906    351   -646   -327       O  
ATOM   3321  C3'   G B  14      16.278   7.434  82.896  1.00209.68           C  
ANISOU 3321  C3'   G B  14    26226  26354  27090    515   -944   -419       C  
ATOM   3322  O3'   G B  14      16.733   8.560  83.664  1.00209.39           O  
ANISOU 3322  O3'   G B  14    26128  26170  27260    634  -1224   -429       O  
ATOM   3323  C2'   G B  14      14.751   7.282  82.943  1.00209.00           C  
ANISOU 3323  C2'   G B  14    26253  26448  26708    541   -942   -473       C  
ATOM   3324  O2'   G B  14      14.086   8.515  83.151  1.00208.92           O  
ANISOU 3324  O2'   G B  14    26287  26472  26620    610  -1168   -485       O  
ATOM   3325  C1'   G B  14      14.425   6.739  81.551  1.00209.08           C  
ANISOU 3325  C1'   G B  14    26295  26539  26606    410   -705   -434       C  
ATOM   3326  N9    G B  14      14.427   5.267  81.428  1.00208.85           N  
ANISOU 3326  N9    G B  14    26278  26566  26510    385   -538   -455       N  
ATOM   3327  C8    G B  14      15.197   4.516  80.565  1.00209.15           C  
ANISOU 3327  C8    G B  14    26282  26594  26592    333   -388   -400       C  
ATOM   3328  N7    G B  14      14.951   3.239  80.613  1.00208.72           N  
ANISOU 3328  N7    G B  14    26256  26605  26442    330   -314   -442       N  
ATOM   3329  C5    G B  14      13.915   3.124  81.525  1.00208.30           C  
ANISOU 3329  C5    G B  14    26239  26599  26304    373   -382   -510       C  
ATOM   3330  C6    G B  14      13.225   1.967  81.981  1.00207.93           C  
ANISOU 3330  C6    G B  14    26205  26618  26180    389   -346   -546       C  
ATOM   3331  O6    G B  14      13.410   0.786  81.649  1.00207.77           O  
ANISOU 3331  O6    G B  14    26179  26618  26146    356   -274   -552       O  
ATOM   3332  N1    G B  14      12.230   2.285  82.916  1.00207.76           N  
ANISOU 3332  N1    G B  14    26197  26648  26093    472   -428   -555       N  
ATOM   3333  C2    G B  14      11.951   3.562  83.365  1.00207.76           C  
ANISOU 3333  C2    G B  14    26221  26657  26062    546   -571   -553       C  
ATOM   3334  N2    G B  14      10.955   3.675  84.258  1.00207.47           N  
ANISOU 3334  N2    G B  14    26200  26714  25913    670   -660   -536       N  
ATOM   3335  N3    G B  14      12.578   4.658  82.932  1.00208.06           N  
ANISOU 3335  N3    G B  14    26259  26625  26169    517   -640   -545       N  
ATOM   3336  C4    G B  14      13.553   4.367  82.019  1.00208.35           C  
ANISOU 3336  C4    G B  14    26258  26591  26314    422   -521   -515       C  
ATOM   3337  P     A B  15      18.047   8.462  84.587  1.00209.00           P  
ANISOU 3337  P     A B  15    25985  25908  27517    748  -1326   -480       P  
ATOM   3338  OP1   A B  15      18.556   9.838  84.784  1.00210.10           O  
ANISOU 3338  OP1   A B  15    26022  25857  27950    816  -1618   -432       O  
ATOM   3339  OP2   A B  15      18.949   7.425  84.027  1.00208.98           O  
ANISOU 3339  OP2   A B  15    25958  25899  27547    611  -1057   -448       O  
ATOM   3340  O5'   A B  15      17.466   7.927  85.984  1.00207.16           O  
ANISOU 3340  O5'   A B  15    25827  25730  27154   1004  -1431   -634       O  
ATOM   3341  C5'   A B  15      17.389   6.531  86.258  1.00205.39           C  
ANISOU 3341  C5'   A B  15    25661  25608  26770   1002  -1198   -704       C  
ATOM   3342  C4'   A B  15      16.128   6.212  87.037  1.00203.75           C  
ANISOU 3342  C4'   A B  15    25525  25569  26322   1178  -1243   -734       C  
ATOM   3343  O4'   A B  15      15.069   5.822  86.114  1.00203.17           O  
ANISOU 3343  O4'   A B  15    25504  25675  26017    979  -1079   -653       O  
ATOM   3344  C3'   A B  15      16.253   5.048  88.003  1.00202.48           C  
ANISOU 3344  C3'   A B  15    25385  25432  26115   1350  -1122   -834       C  
ATOM   3345  O3'   A B  15      16.723   5.503  89.269  1.00201.88           O  
ANISOU 3345  O3'   A B  15    25288  25230  26186   1712  -1331   -944       O  
ATOM   3346  C2'   A B  15      14.817   4.535  88.064  1.00202.02           C  
ANISOU 3346  C2'   A B  15    25369  25589  25799   1361  -1047   -757       C  
ATOM   3347  O2'   A B  15      13.978   5.337  88.880  1.00201.91           O  
ANISOU 3347  O2'   A B  15    25367  25656  25693   1640  -1287   -721       O  
ATOM   3348  C1'   A B  15      14.404   4.663  86.600  1.00202.30           C  
ANISOU 3348  C1'   A B  15    25424  25688  25752   1041   -944   -670       C  
ATOM   3349  N9    A B  15      14.785   3.502  85.770  1.00202.02           N  
ANISOU 3349  N9    A B  15    25390  25666  25701    830   -700   -670       N  
ATOM   3350  C8    A B  15      15.655   3.494  84.711  1.00202.29           C  
ANISOU 3350  C8    A B  15    25409  25640  25813    646   -610   -641       C  
ATOM   3351  N7    A B  15      15.828   2.313  84.170  1.00201.93           N  
ANISOU 3351  N7    A B  15    25381  25652  25694    538   -447   -643       N  
ATOM   3352  C5    A B  15      15.018   1.479  84.922  1.00201.44           C  
ANISOU 3352  C5    A B  15    25335  25669  25534    622   -415   -678       C  
ATOM   3353  C6    A B  15      14.746   0.090  84.846  1.00201.04           C  
ANISOU 3353  C6    A B  15    25294  25691  25399    571   -297   -690       C  
ATOM   3354  N6    A B  15      15.304  -0.720  83.939  1.00200.87           N  
ANISOU 3354  N6    A B  15    25292  25691  25340    440   -223   -690       N  
ATOM   3355  N1    A B  15      13.881  -0.436  85.754  1.00200.87           N  
ANISOU 3355  N1    A B  15    25253  25730  25339    692   -282   -682       N  
ATOM   3356  C2    A B  15      13.333   0.377  86.675  1.00201.01           C  
ANISOU 3356  C2    A B  15    25255  25761  25359    888   -385   -658       C  
ATOM   3357  N3    A B  15      13.497   1.695  86.832  1.00201.26           N  
ANISOU 3357  N3    A B  15    25297  25744  25429    975   -543   -663       N  
ATOM   3358  C4    A B  15      14.364   2.192  85.915  1.00201.51           C  
ANISOU 3358  C4    A B  15    25337  25688  25538    811   -548   -679       C  
