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HEADER    DNA BINDING PROTEIN/DNA                 07-OCT-18   6IIR              
TITLE     COMPLEX STRUCTURE OF THE HRP3 PWWP DOMAIN WITH A 10-BP GC-RICH DNA    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOMA-DERIVED GROWTH FACTOR-RELATED PROTEIN 3;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HRP-3,HEPATOMA-DERIVED GROWTH FACTOR 2,HDGF-2;              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 10-BP GC-RICH DNA;                                         
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HDGFL3, HDGF2, HDGFRP3, CGI-142;                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    GROWTH FACTOR, PWWP DOMAIN, HEPATOMA-DERIVED GROWTH FACTOR-RELATED    
KEYWDS   2 PROTEIN 3, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.WANG,W.TIAN                                                         
REVDAT   1   24-APR-19 6IIR    0                                                
JRNL        AUTH   Z.WANG,W.TIAN                                                
JRNL        TITL   COMPLEX STRUCTURE OF THE HRP3 PWWP DOMAIN WITH A 10-BP       
JRNL        TITL 2 GC-RICH DNA                                                  
JRNL        REF    NUCLEIC ACIDS RES.                         2019              
JRNL        REFN                   ESSN 1362-4962                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.050                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12763                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 623                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.0612 -  3.4777    1.00     3051   153  0.1663 0.2222        
REMARK   3     2  3.4777 -  2.7611    1.00     3026   128  0.2365 0.2782        
REMARK   3     3  2.7611 -  2.4122    1.00     3009   181  0.2955 0.3426        
REMARK   3     4  2.4122 -  2.1918    0.99     3054   161  0.3095 0.3925        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           2144                                  
REMARK   3   ANGLE     :  1.166           2976                                  
REMARK   3   CHIRALITY :  0.056            285                                  
REMARK   3   PLANARITY :  0.007            321                                  
REMARK   3   DIHEDRAL  : 22.986            838                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  56.1630 -28.7894-229.7076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8744 T22:   0.4890                                     
REMARK   3      T33:   0.5522 T12:  -0.2441                                     
REMARK   3      T13:  -0.1441 T23:   0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5503 L22:  -0.0007                                     
REMARK   3      L33:   3.0860 L12:   0.0309                                     
REMARK   3      L13:  -2.6284 L23:   0.0329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2631 S12:  -0.3444 S13:  -0.1190                       
REMARK   3      S21:  -0.1149 S22:  -0.1146 S23:   0.0428                       
REMARK   3      S31:  -0.2816 S32:   0.2482 S33:  -0.1203                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6IIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300009273.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97853                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6IIP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.0, 0.1 M SODIUM         
REMARK 280  MALONATE, PH 8.0, AND 26% POLYETHYLENE GLYCOL 1000, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.97100            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      131.94200            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N2    DG C     5     O2    DC D     6              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A    99     O    VAL B    37     2525     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC D   8   O3'    DC D   8   C3'    -0.053                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DC D   4   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASN A  91       55.91   -154.91                                   
REMARK 500    ASN B  42       28.79     48.19                                   
REMARK 500    ASN B  91       49.35   -142.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   33     GLU A   34                  149.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6IIP   RELATED DB: PDB                                   
REMARK 900 APO-FORM HRP3 PWWP                                                   
REMARK 900 RELATED ID: 6IIQ   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH A BOUND AT-RICH DNA                                   
REMARK 900 RELATED ID: 6IIS   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH BOTH A BOUND DNA AND THE H3K36ME3 PEPTIDE             
REMARK 900 RELATED ID: 6IIT   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH BOTH A BOUND DNA AND THE H3K36ME2 PEPTIDE             
DBREF  6IIR A    1    99  UNP    Q9Y3E1   HDGR3_HUMAN      1     99             
DBREF  6IIR B    1    99  UNP    Q9Y3E1   HDGR3_HUMAN      1     99             
DBREF  6IIR C    1    10  PDB    6IIR     6IIR             1     10             
DBREF  6IIR D    1    10  PDB    6IIR     6IIR             1     10             
SEQADV 6IIR SER A    0  UNP  Q9Y3E1              EXPRESSION TAG                 
SEQADV 6IIR SER B    0  UNP  Q9Y3E1              EXPRESSION TAG                 
SEQRES   1 A  100  SER MET ALA ARG PRO ARG PRO ARG GLU TYR LYS ALA GLY          
SEQRES   2 A  100  ASP LEU VAL PHE ALA LYS MET LYS GLY TYR PRO HIS TRP          
SEQRES   3 A  100  PRO ALA ARG ILE ASP GLU LEU PRO GLU GLY ALA VAL LYS          
SEQRES   4 A  100  PRO PRO ALA ASN LYS TYR PRO ILE PHE PHE PHE GLY THR          
SEQRES   5 A  100  HIS GLU THR ALA PHE LEU GLY PRO LYS ASP LEU PHE PRO          
SEQRES   6 A  100  TYR LYS GLU TYR LYS ASP LYS PHE GLY LYS SER ASN LYS          
SEQRES   7 A  100  ARG LYS GLY PHE ASN GLU GLY LEU TRP GLU ILE GLU ASN          
SEQRES   8 A  100  ASN PRO GLY VAL LYS PHE THR GLY TYR                          
SEQRES   1 B  100  SER MET ALA ARG PRO ARG PRO ARG GLU TYR LYS ALA GLY          
SEQRES   2 B  100  ASP LEU VAL PHE ALA LYS MET LYS GLY TYR PRO HIS TRP          
SEQRES   3 B  100  PRO ALA ARG ILE ASP GLU LEU PRO GLU GLY ALA VAL LYS          
SEQRES   4 B  100  PRO PRO ALA ASN LYS TYR PRO ILE PHE PHE PHE GLY THR          
SEQRES   5 B  100  HIS GLU THR ALA PHE LEU GLY PRO LYS ASP LEU PHE PRO          
SEQRES   6 B  100  TYR LYS GLU TYR LYS ASP LYS PHE GLY LYS SER ASN LYS          
SEQRES   7 B  100  ARG LYS GLY PHE ASN GLU GLY LEU TRP GLU ILE GLU ASN          
SEQRES   8 B  100  ASN PRO GLY VAL LYS PHE THR GLY TYR                          
SEQRES   1 C   10   DG  DC  DG  DC  DG  DC  DG  DC  DG  DC                      
SEQRES   1 D   10   DG  DC  DG  DC  DG  DC  DG  DC  DG  DC                      
FORMUL   5  HOH   *5(H2 O)                                                      
HELIX    1 AA1 GLY A   58  LYS A   60  5                                   3    
HELIX    2 AA2 TYR A   65  GLY A   73  1                                   9    
HELIX    3 AA3 GLY A   80  ASN A   91  1                                  12    
HELIX    4 AA4 GLY B   58  LYS B   60  5                                   3    
HELIX    5 AA5 TYR B   65  GLY B   73  1                                   9    
HELIX    6 AA6 GLY B   80  ASN B   91  1                                  12    
SHEET    1 AA1 5 THR A  54  LEU A  57  0                                        
SHEET    2 AA1 5 TYR A  44  PHE A  48 -1  N  ILE A  46   O  ALA A  55           
SHEET    3 AA1 5 TRP A  25  ILE A  29 -1  N  ARG A  28   O  PHE A  47           
SHEET    4 AA1 5 LEU A  14  ALA A  17 -1  N  ALA A  17   O  TRP A  25           
SHEET    5 AA1 5 LEU A  62  PRO A  64 -1  O  PHE A  63   N  PHE A  16           
SHEET    1 AA2 5 THR B  54  LEU B  57  0                                        
SHEET    2 AA2 5 TYR B  44  PHE B  48 -1  N  ILE B  46   O  ALA B  55           
SHEET    3 AA2 5 TRP B  25  ILE B  29 -1  N  ARG B  28   O  PHE B  47           
SHEET    4 AA2 5 LEU B  14  ALA B  17 -1  N  VAL B  15   O  ALA B  27           
SHEET    5 AA2 5 LEU B  62  PRO B  64 -1  O  PHE B  63   N  PHE B  16           
CRYST1   33.554   33.554  197.913  90.00  90.00 120.00 P 31          6          
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      0.029803  0.017207  0.000000        0.00000                         
SCALE2      0.000000  0.034413  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005053        0.00000                         
ATOM      1  N   ALA A   2      47.681  -6.109-217.860  1.00 85.53           N  
ANISOU    1  N   ALA A   2    15915   6991   9592  -3857   4036   -997       N  
ATOM      2  CA  ALA A   2      47.335  -7.517-217.648  1.00 91.29           C  
ANISOU    2  CA  ALA A   2    16425   7942  10319  -3868   3527   -841       C  
ATOM      3  C   ALA A   2      47.096  -7.821-216.173  1.00106.35           C  
ANISOU    3  C   ALA A   2    18149  10091  12166  -4135   3416   -979       C  
ATOM      4  O   ALA A   2      48.046  -7.914-215.399  1.00116.87           O  
ANISOU    4  O   ALA A   2    19308  11710  13385  -4468   3380  -1227       O  
ATOM      5  CB  ALA A   2      48.436  -8.422-218.197  1.00 81.28           C  
ANISOU    5  CB  ALA A   2    14995   6887   9000  -3985   3207   -866       C  
ATOM      6  N   ARG A   3      45.833  -7.981-215.787  1.00115.21           N  
ANISOU    6  N   ARG A   3    19299  11129  13348  -3979   3363   -809       N  
ATOM      7  CA  ARG A   3      45.491  -8.286-214.401  1.00115.07           C  
ANISOU    7  CA  ARG A   3    19109  11332  13278  -4206   3251   -916       C  
ATOM      8  C   ARG A   3      46.212  -9.527-213.904  1.00109.82           C  
ANISOU    8  C   ARG A   3    18135  11068  12525  -4448   2817   -973       C  
ATOM      9  O   ARG A   3      46.008 -10.618-214.425  1.00117.88           O  
ANISOU    9  O   ARG A   3    19018  12199  13572  -4263   2426   -769       O  
ATOM     10  CB  ARG A   3      43.980  -8.470-214.232  1.00116.48           C  
ANISOU   10  CB  ARG A   3    19354  11366  13537  -3965   3195   -672       C  
ATOM     11  CG  ARG A   3      43.598  -9.315-213.027  1.00117.58           C  
ANISOU   11  CG  ARG A   3    19221  11829  13625  -4114   2873   -699       C  
ATOM     12  CD  ARG A   3      42.336  -8.799-212.372  1.00120.12           C  
ANISOU   12  CD  ARG A   3    19639  12009  13993  -3998   3051   -630       C  
ATOM     13  NE  ARG A   3      42.421  -8.940-210.923  1.00129.46           N  
ANISOU   13  NE  ARG A   3    20658  13429  15102  -4344   3012   -827       N  
ATOM     14  CZ  ARG A   3      41.578  -8.390-210.052  1.00131.27           C  
ANISOU   14  CZ  ARG A   3    20956  13572  15348  -4377   3215   -862       C  
ATOM     15  NH1 ARG A   3      40.566  -7.642-210.472  1.00131.24           N  
ANISOU   15  NH1 ARG A   3    21196  13232  15436  -4080   3494   -701       N  
ATOM     16  NH2 ARG A   3      41.754  -8.586-208.751  1.00127.31           N  
ANISOU   16  NH2 ARG A   3    20251  13363  14757  -4668   3134  -1051       N  
ATOM     17  N   PRO A   4      47.063  -9.363-212.887  1.00107.40           N  
ANISOU   17  N   PRO A   4    17658  11058  12090  -4782   2869  -1246       N  
ATOM     18  CA  PRO A   4      47.835 -10.493-212.382  1.00100.33           C  
ANISOU   18  CA  PRO A   4    16447  10589  11086  -4987   2489  -1288       C  
ATOM     19  C   PRO A   4      46.970 -11.619-211.832  1.00 93.23           C  
ANISOU   19  C   PRO A   4    15373   9837  10215  -4931   2115  -1100       C  
ATOM     20  O   PRO A   4      45.866 -11.408-211.324  1.00 84.03           O  
ANISOU   20  O   PRO A   4    14258   8567   9102  -4826   2169  -1029       O  
ATOM     21  CB  PRO A   4      48.674  -9.870-211.261  1.00 96.65           C  
ANISOU   21  CB  PRO A   4    15857  10414  10454  -5323   2701  -1607       C  
ATOM     22  CG  PRO A   4      47.896  -8.673-210.832  1.00100.19           C  
ANISOU   22  CG  PRO A   4    16524  10597  10947  -5301   3105  -1702       C  
ATOM     23  CD  PRO A   4      47.336  -8.135-212.118  1.00106.77           C  
ANISOU   23  CD  PRO A   4    17664  10965  11940  -4978   3294  -1524       C  
ATOM     24  N   ARG A   5      47.493 -12.827-211.968  1.00 90.16           N  
ANISOU   24  N   ARG A   5    14727   9748   9782  -4887   1717  -1003       N  
ATOM     25  CA  ARG A   5      46.985 -13.964-211.241  1.00 86.55           C  
ANISOU   25  CA  ARG A   5    14003   9574   9308  -4811   1349   -865       C  
ATOM     26  C   ARG A   5      47.385 -13.780-209.803  1.00 86.17           C  
ANISOU   26  C   ARG A   5    13788   9837   9114  -5180   1428  -1077       C  
ATOM     27  O   ARG A   5      48.452 -13.237-209.532  1.00 88.22           O  
ANISOU   27  O   ARG A   5    14015  10256   9249  -5452   1618  -1308       O  
ATOM     28  CB  ARG A   5      47.554 -15.255-211.793  1.00 83.71           C  
ANISOU   28  CB  ARG A   5    13437   9427   8942  -4676    970   -713       C  
ATOM     29  CG  ARG A   5      46.766 -15.777-212.940  1.00 86.35           C  
ANISOU   29  CG  ARG A   5    13854   9539   9417  -4288    794   -468       C  
ATOM     30  CD  ARG A   5      47.214 -17.156-213.269  1.00 86.45           C  
ANISOU   30  CD  ARG A   5    13647   9773   9429  -4181    429   -328       C  
ATOM     31  NE  ARG A   5      48.488 -17.171-213.974  1.00 89.17           N  
ANISOU   31  NE  ARG A   5    13991  10164   9724  -4265    446   -399       N  
ATOM     32  CZ  ARG A   5      49.498 -17.984-213.683  1.00 91.26           C  
ANISOU   32  CZ  ARG A   5    14031  10746   9898  -4382    265   -410       C  
ATOM     33  NH1 ARG A   5      49.391 -18.852-212.683  1.00 87.22           N  
ANISOU   33  NH1 ARG A   5    13275  10530   9334  -4421     64   -344       N  
ATOM     34  NH2 ARG A   5      50.615 -17.929-214.400  1.00 90.98           N  
ANISOU   34  NH2 ARG A   5    14010  10738   9820  -4443    296   -472       N  
ATOM     35  N   PRO A   6      46.547 -14.245-208.873  1.00 79.61           N  
ANISOU   35  N   PRO A   6    12817   9147   8283  -5144   1274   -996       N  
ATOM     36  CA  PRO A   6      46.786 -14.010-207.450  1.00 81.12           C  
ANISOU   36  CA  PRO A   6    12848   9645   8329  -5486   1364  -1194       C  
ATOM     37  C   PRO A   6      48.120 -14.611-207.008  1.00 96.34           C  
ANISOU   37  C   PRO A   6    14479  12056  10071  -5686   1210  -1285       C  
ATOM     38  O   PRO A   6      48.677 -15.452-207.720  1.00112.64           O  
ANISOU   38  O   PRO A   6    16452  14198  12147  -5571    973  -1150       O  
ATOM     39  CB  PRO A   6      45.600 -14.718-206.775  1.00 80.64           C  
ANISOU   39  CB  PRO A   6    12666   9650   8324  -5303   1130  -1007       C  
ATOM     40  CG  PRO A   6      44.584 -14.866-207.849  1.00 66.02           C  
ANISOU   40  CG  PRO A   6    10996   7434   6653  -4907   1054   -775       C  
ATOM     41  CD  PRO A   6      45.379 -15.110-209.087  1.00 65.35           C  
ANISOU   41  CD  PRO A   6    10963   7271   6596  -4797    989   -722       C  
ATOM     42  N   ARG A   7      48.617 -14.179-205.853  1.00 89.51           N  
ANISOU   42  N   ARG A   7    13451  11535   9024  -5920   1352  -1494       N  
ATOM     43  CA  ARG A   7      49.882 -14.667-205.312  1.00 89.99           C  
ANISOU   43  CA  ARG A   7    13205  12122   8865  -6093   1240  -1575       C  
ATOM     44  C   ARG A   7      49.644 -15.464-204.032  1.00 97.56           C  
ANISOU   44  C   ARG A   7    13854  13508   9706  -6147   1022  -1499       C  
ATOM     45  O   ARG A   7      50.542 -16.126-203.505  1.00103.18           O  
ANISOU   45  O   ARG A   7    14265  14707  10233  -6232    871  -1484       O  
ATOM     46  CB  ARG A   7      50.845 -13.500-205.050  1.00 84.43           C  
ANISOU   46  CB  ARG A   7    12543  11544   7993  -6333   1607  -1892       C  
ATOM     47  CG  ARG A   7      52.059 -13.541-205.956  1.00 88.07           C  
ANISOU   47  CG  ARG A   7    12999  12065   8400  -6360   1616  -1934       C  
ATOM     48  CD  ARG A   7      52.674 -12.178-206.185  1.00 89.57           C  
ANISOU   48  CD  ARG A   7    13386  12124   8523  -6525   2044  -2221       C  
ATOM     49  NE  ARG A   7      53.679 -12.265-207.243  1.00 89.08           N  
ANISOU   49  NE  ARG A   7    13356  12036   8453  -6504   2031  -2221       N  
ATOM     50  CZ  ARG A   7      54.939 -12.625-207.043  1.00 94.67           C  
ANISOU   50  CZ  ARG A   7    13815  13203   8953  -6658   1959  -2297       C  
ATOM     51  NH1 ARG A   7      55.362 -12.896-205.812  1.00103.91           N  
ANISOU   51  NH1 ARG A   7    14681  14911   9890  -6839   1909  -2378       N  
ATOM     52  NH2 ARG A   7      55.777 -12.692-208.069  1.00 94.91           N  
ANISOU   52  NH2 ARG A   7    13895  13171   8996  -6625   1949  -2287       N  
ATOM     53  N   GLU A   8      48.424 -15.384-203.526  1.00 90.52           N  
ANISOU   53  N   GLU A   8    13035  12444   8915  -6082   1021  -1438       N  
ATOM     54  CA  GLU A   8      48.022 -16.211-202.405  1.00 91.02           C  
ANISOU   54  CA  GLU A   8    12829  12854   8902  -6088    795  -1324       C  
ATOM     55  C   GLU A   8      46.588 -16.661-202.598  1.00 88.42           C  