ATOM   3359  P     A B  16      17.798   4.637  90.088  1.00200.71           P  
ANISOU 3359  P     A B  16    25148  24954  26159   1876  -1206  -1128       P  
ATOM   3360  OP1   A B  16      18.087   5.353  91.353  1.00200.94           O  
ANISOU 3360  OP1   A B  16    25153  24832  26362   2334  -1486  -1251       O  
ATOM   3361  OP2   A B  16      18.913   4.292  89.171  1.00200.81           O  
ANISOU 3361  OP2   A B  16    25152  24876  26272   1558  -1037  -1144       O  
ATOM   3362  O5'   A B  16      16.985   3.296  90.444  1.00199.01           O  
ANISOU 3362  O5'   A B  16    24979  24933  25702   1918   -965  -1120       O  
ATOM   3363  C5'   A B  16      15.952   3.313  91.443  1.00197.94           C  
ANISOU 3363  C5'   A B  16    24839  24926  25445   2256  -1052  -1064       C  
ATOM   3364  C4'   A B  16      15.374   1.925  91.664  1.00196.50           C  
ANISOU 3364  C4'   A B  16    24663  24892  25106   2242   -782  -1027       C  
ATOM   3365  O4'   A B  16      14.729   1.460  90.451  1.00196.44           O  
ANISOU 3365  O4'   A B  16    24656  25001  24982   1832   -645   -894       O  
ATOM   3366  C3'   A B  16      16.390   0.844  91.986  1.00195.04           C  
ANISOU 3366  C3'   A B  16    24515  24623  24966   2251   -566  -1211       C  
ATOM   3367  O3'   A B  16      16.729   0.865  93.366  1.00193.73           O  
ANISOU 3367  O3'   A B  16    24356  24383  24869   2746   -610  -1357       O  
ATOM   3368  C2'   A B  16      15.634  -0.419  91.589  1.00194.98           C  
ANISOU 3368  C2'   A B  16    24499  24780  24803   2033   -335  -1101       C  
ATOM   3369  O2'   A B  16      14.702  -0.841  92.570  1.00195.00           O  
ANISOU 3369  O2'   A B  16    24449  24900  24742   2345   -282  -1003       O  
ATOM   3370  C1'   A B  16      14.907   0.051  90.324  1.00195.76           C  
ANISOU 3370  C1'   A B  16    24580  24951  24849   1695   -401   -931       C  
ATOM   3371  N9    A B  16      15.655  -0.230  89.089  1.00195.65           N  
ANISOU 3371  N9    A B  16    24602  24891  24845   1332   -326   -967       N  
ATOM   3372  C8    A B  16      16.492   0.623  88.414  1.00195.97           C  
ANISOU 3372  C8    A B  16    24653  24823  24985   1205   -416   -994       C  
ATOM   3373  N7    A B  16      17.075   0.084  87.370  1.00195.86           N  
ANISOU 3373  N7    A B  16    24663  24818  24935    940   -313   -988       N  
ATOM   3374  C5    A B  16      16.620  -1.224  87.374  1.00195.29           C  
ANISOU 3374  C5    A B  16    24611  24858  24734    883   -180   -987       C  
ATOM   3375  C6    A B  16      16.855  -2.319  86.509  1.00194.84           C  
ANISOU 3375  C6    A B  16    24589  24874  24568    677    -90   -980       C  
ATOM   3376  N6    A B  16      17.665  -2.254  85.448  1.00194.81           N  
ANISOU 3376  N6    A B  16    24613  24865  24541    516    -97   -960       N  
ATOM   3377  N1    A B  16      16.223  -3.489  86.783  1.00194.54           N  
ANISOU 3377  N1    A B  16    24544  24920  24451    677    -17   -971       N  
ATOM   3378  C2    A B  16      15.414  -3.555  87.858  1.00194.66           C  
ANISOU 3378  C2    A B  16    24508  24954  24501    875     10   -942       C  
ATOM   3379  N3    A B  16      15.103  -2.590  88.732  1.00195.01           N  
ANISOU 3379  N3    A B  16    24520  24964  24612   1115    -56   -927       N  
ATOM   3380  C4    A B  16      15.745  -1.438  88.432  1.00195.26           C  
ANISOU 3380  C4    A B  16    24574  24903  24712   1105   -171   -967       C  
ATOM   3381  P     G B  17      18.226   0.520  93.831  1.00191.99           P  
ANISOU 3381  P     G B  17    24205  23962  24780   2862   -529  -1660       P  
ATOM   3382  OP1   G B  17      18.307   0.758  95.293  1.00191.83           O  
ANISOU 3382  OP1   G B  17    24185  23866  24837   3492   -620  -1805       O  
ATOM   3383  OP2   G B  17      19.167   1.220  92.923  1.00192.29           O  
ANISOU 3383  OP2   G B  17    24245  23844  24971   2565   -644  -1700       O  
ATOM   3384  O5'   G B  17      18.326  -1.062  93.562  1.00190.10           O  
ANISOU 3384  O5'   G B  17    24025  23837  24368   2601   -198  -1705       O  
ATOM   3385  C5'   G B  17      18.566  -1.978  94.639  1.00188.10           C  
ANISOU 3385  C5'   G B  17    23825  23582  24061   2917     -7  -1893       C  
ATOM   3386  C4'   G B  17      17.915  -3.332  94.387  1.00186.71           C  
ANISOU 3386  C4'   G B  17    23642  23593  23708   2708    230  -1778       C  
ATOM   3387  O4'   G B  17      17.031  -3.264  93.231  1.00187.47           O  
ANISOU 3387  O4'   G B  17    23668  23806  23757   2309    170  -1507       O  
ATOM   3388  C3'   G B  17      18.882  -4.464  94.080  1.00184.49           C  
ANISOU 3388  C3'   G B  17    23483  23312  23302   2467    426  -1988       C  
ATOM   3389  O3'   G B  17      19.344  -5.066  95.289  1.00182.20           O  
ANISOU 3389  O3'   G B  17    23266  22980  22983   2865    593  -2236       O  
ATOM   3390  C2'   G B  17      18.010  -5.415  93.266  1.00185.10           C  
ANISOU 3390  C2'   G B  17    23507  23563  23261   2117    504  -1763       C  
ATOM   3391  O2'   G B  17      17.168  -6.223  94.067  1.00185.13           O  
ANISOU 3391  O2'   G B  17    23435  23662  23244   2346    648  -1665       O  
ATOM   3392  C1'   G B  17      17.180  -4.434  92.438  1.00186.89           C  
ANISOU 3392  C1'   G B  17    23635  23811  23564   1942    314  -1508       C  
ATOM   3393  N9    G B  17      17.806  -4.069  91.157  1.00187.41           N  
ANISOU 3393  N9    G B  17    23747  23842  23618   1571    223  -1509       N  
ATOM   3394  C8    G B  17      18.330  -2.843  90.807  1.00188.03           C  
ANISOU 3394  C8    G B  17    23823  23806  23814   1551     69  -1519       C  
ATOM   3395  N7    G B  17      18.850  -2.814  89.611  1.00188.25           N  
ANISOU 3395  N7    G B  17    23877  23841  23809   1228     47  -1477       N  
ATOM   3396  C5    G B  17      18.671  -4.103  89.130  1.00187.81           C  
ANISOU 3396  C5    G B  17    23859  23917  23583   1039    157  -1458       C  
ATOM   3397  C6    G B  17      19.042  -4.673  87.881  1.00187.80           C  