ANISOU   55  C   GLU A   8    12619  12193   8783  -5888    638  -1111       C  
ATOM     56  O   GLU A   8      45.763 -15.929-203.153  1.00 79.81           O  
ANISOU   56  O   GLU A   8    11824  10651   7850  -5807    815  -1128       O  
ATOM     57  CB  GLU A   8      48.195 -15.465-201.087  1.00 94.75           C  
ANISOU   57  CB  GLU A   8    13189  13633   9178  -6316   1020  -1560       C  
ATOM     58  CG  GLU A   8      49.613 -15.572-200.552  1.00105.00           C  
ANISOU   58  CG  GLU A   8    14213  15484  10199  -6501   1040  -1688       C  
ATOM     59  CD  GLU A   8      49.844 -14.751-199.305  1.00118.69           C  
ANISOU   59  CD  GLU A   8    15853  17535  11711  -6747   1297  -1952       C  
ATOM     60  OE1 GLU A   8      49.114 -13.760-199.096  1.00119.30           O  
ANISOU   60  OE1 GLU A   8    16159  17307  11861  -6808   1559  -2110       O  
ATOM     61  OE2 GLU A   8      50.764 -15.096-198.531  1.00128.22           O  
ANISOU   61  OE2 GLU A   8    16754  19307  12656  -6875   1248  -1997       O  
ATOM     62  N   TYR A   9      46.312 -17.888-202.168  1.00 83.92           N  
ANISOU   62  N   TYR A   9    11817  11858   8210  -5737    319   -882       N  
ATOM     63  CA  TYR A   9      44.988 -18.466-202.289  1.00 79.33           C  
ANISOU   63  CA  TYR A   9    11304  11028   7811  -5429    149   -651       C  
ATOM     64  C   TYR A   9      44.499 -18.846-200.895  1.00 80.44           C  
ANISOU   64  C   TYR A   9    11224  11478   7860  -5513     61   -622       C  
ATOM     65  O   TYR A   9      45.260 -18.766-199.934  1.00 82.57           O  
ANISOU   65  O   TYR A   9    11270  12183   7921  -5780    103   -755       O  
ATOM     66  CB  TYR A   9      45.014 -19.677-203.227  1.00 82.97           C  
ANISOU   66  CB  TYR A   9    11724  11412   8390  -5106   -136   -383       C  
ATOM     67  CG  TYR A   9      45.194 -19.301-204.681  1.00 89.91           C  
ANISOU   67  CG  TYR A   9    12847  11927   9388  -4972    -60   -384       C  
ATOM     68  CD1 TYR A   9      44.106 -18.944-205.471  1.00 88.55           C  
ANISOU   68  CD1 TYR A   9    12923  11332   9390  -4752     -9   -312       C  
ATOM     69  CD2 TYR A   9      46.455 -19.284-205.263  1.00 88.27           C  
ANISOU   69  CD2 TYR A   9    12610  11826   9102  -5060    -35   -454       C  
ATOM     70  CE1 TYR A   9      44.273 -18.587-206.805  1.00 84.72           C  
ANISOU   70  CE1 TYR A   9    12648  10545   8996  -4615     67   -300       C  
ATOM     71  CE2 TYR A   9      46.631 -18.925-206.593  1.00 91.75           C  
ANISOU   71  CE2 TYR A   9    13274  11940   9648  -4937     40   -454       C  
ATOM     72  CZ  TYR A   9      45.540 -18.581-207.359  1.00 90.67           C  
ANISOU   72  CZ  TYR A   9    13379  11391   9682  -4712     90   -374       C  
ATOM     73  OH  TYR A   9      45.733 -18.232-208.680  1.00 97.60           O  
ANISOU   73  OH  TYR A   9    14460  11979  10645  -4578    167   -360       O  
ATOM     74  N   LYS A  10      43.234 -19.237-200.781  1.00 77.34           N  
ANISOU   74  N   LYS A  10    10884  10891   7611  -5294    -55   -456       N  
ATOM     75  CA  LYS A  10      42.693 -19.676-199.502  1.00 75.32           C  
ANISOU   75  CA  LYS A  10    10426  10907   7287  -5341   -153   -402       C  
ATOM     76  C   LYS A  10      41.898 -20.964-199.672  1.00 80.72           C  
ANISOU   76  C   LYS A  10    11037  11527   8108  -5019   -440   -104       C  
ATOM     77  O   LYS A  10      41.381 -21.270-200.759  1.00 71.50           O  
ANISOU   77  O   LYS A  10    10031  10024   7113  -4768   -520     24       O  
ATOM     78  CB  LYS A  10      41.790 -18.616-198.887  1.00 84.59           C  
ANISOU   78  CB  LYS A  10    11750  11913   8479  -5477     74   -563       C  
ATOM     79  CG  LYS A  10      40.538 -18.440-199.687  1.00 87.69           C  
ANISOU   79  CG  LYS A  10    12401  11831   9088  -5199     83   -443       C  
ATOM     80  CD  LYS A  10      39.612 -17.400-199.134  1.00102.70           C  
ANISOU   80  CD  LYS A  10    14462  13543  11016  -5291    325   -572       C  
ATOM     81  CE  LYS A  10      38.443 -17.268-200.078  1.00103.03           C  
ANISOU   81  CE  LYS A  10    14740  13156  11252  -4972    326   -420       C  
ATOM     82  NZ  LYS A  10      38.956 -16.826-201.408  1.00111.49           N  
ANISOU   82  NZ  LYS A  10    16014  13962  12385  -4879    441   -436       N  
ATOM     83  N   ALA A  11      41.803 -21.713-198.581  1.00 84.20           N  
ANISOU   83  N   ALA A  11    11227  12306   8461  -5038   -578     -4       N  
ATOM     84  CA  ALA A  11      41.059 -22.958-198.569  1.00 73.92           C  
ANISOU   84  CA  ALA A  11     9843  10964   7279  -4768   -813    264       C  
ATOM     85  C   ALA A  11      39.704 -22.771-199.248  1.00 70.72           C  
ANISOU   85  C   ALA A  11     9677  10114   7079  -4575   -815    314       C  
ATOM     86  O   ALA A  11      38.961 -21.833-198.943  1.00 65.31           O  
ANISOU   86  O   ALA A  11     9126   9280   6409  -4655   -662    189       O  
ATOM     87  CB  ALA A  11      40.891 -23.451-197.144  1.00 82.67           C  
ANISOU   87  CB  ALA A  11    10695  12450   8266  -4843   -886    329       C  
ATOM     88  N   GLY A  12      39.420 -23.631-200.218  1.00 71.38           N  
ANISOU   88  N   GLY A  12     9815   9998   7309  -4323   -968    487       N  
ATOM     89  CA  GLY A  12      38.114 -23.651-200.840  1.00 70.23           C  
ANISOU   89  CA  GLY A  12     9838   9519   7329  -4126  -1003    557       C  
ATOM     90  C   GLY A  12      38.024 -23.037-202.218  1.00 80.46           C  
ANISOU   90  C   GLY A  12    11370  10487   8715  -4017   -918    510       C  
ATOM     91  O   GLY A  12      37.053 -23.301-202.936  1.00 69.57           O  
ANISOU   91  O   GLY A  12    10088   8888   7459  -3813   -987    603       O  
ATOM     92  N   ASP A  13      39.009 -22.217-202.591  1.00 68.72           N  
ANISOU   92  N   ASP A  13     9966   8989   7156  -4153   -760    365       N  
ATOM     93  CA  ASP A  13      38.990 -21.578-203.900  1.00 71.55           C  
ANISOU   93  CA  ASP A  13    10554   9040   7591  -4043   -654    329       C  
ATOM     94  C   ASP A  13      39.022 -22.626-205.001  1.00 73.90           C  
ANISOU   94  C   ASP A  13    10838   9252   7990  -3820   -851    488       C  
ATOM     95  O   ASP A  13      39.689 -23.648-204.866  1.00 76.86           O  
ANISOU   95  O   ASP A  13    11045   9812   8346  -3817  -1002    575       O  
ATOM     96  CB  ASP A  13      40.170 -20.620-204.059  1.00 86.17           C  
ANISOU   96  CB  ASP A  13    12483  10915   9344  -4252   -443    141       C  
ATOM     97  CG  ASP A  13      39.974 -19.327-203.303  1.00 88.68           C  
ANISOU   97  CG  ASP A  13    12904  11196   9594  -4465   -165    -55       C  
ATOM     98  OD1 ASP A  13      38.821 -18.845-203.212  1.00 99.73           O  
ANISOU   98  OD1 ASP A  13    14433  12395  11067  -4366    -78    -34       O  
ATOM     99  OD2 ASP A  13      40.981 -18.804-202.789  1.00 91.23           O  
ANISOU   99  OD2 ASP A  13    13174  11709   9782  -4738    -20   -237       O  
ATOM    100  N   LEU A  14      38.300 -22.370-206.087  1.00 71.13           N  
ANISOU  100  N   LEU A  14    10657   8633   7737  -3629   -830    530       N  
ATOM    101  CA  LEU A  14      38.298 -23.273-207.228  1.00 78.36           C  
ANISOU  101  CA  LEU A  14    11569   9465   8739  -3438   -991    648       C  
ATOM    102  C   LEU A  14      39.243 -22.713-208.271  1.00 81.16           C  
ANISOU  102  C   LEU A  14    12053   9706   9079  -3442   -887    579       C  
ATOM    103  O   LEU A  14      39.250 -21.510-208.548  1.00 79.01           O  
ANISOU  103  O   LEU A  14    11954   9282   8783  -3474   -674    479       O  
ATOM    104  CB  LEU A  14      36.881 -23.457-207.790  1.00 75.73           C  
ANISOU  104  CB  LEU A  14    11299   8981   8494  -3226  -1054    738       C  
ATOM    105  CG  LEU A  14      35.847 -23.885-206.733  1.00 70.16           C  
ANISOU  105  CG  LEU A  14    10482   8374   7802  -3231  -1133    791       C  
ATOM    106  CD1 LEU A  14      34.414 -23.975-207.281  1.00 60.92           C  
ANISOU  106  CD1 LEU A  14     9361   7093   6693  -3035  -1180    862       C  
ATOM    107  CD2 LEU A  14      36.257 -25.195-206.071  1.00 67.34           C  
ANISOU  107  CD2 LEU A  14     9924   8209   7454  -3284  -1302    872       C  
ATOM    108  N   VAL A  15      40.079 -23.587-208.815  1.00 84.93           N  
ANISOU  108  N   VAL A  15    12448  10249   9571  -3411  -1016    635       N  
ATOM    109  CA  VAL A  15      41.101 -23.175-209.769  1.00 55.11           C  
ANISOU  109  CA  VAL A  15     8769   6394   5774  -3427   -937    573       C  
ATOM    110  C   VAL A  15      41.303 -24.218-210.857  1.00 76.40           C  
ANISOU  110  C   VAL A  15    11438   9041   8551  -3264  -1102    681       C  
ATOM    111  O   VAL A  15      40.724 -25.331-210.817  1.00 61.79           O  
ANISOU  111  O   VAL A  15     9483   7225   6770  -3161  -1265    795       O  
ATOM    112  CB  VAL A  15      42.436 -22.961-209.097  1.00 57.70           C  
ANISOU  112  CB  VAL A  15     9003   6938   5982  -3655   -869    471       C  
ATOM    113  CG1 VAL A  15      42.377 -21.790-208.116  1.00 67.73           C  
ANISOU  113  CG1 VAL A  15    10318   8256   7159  -3866   -657    311       C  
ATOM    114  CG2 VAL A  15      42.848 -24.216-208.383  1.00 58.56           C  
ANISOU  114  CG2 VAL A  15     8874   7313   6064  -3670  -1051    583       C  
ATOM    115  N   PHE A  16      42.127 -23.852-211.834  1.00 56.45           N  
ANISOU  115  N   PHE A  16     9008   6425   6014  -3253  -1038    634       N  
ATOM    116  CA  PHE A  16      42.687 -24.829-212.744  1.00 56.13           C  
ANISOU  116  CA  PHE A  16     8922   6380   6026  -3154  -1174    710       C  
ATOM    117  C   PHE A  16      44.111 -24.992-212.298  1.00 62.25           C  
ANISOU  117  C   PHE A  16     9590   7348   6714  -3309  -1163    674       C  
ATOM    118  O   PHE A  16      44.800 -23.997-212.097  1.00 68.45           O  
ANISOU  118  O   PHE A  16    10432   8167   7407  -3464  -1007    544       O  
ATOM    119  CB  PHE A  16      42.612 -24.369-214.201  1.00 61.29           C  
ANISOU  119  CB  PHE A  16     9743   6826   6720  -3018  -1123    696       C  
ATOM    120  CG  PHE A  16      41.248 -24.471-214.795  1.00 62.66           C  
ANISOU  120  CG  PHE A  16     9967   6883   6957  -2831  -1170    761       C  
ATOM    121  CD1 PHE A  16      40.788 -25.679-215.301  1.00 70.52           C  
ANISOU  121  CD1 PHE A  16    10872   7896   8025  -2720  -1342    844       C  
ATOM    122  CD2 PHE A  16      40.421 -23.372-214.848  1.00 67.36           C  
ANISOU  122  CD2 PHE A  16    10696   7368   7532  -2768  -1023    737       C  
ATOM    123  CE1 PHE A  16      39.524 -25.781-215.863  1.00 59.09           C  
ANISOU  123  CE1 PHE A  16     9444   6399   6608  -2570  -1384    884       C  
ATOM    124  CE2 PHE A  16      39.151 -23.468-215.398  1.00 62.95           C  
ANISOU  124  CE2 PHE A  16    10155   6761   7003  -2581  -1069    810       C  
ATOM    125  CZ  PHE A  16      38.702 -24.676-215.902  1.00 62.37           C  
ANISOU  125  CZ  PHE A  16     9968   6749   6982  -2492  -1260    874       C  
ATOM    126  N   ALA A  17      44.565 -26.223-212.120  1.00 53.66           N  
ANISOU  126  N   ALA A  17     8343   6401   5645  -3272  -1305    785       N  
ATOM    127  CA  ALA A  17      45.958 -26.431-211.719  1.00 71.66           C  
ANISOU  127  CA  ALA A  17    10492   8917   7819  -3389  -1296    778       C  
ATOM    128  C   ALA A  17      46.768 -27.097-212.824  1.00 74.73           C  
ANISOU  128  C   ALA A  17    10892   9248   8255  -3287  -1358    837       C  
ATOM    129  O   ALA A  17      46.236 -27.892-213.621  1.00 70.89           O  
ANISOU  129  O   ALA A  17    10444   8596   7894  -3124  -1449    924       O  
ATOM    130  CB  ALA A  17      46.045 -27.259-210.426  1.00 66.47           C  
ANISOU  130  CB  ALA A  17     9613   8535   7107  -3426  -1371    885       C  
ATOM    131  N   LYS A  18      48.059 -26.769-212.850  1.00 75.52           N  
ANISOU  131  N   LYS A  18    10948   9503   8245  -3400  -1299    774       N  
ATOM    132  CA  LYS A  18      48.959 -27.213-213.897  1.00 68.86           C  
ANISOU  132  CA  LYS A  18    10123   8614   7426  -3325  -1334    808       C  
ATOM    133  C   LYS A  18      50.079 -28.112-213.374  1.00 74.83           C  
ANISOU  133  C   LYS A  18    10667   9666   8099  -3333  -1389    919       C  
ATOM    134  O   LYS A  18      50.813 -27.740-212.467  1.00 87.36           O  
ANISOU  134  O   LYS A  18    12115  11554   9522  -3489  -1335    870       O  
ATOM    135  CB  LYS A  18      49.556 -26.001-214.600  1.00 74.05           C  
ANISOU  135  CB  LYS A  18    10933   9176   8026  -3428  -1196    642       C  
ATOM    136  CG  LYS A  18      50.300 -26.326-215.873  1.00 72.64           C  
ANISOU  136  CG  LYS A  18    10816   8892   7893  -3334  -1228    664       C  
ATOM    137  CD  LYS A  18      49.375 -26.694-217.001  1.00 69.67           C  
ANISOU  137  CD  LYS A  18    10571   8231   7669  -3139  -1296    723       C  
ATOM    138  CE  LYS A  18      50.171 -27.292-218.141  1.00 69.49           C  
ANISOU  138  CE  LYS A  18    10565   8149   7689  -3047  -1349    763       C  
ATOM    139  NZ  LYS A  18      50.867 -28.531-217.652  1.00 73.44           N  
ANISOU  139  NZ  LYS A  18    10878   8843   8183  -3018  -1438    895       N  
ATOM    140  N   MET A  19      50.196 -29.302-213.949  1.00 75.37           N  
ANISOU  140  N   MET A  19    10703   9664   8272  -3161  -1479   1070       N  
ATOM    141  CA  MET A  19      51.329 -30.176-213.701  1.00 70.92           C  
ANISOU  141  CA  MET A  19     9964   9343   7642  -3115  -1505   1204       C  
ATOM    142  C   MET A  19      51.896 -30.611-215.041  1.00 86.93           C  
ANISOU  142  C   MET A  19    12082  11192   9754  -3005  -1524   1227       C  
ATOM    143  O   MET A  19      51.148 -30.740-216.009  1.00 91.97           O  
ANISOU  143  O   MET A  19    12876  11529  10538  -2915  -1551   1202       O  
ATOM    144  CB  MET A  19      50.909 -31.385-212.893  1.00 66.24           C  
ANISOU  144  CB  MET A  19     9229   8840   7101  -2993  -1557   1406       C  
ATOM    145  CG  MET A  19      50.026 -31.069-211.724  1.00 65.79           C  
ANISOU  145  CG  MET A  19     9114   8879   7005  -3071  -1555   1390       C  
ATOM    146  SD  MET A  19      50.859 -31.552-210.206  1.00 78.39           S  
ANISOU  146  SD  MET A  19    10406  10972   8407  -3098  -1543   1542       S  
ATOM    147  CE  MET A  19      51.015 -33.307-210.482  1.00107.57           C  
ANISOU  147  CE  MET A  19    14039  14593  12242  -2827  -1568   1828       C  
ATOM    148  N   LYS A  20      53.203 -30.836-215.116  1.00 84.90           N  
ANISOU  148  N   LYS A  20    11715  11145   9396  -3011  -1508   1273       N  
ATOM    149  CA  LYS A  20      53.794 -31.202-216.401  1.00 89.69           C  
ANISOU  149  CA  LYS A  20    12413  11587  10081  -2913  -1519   1286       C  
ATOM    150  C   LYS A  20      53.184 -32.506-216.882  1.00 87.31           C  
ANISOU  150  C   LYS A  20    12143  11063   9966  -2720  -1565   1435       C  
ATOM    151  O   LYS A  20      53.022 -33.445-216.107  1.00 80.26           O  
ANISOU  151  O   LYS A  20    11127  10269   9098  -2633  -1568   1601       O  
ATOM    152  CB  LYS A  20      55.320 -31.326-216.311  1.00 99.96           C  
ANISOU  152  CB  LYS A  20    13564  13187  11229  -2938  -1492   1332       C  
ATOM    153  CG  LYS A  20      56.106 -30.013-216.468  1.00 99.46           C  
ANISOU  153  CG  LYS A  20    13532  13249  11008  -3145  -1421   1125       C  
ATOM    154  CD  LYS A  20      55.332 -28.807-215.961  1.00103.33           C  
ANISOU  154  CD  LYS A  20    14115  13687  11460  -3322  -1357    943       C  
ATOM    155  CE  LYS A  20      55.972 -27.503-216.383  1.00113.50           C  
ANISOU  155  CE  LYS A  20    15507  14974  12644  -3517  -1238    720       C  
ATOM    156  NZ  LYS A  20      55.232 -26.354-215.796  1.00119.97           N  
ANISOU  156  NZ  LYS A  20    16421  15734  13429  -3687  -1131    552       N  
ATOM    157  N   GLY A  21      52.811 -32.544-218.156  1.00 95.74           N  
ANISOU  157  N   GLY A  21    13378  11836  11161  -2662  -1582   1367       N  
ATOM    158  CA  GLY A  21      52.256 -33.748-218.747  1.00103.31           C  
ANISOU  158  CA  GLY A  21    14379  12580  12294  -2519  -1601   1461       C  
ATOM    159  C   GLY A  21      50.740 -33.742-218.774  1.00107.65           C  
ANISOU  159  C   GLY A  21    15013  12943  12947  -2516  -1630   1405       C  
ATOM    160  O   GLY A  21      50.115 -34.506-219.509  1.00108.40           O  
ANISOU  160  O   GLY A  21    15172  12836  13177  -2442  -1638   1408       O  
ATOM    161  N   TYR A  22      50.148 -32.868-217.971  1.00 98.40           N  
ANISOU  161  N   TYR A  22    13833  11855  11701  -2609  -1636   1340       N  
ATOM    162  CA  TYR A  22      48.701 -32.792-217.870  1.00 78.48           C  
ANISOU  162  CA  TYR A  22    11369   9198   9252  -2604  -1664   1296       C  
ATOM    163  C   TYR A  22      48.230 -31.412-218.274  1.00 69.63           C  
ANISOU  163  C   TYR A  22    10373   8007   8074  -2668  -1649   1144       C  
ATOM    164  O   TYR A  22      48.911 -30.441-218.006  1.00 58.70           O  
ANISOU  164  O   TYR A  22     9000   6727   6577  -2763  -1597   1077       O  
ATOM    165  CB  TYR A  22      48.247 -33.085-216.451  1.00 71.08           C  
ANISOU  165  CB  TYR A  22    10309   8406   8290  -2630  -1664   1385       C  
ATOM    166  CG  TYR A  22      48.714 -34.403-215.884  1.00 72.77           C  
ANISOU  166  CG  TYR A  22    10393   8708   8547  -2543  -1642   1572       C  
ATOM    167  CD1 TYR A  22      50.024 -34.585-215.486  1.00 71.95           C  
ANISOU  167  CD1 TYR A  22    10168   8828   8341  -2528  -1610   1674       C  
ATOM    168  CD2 TYR A  22      47.831 -35.457-215.727  1.00 70.28           C  
ANISOU  168  CD2 TYR A  22    10072   8263   8366  -2470  -1631   1652       C  
ATOM    169  CE1 TYR A  22      50.443 -35.784-214.953  1.00 74.70           C  
ANISOU  169  CE1 TYR A  22    10396   9267   8721  -2408  -1563   1881       C  
ATOM    170  CE2 TYR A  22      48.246 -36.664-215.200  1.00 77.82           C  
ANISOU  170  CE2 TYR A  22    10928   9268   9372  -2369  -1566   1843       C  
ATOM    171  CZ  TYR A  22      49.554 -36.820-214.814  1.00 76.54           C  
ANISOU  171  CZ  TYR A  22    10648   9327   9107  -2322  -1530   1972       C  
ATOM    172  OH  TYR A  22      49.971 -38.016-214.276  1.00 80.96           O  
ANISOU  172  OH  TYR A  22    11105   9948   9707  -2183  -1440   2198       O  
ATOM    173  N   PRO A  23      47.054 -31.318-218.910  1.00 69.32           N  
ANISOU  173  N   PRO A  23    10426   7808   8107  -2614  -1674   1091       N  
ATOM    174  CA  PRO A  23      46.474 -30.011-219.241  1.00 68.44           C  
ANISOU  174  CA  PRO A  23    10434   7632   7940  -2631  -1633    984       C  
ATOM    175  C   PRO A  23      46.010 -29.292-217.993  1.00 65.05           C  
ANISOU  175  C   PRO A  23     9975   7297   7443  -2718  -1592    968       C  
ATOM    176  O   PRO A  23      45.805 -29.968-216.977  1.00 65.05           O  
ANISOU  176  O   PRO A  23     9857   7403   7457  -2743  -1628   1043       O  
ATOM    177  CB  PRO A  23      45.271 -30.371-220.120  1.00 73.25           C  
ANISOU  177  CB  PRO A  23    11089   8115   8625  -2528  -1682    967       C  
ATOM    178  CG  PRO A  23      44.850 -31.698-219.642  1.00 64.33           C  
ANISOU  178  CG  PRO A  23     9855   7002   7586  -2518  -1734   1042       C  
ATOM    179  CD  PRO A  23      46.136 -32.423-219.241  1.00 70.70           C  
ANISOU  179  CD  PRO A  23    10582   7879   8402  -2539  -1720   1130       C  
ATOM    180  N   HIS A  24      45.839 -27.973-218.061  1.00 59.01           N  
ANISOU  180  N   HIS A  24     9323   6488   6611  -2758  -1498    876       N  
ATOM    181  CA  HIS A  24      45.278 -27.231-216.934  1.00 63.42           C  
ANISOU  181  CA  HIS A  24     9874   7109   7113  -2844  -1433    843       C  
ATOM    182  C   HIS A  24      44.013 -27.930-216.400  1.00 61.73           C  
ANISOU  182  C   HIS A  24     9589   6902   6965  -2784  -1518    912       C  
ATOM    183  O   HIS A  24      43.017 -28.066-217.092  1.00 55.86           O  
ANISOU  183  O   HIS A  24     8893   6054   6275  -2673  -1555    919       O  
ATOM    184  CB  HIS A  24      44.959 -25.807-217.335  1.00 58.43           C  
ANISOU  184  CB  HIS A  24     9412   6352   6436  -2844  -1288    750       C  
ATOM    185  CG  HIS A  24      46.158 -25.025-217.763  1.00 70.74           C  
ANISOU  185  CG  HIS A  24    11056   7892   7929  -2931  -1169    663       C  
ATOM    186  ND1 HIS A  24      46.923 -25.381-218.854  1.00 85.59           N  
ANISOU  186  ND1 HIS A  24    12963   9725   9833  -2871  -1207    673       N  
ATOM    187  CD2 HIS A  24      46.728 -23.910-217.253  1.00 70.75           C  
ANISOU  187  CD2 HIS A  24    11123   7918   7841  -3090   -995    548       C  
ATOM    188  CE1 HIS A  24      47.908 -24.513-218.998  1.00 87.38           C  
ANISOU  188  CE1 HIS A  24    13266   9948   9986  -2981  -1073    576       C  
ATOM    189  NE2 HIS A  24      47.816 -23.609-218.039  1.00 74.02           N  
ANISOU  189  NE2 HIS A  24    11601   8298   8224  -3124   -933    491       N  
ATOM    190  N   TRP A  25      44.078 -28.359-215.147  1.00 60.50           N  
ANISOU  190  N   TRP A  25     9303   6896   6787  -2864  -1543    960       N  
ATOM    191  CA  TRP A  25      43.134 -29.321-214.616  1.00 58.16           C  
ANISOU  191  CA  TRP A  25     8915   6617   6564  -2814  -1626   1045       C  
ATOM    192  C   TRP A  25      42.257 -28.736-213.525  1.00 66.03           C  
ANISOU  192  C   TRP A  25     9893   7673   7521  -2873  -1596   1025       C  
ATOM    193  O   TRP A  25      42.769 -28.137-212.577  1.00 67.89           O  
ANISOU  193  O   TRP A  25    10086   8045   7663  -2998  -1532    990       O  
ATOM    194  CB  TRP A  25      43.911 -30.497-214.074  1.00 54.76           C  
ANISOU  194  CB  TRP A  25     8341   6311   6154  -2820  -1670   1157       C  
ATOM    195  CG  TRP A  25      43.144 -31.737-213.938  1.00 63.92           C  
ANISOU  195  CG  TRP A  25     9439   7423   7426  -2745  -1728   1250       C  
ATOM    196  CD1 TRP A  25      42.235 -32.032-212.983  1.00 70.82           C  
ANISOU  196  CD1 TRP A  25    10246   8343   8320  -2758  -1746   1294       C  
ATOM    197  CD2 TRP A  25      43.240 -32.887-214.779  1.00 54.22           C  
ANISOU  197  CD2 TRP A  25     8214   6079   6307  -2660  -1750   1300       C  
ATOM    198  NE1 TRP A  25      41.751 -33.301-213.171  1.00 63.47           N  
ANISOU  198  NE1 TRP A  25     9281   7328   7508  -2691  -1769   1366       N  
ATOM    199  CE2 TRP A  25      42.358 -33.846-214.271  1.00 61.11           C  
ANISOU  199  CE2 TRP A  25     9027   6924   7267  -2636  -1762   1365       C  
ATOM    200  CE3 TRP A  25      43.991 -33.191-215.919  1.00 64.21           C  
ANISOU  200  CE3 TRP A  25     9533   7257   7608  -2613  -1744   1286       C  
ATOM    201  CZ2 TRP A  25      42.201 -35.101-214.861  1.00 58.11           C  
ANISOU  201  CZ2 TRP A  25     8648   6418   7013  -2579  -1745   1404       C  
ATOM    202  CZ3 TRP A  25      43.842 -34.432-216.498  1.00 58.35           C  
ANISOU  202  CZ3 TRP A  25     8785   6399   6986  -2551  -1741   1329       C  
ATOM    203  CH2 TRP A  25      42.951 -35.369-215.972  1.00 62.47           C  
ANISOU  203  CH2 TRP A  25     9256   6882   7597  -2541  -1730   1381       C  
ATOM    204  N   PRO A  26      40.932 -28.934-213.638  1.00 57.74           N  
ANISOU  204  N   PRO A  26     8861   6546   6530  -2796  -1637   1037       N  
ATOM    205  CA  PRO A  26      39.987 -28.388-212.656  1.00 54.68           C  
ANISOU  205  CA  PRO A  26     8462   6203   6112  -2836  -1609   1023       C  
ATOM    206  C   PRO A  26      40.324 -28.871-211.263  1.00 55.27           C  
ANISOU  206  C   PRO A  26     8391   6453   6156  -2936  -1628   1081       C  
ATOM    207  O   PRO A  26      40.478 -30.065-211.053  1.00 65.67           O  
ANISOU  207  O   PRO A  26     9603   7818   7531  -2904  -1696   1180       O  
ATOM    208  CB  PRO A  26      38.643 -28.929-213.117  1.00 53.30           C  
ANISOU  208  CB  PRO A  26     8286   5957   6010  -2727  -1679   1048       C  
ATOM    209  CG  PRO A  26      38.998 -30.202-213.855  1.00 55.00           C  
ANISOU  209  CG  PRO A  26     8454   6135   6309  -2680  -1753   1091       C  
ATOM    210  CD  PRO A  26      40.277 -29.853-214.578  1.00 57.76           C  
ANISOU  210  CD  PRO A  26     8865   6454   6628  -2687  -1715   1065       C  
ATOM    211  N   ALA A  27      40.436 -27.945-210.322  1.00 57.63           N  
ANISOU  211  N   ALA A  27     8683   6852   6360  -3054  -1546   1021       N  
ATOM    212  CA  ALA A  27      41.009 -28.265-209.029  1.00 64.83           C  
ANISOU  212  CA  ALA A  27     9436   7996   7200  -3166  -1551   1065       C  
ATOM    213  C   ALA A  27      40.548 -27.333-207.906  1.00 65.86           C  
ANISOU  213  C   ALA A  27     9556   8222   7245  -3293  -1470    987       C  
ATOM    214  O   ALA A  27      39.802 -26.386-208.127  1.00 55.67           O  
ANISOU  214  O   ALA A  27     8401   6791   5961  -3288  -1389    903       O  
ATOM    215  CB  ALA A  27      42.528 -28.239-209.139  1.00 56.58           C  
ANISOU  215  CB  ALA A  27     8338   7090   6071  -3238  -1519   1053       C  
ATOM    216  N   ARG A  28      41.034 -27.590-206.696  1.00 76.09           N  
ANISOU  216  N   ARG A  28    10684   9775   8451  -3401  -1475   1021       N  
ATOM    217  CA  ARG A  28      40.593 -26.847-205.519  1.00 66.31           C  
ANISOU  217  CA  ARG A  28     9407   8660   7126  -3539  -1403    946       C  
ATOM    218  C   ARG A  28      41.719 -26.694-204.502  1.00 60.74           C  
ANISOU  218  C   ARG A  28     8530   8298   6252  -3718  -1356    911       C  
ATOM    219  O   ARG A  28      42.510 -27.622-204.318  1.00 64.06           O  
ANISOU  219  O   ARG A  28     8791   8914   6635  -3677  -1430   1035       O  
ATOM    220  CB  ARG A  28      39.393 -27.568-204.876  1.00 72.85           C  
ANISOU  220  CB  ARG A  28    10168   9481   8029  -3456  -1493   1053       C  
ATOM    221  CG  ARG A  28      38.948 -26.983-203.557  1.00 78.67           C  
ANISOU  221  CG  ARG A  28    10837  10377   8679  -3592  -1435    997       C  
ATOM    222  CD  ARG A  28      37.969 -27.894-202.858  1.00 73.00           C  
ANISOU  222  CD  ARG A  28    10017   9692   8026  -3511  -1535   1127       C  
ATOM    223  NE  ARG A  28      38.589 -29.078-202.261  1.00 63.76           N  
ANISOU  223  NE  ARG A  28     8655   8738   6835  -3477  -1610   1287       N  
ATOM    224  CZ  ARG A  28      38.090 -30.306-202.375  1.00 67.11           C  
ANISOU  224  CZ  ARG A  28     9038   9085   7377  -3334  -1692   1440       C  
ATOM    225  NH1 ARG A  28      36.975 -30.518-203.076  1.00 57.64           N  
ANISOU  225  NH1 ARG A  28     7957   7633   6312  -3240  -1730   1428       N  
ATOM    226  NH2 ARG A  28      38.704 -31.324-201.798  1.00 78.26           N  
ANISOU  226  NH2 ARG A  28    10286  10684   8766  -3284  -1717   1605       N  
ATOM    227  N   ILE A  29      41.781 -25.537-203.838  1.00 60.55           N  
ANISOU  227  N   ILE A  29     8530   8363   6115  -3914  -1216    743       N  
ATOM    228  CA  ILE A  29      42.695 -25.319-202.719  1.00 62.30           C  
ANISOU  228  CA  ILE A  29     8556   8972   6142  -4124  -1161    676       C  
ATOM    229  C   ILE A  29      42.150 -25.952-201.457  1.00 69.05           C  
ANISOU  229  C   ILE A  29     9223  10054   6958  -4120  -1240    788       C  
ATOM    230  O   ILE A  29      41.119 -25.523-200.949  1.00 72.74           O  
ANISOU  230  O   ILE A  29     9750  10427   7461  -4150  -1205    741       O  
ATOM    231  CB  ILE A  29      42.924 -23.818-202.445  1.00 61.15           C  
ANISOU  231  CB  ILE A  29     8514   8834   5888  -4375   -943    419       C  
ATOM    232  CG1 ILE A  29      43.430 -23.101-203.710  1.00 66.15           C  
ANISOU  232  CG1 ILE A  29     9358   9211   6565  -4375   -829    308       C  
ATOM    233  CG2 ILE A  29      43.900 -23.643-201.326  1.00 61.52           C  
ANISOU  233  CG2 ILE A  29     8330   9338   5709  -4619   -887    326       C  
ATOM    234  CD1 ILE A  29      44.700 -23.679-204.272  1.00 69.07           C  
ANISOU  234  CD1 ILE A  29     9631   9734   6881  -4356   -899    358       C  
ATOM    235  N   ASP A  30      42.830 -26.973-200.948  1.00 66.87           N  
ANISOU  235  N   ASP A  30     8719  10080   6607  -4067  -1335    952       N  
ATOM    236  CA  ASP A  30      42.375 -27.626-199.725  1.00 74.42           C  
ANISOU  236  CA  ASP A  30     9485  11276   7518  -4044  -1399   1085       C  
ATOM    237  C   ASP A  30      42.798 -26.815-198.516  1.00 88.10           C  
ANISOU  237  C   ASP A  30    11058  13393   9023  -4304  -1301    935       C  
ATOM    238  O   ASP A  30      43.643 -25.926-198.613  1.00 81.73           O  
ANISOU  238  O   ASP A  30    10257  12715   8081  -4505  -1185    741       O  
ATOM    239  CB  ASP A  30      42.949 -29.033-199.583  1.00 72.13           C  
ANISOU  239  CB  ASP A  30     9006  11177   7223  -3863  -1500   1345       C  
ATOM    240  CG  ASP A  30      42.080 -30.098-200.202  1.00 74.80           C  
ANISOU  240  CG  ASP A  30     9448  11184   7790  -3625  -1586   1519       C  
ATOM    241  OD1 ASP A  30      40.911 -29.820-200.581  1.00 66.24           O  
ANISOU  241  OD1 ASP A  30     8538   9784   6847  -3598  -1597   1450       O  
ATOM    242  OD2 ASP A  30      42.583 -31.244-200.277  1.00 76.07           O  
ANISOU  242  OD2 ASP A  30     9502  11425   7977  -3464  -1626   1728       O  
ATOM    243  N   GLU A  31      42.203 -27.140-197.378  1.00 84.80           N  
ANISOU  243  N   GLU A  31    10495  13165   8559  -4311  -1338   1014       N  
ATOM    244  CA  GLU A  31      42.610 -26.589-196.105  1.00 85.22           C  
ANISOU  244  CA  GLU A  31    10342  13663   8377  -4549  -1262    900       C  
ATOM    245  C   GLU A  31      44.029 -27.027-195.792  1.00 80.70           C  
ANISOU  245  C   GLU A  31     9501  13576   7587  -4583  -1277    974       C  
ATOM    246  O   GLU A  31      44.452 -28.098-196.218  1.00 78.67           O  
ANISOU  246  O   GLU A  31     9176  13333   7383  -4357  -1372   1208       O  
ATOM    247  CB  GLU A  31      41.641 -27.068-195.022  1.00101.16           C  
ANISOU  247  CB  GLU A  31    12249  15778  10408  -4495  -1324   1021       C  
ATOM    248  CG  GLU A  31      42.261 -27.407-193.675  1.00117.04           C  
ANISOU  248  CG  GLU A  31    13921  18380  12171  -4583  -1335   1099       C  
ATOM    249  CD  GLU A  31      41.314 -28.197-192.785  1.00133.65           C  
ANISOU  249  CD  GLU A  31    15922  20531  14327  -4446  -1418   1297       C  
ATOM    250  OE1 GLU A  31      41.459 -29.438-192.719  1.00136.19           O  
ANISOU  250  OE1 GLU A  31    16122  20934  14689  -4209  -1506   1582       O  
ATOM    251  OE2 GLU A  31      40.421 -27.582-192.159  1.00138.45           O  
ANISOU  251  OE2 GLU A  31    16581  21080  14944  -4571  -1377   1171       O  
ATOM    252  N   LEU A  32      44.773 -26.202-195.066  1.00 85.81           N  
ANISOU  252  N   LEU A  32     9990  14631   7981  -4870  -1167    771       N  
ATOM    253  CA  LEU A  32      45.992 -26.682-194.443  1.00 87.15           C  
ANISOU  253  CA  LEU A  32     9824  15401   7887  -4903  -1191    867       C  
ATOM    254  C   LEU A  32      45.758 -26.806-192.952  1.00100.20           C  
ANISOU  254  C   LEU A  32    11205  17517   9350  -4993  -1198    909       C  
ATOM    255  O   LEU A  32      45.833 -25.817-192.233  1.00115.11           O  
ANISOU  255  O   LEU A  32    13025  19649  11061  -5306  -1078    645       O  
ATOM    256  CB  LEU A  32      47.161 -25.761-194.721  1.00 74.27           C  
ANISOU  256  CB  LEU A  32     8157  14001   6063  -5175  -1063    606       C  
ATOM    257  CG  LEU A  32      48.523 -26.409-194.445  1.00 87.08           C  
ANISOU  257  CG  LEU A  32     9445  16209   7432  -5138  -1109    747       C  
ATOM    258  CD1 LEU A  32      48.965 -26.379-192.967  1.00 90.78           C  
ANISOU  258  CD1 LEU A  32     9553  17360   7580  -5267  -1055    739       C  
ATOM    259  CD2 LEU A  32      48.522 -27.823-194.997  1.00 88.82           C  
ANISOU  259  CD2 LEU A  32     9657  16274   7815  -4734  -1257   1126       C  
ATOM    260  N   PRO A  33      45.466 -28.026-192.476  1.00104.66           N  
ANISOU  260  N   PRO A  33    11617  18200   9950  -4724  -1317   1237       N  
ATOM    261  CA  PRO A  33      45.245 -28.075-191.035  1.00106.16           C  
ANISOU  261  CA  PRO A  33    11541  18853   9942  -4815  -1315   1272       C  
ATOM    262  C   PRO A  33      46.486 -27.726-190.232  1.00114.20           C  
ANISOU  262  C   PRO A  33    12231  20567  10591  -5002  -1225   1178       C  
ATOM    263  O   PRO A  33      47.619 -28.080-190.571  1.00108.44           O  
ANISOU  263  O   PRO A  33    11353  20118   9732  -4934  -1229   1268       O  
ATOM    264  CB  PRO A  33      44.841 -29.529-190.775  1.00101.13           C  
ANISOU  264  CB  PRO A  33    10808  18202   9415  -4454  -1429   1673       C  
ATOM    265  CG  PRO A  33      45.256 -30.284-191.964  1.00100.72           C  
ANISOU  265  CG  PRO A  33    10885  17849   9534  -4205  -1472   1846       C  
ATOM    266  CD  PRO A  33      45.234 -29.331-193.121  1.00104.89           C  
ANISOU  266  CD  PRO A  33    11713  17946  10194  -4355  -1426   1565       C  
ATOM    267  N   GLU A  34      46.226 -26.960-189.187  1.00116.52           N  
ANISOU  267  N   GLU A  34    12479  21046  10749  -5178  -1073    979       N  
ATOM    268  CA  GLU A  34      46.995 -27.014-187.976  1.00107.44           C  
ANISOU  268  CA  GLU A  34    10999  20547   9277  -5210   -964   1005       C  
ATOM    269  C   GLU A  34      47.278 -28.461-187.601  1.00101.07           C  
ANISOU  269  C   GLU A  34     9898  20085   8420  -4897  -1102   1439       C  
ATOM    270  O   GLU A  34      46.417 -29.348-187.740  1.00104.11           O  
ANISOU  270  O   GLU A  34    10337  20212   9007  -4681  -1264   1702       O  
ATOM    271  CB  GLU A  34      46.230 -26.351-186.821  1.00124.87           C  
ANISOU  271  CB  GLU A  34    13212  22829  11405  -5363   -850    833       C  
ATOM    272  CG  GLU A  34      45.055 -25.478-187.251  1.00128.85           C  