ANISOU 3397  C6    G B  17    23901  23998  23456    749    147  -1406       C  
ATOM   3398  O6    G B  17      19.606  -4.120  86.925  1.00188.16           O  
ANISOU 3398  O6    G B  17    23950  24027  23515    606     80  -1342       O  
ATOM   3399  N1    G B  17      18.670  -6.022  87.790  1.00187.37           N  
ANISOU 3399  N1    G B  17    23874  24063  23257    669    205  -1408       N  
ATOM   3400  C2    G B  17      18.029  -6.733  88.789  1.00187.12           C  
ANISOU 3400  C2    G B  17    23812  24057  23229    823    302  -1436       C  
ATOM   3401  N2    G B  17      17.757  -8.021  88.527  1.00186.81           N  
ANISOU 3401  N2    G B  17    23785  24116  23079    704    321  -1419       N  
ATOM   3402  N3    G B  17      17.677  -6.211  89.964  1.00187.17           N  
ANISOU 3402  N3    G B  17    23768  24000  23348   1115    356  -1460       N  
ATOM   3403  C4    G B  17      18.026  -4.894  90.067  1.00187.41           C  
ANISOU 3403  C4    G B  17    23790  23922  23495   1220    261  -1479       C  
ATOM   3404  P     C B  18      20.837  -5.658  95.398  1.00179.22           P  
ANISOU 3404  P     C B  18    23080  22509  22507   2818    724  -2624       P  
ATOM   3405  OP1   C B  18      21.394  -5.236  96.705  1.00178.66           O  
ANISOU 3405  OP1   C B  18    23059  22268  22556   3400    741  -2910       O  
ATOM   3406  OP2   C B  18      21.571  -5.333  94.152  1.00179.31           O  
ANISOU 3406  OP2   C B  18    23137  22492  22500   2360    608  -2609       O  
ATOM   3407  O5'   C B  18      20.587  -7.244  95.425  1.00176.79           O  
ANISOU 3407  O5'   C B  18    22828  22375  21969   2671    963  -2643       O  
ATOM   3408  C5'   C B  18      21.691  -8.152  95.564  1.00173.37           C  
ANISOU 3408  C5'   C B  18    22594  21944  21334   2613   1123  -2984       C  
ATOM   3409  C4'   C B  18      21.313  -9.563  95.119  1.00171.26           C  
ANISOU 3409  C4'   C B  18    22354  21872  20846   2315   1237  -2903       C  
ATOM   3410  O4'   C B  18      20.191  -9.508  94.183  1.00172.22           O  
ANISOU 3410  O4'   C B  18    22302  22089  21044   2014   1094  -2505       O  
ATOM   3411  C3'   C B  18      22.423 -10.327  94.398  1.00168.71           C  
ANISOU 3411  C3'   C B  18    22242  21624  20236   1965   1242  -3129       C  
ATOM   3412  O3'   C B  18      23.095 -11.194  95.303  1.00166.48           O  
ANISOU 3412  O3'   C B  18    22140  21354  19759   2184   1463  -3490       O  
ATOM   3413  C2'   C B  18      21.666 -11.111  93.330  1.00168.98           C  
ANISOU 3413  C2'   C B  18    22198  21832  20176   1565   1134  -2838       C  
ATOM   3414  O2'   C B  18      21.134 -12.331  93.818  1.00168.35           O  
ANISOU 3414  O2'   C B  18    22103  21854  20007   1617   1268  -2831       O  
ATOM   3415  C1'   C B  18      20.540 -10.145  92.968  1.00171.09           C  
ANISOU 3415  C1'   C B  18    22236  22051  20718   1563    997  -2478       C  
ATOM   3416  N1    C B  18      20.913  -9.055  91.932  1.00171.19           N  
ANISOU 3416  N1    C B  18    22235  22006  20803   1350    802  -2379       N  
ATOM   3417  C2    C B  18      21.564  -9.382  90.707  1.00170.48           C  
ANISOU 3417  C2    C B  18    22237  22009  20530   1001    687  -2367       C  
ATOM   3418  O2    C B  18      21.877 -10.556  90.461  1.00169.40           O  
ANISOU 3418  O2    C B  18    22217  22006  20142    857    702  -2463       O  
ATOM   3419  N3    C B  18      21.878  -8.373  89.845  1.00171.05           N  
ANISOU 3419  N3    C B  18    22267  22027  20697    870    549  -2243       N  
ATOM   3420  C4    C B  18      21.512  -7.113  90.115  1.00172.15           C  
ANISOU 3420  C4    C B  18    22284  22027  21096   1021    499  -2142       C  
ATOM   3421  N4    C B  18      21.841  -6.162  89.240  1.00172.80           N  
ANISOU 3421  N4    C B  18    22321  22058  21277    882    373  -2015       N  
ATOM   3422  C5    C B  18      20.840  -6.767  91.323  1.00172.76           C  
ANISOU 3422  C5    C B  18    22285  22025  21333   1360    563  -2163       C  
ATOM   3423  C6    C B  18      20.538  -7.757  92.173  1.00172.19           C  
ANISOU 3423  C6    C B  18    22242  22012  21170   1527    720  -2261       C  
ATOM   3424  P     A B  20      25.058  -6.862  89.847  1.00130.19           P  
ANISOU 3424  P     A B  20    17301  16585  15579    912    523  -2651       P  
ATOM   3425  OP1   A B  20      24.552  -7.423  91.114  1.00129.37           O  
ANISOU 3425  OP1   A B  20    17232  16455  15467   1190    663  -2844       O  
ATOM   3426  OP2   A B  20      26.385  -6.215  89.805  1.00129.78           O  
ANISOU 3426  OP2   A B  20    17305  16397  15607    919    497  -2790       O  
ATOM   3427  O5'   A B  20      25.018  -8.000  88.721  1.00130.17           O  
ANISOU 3427  O5'   A B  20    17380  16849  15230    617    479  -2532       O  
ATOM   3428  C5'   A B  20      24.912  -7.641  87.334  1.00132.14           C  
ANISOU 3428  C5'   A B  20    17542  17189  15478    411    332  -2228       C  
ATOM   3429  C4'   A B  20      25.767  -8.553  86.455  1.00131.76           C  
ANISOU 3429  C4'   A B  20    17646  17359  15056    244    263  -2241       C  
ATOM   3430  O4'   A B  20      26.863  -9.099  87.238  1.00129.75           O  
ANISOU 3430  O4'   A B  20    17598  17114  14586    294    371  -2588       O  
ATOM   3431  C3'   A B  20      25.029  -9.743  85.851  1.00132.20           C  
ANISOU 3431  C3'   A B  20    17731  17626  14872    147    154  -2142       C  
ATOM   3432  O3'   A B  20      24.658  -9.569  84.414  1.00135.08           O  
ANISOU 3432  O3'   A B  20    17995  18094  15234     68    -26  -1824       O  
ATOM   3433  C2'   A B  20      25.916 -10.962  86.127  1.00129.18           C  
ANISOU 3433  C2'   A B  20    17590  17417  14074    105    164  -2408       C  
ATOM   3434  O2'   A B  20      26.736 -11.315  85.036  1.00128.26           O  
ANISOU 3434  O2'   A B  20    17579  17511  13645      7      1  -2316       O  
ATOM   3435  C1'   A B  20      26.773 -10.503  87.311  1.00127.94           C  
ANISOU 3435  C1'   A B  20    17528  17092  13991    234    364  -2723       C  