ANISOU  272  CG  GLU A  34    14082  22723  12154  -5494   -816    596       C  
ATOM    273  CD  GLU A  34      43.783 -26.293-187.504  1.00132.90           C  
ANISOU  273  CD  GLU A  34    14705  22838  12954  -5291  -1014    839       C  
ATOM    274  OE1 GLU A  34      43.845 -27.541-187.469  1.00137.44           O  
ANISOU  274  OE1 GLU A  34    15104  23561  13556  -5051  -1180   1184       O  
ATOM    275  OE2 GLU A  34      42.713 -25.688-187.720  1.00126.95           O  
ANISOU  275  OE2 GLU A  34    14213  21632  12392  -5364   -989    690       O  
ATOM    276  N   GLY A  35      48.487 -28.705-187.112  1.00111.80           N  
ANISOU  276  N   GLY A  35    10943  22031   9504  -4861  -1014   1524       N  
ATOM    277  CA  GLY A  35      48.808 -30.004-186.541  1.00107.14           C  
ANISOU  277  CA  GLY A  35    10037  21832   8839  -4542  -1077   1944       C  
ATOM    278  C   GLY A  35      49.766 -30.797-187.385  1.00105.85           C  
ANISOU  278  C   GLY A  35     9786  21744   8689  -4313  -1137   2180       C  
ATOM    279  O   GLY A  35      50.399 -31.701-186.860  1.00 91.37           O  
ANISOU  279  O   GLY A  35     7641  20339   6735  -4061  -1110   2488       O  
ATOM    280  N   ALA A  36      49.910 -30.421-188.659  1.00104.79           N  
ANISOU  280  N   ALA A  36     9917  21205   8695  -4396  -1195   2028       N  
ATOM    281  CA  ALA A  36      50.750 -31.179-189.564  1.00100.92           C  
ANISOU  281  CA  ALA A  36     9392  20720   8231  -4168  -1260   2252       C  
ATOM    282  C   ALA A  36      52.158 -30.659-189.767  1.00103.49           C  
ANISOU  282  C   ALA A  36     9554  21431   8337  -4305  -1133   2088       C  
ATOM    283  O   ALA A  36      52.532 -29.609-189.282  1.00102.18           O  
ANISOU  283  O   ALA A  36     9330  21512   7983  -4610   -976   1765       O  
ATOM    284  CB  ALA A  36      50.061 -31.296-190.882  1.00 96.36           C  
ANISOU  284  CB  ALA A  36     9194  19475   7941  -4122  -1412   2251       C  
ATOM    285  N   VAL A  37      52.909 -31.429-190.534  1.00103.17           N  
ANISOU  285  N   VAL A  37     9469  21407   8325  -4063  -1190   2321       N  
ATOM    286  CA  VAL A  37      54.197 -31.011-191.014  1.00100.12           C  
ANISOU  286  CA  VAL A  37     8977  21284   7781  -4172  -1102   2179       C  
ATOM    287  C   VAL A  37      53.978 -29.821-191.931  1.00 99.49           C  
ANISOU  287  C   VAL A  37     9244  20758   7798  -4502  -1092   1772       C  
ATOM    288  O   VAL A  37      53.035 -29.801-192.739  1.00 98.18           O  
ANISOU  288  O   VAL A  37     9415  19995   7892  -4493  -1219   1745       O  
ATOM    289  CB  VAL A  37      54.924 -32.164-191.773  1.00 92.29           C  
ANISOU  289  CB  VAL A  37     7921  20300   6847  -3800  -1172   2540       C  
ATOM    290  CG1 VAL A  37      56.262 -31.705-192.335  1.00 91.71           C  
ANISOU  290  CG1 VAL A  37     7741  20489   6618  -3921  -1090   2380       C  
ATOM    291  CG2 VAL A  37      55.085 -33.346-190.848  1.00 93.17           C  
ANISOU  291  CG2 VAL A  37     7710  20789   6901  -3435  -1135   2953       C  
ATOM    292  N   LYS A  38      54.828 -28.814-191.772  1.00 94.22           N  
ANISOU  292  N   LYS A  38     8495  20382   6922  -4793   -915   1455       N  
ATOM    293  CA  LYS A  38      54.688 -27.576-192.510  1.00 88.11           C  
ANISOU  293  CA  LYS A  38     8047  19205   6226  -5108   -834   1050       C  
ATOM    294  C   LYS A  38      55.057 -27.779-193.975  1.00 88.31           C  
ANISOU  294  C   LYS A  38     8274  18864   6417  -5024   -939   1083       C  
ATOM    295  O   LYS A  38      56.102 -28.344-194.294  1.00 97.51           O  
ANISOU  295  O   LYS A  38     9250  20325   7475  -4876   -956   1248       O  
ATOM    296  CB  LYS A  38      55.559 -26.497-191.869  1.00103.04           C  
ANISOU  296  CB  LYS A  38     9797  21541   7814  -5424   -579    720       C  
ATOM    297  CG  LYS A  38      54.810 -25.515-190.968  1.00118.14           C  
ANISOU  297  CG  LYS A  38    11815  23413   9658  -5680   -430    435       C  
ATOM    298  CD  LYS A  38      54.428 -24.268-191.762  1.00130.17           C  
ANISOU  298  CD  LYS A  38    13748  24377  11334  -5937   -315     53       C  
ATOM    299  CE  LYS A  38      54.765 -22.980-191.003  1.00126.14           C  
ANISOU  299  CE  LYS A  38    13243  24119  10566  -6279    -26   -341       C  
ATOM    300  NZ  LYS A  38      54.244 -21.753-191.683  1.00120.59           N  
ANISOU  300  NZ  LYS A  38    12955  22823  10039  -6492    123   -690       N  
ATOM    301  N   PRO A  39      54.201 -27.307-194.880  1.00 85.38           N  
ANISOU  301  N   PRO A  39     8285  17847   6308  -5110   -997    927       N  
ATOM    302  CA  PRO A  39      54.435 -27.459-196.316  1.00 88.38           C  
ANISOU  302  CA  PRO A  39     8887  17835   6857  -5043  -1098    944       C  
ATOM    303  C   PRO A  39      55.647 -26.663-196.760  1.00 90.43           C  
ANISOU  303  C   PRO A  39     9127  18271   6962  -5245   -933    690       C  
ATOM    304  O   PRO A  39      56.185 -25.876-195.979  1.00 95.81           O  
ANISOU  304  O   PRO A  39     9663  19323   7416  -5470   -727    463       O  
ATOM    305  CB  PRO A  39      53.154 -26.908-196.939  1.00 85.51           C  
ANISOU  305  CB  PRO A  39     8941  16725   6825  -5086  -1089    792       C  
ATOM    306  CG  PRO A  39      52.662 -25.933-195.925  1.00 89.11           C  
ANISOU  306  CG  PRO A  39     9376  17313   7169  -5371   -948    528       C  
ATOM    307  CD  PRO A  39      52.985 -26.527-194.598  1.00 90.89           C  
ANISOU  307  CD  PRO A  39     9226  18156   7154  -5282   -944    712       C  
ATOM    308  N   PRO A  40      56.096 -26.890-198.000  1.00 98.25           N  
ANISOU  308  N   PRO A  40    10258  19015   8057  -5166  -1017    732       N  
ATOM    309  CA  PRO A  40      57.103 -26.019-198.617  1.00 90.70           C  
ANISOU  309  CA  PRO A  40     9360  18095   7006  -5379   -857    456       C  
ATOM    310  C   PRO A  40      56.597 -24.595-198.595  1.00 92.36           C  
ANISOU  310  C   PRO A  40     9841  17973   7279  -5691   -643     58       C  
ATOM    311  O   PRO A  40      55.376 -24.398-198.601  1.00 92.19           O  
ANISOU  311  O   PRO A  40    10047  17515   7468  -5690   -677     30       O  
ATOM    312  CB  PRO A  40      57.200 -26.522-200.066  1.00 85.58           C  
ANISOU  312  CB  PRO A  40     8938  16998   6579  -5184   -989    585       C  
ATOM    313  CG  PRO A  40      56.490 -27.825-200.117  1.00 82.88           C  
ANISOU  313  CG  PRO A  40     8626  16407   6457  -4762  -1134    982       C  
ATOM    314  CD  PRO A  40      55.795 -28.086-198.808  1.00 95.08           C  
ANISOU  314  CD  PRO A  40     9986  18224   7916  -4752  -1162   1084       C  
ATOM    315  N   ALA A  41      57.486 -23.632-198.640  1.00 96.14           N  
ANISOU  315  N   ALA A  41    10309  18636   7582  -5935   -411   -232       N  
ATOM    316  CA  ALA A  41      57.067 -22.267-198.547  1.00 94.92           C  
ANISOU  316  CA  ALA A  41    10433  18167   7467  -6209   -159   -606       C  
ATOM    317  C   ALA A  41      56.181 -21.949-199.708  1.00 94.54           C  
ANISOU  317  C   ALA A  41    10806  17350   7765  -6161   -199   -652       C  
ATOM    318  O   ALA A  41      56.392 -22.426-200.788  1.00 97.70           O  
ANISOU  318  O   ALA A  41    11299  17503   8317  -6008   -359   -503       O  
ATOM    319  CB  ALA A  41      58.273 -21.374-198.556  1.00 83.52           C  
ANISOU  319  CB  ALA A  41     8932  17010   5792  -6449     89   -880       C  
ATOM    320  N   ASN A  42      55.121 -21.220-199.454  1.00 89.48           N  
ANISOU  320  N   ASN A  42    10408  16352   7239  -6277    -46   -842       N  
ATOM    321  CA  ASN A  42      54.279 -20.696-200.500  1.00 92.09           C  
ANISOU  321  CA  ASN A  42    11137  15968   7883  -6229    -27   -893       C  
ATOM    322  C   ASN A  42      53.836 -21.726-201.509  1.00 99.31           C  
ANISOU  322  C   ASN A  42    12149  16540   9045  -5975   -310   -610       C  
ATOM    323  O   ASN A  42      53.681 -21.428-202.668  1.00104.36           O  
ANISOU  323  O   ASN A  42    13095  16660   9898  -5930   -279   -652       O  
ATOM    324  CB  ASN A  42      54.845 -19.470-201.171  1.00106.05           C  
ANISOU  324  CB  ASN A  42    13158  17478   9659  -6404    253  -1190       C  
ATOM    325  CG  ASN A  42      53.839 -18.353-201.214  1.00115.30           C  
ANISOU  325  CG  ASN A  42    14672  18136  10999  -6476    478  -1381       C  
ATOM    326  OD1 ASN A  42      52.948 -18.303-200.386  1.00126.98           O  
ANISOU  326  OD1 ASN A  42    16150  19589  12509  -6474    482  -1369       O  
ATOM    327  ND2 ASN A  42      53.954 -17.476-202.184  1.00108.12           N  
ANISOU  327  ND2 ASN A  42    14058  16822  10201  -6523    678  -1543       N  
ATOM    328  N   LYS A  43      53.575 -22.926-201.047  1.00 92.99           N  
ANISOU  328  N   LYS A  43    11100  16019   8213  -5767   -555   -306       N  
ATOM    329  CA  LYS A  43      53.081 -23.967-201.897  1.00 81.41           C  
ANISOU  329  CA  LYS A  43     9765  14153   7013  -5360   -743     10       C  
ATOM    330  C   LYS A  43      51.748 -24.299-201.301  1.00 88.54           C  
ANISOU  330  C   LYS A  43    10711  14871   8061  -5219   -821    146       C  
ATOM    331  O   LYS A  43      51.607 -24.301-200.094  1.00 86.17           O  
ANISOU  331  O   LYS A  43    10185  14959   7595  -5330   -821    144       O  
ATOM    332  CB  LYS A  43      53.986 -25.175-201.834  1.00 87.62           C  
ANISOU  332  CB  LYS A  43    10291  15298   7702  -5138   -899    288       C  
ATOM    333  CG  LYS A  43      54.905 -25.319-203.023  1.00 97.61           C  
ANISOU  333  CG  LYS A  43    11683  16348   9058  -5016   -920    325       C  
ATOM    334  CD  LYS A  43      54.970 -26.757-203.485  1.00104.08           C  
ANISOU  334  CD  LYS A  43    12240  17514   9792  -4758  -1059    641       C  
ATOM    335  CE  LYS A  43      56.254 -27.054-204.230  1.00102.93           C  
ANISOU  335  CE  LYS A  43    12239  17080   9790  -4568  -1105    735       C  
ATOM    336  NZ  LYS A  43      56.230 -28.428-204.791  1.00 99.88           N  
ANISOU  336  NZ  LYS A  43    11854  16501   9595  -4183  -1243   1093       N  
ATOM    337  N   TYR A  44      50.759 -24.544-202.145  1.00 89.06           N  
ANISOU  337  N   TYR A  44    11047  14373   8417  -4983   -886    257       N  
ATOM    338  CA  TYR A  44      49.394 -24.774-201.666  1.00 82.54           C  
ANISOU  338  CA  TYR A  44    10295  13328   7740  -4870   -943    352       C  
ATOM    339  C   TYR A  44      48.913 -26.213-201.859  1.00 76.65           C  
ANISOU  339  C   TYR A  44     9501  12470   7152  -4524  -1136    685       C  
ATOM    340  O   TYR A  44      49.303 -26.882-202.813  1.00 74.53           O  
ANISOU  340  O   TYR A  44     9285  12046   6986  -4333  -1209    819       O  
ATOM    341  CB  TYR A  44      48.430 -23.809-202.355  1.00 75.17           C  
ANISOU  341  CB  TYR A  44     9705  11860   6995  -4900   -827    189       C  
ATOM    342  CG  TYR A  44      48.534 -22.415-201.828  1.00 84.80           C  
ANISOU  342  CG  TYR A  44    10985  13149   8084  -5240   -591   -126       C  
ATOM    343  CD1 TYR A  44      49.710 -21.682-201.972  1.00 96.13           C  
ANISOU  343  CD1 TYR A  44    12387  14790   9347  -5497   -435   -348       C  
ATOM    344  CD2 TYR A  44      47.478 -21.834-201.149  1.00 88.24           C  
ANISOU  344  CD2 TYR A  44    11508  13457   8562  -5322   -503   -213       C  
ATOM    345  CE1 TYR A  44      49.827 -20.396-201.462  1.00 89.66           C  
ANISOU  345  CE1 TYR A  44    11631  14028   8407  -5846   -174   -667       C  
ATOM    346  CE2 TYR A  44      47.584 -20.550-200.631  1.00 90.25           C  
ANISOU  346  CE2 TYR A  44    11828  13760   8701  -5651   -246   -516       C  
ATOM    347  CZ  TYR A  44      48.756 -19.834-200.799  1.00 93.35           C  
ANISOU  347  CZ  TYR A  44    12201  14337   8932  -5913    -70   -748       C  
ATOM    348  OH  TYR A  44      48.859 -18.560-200.291  1.00 95.75           O  
ANISOU  348  OH  TYR A  44    12604  14641   9137  -6112    248  -1035       O  
ATOM    349  N   PRO A  45      48.080 -26.695-200.928  1.00 75.07           N  
ANISOU  349  N   PRO A  45     9201  12351   6971  -4456  -1199    809       N  
ATOM    350  CA  PRO A  45      47.508 -28.043-200.983  1.00 74.46           C  
ANISOU  350  CA  PRO A  45     9089  12151   7050  -4155  -1342   1108       C  
ATOM    351  C   PRO A  45      46.405 -28.177-202.024  1.00 71.53           C  
ANISOU  351  C   PRO A  45     9006  11210   6960  -3991  -1383   1128       C  
ATOM    352  O   PRO A  45      45.294 -27.643-201.878  1.00 67.71           O  
ANISOU  352  O   PRO A  45     8663  10496   6567  -4032  -1358   1036       O  
ATOM    353  CB  PRO A  45      46.958 -28.259-199.566  1.00 80.83           C  
ANISOU  353  CB  PRO A  45     9704  13248   7760  -4194  -1360   1179       C  
ATOM    354  CG  PRO A  45      46.838 -26.894-198.968  1.00 78.08           C  
ANISOU  354  CG  PRO A  45     9380  13009   7276  -4509  -1231    883       C  
ATOM    355  CD  PRO A  45      47.925 -26.081-199.599  1.00 80.16           C  
ANISOU  355  CD  PRO A  45     9688  13340   7429  -4691  -1124    677       C  
ATOM    356  N   ILE A  46      46.717 -28.922-203.073  1.00 66.52           N  
ANISOU  356  N   ILE A  46     8445  10378   6451  -3802  -1442   1252       N  
ATOM    357  CA  ILE A  46      45.814 -29.059-204.200  1.00 67.57           C  
ANISOU  357  CA  ILE A  46     8827  10026   6820  -3661  -1478   1253       C  
ATOM    358  C   ILE A  46      45.028 -30.369-204.215  1.00 66.42           C  
ANISOU  358  C   ILE A  46     8667   9729   6840  -3438  -1570   1474       C  
ATOM    359  O   ILE A  46      45.601 -31.426-204.000  1.00 69.43           O  
ANISOU  359  O   ILE A  46     8901  10271   7208  -3310  -1599   1672       O  
ATOM    360  CB  ILE A  46      46.603 -28.947-205.509  1.00 69.09           C  
ANISOU  360  CB  ILE A  46     9141  10058   7054  -3621  -1464   1206       C  
ATOM    361  CG1 ILE A  46      47.560 -27.752-205.445  1.00 62.49           C  
ANISOU  361  CG1 ILE A  46     8297   9408   6037  -3856  -1349    992       C  
ATOM    362  CG2 ILE A  46      45.668 -28.789-206.682  1.00 66.77           C  
ANISOU  362  CG2 ILE A  46     9099   9313   6959  -3517  -1480   1157       C  
ATOM    363  CD1 ILE A  46      46.854 -26.401-205.469  1.00 59.01           C  
ANISOU  363  CD1 ILE A  46     8047   8763   5610  -4017  -1227    764       C  
ATOM    364  N   PHE A  47      43.719 -30.274-204.493  1.00 74.02           N  
ANISOU  364  N   PHE A  47     9785  10385   7954  -3392  -1594   1435       N  
ATOM    365  CA  PHE A  47      42.825 -31.418-204.742  1.00 67.27           C  
ANISOU  365  CA  PHE A  47     8963   9320   7279  -3213  -1659   1586       C  
ATOM    366  C   PHE A  47      42.316 -31.404-206.193  1.00 67.29           C  
ANISOU  366  C   PHE A  47     9173   8955   7437  -3130  -1679   1516       C  
ATOM    367  O   PHE A  47      41.543 -30.524-206.588  1.00 70.06           O  
ANISOU  367  O   PHE A  47     9667   9138   7816  -3173  -1664   1377       O  
ATOM    368  CB  PHE A  47      41.631 -31.395-203.770  1.00 62.28           C  
ANISOU  368  CB  PHE A  47     8297   8699   6666  -3239  -1675   1597       C  
ATOM    369  CG  PHE A  47      40.598 -32.494-204.015  1.00 69.31           C  
ANISOU  369  CG  PHE A  47     9231   9367   7738  -3091  -1722   1715       C  
ATOM    370  CD1 PHE A  47      40.726 -33.739-203.404  1.00 65.03           C  
ANISOU  370  CD1 PHE A  47     8554   8925   7230  -2983  -1719   1923       C  
ATOM    371  CD2 PHE A  47      39.495 -32.275-204.832  1.00 73.88           C  
ANISOU  371  CD2 PHE A  47     9975   9657   8439  -3062  -1746   1617       C  
ATOM    372  CE1 PHE A  47      39.793 -34.743-203.610  1.00 65.80           C  
ANISOU  372  CE1 PHE A  47     8701   8805   7496  -2878  -1724   2007       C  
ATOM    373  CE2 PHE A  47      38.548 -33.287-205.050  1.00 62.13           C  
ANISOU  373  CE2 PHE A  47     8509   7998   7099  -2963  -1775   1693       C  
ATOM    374  CZ  PHE A  47      38.703 -34.517-204.435  1.00 61.07           C  
ANISOU  374  CZ  PHE A  47     8259   7933   7012  -2886  -1756   1875       C  
ATOM    375  N   PHE A  48      42.740 -32.366-206.999  1.00 60.92           N  
ANISOU  375  N   PHE A  48     8381   8040   6725  -3003  -1699   1617       N  
ATOM    376  CA  PHE A  48      42.280 -32.402-208.384  1.00 67.05           C  
ANISOU  376  CA  PHE A  48     9331   8515   7631  -2935  -1718   1543       C  
ATOM    377  C   PHE A  48      40.896 -33.031-208.466  1.00 65.18           C  
ANISOU  377  C   PHE A  48     9136   8100   7528  -2869  -1752   1565       C  
ATOM    378  O   PHE A  48      40.678 -34.079-207.895  1.00 55.70           O  
ANISOU  378  O   PHE A  48     7848   6926   6388  -2813  -1748   1698       O  
ATOM    379  CB  PHE A  48      43.278 -33.166-209.254  1.00 67.90           C  
ANISOU  379  CB  PHE A  48     9441   8574   7785  -2845  -1711   1617       C  
ATOM    380  CG  PHE A  48      44.609 -32.477-209.364  1.00 71.48           C  
ANISOU  380  CG  PHE A  48     9863   9196   8100  -2916  -1681   1569       C  
ATOM    381  CD1 PHE A  48      45.648 -32.810-208.511  1.00 59.88           C  
ANISOU  381  CD1 PHE A  48     8211   8033   6508  -2927  -1658   1686       C  
ATOM    382  CD2 PHE A  48      44.805 -31.470-210.295  1.00 66.60           C  
ANISOU  382  CD2 PHE A  48     9387   8458   7461  -2973  -1662   1409       C  
ATOM    383  CE1 PHE A  48      46.871 -32.160-208.603  1.00 64.52           C  
ANISOU  383  CE1 PHE A  48     8751   8818   6947  -3016  -1625   1621       C  
ATOM    384  CE2 PHE A  48      46.030 -30.800-210.387  1.00 57.56           C  
ANISOU  384  CE2 PHE A  48     8217   7466   6185  -3064  -1614   1343       C  
ATOM    385  CZ  PHE A  48      47.060 -31.158-209.544  1.00 55.49           C  
ANISOU  385  CZ  PHE A  48     7764   7524   5796  -3097  -1601   1438       C  
ATOM    386  N   PHE A  49      39.961 -32.381-209.158  1.00 57.10           N  
ANISOU  386  N   PHE A  49     8241   6912   6541  -2873  -1769   1439       N  
ATOM    387  CA  PHE A  49      38.629 -32.958-209.349  1.00 52.60           C  
ANISOU  387  CA  PHE A  49     7697   6212   6078  -2823  -1803   1438       C  
ATOM    388  C   PHE A  49      38.677 -34.098-210.356  1.00 56.12           C  
ANISOU  388  C   PHE A  49     8171   6507   6645  -2746  -1804   1468       C  
ATOM    389  O   PHE A  49      39.537 -34.120-211.229  1.00 69.40           O  
ANISOU  389  O   PHE A  49     9900   8138   8331  -2718  -1793   1452       O  
ATOM    390  CB  PHE A  49      37.640 -31.901-209.821  1.00 52.14           C  
ANISOU  390  CB  PHE A  49     7743   6075   5992  -2827  -1811   1311       C  
ATOM    391  CG  PHE A  49      37.260 -30.924-208.769  1.00 62.25           C  
ANISOU  391  CG  PHE A  49     9009   7460   7183  -2902  -1782   1277       C  
ATOM    392  CD1 PHE A  49      36.565 -31.334-207.656  1.00 60.31           C  
ANISOU  392  CD1 PHE A  49     8668   7299   6948  -2930  -1802   1335       C  
ATOM    393  CD2 PHE A  49      37.589 -29.582-208.890  1.00 63.37           C  
ANISOU  393  CD2 PHE A  49     9241   7603   7235  -2952  -1711   1180       C  
ATOM    394  CE1 PHE A  49      36.209 -30.424-206.668  1.00 63.66           C  
ANISOU  394  CE1 PHE A  49     9078   7823   7288  -3009  -1767   1294       C  
ATOM    395  CE2 PHE A  49      37.238 -28.670-207.904  1.00 58.08           C  
ANISOU  395  CE2 PHE A  49     8567   7012   6487  -3039  -1650   1132       C  
ATOM    396  CZ  PHE A  49      36.548 -29.095-206.790  1.00 59.10           C  
ANISOU  396  CZ  PHE A  49     8593   7241   6623  -3069  -1686   1187       C  
ATOM    397  N   GLY A  50      37.738 -35.030-210.257  1.00 54.31           N  
ANISOU  397  N   GLY A  50     7919   6203   6515  -2728  -1803   1494       N  
ATOM    398  CA  GLY A  50      37.710 -36.170-211.145  1.00 53.24           C  
ANISOU  398  CA  GLY A  50     7813   5916   6501  -2688  -1767   1497       C  
ATOM    399  C   GLY A  50      38.589 -37.301-210.680  1.00 59.00           C  
ANISOU  399  C   GLY A  50     8481   6640   7296  -2640  -1684   1660       C  
ATOM    400  O   GLY A  50      38.153 -38.461-210.606  1.00 69.05           O  
ANISOU  400  O   GLY A  50     9745   7803   8688  -2623  -1606   1711       O  
ATOM    401  N   THR A  51      39.836 -36.977-210.364  1.00 61.66           N  
ANISOU  401  N   THR A  51     8773   7105   7550  -2614  -1678   1745       N  
ATOM    402  CA  THR A  51      40.798 -37.991-209.947  1.00 60.29           C  
ANISOU  402  CA  THR A  51     8525   6972   7411  -2530  -1589   1934       C  
ATOM    403  C   THR A  51      40.862 -38.093-208.421  1.00 65.32           C  
ANISOU  403  C   THR A  51     9022   7822   7976  -2517  -1570   2087       C  
ATOM    404  O   THR A  51      41.020 -39.186-207.867  1.00 71.51           O  
ANISOU  404  O   THR A  51     9742   8605   8825  -2426  -1470   2268       O  
ATOM    405  CB  THR A  51      42.171 -37.667-210.491  1.00 62.09           C  
ANISOU  405  CB  THR A  51     8754   7271   7567  -2499  -1590   1952       C  
ATOM    406  OG1 THR A  51      42.532 -36.365-210.037  1.00 74.74           O  
ANISOU  406  OG1 THR A  51    10319   9072   9006  -2580  -1657   1882       O  
ATOM    407  CG2 THR A  51      42.134 -37.619-212.008  1.00 58.22           C  
ANISOU  407  CG2 THR A  51     8396   6577   7147  -2503  -1604   1811       C  
ATOM    408  N   HIS A  52      40.719 -36.941-207.762  1.00 60.89           N  
ANISOU  408  N   HIS A  52     8416   7441   7277  -2606  -1646   2014       N  
ATOM    409  CA  HIS A  52      40.827 -36.809-206.310  1.00 67.62           C  
ANISOU  409  CA  HIS A  52     9119   8553   8021  -2623  -1642   2125       C  
ATOM    410  C   HIS A  52      42.277 -37.020-205.880  1.00 69.70           C  
ANISOU  410  C   HIS A  52     9246   9069   8168  -2563  -1599   2281       C  
ATOM    411  O   HIS A  52      42.559 -37.261-204.715  1.00 83.74           O  
ANISOU  411  O   HIS A  52    10863  11102   9851  -2534  -1571   2431       O  
ATOM    412  CB  HIS A  52      39.870 -37.781-205.580  1.00 61.14           C  
ANISOU  412  CB  HIS A  52     8259   7666   7303  -2575  -1593   2238       C  
ATOM    413  CG  HIS A  52      38.424 -37.519-205.858  1.00 61.67           C  
ANISOU  413  CG  HIS A  52     8423   7560   7449  -2648  -1641   2082       C  
ATOM    414  ND1 HIS A  52      37.402 -38.250-205.297  1.00 61.97           N  
ANISOU  414  ND1 HIS A  52     8442   7525   7577  -2639  -1603   2132       N  
ATOM    415  CD2 HIS A  52      37.828 -36.588-206.643  1.00 68.87           C  
ANISOU  415  CD2 HIS A  52     9442   8378   8347  -2719  -1714   1886       C  
ATOM    416  CE1 HIS A  52      36.241 -37.784-205.719  1.00 63.01           C  
ANISOU  416  CE1 HIS A  52     8653   7550   7740  -2712  -1664   1964       C  
ATOM    417  NE2 HIS A  52      36.474 -36.771-206.536  1.00 61.44           N  
ANISOU  417  NE2 HIS A  52     8528   7342   7475  -2748  -1729   1825       N  
ATOM    418  N   GLU A  53      43.195 -36.913-206.831  1.00 66.92           N  
ANISOU  418  N   GLU A  53     8946   8674   7807  -2541  -1593   2246       N  
ATOM    419  CA  GLU A  53      44.612 -36.898-206.519  1.00 66.33           C  
ANISOU  419  CA  GLU A  53     8734   8882   7587  -2503  -1565   2360       C  
ATOM    420  C   GLU A  53      44.940 -35.594-205.845  1.00 76.41           C  
ANISOU  420  C   GLU A  53     9926  10447   8659  -2666  -1615   2234       C  
ATOM    421  O   GLU A  53      44.158 -34.648-205.946  1.00 69.68           O  
ANISOU  421  O   GLU A  53     9175   9491   7809  -2792  -1657   2044       O  
ATOM    422  CB  GLU A  53      45.453 -37.040-207.777  1.00 65.51           C  
ANISOU  422  CB  GLU A  53     8720   8643   7528  -2453  -1549   2330       C  
ATOM    423  CG  GLU A  53      45.124 -38.254-208.596  1.00 90.37           C  
ANISOU  423  CG  GLU A  53    11977  11477  10885  -2327  -1477   2405       C  
ATOM    424  CD  GLU A  53      46.019 -38.372-209.796  1.00110.41           C  
ANISOU  424  CD  GLU A  53    14591  13905  13454  -2283  -1458   2375       C  
ATOM    425  OE1 GLU A  53      47.089 -39.003-209.662  1.00119.91           O  
ANISOU  425  OE1 GLU A  53    15701  15241  14619  -2162  -1383   2558       O  
ATOM    426  OE2 GLU A  53      45.664 -37.816-210.862  1.00118.96           O  
ANISOU  426  OE2 GLU A  53    15819  14792  14587  -2358  -1514   2180       O  
ATOM    427  N   THR A  54      46.095 -35.524-205.180  1.00 67.72           N  
ANISOU  427  N   THR A  54     8637   9720   7372  -2667  -1590   2332       N  
ATOM    428  CA  THR A  54      46.476 -34.305-204.484  1.00 65.52           C  
ANISOU  428  CA  THR A  54     8261   9753   6880  -2861  -1608   2184       C  
ATOM    429  C   THR A  54      47.945 -33.945-204.723  1.00 80.49           C  
ANISOU  429  C   THR A  54    10055  11924   8603  -2907  -1586   2163       C  
ATOM    430  O   THR A  54      48.768 -34.805-205.043  1.00 92.41           O  
ANISOU  430  O   THR A  54    11496  13497  10119  -2748  -1558   2342       O  
ATOM    431  CB  THR A  54      46.248 -34.412-202.960  1.00 73.34           C  
ANISOU  431  CB  THR A  54     9045  11082   7739  -2887  -1601   2290       C  
ATOM    432  OG1 THR A  54      47.079 -35.445-202.424  1.00 87.01           O  
ANISOU  432  OG1 THR A  54    10571  13097   9391  -2714  -1555   2566       O  
ATOM    433  CG2 THR A  54      44.790 -34.743-202.627  1.00 61.27           C  
ANISOU  433  CG2 THR A  54     7603   9308   6368  -2854  -1620   2307       C  
ATOM    434  N   ALA A  55      48.267 -32.667-204.570  1.00 67.00           N  
ANISOU  434  N   ALA A  55     8343  10373   6741  -3128  -1577   1940       N  
ATOM    435  CA  ALA A  55      49.660 -32.231-204.575  1.00 74.45           C  
ANISOU  435  CA  ALA A  55     9150  11661   7475  -3222  -1543   1891       C  
ATOM    436  C   ALA A  55      49.805 -30.835-204.000  1.00 77.15           C  
ANISOU  436  C   ALA A  55     9459  12225   7630  -3514  -1494   1630       C  
ATOM    437  O   ALA A  55      48.835 -30.192-203.596  1.00 77.36           O  
ANISOU  437  O   ALA A  55     9575  12124   7695  -3628  -1481   1499       O  
ATOM    438  CB  ALA A  55      50.245 -32.270-205.990  1.00 64.68           C  
ANISOU  438  CB  ALA A  55     8070  10170   6335  -3162  -1542   1847       C  
ATOM    439  N   PHE A  56      51.041 -30.370-203.960  1.00 84.84           N  
ANISOU  439  N   PHE A  56    10300  13540   8396  -3644  -1449   1547       N  
ATOM    440  CA  PHE A  56      51.292 -29.014-203.551  1.00 69.04           C  
ANISOU  440  CA  PHE A  56     8288  11725   6219  -3956  -1360   1259       C  
ATOM    441  C   PHE A  56      51.793 -28.244-204.732  1.00 63.81           C  
ANISOU  441  C   PHE A  56     7825  10822   5597  -4052  -1300   1063       C  
ATOM    442  O   PHE A  56      52.661 -28.716-205.458  1.00 81.37           O  
ANISOU  442  O   PHE A  56    10025  13073   7819  -3946  -1325   1150       O  
ATOM    443  CB  PHE A  56      52.285 -28.967-202.404  1.00 74.73           C  
ANISOU  443  CB  PHE A  56     8666  13108   6622  -4091  -1328   1272       C  
ATOM    444  CG  PHE A  56      51.672 -29.276-201.066  1.00 87.64           C  
ANISOU  444  CG  PHE A  56    10115  15011   8175  -4086  -1352   1378       C  
ATOM    445  CD1 PHE A  56      51.205 -28.261-200.253  1.00 82.93           C  
ANISOU  445  CD1 PHE A  56     9507  14529   7472  -4358  -1280   1144       C  
ATOM    446  CD2 PHE A  56      51.549 -30.588-200.625  1.00 84.42           C  
ANISOU  446  CD2 PHE A  56     9552  14721   7802  -3805  -1425   1715       C  
ATOM    447  CE1 PHE A  56      50.636 -28.547-199.023  1.00 85.87           C  
ANISOU  447  CE1 PHE A  56     9705  15157   7766  -4355  -1305   1240       C  
ATOM    448  CE2 PHE A  56      50.983 -30.877-199.394  1.00 74.07           C  
ANISOU  448  CE2 PHE A  56     8071  13658   6414  -3791  -1439   1824       C  
ATOM    449  CZ  PHE A  56      50.523 -29.860-198.593  1.00 77.85           C  
ANISOU  449  CZ  PHE A  56     8527  14273   6779  -4067  -1393   1585       C  
ATOM    450  N   LEU A  57      51.238 -27.050-204.917  1.00 71.27           N  
ANISOU  450  N   LEU A  57     8973  11525   6582  -4243  -1203    810       N  
ATOM    451  CA  LEU A  57      51.606 -26.162-206.016  1.00 62.67           C  
ANISOU  451  CA  LEU A  57     8103  10171   5537  -4342  -1107    612       C  
ATOM    452  C   LEU A  57      51.638 -24.722-205.571  1.00 83.88           C  
ANISOU  452  C   LEU A  57    10857  12916   8099  -4664   -920    306       C  
ATOM    453  O   LEU A  57      50.935 -24.350-204.634  1.00 92.09           O  
ANISOU  453  O   LEU A  57    11865  14023   9102  -4774   -874    241       O  
ATOM    454  CB  LEU A  57      50.614 -26.291-207.159  1.00 65.32           C  
ANISOU  454  CB  LEU A  57     8725   9949   6145  -4144  -1151    660       C  
ATOM    455  CG  LEU A  57      50.776 -27.463-208.118  1.00 76.61           C  
ANISOU  455  CG  LEU A  57    10177  11209   7721  -3874  -1277    872       C  
ATOM    456  CD1 LEU A  57      49.473 -27.674-208.883  1.00 79.50           C  
ANISOU  456  CD1 LEU A  57    10765  11114   8327  -3704  -1329    917       C  
ATOM    457  CD2 LEU A  57      51.914 -27.147-209.083  1.00 66.69           C  
ANISOU  457  CD2 LEU A  57     8973   9950   6416  -3917  -1231    788       C  
ATOM    458  N   GLY A  58      52.429 -23.906-206.263  1.00 77.92           N  
ANISOU  458  N   GLY A  58    10208  12109   7288  -4820   -791    113       N  
ATOM    459  CA  GLY A  58      52.468 -22.475-205.999  1.00 69.22           C  
ANISOU  459  CA  GLY A  58     9225  10980   6096  -5136   -554   -201       C  
ATOM    460  C   GLY A  58      51.642 -21.701-207.018  1.00 64.31           C  
ANISOU  460  C   GLY A  58     8970   9775   5692  -5066   -439   -282       C  
ATOM    461  O   GLY A  58      51.375 -22.208-208.119  1.00 62.68           O  
ANISOU  461  O   GLY A  58     8903   9252   5663  -4809   -547   -132       O  
ATOM    462  N   PRO A  59      51.234 -20.469-206.659  1.00 69.54           N  
ANISOU  462  N   PRO A  59     9785  10306   6332  -5290   -202   -516       N  
ATOM    463  CA  PRO A  59      50.397 -19.545-207.449  1.00 80.95           C  
ANISOU  463  CA  PRO A  59    11576  11228   7953  -5231    -29   -596       C  
ATOM    464  C   PRO A  59      50.746 -19.481-208.936  1.00 75.40           C  
ANISOU  464  C   PRO A  59    11069  10212   7367  -5073    -19   -558       C  
ATOM    465  O   PRO A  59      49.859 -19.280-209.768  1.00 73.58           O  
ANISOU  465  O   PRO A  59    11070   9571   7315  -4862      0   -479       O  
ATOM    466  CB  PRO A  59      50.667 -18.193-206.795  1.00 82.23           C  
ANISOU  466  CB  PRO A  59    11808  11450   7983  -5598    297   -913       C  
ATOM    467  CG  PRO A  59      51.021 -18.516-205.412  1.00 84.90           C  
ANISOU  467  CG  PRO A  59    11832  12312   8114  -5805    238   -963       C  
ATOM    468  CD  PRO A  59      51.700 -19.849-205.409  1.00 79.33           C  
ANISOU  468  CD  PRO A  59    10848  11956   7339  -5641    -51   -736       C  
ATOM    469  N   LYS A  60      52.031 -19.635-209.243  1.00 76.97           N  
ANISOU  469  N   LYS A  60    11159  10639   7448  -5176    -29   -613       N  
ATOM    470  CA  LYS A  60      52.533 -19.686-210.610  1.00 80.26           C  
ANISOU  470  CA  LYS A  60    11721  10823   7952  -5038    -41   -573       C  
ATOM    471  C   LYS A  60      51.795 -20.724-211.467  1.00 87.35           C  
ANISOU  471  C   LYS A  60    12668  11474   9046  -4664   -282   -300       C  
ATOM    472  O   LYS A  60      51.664 -20.570-212.686  1.00 86.82           O  
ANISOU  472  O   LYS A  60    12799  11085   9103  -4505   -264   -264       O  
ATOM    473  CB  LYS A  60      54.030 -19.988-210.576  1.00 90.75           C  
ANISOU  473  CB  LYS A  60    12839  12542   9098  -5189    -75   -631       C  
ATOM    474  CG  LYS A  60      54.604 -20.524-211.872  1.00 98.19           C  
ANISOU  474  CG  LYS A  60    13844  13339  10126  -4990   -186   -512       C  
ATOM    475  CD  LYS A  60      55.952 -21.167-211.622  1.00106.75           C  
ANISOU  475  CD  LYS A  60    14648  14889  11023  -5072   -285   -489       C  
ATOM    476  CE  LYS A  60      55.850 -22.202-210.513  1.00110.65           C  
ANISOU  476  CE  LYS A  60    14841  15775  11428  -5004   -472   -311       C  
ATOM    477  NZ  LYS A  60      56.780 -23.338-210.736  1.00111.38           N  
ANISOU  477  NZ  LYS A  60    14715  16150  11455  -4850   -648   -116       N  
ATOM    478  N   ASP A  61      51.292 -21.774-210.828  1.00 85.71           N  
ANISOU  478  N   ASP A  61    12280  11426   8861  -4532   -491   -117       N  
ATOM    479  CA  ASP A  61      50.594 -22.830-211.563  1.00 77.81           C  
ANISOU  479  CA  ASP A  61    11310  10217   8036  -4216   -698    115       C  
ATOM    480  C   ASP A  61      49.102 -22.851-211.307  1.00 77.20           C  
ANISOU  480  C   ASP A  61    11319   9930   8083  -4089   -731    187       C  
ATOM    481  O   ASP A  61      48.416 -23.774-211.736  1.00 88.89           O  
ANISOU  481  O   ASP A  61    12795  11285   9693  -3863   -896    360       O  
ATOM    482  CB  ASP A  61      51.185 -24.188-211.218  1.00 72.21           C  
ANISOU  482  CB  ASP A  61    10346   9807   7284  -4121   -897    299       C  
ATOM    483  CG  ASP A  61      52.622 -24.307-211.650  1.00 84.45           C  
ANISOU  483  CG  ASP A  61    11807  11556   8723  -4187   -889    268       C  
ATOM    484  OD1 ASP A  61      52.921 -23.924-212.799  1.00 86.33           O  
ANISOU  484  OD1 ASP A  61    12220  11555   9026  -4150   -835    209       O  
ATOM    485  OD2 ASP A  61      53.458 -24.747-210.836  1.00 86.24           O  
ANISOU  485  OD2 ASP A  61    11782  12202   8783  -4274   -927    305       O  
ATOM    486  N   LEU A  62      48.584 -21.838-210.624  1.00 77.23           N  
ANISOU  486  N   LEU A  62    11403   9896   8046  -4243   -557     46       N  
ATOM    487  CA  LEU A  62      47.155 -21.823-210.354  1.00 78.33           C  
ANISOU  487  CA  LEU A  62    11616   9853   8291  -4118   -582    118       C  
ATOM    488  C   LEU A  62      46.444 -20.694-211.090  1.00 78.35           C  
ANISOU  488  C   LEU A  62    11900   9491   8376  -4059   -385     41       C  