ATOM   3436  N9    A B  20      26.323 -10.893  88.679  1.00126.52           N  
ANISOU 3436  N9    A B  20    17383  16813  13876    413    543  -2974       N  
ATOM   3437  C8    A B  20      26.958 -10.566  89.851  1.00124.86           C  
ANISOU 3437  C8    A B  20    17263  16435  13742    632    720  -3301       C  
ATOM   3438  N7    A B  20      26.428 -11.098  90.924  1.00123.79           N  
ANISOU 3438  N7    A B  20    17149  16265  13620    830    875  -3473       N  
ATOM   3439  C5    A B  20      25.369 -11.844  90.442  1.00124.77           C  
ANISOU 3439  C5    A B  20    17177  16536  13692    692    791  -3228       C  
ATOM   3440  C6    A B  20      24.408 -12.660  91.089  1.00124.85           C  
ANISOU 3440  C6    A B  20    17129  16584  13725    789    883  -3208       C  
ATOM   3441  N6    A B  20      24.383 -12.849  92.409  1.00124.41           N  
ANISOU 3441  N6    A B  20    17114  16441  13714   1091   1113  -3445       N  
ATOM   3442  N1    A B  20      23.477 -13.281  90.322  1.00125.69           N  
ANISOU 3442  N1    A B  20    17118  16809  13830    602    725  -2926       N  
ATOM   3443  C2    A B  20      23.515 -13.107  88.993  1.00126.65           C  
ANISOU 3443  C2    A B  20    17206  17015  13899    380    493  -2710       C  
ATOM   3444  N3    A B  20      24.366 -12.366  88.269  1.00126.99           N  
ANISOU 3444  N3    A B  20    17301  17060  13890    302    411  -2688       N  
ATOM   3445  C4    A B  20      25.287 -11.754  89.058  1.00126.20           C  
ANISOU 3445  C4    A B  20    17299  16835  13817    442    571  -2944       C  
ATOM   3446  P     G B  21      25.538  -8.807  83.270  1.00137.39           P  
ANISOU 3446  P     G B  21    18259  18441  15504     43   -104  -1617       P  
ATOM   3447  OP1   G B  21      26.694  -9.661  82.936  1.00135.69           O  
ANISOU 3447  OP1   G B  21    18237  18446  14872      6   -179  -1708       O  
ATOM   3448  OP2   G B  21      25.760  -7.404  83.691  1.00138.81           O  
ANISOU 3448  OP2   G B  21    18319  18386  16038     84      8  -1591       O  
ATOM   3449  O5'   G B  21      24.504  -8.759  82.009  1.00139.90           O  
ANISOU 3449  O5'   G B  21    18438  18828  15890     67   -261  -1313       O  
ATOM   3450  C5'   G B  21      24.616  -9.642  80.839  1.00140.63           C  
ANISOU 3450  C5'   G B  21    18592  19158  15685    110   -478  -1179       C  
ATOM   3451  C4'   G B  21      23.724 -10.887  80.965  1.00141.08           C  
ANISOU 3451  C4'   G B  21    18688  19288  15626    105   -623  -1262       C  
ATOM   3452  O4'   G B  21      23.697 -11.308  82.366  1.00140.45           O  
ANISOU 3452  O4'   G B  21    18680  19129  15556     30   -466  -1524       O  
ATOM   3453  C3'   G B  21      22.241 -10.725  80.562  1.00143.33           C  
ANISOU 3453  C3'   G B  21    18804  19463  16192    157   -691  -1116       C  
ATOM   3454  O3'   G B  21      21.992 -11.187  79.210  1.00144.35           O  
ANISOU 3454  O3'   G B  21    18918  19725  16205    298   -957   -950       O  
ATOM   3455  C2'   G B  21      21.534 -11.604  81.596  1.00142.93           C  
ANISOU 3455  C2'   G B  21    18760  19357  16189     89   -659  -1277       C  
ATOM   3456  O2'   G B  21      21.561 -12.981  81.257  1.00142.19           O  
ANISOU 3456  O2'   G B  21    18756  19421  15849     96   -897  -1324       O  
ATOM   3457  C1'   G B  21      22.362 -11.352  82.834  1.00141.63           C  
ANISOU 3457  C1'   G B  21    18692  19140  15980     38   -426  -1494       C  
ATOM   3458  N9    G B  21      22.048 -10.088  83.556  1.00142.57           N  
ANISOU 3458  N9    G B  21    18696  19051  16423     70   -222  -1485       N  
ATOM   3459  C8    G B  21      22.118  -8.797  83.064  1.00143.68           C  
ANISOU 3459  C8    G B  21    18738  19098  16755     93   -194  -1333       C  
ATOM   3460  N7    G B  21      21.963  -7.879  83.961  1.00144.16           N  
ANISOU 3460  N7    G B  21    18734  18989  17052    139    -56  -1388       N  
ATOM   3461  C5    G B  21      21.647  -8.581  85.106  1.00143.48           C  
ANISOU 3461  C5    G B  21    18690  18882  16945    186     34  -1564       C  
ATOM   3462  C6    G B  21      21.302  -8.101  86.388  1.00143.73           C  
ANISOU 3462  C6    G B  21    18674  18770  17165    328    170  -1668       C  
ATOM   3463  O6    G B  21      21.145  -6.927  86.738  1.00144.65           O  
ANISOU 3463  O6    G B  21    18706  18749  17506    424    192  -1626       O  
ATOM   3464  N1    G B  21      21.025  -9.143  87.279  1.00142.86           N  
ANISOU 3464  N1    G B  21    18613  18701  16968    394    257  -1808       N  
ATOM   3465  C2    G B  21      21.145 -10.486  86.981  1.00141.88           C  
ANISOU 3465  C2    G B  21    18581  18726  16602    291    201  -1863       C  
ATOM   3466  N2    G B  21      20.872 -11.344  87.975  1.00141.04           N  
ANISOU 3466  N2    G B  21    18502  18631  16458    380    319  -1995       N  
ATOM   3467  N3    G B  21      21.486 -10.953  85.778  1.00141.70           N  
ANISOU 3467  N3    G B  21    18616  18841  16384    151     21  -1781       N  
ATOM   3468  C4    G B  21      21.678  -9.947  84.878  1.00142.53           C  
ANISOU 3468  C4    G B  21    18663  18917  16575    125    -48  -1622       C  
ATOM   3469  P     C B  22      20.488 -11.252  78.571  1.00146.38           P  
ANISOU 3469  P     C B  22    19025  19872  16720    399  -1091   -838       P  
ATOM   3470  OP1   C B  22      20.163 -12.682  78.352  1.00145.77           O  
ANISOU 3470  OP1   C B  22    18995  19885  16508    441  -1374   -896       O  
ATOM   3471  OP2   C B  22      20.442 -10.313  77.430  1.00147.59           O  
ANISOU 3471  OP2   C B  22    19102  20021  16954    571  -1107   -647       O  
ATOM   3472  O5'   C B  22      19.502 -10.699  79.716  1.00147.70           O  
ANISOU 3472  O5'   C B  22    19082  19822  17217    269   -853   -902       O  
ATOM   3473  C5'   C B  22      18.115 -11.098  79.749  1.00149.41           C  
ANISOU 3473  C5'   C B  22    19182  19928  17661    282   -924   -871       C  
ATOM   3474  C4'   C B  22      17.768 -11.786  81.066  1.00149.99           C  