ATOM    489  O   LEU A  62      46.994 -19.614-211.286  1.00 81.85           O  
ANISOU  489  O   LEU A  62    12482   9850   8766  -4213   -147   -128       O  
ATOM    490  CB  LEU A  62      46.903 -21.738-208.851  1.00 73.46           C  
ANISOU  490  CB  LEU A  62    10844   9494   7572  -4290   -560     68       C  
ATOM    491  CG  LEU A  62      47.725 -22.748-208.043  1.00 67.31           C  
ANISOU  491  CG  LEU A  62     9768   9135   6673  -4347   -716    154       C  
ATOM    492  CD1 LEU A  62      47.466 -22.604-206.570  1.00 73.82           C  
ANISOU  492  CD1 LEU A  62    10429  10241   7378  -4517   -685    103       C  
ATOM    493  CD2 LEU A  62      47.427 -24.145-208.484  1.00 65.03           C  
ANISOU  493  CD2 LEU A  62     9401   8802   6504  -4080   -947    398       C  
ATOM    494  N   PHE A  63      45.218 -20.984-211.507  1.00 73.61           N  
ANISOU  494  N   PHE A  63    11376   8691   7902  -3826   -472    174       N  
ATOM    495  CA  PHE A  63      44.399 -20.077-212.295  1.00 82.23           C  
ANISOU  495  CA  PHE A  63    12709   9465   9069  -3688   -310    167       C  
ATOM    496  C   PHE A  63      42.984 -20.084-211.751  1.00 86.00           C  
ANISOU  496  C   PHE A  63    13191   9886   9598  -3581   -336    243       C  
ATOM    497  O   PHE A  63      42.347 -21.130-211.747  1.00 82.27           O  
ANISOU  497  O   PHE A  63    12598   9477   9184  -3439   -562    381       O  
ATOM    498  CB  PHE A  63      44.368 -20.498-213.768  1.00 71.26           C  
ANISOU  498  CB  PHE A  63    11397   7913   7764  -3453   -410    278       C  
ATOM    499  CG  PHE A  63      45.722 -20.633-214.391  1.00 74.78           C  
ANISOU  499  CG  PHE A  63    11830   8413   8171  -3528   -415    226       C  
ATOM    500  CD1 PHE A  63      46.507 -21.752-214.156  1.00 73.70           C  
ANISOU  500  CD1 PHE A  63    11489   8508   8006  -3571   -613    278       C  
ATOM    501  CD2 PHE A  63      46.209 -19.649-215.225  1.00 77.75           C  
ANISOU  501  CD2 PHE A  63    12400   8602   8537  -3541   -204    137       C  
ATOM    502  CE1 PHE A  63      47.756 -21.877-214.732  1.00 74.21           C  
ANISOU  502  CE1 PHE A  63    11534   8636   8026  -3630   -615    238       C  
ATOM    503  CE2 PHE A  63      47.455 -19.769-215.805  1.00 72.76           C  
ANISOU  503  CE2 PHE A  63    11754   8025   7866  -3616   -209     84       C  
ATOM    504  CZ  PHE A  63      48.233 -20.878-215.558  1.00 68.24           C  
ANISOU  504  CZ  PHE A  63    10968   7702   7258  -3663   -421    132       C  
ATOM    505  N   PRO A  64      42.489 -18.926-211.288  1.00 82.53           N  
ANISOU  505  N   PRO A  64    12895   9323   9141  -3654    -87    147       N  
ATOM    506  CA  PRO A  64      41.109 -18.815-210.806  1.00 82.89           C  
ANISOU  506  CA  PRO A  64    12960   9305   9230  -3539    -87    221       C  
ATOM    507  C   PRO A  64      40.102 -19.450-211.768  1.00 72.18           C  
ANISOU  507  C   PRO A  64    11612   7850   7963  -3229   -260    403       C  
ATOM    508  O   PRO A  64      40.206 -19.219-212.968  1.00 70.14           O  
ANISOU  508  O   PRO A  64    11472   7444   7734  -3075   -216    445       O  
ATOM    509  CB  PRO A  64      40.913 -17.305-210.704  1.00 89.14           C  
ANISOU  509  CB  PRO A  64    13982   9881  10006  -3605    278    101       C  
ATOM    510  CG  PRO A  64      42.261 -16.813-210.299  1.00 89.23           C  
ANISOU  510  CG  PRO A  64    13990   9989   9924  -3914    438   -101       C  
ATOM    511  CD  PRO A  64      43.250 -17.689-211.046  1.00 89.79           C  
ANISOU  511  CD  PRO A  64    13952  10178   9987  -3885    228    -54       C  
ATOM    512  N   TYR A  65      39.157 -20.235-211.250  1.00 71.57           N  
ANISOU  512  N   TYR A  65    11402   7876   7917  -3152   -444    500       N  
ATOM    513  CA  TYR A  65      38.285 -21.046-212.106  1.00 68.22           C  
ANISOU  513  CA  TYR A  65    10934   7428   7557  -2908   -634    645       C  
ATOM    514  C   TYR A  65      37.513 -20.211-213.104  1.00 74.85           C  
ANISOU  514  C   TYR A  65    11946   8085   8407  -2684   -489    701       C  
ATOM    515  O   TYR A  65      37.706 -20.360-214.308  1.00 82.63           O  
ANISOU  515  O   TYR A  65    12974   9014   9406  -2542   -526    749       O  
ATOM    516  CB  TYR A  65      37.312 -21.880-211.267  1.00 63.12           C  
ANISOU  516  CB  TYR A  65    10131   6915   6936  -2892   -805    715       C  
ATOM    517  CG  TYR A  65      36.264 -22.634-212.074  1.00 60.52           C  
ANISOU  517  CG  TYR A  65     9753   6583   6658  -2674   -966    829       C  
ATOM    518  CD1 TYR A  65      36.616 -23.391-213.177  1.00 58.81           C  
ANISOU  518  CD1 TYR A  65     9506   6364   6474  -2584  -1091    868       C  
ATOM    519  CD2 TYR A  65      34.922 -22.604-211.714  1.00 68.86           C  
ANISOU  519  CD2 TYR A  65    10781   7664   7718  -2576   -986    884       C  
ATOM    520  CE1 TYR A  65      35.657 -24.081-213.917  1.00 64.18           C  
ANISOU  520  CE1 TYR A  65    10126   7077   7182  -2421  -1222    940       C  
ATOM    521  CE2 TYR A  65      33.951 -23.299-212.446  1.00 71.11           C  
ANISOU  521  CE2 TYR A  65    10998   7997   8025  -2404  -1126    965       C  
ATOM    522  CZ  TYR A  65      34.327 -24.041-213.549  1.00 70.26           C  
ANISOU  522  CZ  TYR A  65    10856   7899   7942  -2338  -1241    983       C  
ATOM    523  OH  TYR A  65      33.375 -24.741-214.294  1.00 66.95           O  
ANISOU  523  OH  TYR A  65    10353   7560   7526  -2202  -1365   1031       O  
ATOM    524  N   LYS A  66      36.646 -19.336-212.611  1.00 74.70           N  
ANISOU  524  N   LYS A  66    12020   7989   8375  -2639   -314    705       N  
ATOM    525  CA  LYS A  66      35.795 -18.535-213.486  1.00 89.59           C  
ANISOU  525  CA  LYS A  66    14056   9729  10256  -2380   -156    799       C  
ATOM    526  C   LYS A  66      36.583 -17.724-214.530  1.00 94.52           C  
ANISOU  526  C   LYS A  66    14865  10178  10871  -2318     48    780       C  
ATOM    527  O   LYS A  66      36.293 -17.787-215.733  1.00 91.52           O  
ANISOU  527  O   LYS A  66    14515   9774  10486  -2084     16    887       O  
ATOM    528  CB  LYS A  66      34.933 -17.604-212.634  1.00 93.96           C  
ANISOU  528  CB  LYS A  66    14700  10205  10794  -2368     60    797       C  
ATOM    529  CG  LYS A  66      33.788 -18.318-211.938  1.00 91.83           C  
ANISOU  529  CG  LYS A  66    14267  10094  10530  -2323   -134    866       C  
ATOM    530  CD  LYS A  66      33.458 -17.677-210.597  1.00101.15           C  
ANISOU  530  CD  LYS A  66    15482  11251  11700  -2473     27    792       C  
ATOM    531  CE  LYS A  66      32.187 -16.837-210.677  1.00103.57           C  
ANISOU  531  CE  LYS A  66    15899  11459  11993  -2242    215    896       C  
ATOM    532  NZ  LYS A  66      32.105 -15.839-209.577  1.00 98.97           N  
ANISOU  532  NZ  LYS A  66    15436  10763  11407  -2392    492    798       N  
ATOM    533  N   GLU A  67      37.586 -16.982-214.062  1.00 94.97           N  
ANISOU  533  N   GLU A  67    15033  10137  10916  -2540    262    635       N  
ATOM    534  CA  GLU A  67      38.380 -16.088-214.917  1.00 93.27           C  
ANISOU  534  CA  GLU A  67    15017   9728  10695  -2520    511    592       C  
ATOM    535  C   GLU A  67      39.030 -16.814-216.078  1.00 76.50           C  
ANISOU  535  C   GLU A  67    12835   7653   8578  -2435    320    639       C  
ATOM    536  O   GLU A  67      39.089 -16.302-217.190  1.00 85.89           O  
ANISOU  536  O   GLU A  67    14160   8708   9766  -2251    449    704       O  
ATOM    537  CB  GLU A  67      39.471 -15.378-214.097  1.00 93.74           C  
ANISOU  537  CB  GLU A  67    15158   9734  10727  -2851    741    381       C  
ATOM    538  CG  GLU A  67      39.991 -14.080-214.706  1.00102.12           C  
ANISOU  538  CG  GLU A  67    16488  10525  11788  -2848   1132    315       C  
ATOM    539  CD  GLU A  67      41.353 -13.670-214.154  1.00110.18           C  
ANISOU  539  CD  GLU A  67    17538  11560  12763  -3217   1294     75       C  
ATOM    540  OE1 GLU A  67      41.631 -14.004-212.981  1.00101.93           O  
ANISOU  540  OE1 GLU A  67    16340  10717  11671  -3481   1206    -50       O  
ATOM    541  OE2 GLU A  67      42.131 -12.998-214.882  1.00110.26           O  
ANISOU  541  OE2 GLU A  67    17717  11403  12773  -3245   1519      8       O  
ATOM    542  N   TYR A  68      39.545 -18.000-215.804  1.00 67.49           N  
ANISOU  542  N   TYR A  68    11495   6704   7444  -2565     32    610       N  
ATOM    543  CA  TYR A  68      40.306 -18.728-216.796  1.00 75.63           C  
ANISOU  543  CA  TYR A  68    12470   7779   8487  -2525   -134    632       C  
ATOM    544  C   TYR A  68      39.522 -19.931-217.305  1.00 73.19           C  
ANISOU  544  C   TYR A  68    12001   7601   8208  -2353   -422    754       C  
ATOM    545  O   TYR A  68      40.067 -20.807-217.985  1.00 70.44           O  
ANISOU  545  O   TYR A  68    11569   7317   7880  -2341   -597    768       O  
ATOM    546  CB  TYR A  68      41.651 -19.167-216.217  1.00 76.95           C  
ANISOU  546  CB  TYR A  68    12542   8063   8634  -2797   -201    508       C  
ATOM    547  CG  TYR A  68      42.667 -18.043-216.100  1.00 78.80           C  
ANISOU  547  CG  TYR A  68    12931   8187   8822  -2983     85    357       C  
ATOM    548  CD1 TYR A  68      43.447 -17.667-217.193  1.00 75.47           C  
ANISOU  548  CD1 TYR A  68    12632   7644   8400  -2938    185    337       C  
ATOM    549  CD2 TYR A  68      42.867 -17.375-214.899  1.00 77.53           C  
ANISOU  549  CD2 TYR A  68    12788   8057   8613  -3225    266    216       C  
ATOM    550  CE1 TYR A  68      44.385 -16.641-217.097  1.00 74.85           C  
ANISOU  550  CE1 TYR A  68    12701   7459   8279  -3131    471    179       C  
ATOM    551  CE2 TYR A  68      43.809 -16.348-214.792  1.00 82.99           C  
ANISOU  551  CE2 TYR A  68    13619   8659   9254  -3436    557     42       C  
ATOM    552  CZ  TYR A  68      44.564 -15.988-215.899  1.00 83.90           C  
ANISOU  552  CZ  TYR A  68    13865   8638   9376  -3389    663     23       C  
ATOM    553  OH  TYR A  68      45.497 -14.977-215.808  1.00 82.45           O  
ANISOU  553  OH  TYR A  68    13825   8360   9144  -3616    972   -165       O  
ATOM    554  N   LYS A  69      38.230 -19.948-216.998  1.00 71.28           N  
ANISOU  554  N   LYS A  69    11720   7398   7964  -2227   -451    832       N  
ATOM    555  CA  LYS A  69      37.382 -21.071-217.361  1.00 69.42           C  
ANISOU  555  CA  LYS A  69    11322   7308   7745  -2104   -700    917       C  
ATOM    556  C   LYS A  69      37.414 -21.445-218.832  1.00 70.36           C  
ANISOU  556  C   LYS A  69    11434   7445   7855  -1931   -783    974       C  
ATOM    557  O   LYS A  69      37.672 -22.587-219.189  1.00 83.07           O  
ANISOU  557  O   LYS A  69    12917   9149   9497  -1968   -986    965       O  
ATOM    558  CB  LYS A  69      35.941 -20.791-216.975  1.00 70.81           C  
ANISOU  558  CB  LYS A  69    11479   7528   7897  -1969   -672    993       C  
ATOM    559  CG  LYS A  69      35.033 -21.925-217.385  1.00 74.58           C  
ANISOU  559  CG  LYS A  69    11782   8180   8377  -1866   -910   1054       C  
ATOM    560  CD  LYS A  69      33.757 -21.887-216.594  1.00 82.56           C  
ANISOU  560  CD  LYS A  69    12726   9276   9368  -1819   -923   1098       C  
ATOM    561  CE  LYS A  69      32.729 -22.824-217.174  1.00 80.05           C  
ANISOU  561  CE  LYS A  69    12246   9145   9025  -1702  -1112   1147       C  
ATOM    562  NZ  LYS A  69      31.402 -22.553-216.573  1.00 87.66           N  
ANISOU  562  NZ  LYS A  69    13160  10201   9944  -1613  -1089   1203       N  
ATOM    563  N   ASP A  70      37.141 -20.494-219.698  1.00 71.69           N  
ANISOU  563  N   ASP A  70    11738   7526   7975  -1735   -609   1037       N  
ATOM    564  CA  ASP A  70      36.901 -20.870-221.075  1.00 81.27           C  
ANISOU  564  CA  ASP A  70    12908   8819   9152  -1543   -701   1105       C  
ATOM    565  C   ASP A  70      38.185 -21.037-221.875  1.00 81.36           C  
ANISOU  565  C   ASP A  70    12968   8758   9185  -1605   -713   1052       C  
ATOM    566  O   ASP A  70      38.174 -21.630-222.945  1.00 87.28           O  
ANISOU  566  O   ASP A  70    13650   9595   9917  -1506   -835   1078       O  
ATOM    567  CB  ASP A  70      35.962 -19.865-221.722  1.00 90.37           C  
ANISOU  567  CB  ASP A  70    14152   9965  10221  -1259   -519   1233       C  
ATOM    568  CG  ASP A  70      34.806 -19.494-220.806  1.00 97.98           C  
ANISOU  568  CG  ASP A  70    15096  10969  11163  -1203   -456   1286       C  
ATOM    569  OD1 ASP A  70      34.652 -20.150-219.757  1.00 92.06           O  
ANISOU  569  OD1 ASP A  70    14241  10277  10461  -1386   -591   1219       O  
ATOM    570  OD2 ASP A  70      34.031 -18.579-221.145  1.00104.99           O  
ANISOU  570  OD2 ASP A  70    16068  11843  11981   -961   -268   1409       O  
ATOM    571  N   LYS A  71      39.304 -20.569-221.344  1.00 76.67           N  
ANISOU  571  N   LYS A  71    12477   8032   8622  -1788   -593    964       N  
ATOM    572  CA  LYS A  71      40.582 -20.934-221.942  1.00 72.72           C  
ANISOU  572  CA  LYS A  71    11985   7500   8143  -1883   -644    902       C  
ATOM    573  C   LYS A  71      40.926 -22.399-221.589  1.00 79.71           C  
ANISOU  573  C   LYS A  71    12683   8523   9082  -2023   -905    867       C  
ATOM    574  O   LYS A  71      41.647 -23.080-222.326  1.00 81.44           O  
ANISOU  574  O   LYS A  71    12859   8760   9322  -2035  -1010    852       O  
ATOM    575  CB  LYS A  71      41.679 -19.969-221.485  1.00 78.02           C  
ANISOU  575  CB  LYS A  71    12808   8024   8810  -2051   -420    804       C  
ATOM    576  CG  LYS A  71      43.070 -20.297-222.011  1.00 94.75           C  
ANISOU  576  CG  LYS A  71    14928  10132  10939  -2166   -464    733       C  
ATOM    577  CD  LYS A  71      43.310 -19.632-223.367  1.00105.00           C  
ANISOU  577  CD  LYS A  71    16373  11306  12214  -1994   -329    775       C  
ATOM    578  CE  LYS A  71      44.581 -20.140-224.042  1.00108.34           C  
ANISOU  578  CE  LYS A  71    16774  11741  12649  -2080   -416    719       C  
ATOM    579  NZ  LYS A  71      44.753 -21.624-223.898  1.00111.98           N  
ANISOU  579  NZ  LYS A  71    17031  12367  13151  -2148   -705    720       N  
ATOM    580  N   PHE A  72      40.368 -22.904-220.492  1.00 82.40           N  
ANISOU  580  N   PHE A  72    12913   8949   9445  -2110   -993    866       N  
ATOM    581  CA  PHE A  72      40.809 -24.203-219.975  1.00 75.65           C  
ANISOU  581  CA  PHE A  72    11901   8197   8645  -2246  -1182    847       C  
ATOM    582  C   PHE A  72      39.727 -25.256-219.769  1.00 70.73           C  
ANISOU  582  C   PHE A  72    11133   7682   8058  -2202  -1346    892       C  
ATOM    583  O   PHE A  72      40.036 -26.426-219.552  1.00 74.42           O  
ANISOU  583  O   PHE A  72    11485   8206   8584  -2280  -1476    892       O  
ATOM    584  CB  PHE A  72      41.543 -23.984-218.659  1.00 71.20           C  
ANISOU  584  CB  PHE A  72    11318   7662   8072  -2451  -1124    791       C  
ATOM    585  CG  PHE A  72      42.797 -23.198-218.816  1.00 80.34           C  
ANISOU  585  CG  PHE A  72    12581   8755   9189  -2555   -978    713       C  
ATOM    586  CD1 PHE A  72      43.683 -23.498-219.833  1.00 77.39           C  
ANISOU  586  CD1 PHE A  72    12227   8351   8825  -2527  -1015    707       C  
ATOM    587  CD2 PHE A  72      43.080 -22.141-217.977  1.00 81.74           C  
ANISOU  587  CD2 PHE A  72    12841   8902   9315  -2694   -786    631       C  
ATOM    588  CE1 PHE A  72      44.839 -22.776-219.996  1.00 77.79           C  
ANISOU  588  CE1 PHE A  72    12371   8352   8833  -2632   -876    626       C  
ATOM    589  CE2 PHE A  72      44.235 -21.405-218.140  1.00 77.27           C  
ANISOU  589  CE2 PHE A  72    12371   8285   8703  -2819   -628    532       C  
ATOM    590  CZ  PHE A  72      45.117 -21.724-219.153  1.00 76.15           C  
ANISOU  590  CZ  PHE A  72    12243   8121   8570  -2785   -678    533       C  
ATOM    591  N   GLY A  73      38.466 -24.845-219.844  1.00 66.47           N  
ANISOU  591  N   GLY A  73    10601   7174   7483  -2074  -1318    932       N  
ATOM    592  CA  GLY A  73      37.363 -25.719-219.510  1.00 63.13           C  
ANISOU  592  CA  GLY A  73    10039   6868   7079  -2059  -1449    955       C  
ATOM    593  C   GLY A  73      36.844 -26.601-220.631  1.00 68.76           C  
ANISOU  593  C   GLY A  73    10661   7674   7790  -1971  -1568    952       C  
ATOM    594  O   GLY A  73      35.804 -27.238-220.484  1.00 68.79           O  
ANISOU  594  O   GLY A  73    10553   7792   7793  -1960  -1652    952       O  
ATOM    595  N   LYS A  74      37.569 -26.649-221.743  1.00 77.81           N  
ANISOU  595  N   LYS A  74    11850   8784   8929  -1928  -1567    935       N  
ATOM    596  CA  LYS A  74      37.168 -27.456-222.888  1.00 73.20           C  
ANISOU  596  CA  LYS A  74    11178   8305   8330  -1866  -1663    908       C  
ATOM    597  C   LYS A  74      37.436 -28.935-222.643  1.00 72.46           C  
ANISOU  597  C   LYS A  74    10979   8215   8339  -2015  -1774    856       C  
ATOM    598  O   LYS A  74      38.458 -29.308-222.058  1.00 82.76           O  
ANISOU  598  O   LYS A  74    12302   9421   9720  -2126  -1774    859       O  
ATOM    599  CB  LYS A  74      37.903 -26.990-224.134  1.00 80.13           C  
ANISOU  599  CB  LYS A  74    12141   9139   9166  -1773  -1613    909       C  
ATOM    600  CG  LYS A  74      37.902 -25.481-224.307  1.00 87.91           C  
ANISOU  600  CG  LYS A  74    13271  10059  10072  -1630  -1446    974       C  
ATOM    601  CD  LYS A  74      38.649 -25.069-225.563  1.00 99.06           C  
ANISOU  601  CD  LYS A  74    14768  11423  11446  -1534  -1389    981       C  
ATOM    602  CE  LYS A  74      39.109 -23.616-225.487  1.00101.63           C  
ANISOU  602  CE  LYS A  74    15283  11593  11739  -1459  -1173   1029       C  
ATOM    603  NZ  LYS A  74      37.964 -22.669-225.404  1.00 99.73           N  
ANISOU  603  NZ  LYS A  74    15082  11396  11413  -1268  -1043   1126       N  
ATOM    604  N   SER A  75      36.511 -29.769-223.097  1.00 61.33           N  
ANISOU  604  N   SER A  75     9453   6932   6919  -2014  -1848    808       N  
ATOM    605  CA  SER A  75      36.596 -31.214-222.896  1.00 74.41           C  
ANISOU  605  CA  SER A  75    11022   8570   8682  -2154  -1907    751       C  
ATOM    606  C   SER A  75      37.907 -31.794-223.420  1.00 70.93           C  
ANISOU  606  C   SER A  75    10625   8006   8319  -2207  -1901    733       C  
ATOM    607  O   SER A  75      38.508 -31.279-224.358  1.00 74.35           O  
ANISOU  607  O   SER A  75    11122   8421   8705  -2136  -1882    727       O  
ATOM    608  CB  SER A  75      35.414 -31.904-223.572  1.00 78.56           C  
ANISOU  608  CB  SER A  75    11423   9268   9160  -2161  -1953    664       C  
ATOM    609  OG  SER A  75      35.668 -33.280-223.757  1.00 86.47           O  
ANISOU  609  OG  SER A  75    12372  10214  10267  -2298  -1963    583       O  
ATOM    610  N   ASN A  76      38.350 -32.874-222.805  1.00 70.60           N  
ANISOU  610  N   ASN A  76    10549   7881   8394  -2318  -1902    738       N  
ATOM    611  CA  ASN A  76      39.607 -33.487-223.186  1.00 69.36           C  
ANISOU  611  CA  ASN A  76    10428   7611   8314  -2354  -1881    744       C  
ATOM    612  C   ASN A  76      39.573 -34.919-222.683  1.00 67.98           C  
ANISOU  612  C   ASN A  76    10191   7371   8266  -2450  -1855    745       C  
ATOM    613  O   ASN A  76      38.851 -35.203-221.733  1.00 73.75           O  
ANISOU  613  O   ASN A  76    10869   8128   9024  -2492  -1854    770       O  
ATOM    614  CB  ASN A  76      40.773 -32.677-222.613  1.00 84.01           C  
ANISOU  614  CB  ASN A  76    12357   9411  10151  -2341  -1852    824       C  
ATOM    615  CG  ASN A  76      42.014 -33.497-222.417  1.00 88.39           C  
ANISOU  615  CG  ASN A  76    12906   9886  10791  -2389  -1828    872       C  
ATOM    616  OD1 ASN A  76      42.708 -33.844-223.373  1.00 96.93           O  
ANISOU  616  OD1 ASN A  76    14018  10913  11897  -2373  -1819    844       O  
ATOM    617  ND2 ASN A  76      42.299 -33.825-221.172  1.00 78.25           N  
ANISOU  617  ND2 ASN A  76    11575   8614   9543  -2435  -1812    957       N  
ATOM    618  N   LYS A  77      40.314 -35.829-223.317  1.00 77.48           N  
ANISOU  618  N   LYS A  77    11408   8479   9552  -2481  -1814    722       N  
ATOM    619  CA  LYS A  77      40.116 -37.265-223.077  1.00 79.43           C  
ANISOU  619  CA  LYS A  77    11614   8638   9928  -2565  -1739    705       C  
ATOM    620  C   LYS A  77      40.965 -37.917-221.976  1.00 81.04           C  
ANISOU  620  C   LYS A  77    11818   8741  10233  -2564  -1670    853       C  
ATOM    621  O   LYS A  77      40.817 -39.123-221.720  1.00 81.01           O  
ANISOU  621  O   LYS A  77    11796   8635  10348  -2613  -1569    865       O  
ATOM    622  CB  LYS A  77      40.350 -38.046-224.372  1.00 91.85           C  
ANISOU  622  CB  LYS A  77    13203  10149  11547  -2606  -1688    590       C  
ATOM    623  CG  LYS A  77      39.601 -37.507-225.561  1.00 92.82           C  
ANISOU  623  CG  LYS A  77    13297  10421  11549  -2599  -1749    450       C  
ATOM    624  CD  LYS A  77      39.620 -38.531-226.673  1.00 96.18           C  
ANISOU  624  CD  LYS A  77    13709  10809  12027  -2690  -1677    304       C  
ATOM    625  CE  LYS A  77      38.752 -38.103-227.851  1.00102.99           C  
ANISOU  625  CE  LYS A  77    14501  11891  12740  -2693  -1737    155       C  
ATOM    626  NZ  LYS A  77      38.794 -39.096-228.964  1.00 94.68           N  
ANISOU  626  NZ  LYS A  77    13422  10829  11722  -2812  -1657    -17       N  
ATOM    627  N   ARG A  78      41.858 -37.150-221.349  1.00 67.55           N  
ANISOU  627  N   ARG A  78    10124   7073   8469  -2510  -1702    965       N  
ATOM    628  CA  ARG A  78      42.672 -37.672-220.247  1.00 66.46           C  
ANISOU  628  CA  ARG A  78     9949   6920   8382  -2491  -1644   1124       C  
ATOM    629  C   ARG A  78      41.751 -38.208-219.137  1.00 68.32           C  
ANISOU  629  C   ARG A  78    10123   7169   8667  -2526  -1614   1173       C  
ATOM    630  O   ARG A  78      40.763 -37.566-218.772  1.00 65.48           O  
ANISOU  630  O   ARG A  78     9744   6890   8247  -2555  -1678   1120       O  
ATOM    631  CB  ARG A  78      43.612 -36.587-219.694  1.00 65.60           C  
ANISOU  631  CB  ARG A  78     9836   6927   8161  -2463  -1690   1197       C  
ATOM    632  CG  ARG A  78      44.554 -35.958-220.711  1.00 78.05           C  
ANISOU  632  CG  ARG A  78    11479   8494   9681  -2437  -1708   1149       C  
ATOM    633  CD  ARG A  78      45.610 -36.935-221.182  1.00 78.68           C  
ANISOU  633  CD  ARG A  78    11561   8494   9839  -2399  -1641   1211       C  
ATOM    634  NE  ARG A  78      46.402 -37.415-220.066  1.00 73.00           N  
ANISOU  634  NE  ARG A  78    10762   7851   9125  -2367  -1589   1381       N  
ATOM    635  CZ  ARG A  78      47.528 -36.842-219.661  1.00 75.52           C  
ANISOU  635  CZ  ARG A  78    11041   8311   9342  -2354  -1600   1451       C  
ATOM    636  NH1 ARG A  78      47.977 -35.773-220.298  1.00 76.02           N  
ANISOU  636  NH1 ARG A  78    11162   8407   9313  -2383  -1647   1353       N  
ATOM    637  NH2 ARG A  78      48.198 -37.336-218.619  1.00 72.25           N  
ANISOU  637  NH2 ARG A  78    10520   8026   8907  -2311  -1550   1618       N  
ATOM    638  N   LYS A  79      42.062 -39.395-218.627  1.00 67.79           N  
ANISOU  638  N   LYS A  79    10030   7014   8711  -2511  -1499   1283       N  
ATOM    639  CA  LYS A  79      41.173 -40.078-217.701  1.00 68.24           C  
ANISOU  639  CA  LYS A  79    10042   7050   8837  -2543  -1439   1326       C  
ATOM    640  C   LYS A  79      40.837 -39.207-216.485  1.00 72.13           C  
ANISOU  640  C   LYS A  79    10470   7706   9229  -2543  -1527   1391       C  
ATOM    641  O   LYS A  79      41.729 -38.671-215.814  1.00 63.68           O  
ANISOU  641  O   LYS A  79     9360   6756   8079  -2499  -1554   1503       O  
ATOM    642  CB  LYS A  79      41.795 -41.410-217.250  1.00 92.31           C  
ANISOU  642  CB  LYS A  79    13084   9975  12015  -2487  -1265   1485       C  
ATOM    643  CG  LYS A  79      41.926 -42.484-218.354  1.00108.39           C  
ANISOU  643  CG  LYS A  79    15197  11801  14184  -2512  -1120   1405       C  
ATOM    644  CD  LYS A  79      41.462 -43.881-217.878  1.00105.26           C  
ANISOU  644  CD  LYS A  79    14817  11227  13950  -2531   -904   1463       C  
ATOM    645  CE  LYS A  79      42.426 -44.988-218.309  1.00103.21           C  
ANISOU  645  CE  LYS A  79    14623  10771  13821  -2457   -690   1562       C  
ATOM    646  NZ  LYS A  79      41.838 -45.908-219.334  1.00110.23           N  
ANISOU  646  NZ  LYS A  79    15598  11445  14840  -2587   -527   1361       N  
ATOM    647  N   GLY A  80      39.546 -39.053-216.215  1.00 66.31           N  
ANISOU  647  N   GLY A  80     9715   6996   8486  -2603  -1564   1308       N  
ATOM    648  CA  GLY A  80      39.108 -38.204-215.122  1.00 61.57           C  
ANISOU  648  CA  GLY A  80     9062   6538   7793  -2611  -1639   1349       C  
ATOM    649  C   GLY A  80      38.879 -36.719-215.417  1.00 60.88           C  
ANISOU  649  C   GLY A  80     9006   6552   7573  -2615  -1745   1256       C  
ATOM    650  O   GLY A  80      38.281 -36.019-214.606  1.00 64.65           O  
ANISOU  650  O   GLY A  80     9455   7124   7985  -2634  -1786   1260       O  
ATOM    651  N   PHE A  81      39.330 -36.214-216.554  1.00 72.37           N  
ANISOU  651  N   PHE A  81    10528   7979   8989  -2590  -1770   1179       N  
ATOM    652  CA  PHE A  81      39.185 -34.773-216.830  1.00 51.95           C  
ANISOU  652  CA  PHE A  81     7991   5464   6283  -2571  -1826   1114       C  
ATOM    653  C   PHE A  81      37.739 -34.331-216.947  1.00 73.05           C  
ANISOU  653  C   PHE A  81    10657   8186   8913  -2569  -1865   1034       C  
ATOM    654  O   PHE A  81      37.329 -33.367-216.297  1.00 61.23           O  
ANISOU  654  O   PHE A  81     9166   6759   7340  -2562  -1878   1043       O  
ATOM    655  CB  PHE A  81      39.897 -34.400-218.120  1.00 53.76           C  
ANISOU  655  CB  PHE A  81     8296   5646   6485  -2531  -1829   1055       C  
ATOM    656  CG  PHE A  81      39.957 -32.911-218.381  1.00 59.32           C  
ANISOU  656  CG  PHE A  81     9073   6393   7074  -2497  -1840   1014       C  
ATOM    657  CD1 PHE A  81      40.934 -32.127-217.786  1.00 51.05           C  
ANISOU  657  CD1 PHE A  81     8050   5381   5965  -2524  -1807   1051       C  
ATOM    658  CD2 PHE A  81      39.051 -32.304-219.236  1.00 62.63           C  
ANISOU  658  CD2 PHE A  81     9530   6830   7436  -2437  -1858    939       C  
ATOM    659  CE1 PHE A  81      41.021 -30.741-218.065  1.00 60.30           C  
ANISOU  659  CE1 PHE A  81     9315   6553   7043  -2506  -1767   1000       C  
ATOM    660  CE2 PHE A  81      39.105 -30.949-219.492  1.00 58.63           C  
ANISOU  660  CE2 PHE A  81     9108   6334   6833  -2379  -1824    925       C  
ATOM    661  CZ  PHE A  81      40.098 -30.160-218.904  1.00 51.00           C  
ANISOU  661  CZ  PHE A  81     8196   5351   5829  -2421  -1766    949       C  
ATOM    662  N   ASN A  82      36.977 -35.025-217.794  1.00 63.46           N  
ANISOU  662  N   ASN A  82     9423   6953   7736  -2579  -1869    947       N  
ATOM    663  CA  ASN A  82      35.596 -34.656-218.016  1.00 69.55           C  
ANISOU  663  CA  ASN A  82    10159   7825   8441  -2569  -1907    870       C  
ATOM    664  C   ASN A  82      34.791 -34.876-216.758  1.00 63.82           C  
ANISOU  664  C   ASN A  82     9371   7141   7738  -2616  -1909    911       C  
ATOM    665  O   ASN A  82      33.796 -34.197-216.531  1.00 64.79           O  
ANISOU  665  O   ASN A  82     9470   7366   7782  -2588  -1941    889       O  
ATOM    666  CB  ASN A  82      35.000 -35.444-219.185  1.00 67.47           C  
ANISOU  666  CB  ASN A  82     9858   7586   8191  -2602  -1904    745       C  
ATOM    667  CG  ASN A  82      35.570 -35.006-220.524  1.00 70.82           C  
ANISOU  667  CG  ASN A  82    10333   8017   8557  -2538  -1916    695       C  
ATOM    668  OD1 ASN A  82      35.825 -33.823-220.741  1.00 83.06           O  
ANISOU  668  OD1 ASN A  82    11940   9602  10015  -2441  -1935    732       O  
ATOM    669  ND2 ASN A  82      35.783 -35.960-221.423  1.00 62.22           N  
ANISOU  669  ND2 ASN A  82     9232   6884   7525  -2596  -1883    608       N  
ATOM    670  N   GLU A  83      35.237 -35.816-215.928  1.00 59.89           N  
ANISOU  670  N   GLU A  83     8845   6569   7342  -2670  -1863    987       N  
ATOM    671  CA  GLU A  83      34.599 -36.040-214.631  1.00 57.21           C  
ANISOU  671  CA  GLU A  83     8445   6268   7026  -2709  -1856   1048       C  
ATOM    672  C   GLU A  83      34.914 -34.870-213.696  1.00 60.58           C  
ANISOU  672  C   GLU A  83     8881   6773   7364  -2682  -1886   1119       C  
ATOM    673  O   GLU A  83      34.111 -34.500-212.840  1.00 64.23           O  
ANISOU  673  O   GLU A  83     9306   7308   7792  -2698  -1904   1131       O  
ATOM    674  CB  GLU A  83      35.045 -37.388-214.035  1.00 53.88           C  
ANISOU  674  CB  GLU A  83     7992   5745   6734  -2748  -1769   1135       C  
ATOM    675  CG  GLU A  83      34.458 -38.688-214.761  1.00 54.94           C  
ANISOU  675  CG  GLU A  83     8122   5776   6977  -2819  -1685   1036       C  
ATOM    676  CD  GLU A  83      35.182 -39.052-216.077  1.00 70.18           C  
ANISOU  676  CD  GLU A  83    10109   7616   8941  -2814  -1647    967       C  
ATOM    677  OE1 GLU A  83      36.178 -38.373-216.477  1.00 60.48           O  
ANISOU  677  OE1 GLU A  83     8924   6394   7660  -2744  -1690   1007       O  
ATOM    678  OE2 GLU A  83      34.745 -40.028-216.719  1.00 65.28           O  
ANISOU  678  OE2 GLU A  83     9489   6918   8398  -2895  -1560    858       O  
ATOM    679  N   GLY A  84      36.070 -34.254-213.891  1.00 57.67           N  
ANISOU  679  N   GLY A  84     8564   6394   6953  -2655  -1877   1149       N  
ATOM    680  CA  GLY A  84      36.468 -33.135-213.052  1.00 51.85           C  
ANISOU  680  CA  GLY A  84     7840   5735   6127  -2666  -1872   1182       C  
ATOM    681  C   GLY A  84      35.698 -31.879-213.392  1.00 73.13           C  
ANISOU  681  C   GLY A  84    10601   8453   8734  -2626  -1874   1108       C  
ATOM    682  O   GLY A  84      35.310 -31.099-212.514  1.00 61.12           O  
ANISOU  682  O   GLY A  84     9080   6989   7156  -2648  -1854   1116       O  
ATOM    683  N   LEU A  85      35.500 -31.673-214.687  1.00 71.83           N  
ANISOU  683  N   LEU A  85    10492   8249   8550  -2556  -1883   1046       N  
ATOM    684  CA  LEU A  85      34.674 -30.585-215.176  1.00 66.55           C  
ANISOU  684  CA  LEU A  85     9878   7614   7792  -2470  -1866   1006       C  
ATOM    685  C   LEU A  85      33.297 -30.650-214.533  1.00 71.61           C  
ANISOU  685  C   LEU A  85    10450   8341   8418  -2467  -1892   1007       C  
ATOM    686  O   LEU A  85      32.701 -29.634-214.161  1.00 67.07           O  
ANISOU  686  O   LEU A  85     9910   7801   7772  -2416  -1851   1017       O  
ATOM    687  CB  LEU A  85      34.545 -30.676-216.686  1.00 65.80           C  
ANISOU  687  CB  LEU A  85     9808   7519   7675  -2386  -1883    954       C  
ATOM    688  CG  LEU A  85      35.818 -30.388-217.471  1.00 69.76           C  
ANISOU  688  CG  LEU A  85    10394   7937   8176  -2366  -1851    948       C  
ATOM    689  CD1 LEU A  85      35.456 -30.141-218.939  1.00 69.63           C  
ANISOU  689  CD1 LEU A  85    10403   7956   8099  -2254  -1858    903       C  
ATOM    690  CD2 LEU A  85      36.522 -29.184-216.881  1.00 65.64           C  
ANISOU  690  CD2 LEU A  85     9965   7373   7603  -2377  -1767    972       C  
ATOM    691  N   TRP A  86      32.800 -31.871-214.408  1.00 63.85           N  
ANISOU  691  N   TRP A  86     9374   7379   7506  -2525  -1939    994       N  
ATOM    692  CA  TRP A  86      31.505 -32.091-213.818  1.00 72.41           C  
ANISOU  692  CA  TRP A  86    10380   8553   8581  -2542  -1965    983       C  
ATOM    693  C   TRP A  86      31.549 -31.678-212.354  1.00 75.17           C  
ANISOU  693  C   TRP A  86    10722   8909   8930  -2588  -1944   1050       C  
ATOM    694  O   TRP A  86      30.788 -30.809-211.930  1.00 77.69           O  
ANISOU  694  O   TRP A  86    11051   9287   9180  -2547  -1929   1053       O  
ATOM    695  CB  TRP A  86      31.082 -33.556-213.961  1.00 77.21           C  
ANISOU  695  CB  TRP A  86    10902   9156   9277  -2625  -1983    939       C  
ATOM    696  CG  TRP A  86      29.658 -33.792-213.567  1.00 84.62           C  
ANISOU  696  CG  TRP A  86    11752  10208  10190  -2653  -2006    899       C  
ATOM    697  CD1 TRP A  86      28.582 -33.838-214.396  1.00 78.91           C  
ANISOU  697  CD1 TRP A  86    10965   9628   9390  -2630  -2033    805       C  
ATOM    698  CD2 TRP A  86      29.151 -33.999-212.240  1.00 80.33           C  
ANISOU  698  CD2 TRP A  86    11161   9680   9681  -2709  -2005    949       C  
ATOM    699  NE1 TRP A  86      27.437 -34.062-213.670  1.00 70.89           N  
ANISOU  699  NE1 TRP A  86     9865   8712   8360  -2675  -2048    789       N  
ATOM    700  CE2 TRP A  86      27.761 -34.161-212.345  1.00 67.78           C  
ANISOU  700  CE2 TRP A  86     9488   8224   8042  -2722  -2031    878       C  
ATOM    701  CE3 TRP A  86      29.737 -34.062-210.978  1.00 85.69           C  
ANISOU  701  CE3 TRP A  86    11843  10304  10412  -2750  -1984   1048       C  
ATOM    702  CZ2 TRP A  86      26.953 -34.380-211.243  1.00 75.12           C  
ANISOU  702  CZ2 TRP A  86    10356   9200   8989  -2775  -2035    902       C  
ATOM    703  CZ3 TRP A  86      28.932 -34.285-209.884  1.00 80.74           C  
ANISOU  703  CZ3 TRP A  86    11150   9729   9798  -2797  -1989   1077       C  
ATOM    704  CH2 TRP A  86      27.557 -34.437-210.021  1.00 77.47           C  
ANISOU  704  CH2 TRP A  86    10671   9414   9349  -2809  -2014   1004       C  
ATOM    705  N   GLU A  87      32.453 -32.290-211.591  1.00 61.45           N  