ANISOU 3474  C4'   C B  22    19243  19954  17790    172   -835   -984       C  
ATOM   3475  O4'   C B  22      18.805 -11.508  82.050  1.00148.71           O  
ANISOU 3475  O4'   C B  22    19190  19824  17488    107   -632  -1131       O  
ATOM   3476  C3'   C B  22      16.495 -11.301  81.737  1.00152.39           C  
ANISOU 3476  C3'   C B  22    19395  20099  18407    157   -698   -924       C  
ATOM   3477  O3'   C B  22      15.352 -11.967  81.239  1.00155.38           O  
ANISOU 3477  O3'   C B  22    19662  20418  18957    192   -883   -838       O  
ATOM   3478  C2'   C B  22      16.767 -11.640  83.196  1.00150.87           C  
ANISOU 3478  C2'   C B  22    19230  19900  18195    112   -507  -1042       C  
ATOM   3479  O2'   C B  22      16.624 -13.022  83.475  1.00150.33           O  
ANISOU 3479  O2'   C B  22    19158  19873  18086     82   -607  -1082       O  
ATOM   3480  C1'   C B  22      18.223 -11.228  83.316  1.00149.05           C  
ANISOU 3480  C1'   C B  22    19159  19747  17726     98   -422  -1178       C  
ATOM   3481  N1    C B  22      18.429  -9.734  83.676  1.00149.13           N  
ANISOU 3481  N1    C B  22    19142  19657  17864    135   -251  -1167       N  
ATOM   3482  C2    C B  22      18.255  -9.292  85.015  1.00148.75           C  
ANISOU 3482  C2    C B  22    19061  19513  17943    210    -66  -1246       C  
ATOM   3483  O2    C B  22      17.950 -10.106  85.900  1.00148.12           O  
ANISOU 3483  O2    C B  22    18978  19442  17860    253      9  -1319       O  
ATOM   3484  N3    C B  22      18.413  -7.963  85.294  1.00149.11           N  
ANISOU 3484  N3    C B  22    19075  19461  18121    274      8  -1231       N  
ATOM   3485  C4    C B  22      18.761  -7.102  84.323  1.00149.65           C  
ANISOU 3485  C4    C B  22    19134  19519  18208    228    -58  -1136       C  
ATOM   3486  N4    C B  22      18.933  -5.820  84.656  1.00150.10           N  
ANISOU 3486  N4    C B  22    19148  19465  18416    286    -15  -1122       N  
ATOM   3487  C5    C B  22      18.918  -7.519  82.963  1.00149.98           C  
ANISOU 3487  C5    C B  22    19195  19661  18128    166   -194  -1034       C  
ATOM   3488  C6    C B  22      18.763  -8.826  82.690  1.00149.61           C  
ANISOU 3488  C6    C B  22    19192  19717  17937    141   -302  -1061       C  
ATOM   3489  P     U B  23      13.981 -11.152  81.063  1.00159.01           P  
ANISOU 3489  P     U B  23    19974  20733  19708    230   -833   -723       P  
ATOM   3490  OP1   U B  23      12.971 -12.076  80.497  1.00159.92           O  
ANISOU 3490  OP1   U B  23    19982  20773  20008    277  -1067   -665       O  
ATOM   3491  OP2   U B  23      14.287  -9.883  80.358  1.00159.17           O  
ANISOU 3491  OP2   U B  23    20038  20756  19685    284   -770   -701       O  
ATOM   3492  O5'   U B  23      13.555 -10.806  82.575  1.00161.10           O  
ANISOU 3492  O5'   U B  23    20172  20951  20087    182   -582   -712       O  
ATOM   3493  C5'   U B  23      13.172 -11.842  83.492  1.00163.06           C  
ANISOU 3493  C5'   U B  23    20345  21190  20419    161   -556   -697       C  
ATOM   3494  C4'   U B  23      13.135 -11.315  84.918  1.00164.82           C  
ANISOU 3494  C4'   U B  23    20537  21406  20680    219   -293   -695       C  
ATOM   3495  O4'   U B  23      14.408 -10.705  85.246  1.00163.97           O  
ANISOU 3495  O4'   U B  23    20581  21349  20371    242   -174   -854       O  
ATOM   3496  C3'   U B  23      12.125 -10.215  85.158  1.00167.32           C  
ANISOU 3496  C3'   U B  23    20754  21666  21155    288   -210   -567       C  
ATOM   3497  O3'   U B  23      10.843 -10.759  85.386  1.00170.40           O  
ANISOU 3497  O3'   U B  23    20971  22004  21770    303   -239   -400       O  
ATOM   3498  C2'   U B  23      12.693  -9.517  86.388  1.00166.37           C  
ANISOU 3498  C2'   U B  23    20679  21571  20963    416    -12   -632       C  
ATOM   3499  O2'   U B  23      12.362 -10.167  87.602  1.00166.45           O  
ANISOU 3499  O2'   U B  23    20599  21594  21049    540    120   -578       O  
ATOM   3500  C1'   U B  23      14.201  -9.606  86.124  1.00164.75           C  
ANISOU 3500  C1'   U B  23    20645  21404  20547    362    -14   -832       C  
ATOM   3501  N1    U B  23      14.783  -8.340  85.507  1.00164.92           N  
ANISOU 3501  N1    U B  23    20742  21407  20514    343    -41   -867       N  
ATOM   3502  C2    U B  23      15.147  -7.279  86.339  1.00164.97           C  
ANISOU 3502  C2    U B  23    20768  21369  20544    467     56   -919       C  
ATOM   3503  O2    U B  23      15.061  -7.313  87.557  1.00164.87           O  
ANISOU 3503  O2    U B  23    20731  21342  20569    638    163   -955       O  
ATOM   3504  N3    U B  23      15.630  -6.165  85.679  1.00165.23           N  
ANISOU 3504  N3    U B  23    20839  21367  20572    427      4   -919       N  
ATOM   3505  C4    U B  23      15.750  -5.989  84.305  1.00165.55           C  
ANISOU 3505  C4    U B  23    20899  21430  20574    310    -93   -859       C  
ATOM   3506  O4    U B  23      16.224  -4.946  83.864  1.00165.84           O  
ANISOU 3506  O4    U B  23    20950  21430  20630    302   -106   -840       O  
ATOM   3507  C5    U B  23      15.357  -7.130  83.507  1.00165.53           C  
ANISOU 3507  C5    U B  23    20887  21484  20524    243   -189   -820       C  
ATOM   3508  C6    U B  23      14.890  -8.231  84.121  1.00165.26           C  
ANISOU 3508  C6    U B  23    20814  21467  20512    248   -181   -829       C  
ATOM   3509  P     U B  24       9.562 -10.051  84.746  1.00173.46           P  
ANISOU 3509  P     U B  24    21267  22325  22315    305   -313   -274       P  
ATOM   3510  OP1   U B  24       8.404 -10.956  84.928  1.00174.71           O  
ANISOU 3510  OP1   U B  24    21235  22411  22736    302   -375   -108       O  
ATOM   3511  OP2   U B  24       9.921  -9.583  83.387  1.00173.01           O  
ANISOU 3511  OP2   U B  24    21320  22250  22165    262   -445   -378       O  
ATOM   3512  O5'   U B  24       9.358  -8.776  85.695  1.00175.63           O  
ANISOU 3512  O5'   U B  24    21547  22652  22531    426   -145   -222       O  
ATOM   3513  C5'   U B  24       9.014  -8.946  87.077  1.00178.09           C  
ANISOU 3513  C5'   U B  24    21763  23010  22892    582      4   -107       C  
ATOM   3514  C4'   U B  24       9.036  -7.619  87.818  1.00179.96           C  
ANISOU 3514  C4'   U B  24    22046  23310  23019    763     80    -97       C  
ATOM   3515  O4'   U B  24      10.386  -7.101  87.846  1.00179.17           O  
ANISOU 3515  O4'   U B  24    22100  23207  22770    781    102   -300       O  
ATOM   3516  C3'   U B  24       8.219  -6.506  87.182  1.00181.97           C  
ANISOU 3516  C3'   U B  24    22322  23574  23242    734    -12    -48       C  
ATOM   3517  O3'   U B  24       6.835  -6.622  87.551  1.00185.06           O  
ANISOU 3517  O3'   U B  24    22572  24004  23741    812     -5    171       O  
ATOM   3518  C2'   U B  24       8.878  -5.249  87.755  1.00180.79           C  
ANISOU 3518  C2'   U B  24    22280  23471  22942    884     -4   -134       C  
ATOM   3519  O2'   U B  24       8.355  -4.874  89.017  1.00181.11           O  
ANISOU 3519  O2'   U B  24    22253  23599  22962   1165     34      3       O  
ATOM   3520  C1'   U B  24      10.347  -5.681  87.893  1.00179.42           C  
ANISOU 3520  C1'   U B  24    22190  23252  22728    864     53   -315       C  
ATOM   3521  N1    U B  24      11.254  -5.111  86.819  1.00178.67           N  
ANISOU 3521  N1    U B  24    22217  23109  22561    696    -20   -460       N  
ATOM   3522  C2    U B  24      11.865  -3.874  87.027  1.00178.36           C  
ANISOU 3522  C2    U B  24    22249  23050  22471    773    -59   -531       C  
ATOM   3523  O2    U B  24      11.736  -3.219  88.050  1.00178.38           O  
ANISOU 3523  O2    U B  24    22238  23069  22469    995    -72   -513       O  
ATOM   3524  N3    U B  24      12.648  -3.432  85.981  1.00178.16           N  
ANISOU 3524  N3    U B  24    22298  22980  22415    620   -106   -608       N  
ATOM   3525  C4    U B  24      12.880  -4.079  84.775  1.00178.11           C  
ANISOU 3525  C4    U B  24    22315  22973  22388    453   -125   -620       C  
ATOM   3526  O4    U B  24      13.605  -3.556  83.935  1.00178.10           O  
ANISOU 3526  O4    U B  24    22367  22950  22354    386   -155   -652       O  
ATOM   3527  C5    U B  24      12.204  -5.351  84.624  1.00178.22           C  
ANISOU 3527  C5    U B  24    22268  23007  22440    411   -130   -570       C  
ATOM   3528  C6    U B  24      11.432  -5.807  85.626  1.00178.52           C  
ANISOU 3528  C6    U B  24    22218  23064  22545    507    -75   -491       C  
ATOM   3529  P     C B  25       5.682  -6.098  86.560  1.00187.51           P  
ANISOU 3529  P     C B  25    22876  24286  24082    699   -113    210       P  
ATOM   3530  OP1   C B  25       4.419  -6.781  86.925  1.00188.73           O  
ANISOU 3530  OP1   C B  25    22839  24432  24438    735    -98    442       O  
ATOM   3531  OP2   C B  25       6.188  -6.186  85.166  1.00187.06           O  
ANISOU 3531  OP2   C B  25    22924  24131  24020    524   -204     19       O  
ATOM   3532  O5'   C B  25       5.566  -4.552  86.962  1.00188.86           O  
ANISOU 3532  O5'   C B  25    23152  24575  24029    831   -138    206       O  
ATOM   3533  C5'   C B  25       5.479  -3.552  85.962  1.00190.09           C  
ANISOU 3533  C5'   C B  25    23454  24717  24054    726   -221     56       C  
ATOM   3534  C4'   C B  25       5.701  -2.181  86.563  1.00191.33           C  
ANISOU 3534  C4'   C B  25    23710  24984  24003    874   -277     37       C  
ATOM   3535  O4'   C B  25       7.080  -2.070  87.009  1.00191.32           O  
ANISOU 3535  O4'   C B  25    23751  24943  23999    934   -258    -64       O  
ATOM   3536  C3'   C B  25       5.513  -1.032  85.593  1.00192.07           C  
ANISOU 3536  C3'   C B  25    23947  25085  23947    777   -363    -91       C  
ATOM   3537  O3'   C B  25       4.138  -0.644  85.531  1.00193.65           O  
ANISOU 3537  O3'   C B  25    24159  25381  24038    806   -411    -14       O  
ATOM   3538  C2'   C B  25       6.397   0.056  86.201  1.00191.29           C  
ANISOU 3538  C2'   C B  25    23927  25023  23732    899   -444   -147       C  
ATOM   3539  O2'   C B  25       5.765   0.755  87.260  1.00191.17           O  
ANISOU 3539  O2'   C B  25    23914  25158  23563   1136   -555    -33       O  
ATOM   3540  C1'   C B  25       7.577  -0.765  86.734  1.00191.13           C  
ANISOU 3540  C1'   C B  25    23847  24921  23853    938   -360   -173       C  
ATOM   3541  N1    C B  25       8.764  -0.861  85.766  1.00190.88           N  
ANISOU 3541  N1    C B  25    23874  24769  23883    758   -327   -324       N  
ATOM   3542  C2    C B  25       9.673   0.224  85.640  1.00190.62           C  
ANISOU 3542  C2    C B  25    23914  24694  23818    766   -400   -412       C  
ATOM   3543  O2    C B  25       9.503   1.255  86.309  1.00190.53           O  
ANISOU 3543  O2    C B  25    23930  24731  23733    921   -525   -394       O  
ATOM   3544  N3    C B  25      10.715   0.108  84.765  1.00190.55           N  
ANISOU 3544  N3    C B  25    23935  24597  23869    625   -356   -493       N  
ATOM   3545  C4    C B  25      10.888  -1.021  84.062  1.00190.55           C  
ANISOU 3545  C4    C B  25    23917  24572  23913    511   -276   -506       C  
ATOM   3546  N4    C B  25      11.932  -1.085  83.229  1.00190.46           N  
ANISOU 3546  N4    C B  25    23937  24511  23919    426   -254   -557       N  
ATOM   3547  C5    C B  25       9.988  -2.129  84.175  1.00190.77           C  
ANISOU 3547  C5    C B  25    23879  24627  23977    504   -243   -446       C  
ATOM   3548  C6    C B  25       8.960  -2.011  85.031  1.00191.00           C  
ANISOU 3548  C6    C B  25    23857  24722  23992    614   -254   -349       C  
ATOM   3549  P     C B  26       3.459  -0.317  84.113  1.00194.78           P  
ANISOU 3549  P     C B  26    24403  25466  24139    650   -423   -164       P  
ATOM   3550  OP1   C B  26       2.500   0.795  84.319  1.00194.22           O  
ANISOU 3550  OP1   C B  26    24442  25552  23800    718   -511   -160       O  
ATOM   3551  OP2   C B  26       2.990  -1.594  83.528  1.00195.51           O  
ANISOU 3551  OP2   C B  26    24379  25429  24477    572   -375   -139       O  
ATOM   3552  O5'   C B  26       4.699   0.205  83.231  1.00195.61           O  
ANISOU 3552  O5'   C B  26    24612  25476  24234    560   -413   -349       O  
ATOM   3553  C5'   C B  26       4.498   1.074  82.125  1.00196.21           C  
ANISOU 3553  C5'   C B  26    24828  25539  24185    507   -424   -508       C  
ATOM   3554  C4'   C B  26       5.241   2.385  82.333  1.00196.96           C  
ANISOU 3554  C4'   C B  26    25016  25691  24128    531   -494   -548       C  
ATOM   3555  O4'   C B  26       6.623   2.121  82.687  1.00197.49           O  
ANISOU 3555  O4'   C B  26    25015  25685  24337    533   -477   -515       O  
ATOM   3556  C3'   C B  26       5.325   3.272  81.107  1.00197.42           C  
ANISOU 3556  C3'   C B  26    25203  25716  24091    478   -471   -705       C  
ATOM   3557  O3'   C B  26       4.127   4.046  80.970  1.00197.89           O  
ANISOU 3557  O3'   C B  26    25391  25887  23911    497   -523   -782       O  
ATOM   3558  C2'   C B  26       6.542   4.140  81.431  1.00197.18           C  
ANISOU 3558  C2'   C B  26    25174  25671  24075    484   -537   -682       C  
ATOM   3559  O2'   C B  26       6.235   5.233  82.281  1.00196.73           O  
ANISOU 3559  O2'   C B  26    25180  25731  23838    561   -712   -658       O  
ATOM   3560  C1'   C B  26       7.458   3.145  82.157  1.00197.47           C  
ANISOU 3560  C1'   C B  26    25080  25644  24307    501   -507   -586       C  
ATOM   3561  N1    C B  26       8.534   2.519  81.264  1.00197.64           N  
ANISOU 3561  N1    C B  26    25059  25547  24486    432   -399   -612       N  
ATOM   3562  C2    C B  26       9.663   3.283  80.861  1.00197.71           C  
ANISOU 3562  C2    C B  26    25075  25498  24546    410   -399   -616       C  
ATOM   3563  O2    C B  26       9.773   4.465  81.225  1.00197.57           O  
ANISOU 3563  O2    C B  26    25091  25496  24481    432   -505   -615       O  
ATOM   3564  N3    C B  26      10.608   2.692  80.073  1.00197.99           N  
ANISOU 3564  N3    C B  26    25072  25468  24689    383   -309   -601       N  
ATOM   3565  C4    C B  26      10.471   1.412  79.695  1.00198.03           C  
ANISOU 3565  C4    C B  26    25049  25465  24730    388   -260   -607       C  
ATOM   3566  N4    C B  26      11.426   0.883  78.924  1.00198.27           N  
ANISOU 3566  N4    C B  26    25055  25465  24814    403   -216   -581       N  
ATOM   3567  C5    C B  26       9.343   0.621  80.092  1.00197.93           C  
ANISOU 3567  C5    C B  26    25020  25479  24706    395   -281   -619       C  
ATOM   3568  C6    C B  26       8.413   1.205  80.868  1.00197.76           C  
ANISOU 3568  C6    C B  26    25021  25521  24598    412   -330   -608       C  
ATOM   3569  P     A B  27       3.371   4.132  79.554  1.00198.50           P  
ANISOU 3569  P     A B  27    25586  25908  23926    483   -424   -984       P  
ATOM   3570  OP1   A B  27       2.064   4.796  79.777  1.00197.60           O  
ANISOU 3570  OP1   A B  27    25606  25941  23531    501   -492  -1051       O  
ATOM   3571  OP2   A B  27       3.411   2.791  78.923  1.00199.19           O  
ANISOU 3571  OP2   A B  27    25566  25843  24273    497   -338   -992       O  
ATOM   3572  O5'   A B  27       4.319   5.107  78.696  1.00199.32           O  
ANISOU 3572  O5'   A B  27    25769  25968  23995    478   -379  -1081       O  
ATOM   3573  C5'   A B  27       4.374   6.513  78.988  1.00199.65           C  
ANISOU 3573  C5'   A B  27    25925  26118  23814    465   -485  -1114       C  
ATOM   3574  C4'   A B  27       5.643   7.150  78.433  1.00201.08           C  
ANISOU 3574  C4'   A B  27    26073  26211  24116    451   -449  -1091       C  
ATOM   3575  O4'   A B  27       6.799   6.374  78.839  1.00202.43           O  
ANISOU 3575  O4'   A B  27    26075  26286  24552    435   -436   -938       O  
ATOM   3576  C3'   A B  27       5.722   7.238  76.914  1.00201.58           C  
ANISOU 3576  C3'   A B  27    26191  26189  24210    510   -260  -1219       C  
ATOM   3577  O3'   A B  27       5.127   8.459  76.463  1.00201.24           O  
ANISOU 3577  O3'   A B  27    26320  26224  23917    523   -265  -1373       O  
ATOM   3578  C2'   A B  27       7.230   7.211  76.656  1.00202.63           C  
ANISOU 3578  C2'   A B  27    26181  26220  24588    509   -212  -1067       C  
ATOM   3579  O2'   A B  27       7.831   8.492  76.746  1.00202.79           O  
ANISOU 3579  O2'   A B  27    26208  26246  24599    470   -284  -1018       O  
ATOM   3580  C1'   A B  27       7.739   6.302  77.777  1.00203.17           C  
ANISOU 3580  C1'   A B  27    26119  26273  24803    452   -301   -926       C  
ATOM   3581  N9    A B  27       7.900   4.898  77.376  1.00203.61           N  
ANISOU 3581  N9    A B  27    26095  26262  25003    492   -208   -905       N  
ATOM   3582  C8    A B  27       7.049   3.858  77.649  1.00203.48           C  
ANISOU 3582  C8    A B  27    26066  26253  24996    500   -221   -934       C  
ATOM   3583  N7    A B  27       7.443   2.704  77.168  1.00203.95           N  
ANISOU 3583  N7    A B  27    26047  26238  25207    549   -180   -909       N  
ATOM   3584  C5    A B  27       8.637   2.998  76.535  1.00204.32           C  
ANISOU 3584  C5    A B  27    26065  26252  25315    588   -122   -850       C  
ATOM   3585  C6    A B  27       9.562   2.195  75.831  1.00204.79           C  
ANISOU 3585  C6    A B  27    26057  26271  25483    677    -88   -784       C  
ATOM   3586  N6    A B  27       9.387   0.886  75.630  1.00204.90           N  
ANISOU 3586  N6    A B  27    26030  26256  25565    741   -139   -796       N  
ATOM   3587  N1    A B  27      10.658   2.803  75.307  1.00205.21           N  
ANISOU 3587  N1    A B  27    26080  26322  25570    717    -24   -688       N  
ATOM   3588  C2    A B  27      10.820   4.124  75.498  1.00205.22           C  
ANISOU 3588  C2    A B  27    26101  26328  25546    652     -6   -667       C  
ATOM   3589  N3    A B  27      10.026   4.980  76.154  1.00204.69           N  
ANISOU 3589  N3    A B  27    26107  26293  25374    565    -71   -745       N  
ATOM   3590  C4    A B  27       8.940   4.347  76.654  1.00204.22           C  
ANISOU 3590  C4    A B  27    26092  26266  25234    544   -123   -835       C  
ATOM   3591  P     G B  28       4.182   8.479  75.165  1.00200.86           P  
ANISOU 3591  P     G B  28    26436  26161  23719    646    -89  -1635       P  
ATOM   3592  OP1   G B  28       3.490   9.790  75.132  1.00199.51           O  
ANISOU 3592  OP1   G B  28    26473  26124  23207    617   -150  -1798       O  
ATOM   3593  OP2   G B  28       3.383   7.231  75.153  1.00200.90           O  
ANISOU 3593  OP2   G B  28    26414  26119  23800    692    -63  -1687       O  
ATOM   3594  O5'   G B  28       5.229   8.399  73.950  1.00202.16           O  
ANISOU 3594  O5'   G B  28    26521  26195  24095    792    104  -1603       O  
ATOM   3595  C5'   G B  28       6.003   9.548  73.570  1.00202.91           C  
ANISOU 3595  C5'   G B  28    26615  26293  24190    795    146  -1544       C  
ATOM   3596  C4'   G B  28       7.229   9.145  72.760  1.00204.79           C  
ANISOU 3596  C4'   G B  28    26686  26422  24705    930    293  -1371       C  
ATOM   3597  O4'   G B  28       7.955   8.111  73.468  1.00206.10           O  
ANISOU 3597  O4'   G B  28    26685  26546  25077    847    202  -1181       O  
ATOM   3598  C3'   G B  28       6.936   8.570  71.378  1.00204.78           C  
ANISOU 3598  C3'   G B  28    26727  26360  24721   1236    497  -1507       C  
ATOM   3599  O3'   G B  28       6.901   9.616  70.409  1.00204.34           O  
ANISOU 3599  O3'   G B  28    26764  26312  24563   1403    668  -1605       O  
ATOM   3600  C2'   G B  28       8.112   7.616  71.143  1.00206.40           C  
ANISOU 3600  C2'   G B  28    26733  26502  25188   1330    516  -1265       C  
ATOM   3601  O2'   G B  28       9.234   8.247  70.551  1.00207.41           O  
ANISOU 3601  O2'   G B  28    26752  26617  25438   1421    629  -1063       O  
ATOM   3602  C1'   G B  28       8.451   7.142  72.559  1.00206.98           C  
ANISOU 3602  C1'   G B  28    26713  26592  25339   1045    323  -1126       C  
ATOM   3603  N9    G B  28       7.879   5.833  72.893  1.00207.12           N  
ANISOU 3603  N9    G B  28    26722  26591  25384   1045    244  -1187       N  
ATOM   3604  C8    G B  28       6.663   5.583  73.492  1.00206.39           C  
ANISOU 3604  C8    G B  28    26716  26526  25176    955    159  -1331       C  
ATOM   3605  N7    G B  28       6.409   4.314  73.656  1.00206.75           N  
ANISOU 3605  N7    G B  28    26695  26525  25337    976     98  -1320       N  
ATOM   3606  C5    G B  28       7.514   3.673  73.109  1.00207.70           C  
ANISOU 3606  C5    G B  28    26703  26598  25614   1095    124  -1189       C  
ATOM   3607  C6    G B  28       7.798   2.283  72.977  1.00208.29           C  
ANISOU 3607  C6    G B  28    26685  26624  25833   1178     44  -1131       C  
ATOM   3608  O6    G B  28       7.113   1.321  73.354  1.00208.25           O  
ANISOU 3608  O6    G B  28    26651  26578  25895   1143    -59  -1175       O  
ATOM   3609  N1    G B  28       9.037   2.060  72.365  1.00209.02           N  
ANISOU 3609  N1    G B  28    26701  26726  25990   1314     74   -985       N  
ATOM   3610  C2    G B  28       9.887   3.052  71.918  1.00209.35           C  
ANISOU 3610  C2    G B  28    26730  26802  26012   1367    195   -878       C  
ATOM   3611  N2    G B  28      11.030   2.645  71.346  1.00210.11           N  
ANISOU 3611  N2    G B  28    26737  26923  26171   1523    210   -704       N  
ATOM   3612  N3    G B  28       9.630   4.357  72.025  1.00208.97           N  
ANISOU 3612  N3    G B  28    26745  26769  25884   1281    278   -922       N  
ATOM   3613  C4    G B  28       8.428   4.594  72.629  1.00208.00           C  
ANISOU 3613  C4    G B  28    26726  26656  25648   1147    225  -1094       C  
TER    3614        G B  28                                                      
HETATM 3615  C   ACT A 501      27.203 -14.240 101.083  1.00 54.29           C  
HETATM 3616  O   ACT A 501      26.355 -13.384 100.711  1.00 53.01           O  
HETATM 3617  OXT ACT A 501      28.417 -14.248 100.760  1.00 54.97           O  
HETATM 3618  CH3 ACT A 501      26.724 -15.386 102.006  1.00 54.07           C  
HETATM 3619  O   HOH A 601      31.343 -11.577  78.495  1.00 33.40           O  
HETATM 3620  O   HOH A 602      38.997 -17.637  74.061  1.00 46.68           O  
HETATM 3621  O   HOH A 603      44.963 -26.348  95.186  1.00 53.53           O  
HETATM 3622  O   HOH A 604      19.688 -13.079 130.218  1.00 40.65           O  
HETATM 3623  O   HOH A 605      32.577  -8.033 111.088  1.00 13.72           O  
HETATM 3624  O   HOH A 606      20.955  -2.378 124.865  1.00 64.20           O  
HETATM 3625  O   HOH A 607      36.203 -18.978  61.808  1.00 17.07           O  
HETATM 3626  O   HOH A 608      49.519  -1.201  77.833  1.00 55.99           O  
HETATM 3627  O   HOH A 609      52.129  -3.244  81.954  1.00 51.75           O  
CONECT 1092 1540                                                                
CONECT 1540 1092                                                                
CONECT 3615 3616 3617 3618                                                      
CONECT 3616 3615                                                                
CONECT 3617 3615                                                                
CONECT 3618 3615                                                                
MASTER      421    0    1   17   17    0    2    6 3625    2    6   41          
END

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Related entries of code: 5hsw

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	5hsw
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	KSHV SOX
Ligand Name	31-mer K12-31 RNA
EC.Number	E.C.3.1.-.-
Resolution	3.3(Å)
Affinity (Kd/Ki/IC50)	Kd=48.9uM
Release Year	2017
Protein/NA Sequence	Check fasta file
Primary Reference	(2017) Nucleic Acids Res. Vol. 45: pp. 4756-4767

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P88925
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

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