ANISOU  705  N   GLU A  87     8960   7129   7259  -2664  -1933   1109       N  
ATOM    706  CA  GLU A  87      32.498 -32.081-210.147  1.00 64.99           C  
ANISOU  706  CA  GLU A  87     9365   7631   7696  -2724  -1919   1172       C  
ATOM    707  C   GLU A  87      32.685 -30.607-209.744  1.00 68.30           C  
ANISOU  707  C   GLU A  87     9854   8080   8016  -2719  -1867   1155       C  
ATOM    708  O   GLU A  87      32.123 -30.155-208.743  1.00 79.28           O  
ANISOU  708  O   GLU A  87    11219   9532   9373  -2753  -1850   1165       O  
ATOM    709  CB  GLU A  87      33.618 -32.921-209.521  1.00 55.82           C  
ANISOU  709  CB  GLU A  87     8152   6467   6591  -2776  -1902   1260       C  
ATOM    710  CG  GLU A  87      33.210 -34.351-209.218  1.00 56.90           C  
ANISOU  710  CG  GLU A  87     8212   6572   6835  -2797  -1899   1313       C  
ATOM    711  CD  GLU A  87      34.321 -35.120-208.546  1.00 66.67           C  
ANISOU  711  CD  GLU A  87     9394   7822   8114  -2804  -1855   1442       C  
ATOM    712  OE1 GLU A  87      35.478 -34.675-208.644  1.00 69.09           O  
ANISOU  712  OE1 GLU A  87     9716   8168   8366  -2795  -1845   1469       O  
ATOM    713  OE2 GLU A  87      34.036 -36.135-207.882  1.00 77.37           O  
ANISOU  713  OE2 GLU A  87    10685   9167   9545  -2811  -1818   1526       O  
ATOM    714  N   ILE A  88      33.464 -29.855-210.513  1.00 60.79           N  
ANISOU  714  N   ILE A  88     8999   7075   7024  -2686  -1821   1120       N  
ATOM    715  CA  ILE A  88      33.845 -28.515-210.081  1.00 68.19           C  
ANISOU  715  CA  ILE A  88    10018   8012   7880  -2715  -1723   1090       C  
ATOM    716  C   ILE A  88      32.640 -27.594-210.156  1.00 65.47           C  
ANISOU  716  C   ILE A  88     9733   7657   7487  -2630  -1671   1069       C  
ATOM    717  O   ILE A  88      32.577 -26.570-209.468  1.00 73.15           O  
ANISOU  717  O   ILE A  88    10764   8625   8406  -2666  -1566   1047       O  
ATOM    718  CB  ILE A  88      35.028 -27.962-210.921  1.00 59.08           C  
ANISOU  718  CB  ILE A  88     8962   6788   6698  -2709  -1661   1053       C  
ATOM    719  CG1 ILE A  88      35.602 -26.683-210.302  1.00 61.13           C  
ANISOU  719  CG1 ILE A  88     9301   7047   6878  -2796  -1523    998       C  
ATOM    720  CG2 ILE A  88      34.633 -27.776-212.366  1.00 54.27           C  
ANISOU  720  CG2 ILE A  88     8430   6101   6089  -2571  -1664   1034       C  
ATOM    721  CD1 ILE A  88      36.863 -26.174-210.984  1.00 64.05           C  
ANISOU  721  CD1 ILE A  88     9758   7362   7218  -2826  -1447    949       C  
ATOM    722  N   GLU A  89      31.669 -27.982-210.976  1.00 69.91           N  
ANISOU  722  N   GLU A  89    10270   8234   8058  -2521  -1731   1074       N  
ATOM    723  CA  GLU A  89      30.408 -27.253-211.088  1.00 77.68           C  
ANISOU  723  CA  GLU A  89    11276   9259   8979  -2407  -1692   1081       C  
ATOM    724  C   GLU A  89      29.359 -27.740-210.086  1.00 80.07           C  
ANISOU  724  C   GLU A  89    11471   9656   9297  -2452  -1750   1098       C  
ATOM    725  O   GLU A  89      28.752 -26.933-209.380  1.00 79.89           O  
ANISOU  725  O   GLU A  89    11476   9651   9230  -2432  -1681   1110       O  
ATOM    726  CB  GLU A  89      29.849 -27.375-212.507  1.00 82.96           C  
ANISOU  726  CB  GLU A  89    11940   9971   9611  -2261  -1725   1076       C  
ATOM    727  CG  GLU A  89      30.633 -26.604-213.563  1.00 89.00           C  
ANISOU  727  CG  GLU A  89    12828  10650  10338  -2169  -1640   1074       C  
ATOM    728  CD  GLU A  89      30.258 -25.135-213.619  1.00 92.71           C  
ANISOU  728  CD  GLU A  89    13422  11076  10728  -2033  -1476   1113       C  
ATOM    729  OE1 GLU A  89      29.319 -24.722-212.908  1.00102.54           O  
ANISOU  729  OE1 GLU A  89    14651  12369  11941  -1997  -1435   1143       O  
ATOM    730  OE2 GLU A  89      30.905 -24.392-214.380  1.00 92.52           O  
ANISOU  730  OE2 GLU A  89    13520  10958  10677  -1957  -1368   1120       O  
ATOM    731  N   ASN A  90      29.166 -29.058-210.022  1.00 81.35           N  
ANISOU  731  N   ASN A  90    11521   9862   9526  -2516  -1855   1096       N  
ATOM    732  CA  ASN A  90      28.005 -29.656-209.355  1.00 82.34           C  
ANISOU  732  CA  ASN A  90    11541  10080   9666  -2546  -1911   1101       C  
ATOM    733  C   ASN A  90      28.251 -30.220-207.957  1.00 80.51           C  
ANISOU  733  C   ASN A  90    11244   9852   9493  -2672  -1925   1141       C  
ATOM    734  O   ASN A  90      27.303 -30.491-207.225  1.00 77.42           O  
ANISOU  734  O   ASN A  90    10780   9530   9106  -2699  -1951   1150       O  
ATOM    735  CB  ASN A  90      27.440 -30.776-210.223  1.00 90.40           C  
ANISOU  735  CB  ASN A  90    12477  11153  10718  -2546  -1982   1053       C  
ATOM    736  CG  ASN A  90      27.360 -30.394-211.676  1.00 91.97           C  
ANISOU  736  CG  ASN A  90    12711  11389  10847  -2430  -1978   1015       C  
ATOM    737  OD1 ASN A  90      26.565 -29.541-212.062  1.00 97.65           O  
ANISOU  737  OD1 ASN A  90    13437  12205  11461  -2301  -1953   1026       O  
ATOM    738  ND2 ASN A  90      28.190 -31.025-212.497  1.00 88.31           N  
ANISOU  738  ND2 ASN A  90    12263  10858  10433  -2460  -1993    983       N  
ATOM    739  N   ASN A  91      29.515 -30.412-207.596  1.00 73.35           N  
ANISOU  739  N   ASN A  91    10351   8900   8620  -2743  -1906   1171       N  
ATOM    740  CA  ASN A  91      29.860 -30.986-206.301  1.00 61.02           C  
ANISOU  740  CA  ASN A  91     8705   7387   7092  -2841  -1913   1234       C  
ATOM    741  C   ASN A  91      31.242 -30.552-205.884  1.00 69.40           C  
ANISOU  741  C   ASN A  91     9785   8469   8116  -2900  -1866   1255       C  
ATOM    742  O   ASN A  91      32.085 -31.385-205.597  1.00 60.24           O  
ANISOU  742  O   ASN A  91     8561   7337   6993  -2934  -1877   1323       O  
ATOM    743  CB  ASN A  91      29.767 -32.525-206.359  1.00 65.94           C  
ANISOU  743  CB  ASN A  91     9249   7987   7820  -2862  -1953   1277       C  
ATOM    744  CG  ASN A  91      29.991 -33.187-205.011  1.00 64.34           C  
ANISOU  744  CG  ASN A  91     8950   7845   7649  -2927  -1943   1376       C  
ATOM    745  OD1 ASN A  91      29.760 -32.587-203.964  1.00 75.52           O  
ANISOU  745  OD1 ASN A  91    10333   9355   9006  -2966  -1936   1393       O  
ATOM    746  ND2 ASN A  91      30.450 -34.439-205.034  1.00 69.16           N  
ANISOU  746  ND2 ASN A  91     9518   8406   8352  -2929  -1923   1449       N  
ATOM    747  N   PRO A  92      31.479 -29.229-205.827  1.00 69.01           N  
ANISOU  747  N   PRO A  92     9821   8417   7982  -2913  -1789   1197       N  
ATOM    748  CA  PRO A  92      32.847 -28.716-205.712  1.00 60.35           C  
ANISOU  748  CA  PRO A  92     8753   7345   6832  -2988  -1725   1176       C  
ATOM    749  C   PRO A  92      33.485 -29.014-204.356  1.00 67.63           C  
ANISOU  749  C   PRO A  92     9548   8437   7711  -3108  -1724   1223       C  
ATOM    750  O   PRO A  92      34.697 -28.857-204.180  1.00 59.70           O  
ANISOU  750  O   PRO A  92     8516   7522   6647  -3182  -1687   1216       O  
ATOM    751  CB  PRO A  92      32.661 -27.212-205.917  1.00 74.88           C  
ANISOU  751  CB  PRO A  92    10730   9120   8603  -2984  -1603   1087       C  
ATOM    752  CG  PRO A  92      31.273 -26.954-205.385  1.00 83.71           C  
ANISOU  752  CG  PRO A  92    11838  10251   9718  -2945  -1602   1093       C  
ATOM    753  CD  PRO A  92      30.469 -28.159-205.726  1.00 68.35           C  
ANISOU  753  CD  PRO A  92     9806   8317   7847  -2871  -1730   1151       C  
ATOM    754  N   GLY A  93      32.673 -29.475-203.413  1.00 71.54           N  
ANISOU  754  N   GLY A  93     9951   9006   8223  -3124  -1763   1275       N  
ATOM    755  CA  GLY A  93      33.132 -29.701-202.061  1.00 68.86           C  
ANISOU  755  CA  GLY A  93     9475   8864   7823  -3223  -1757   1331       C  
ATOM    756  C   GLY A  93      33.499 -31.124-201.694  1.00 68.81           C  
ANISOU  756  C   GLY A  93     9336   8935   7871  -3184  -1813   1480       C  
ATOM    757  O   GLY A  93      33.745 -31.392-200.507  1.00 73.30           O  
ANISOU  757  O   GLY A  93     9770   9700   8381  -3237  -1808   1558       O  
ATOM    758  N   VAL A  94      33.548 -32.025-202.679  1.00 68.45           N  
ANISOU  758  N   VAL A  94     9328   8747   7932  -3089  -1844   1525       N  
ATOM    759  CA  VAL A  94      33.929 -33.409-202.408  1.00 72.34           C  
ANISOU  759  CA  VAL A  94     9723   9267   8495  -3034  -1847   1678       C  
ATOM    760  C   VAL A  94      35.154 -33.408-201.530  1.00 82.00           C  
ANISOU  760  C   VAL A  94    10819  10729   9608  -3070  -1817   1772       C  
ATOM    761  O   VAL A  94      36.169 -32.755-201.852  1.00 77.11           O  
ANISOU  761  O   VAL A  94    10214  10183   8900  -3112  -1797   1717       O  
ATOM    762  CB  VAL A  94      34.298 -34.221-203.666  1.00 71.69           C  
ANISOU  762  CB  VAL A  94     9709   9010   8519  -2952  -1842   1694       C  
ATOM    763  CG1 VAL A  94      33.821 -35.663-203.536  1.00 62.22           C  
ANISOU  763  CG1 VAL A  94     8469   7722   7449  -2897  -1812   1803       C  
ATOM    764  CG2 VAL A  94      33.802 -33.565-204.923  1.00 74.34           C  
ANISOU  764  CG2 VAL A  94    10180   9192   8873  -2938  -1867   1547       C  
ATOM    765  N   LYS A  95      35.049 -34.107-200.411  1.00 68.89           N  
ANISOU  765  N   LYS A  95     9022   9216   7936  -3055  -1806   1912       N  
ATOM    766  CA  LYS A  95      36.178 -34.282-199.514  1.00 64.13           C  
ANISOU  766  CA  LYS A  95     8253   8908   7206  -3061  -1776   2039       C  
ATOM    767  C   LYS A  95      36.759 -32.956-199.067  1.00 68.91           C  
ANISOU  767  C   LYS A  95     8820   9732   7631  -3212  -1767   1903       C  
ATOM    768  O   LYS A  95      37.945 -32.877-198.728  1.00 87.52           O  
ANISOU  768  O   LYS A  95    11053  12347   9852  -3244  -1741   1949       O  
ATOM    769  CB  LYS A  95      37.251 -35.132-200.192  1.00 67.16           C  
ANISOU  769  CB  LYS A  95     8623   9264   7630  -2949  -1741   2162       C  
ATOM    770  CG  LYS A  95      36.697 -36.435-200.747  1.00 80.39           C  
ANISOU  770  CG  LYS A  95    10367  10679   9499  -2824  -1704   2265       C  
ATOM    771  CD  LYS A  95      37.782 -37.368-201.240  1.00 81.92           C  
ANISOU  771  CD  LYS A  95    10539  10853   9735  -2698  -1633   2418       C  
ATOM    772  CE  LYS A  95      37.197 -38.710-201.648  1.00 68.23           C  
ANISOU  772  CE  LYS A  95     8876   8850   8199  -2596  -1545   2512       C  
ATOM    773  NZ  LYS A  95      38.207 -39.490-202.415  1.00 71.39           N  
ANISOU  773  NZ  LYS A  95     9305   9159   8661  -2481  -1459   2619       N  
ATOM    774  N   PHE A  96      35.944 -31.904-199.057  1.00 74.72           N  
ANISOU  774  N   PHE A  96     9656  10380   8355  -3311  -1768   1732       N  
ATOM    775  CA  PHE A  96      36.469 -30.635-198.545  1.00 82.49           C  
ANISOU  775  CA  PHE A  96    10615  11554   9172  -3481  -1712   1585       C  
ATOM    776  C   PHE A  96      36.314 -30.527-197.039  1.00 82.23           C  
ANISOU  776  C   PHE A  96    10410  11819   9016  -3579  -1699   1616       C  
ATOM    777  O   PHE A  96      35.192 -30.463-196.509  1.00 66.12           O  
ANISOU  777  O   PHE A  96     8386   9715   7021  -3585  -1715   1606       O  
ATOM    778  CB  PHE A  96      35.813 -29.434-199.194  1.00 80.15           C  
ANISOU  778  CB  PHE A  96    10516  11031   8906  -3540  -1666   1391       C  
ATOM    779  CG  PHE A  96      36.462 -28.142-198.816  1.00 78.13           C  
ANISOU  779  CG  PHE A  96    10270  10917   8497  -3728  -1557   1221       C  
ATOM    780  CD1 PHE A  96      37.840 -28.033-198.825  1.00 80.29           C  
ANISOU  780  CD1 PHE A  96    10458  11400   8650  -3812  -1520   1198       C  
ATOM    781  CD2 PHE A  96      35.708 -27.043-198.449  1.00 70.65           C  
ANISOU  781  CD2 PHE A  96     9418   9902   7525  -3829  -1468   1076       C  
ATOM    782  CE1 PHE A  96      38.452 -26.852-198.476  1.00 84.57           C  
ANISOU  782  CE1 PHE A  96    11007  12083   9045  -4022  -1393   1009       C  
ATOM    783  CE2 PHE A  96      36.322 -25.858-198.091  1.00 65.06           C  
ANISOU  783  CE2 PHE A  96     8734   9303   6683  -4029  -1322    896       C  
ATOM    784  CZ  PHE A  96      37.691 -25.765-198.109  1.00 69.02           C  
ANISOU  784  CZ  PHE A  96     9148  10016   7062  -4139  -1283    850       C  
ATOM    785  N   THR A  97      37.469 -30.491-196.377  1.00 81.83           N  
ANISOU  785  N   THR A  97    10181  12120   8792  -3657  -1670   1648       N  
ATOM    786  CA  THR A  97      37.576 -30.491-194.930  1.00 80.48           C  
ANISOU  786  CA  THR A  97     9792  12327   8460  -3748  -1657   1696       C  
ATOM    787  C   THR A  97      37.627 -29.089-194.381  1.00 89.99           C  
ANISOU  787  C   THR A  97    11002  13675   9514  -3996  -1572   1454       C  
ATOM    788  O   THR A  97      37.275 -28.860-193.227  1.00 89.70           O  
ANISOU  788  O   THR A  97    10840  13867   9374  -4100  -1554   1433       O  
ATOM    789  CB  THR A  97      38.837 -31.211-194.467  1.00 84.96           C  
ANISOU  789  CB  THR A  97    10123  13279   8879  -3697  -1658   1870       C  
ATOM    790  OG1 THR A  97      38.987 -32.427-195.202  1.00 96.82           O  
ANISOU  790  OG1 THR A  97    11661  14594  10531  -3468  -1690   2077       O  
ATOM    791  CG2 THR A  97      38.725 -31.545-192.997  1.00103.99           C  
ANISOU  791  CG2 THR A  97    12292  16072  11148  -3717  -1660   1992       C  
ATOM    792  N   GLY A  98      38.099 -28.160-195.209  1.00102.72           N  
ANISOU  792  N   GLY A  98    12764  15151  11115  -4096  -1498   1267       N  
ATOM    793  CA  GLY A  98      38.280 -26.776-194.805  1.00 97.24           C  
ANISOU  793  CA  GLY A  98    12107  14555  10286  -4351  -1361   1012       C  
ATOM    794  C   GLY A  98      37.137 -26.242-193.969  1.00 95.77           C  
ANISOU  794  C   GLY A  98    11952  14326  10110  -4434  -1319    933       C  
ATOM    795  O   GLY A  98      37.310 -25.871-192.810  1.00 96.06           O  
ANISOU  795  O   GLY A  98    11828  14692   9979  -4616  -1263    856       O  
ATOM    796  N   TYR A  99      35.949 -26.241-194.552  1.00 92.09           N  
ANISOU  796  N   TYR A  99    11678  13481   9830  -4296  -1347    956       N  
ATOM    797  CA  TYR A  99      34.774 -25.781-193.845  1.00 80.17           C  
ANISOU  797  CA  TYR A  99    10210  11905   8346  -4341  -1312    900       C  
ATOM    798  C   TYR A  99      33.539 -26.447-194.395  1.00 79.95           C  
ANISOU  798  C   TYR A  99    10288  11579   8512  -4120  -1418   1033       C  
ATOM    799  O   TYR A  99      33.614 -27.489-195.046  1.00 91.53           O  
ANISOU  799  O   TYR A  99    11742  12957  10078  -3950  -1528   1186       O  
ATOM    800  CB  TYR A  99      34.648 -24.264-193.941  1.00 69.09           C  
ANISOU  800  CB  TYR A  99     8984  10365   6904  -4515  -1113    652       C  
ATOM    801  CG  TYR A  99      34.659 -23.702-195.358  1.00 80.38           C  
ANISOU  801  CG  TYR A  99    10664  11433   8444  -4424  -1039    588       C  
ATOM    802  CD1 TYR A  99      35.805 -23.095-195.880  1.00 77.74           C  
ANISOU  802  CD1 TYR A  99    10382  11123   8034  -4546   -923    457       C  
ATOM    803  CD2 TYR A  99      33.515 -23.748-196.166  1.00 78.14           C  
ANISOU  803  CD2 TYR A  99    10553  10814   8324  -4220  -1076    656       C  
ATOM    804  CE1 TYR A  99      35.818 -22.564-197.166  1.00 78.36           C  
ANISOU  804  CE1 TYR A  99    10690  10873   8209  -4453   -844    409       C  
ATOM    805  CE2 TYR A  99      33.524 -23.219-197.455  1.00 75.72           C  
ANISOU  805  CE2 TYR A  99    10455  10217   8096  -4120  -1003    614       C  
ATOM    806  CZ  TYR A  99      34.676 -22.627-197.948  1.00 80.52           C  
ANISOU  806  CZ  TYR A  99    11125  10829   8639  -4231   -884    496       C  
ATOM    807  OH  TYR A  99      34.687 -22.107-199.229  1.00 84.67           O  
ANISOU  807  OH  TYR A  99    11859  11068   9242  -4119   -803    468       O  
ATOM    808  OXT TYR A  99      32.442 -25.946-194.190  1.00 93.25           O  
ANISOU  808  OXT TYR A  99    12067  13118  10247  -4117  -1382    978       O  
TER     809      TYR A  99                                                      
ATOM    810  N   MET B   1      89.814  -8.096-238.740  1.00105.42           N  
ANISOU  810  N   MET B   1    15896  14774   9386  -7909   4102  -3818       N  
ATOM    811  CA  MET B   1      89.761  -8.588-240.108  1.00119.42           C  
ANISOU  811  CA  MET B   1    17866  16209  11300  -7595   3892  -3635       C  
ATOM    812  C   MET B   1      89.002  -9.916-240.180  1.00127.63           C  
ANISOU  812  C   MET B   1    18863  17203  12428  -7243   3393  -3385       C  
ATOM    813  O   MET B   1      89.133 -10.768-239.297  1.00133.75           O  
ANISOU  813  O   MET B   1    19322  18410  13087  -7283   3131  -3349       O  
ATOM    814  CB  MET B   1      91.187  -8.711-240.675  1.00118.15           C  
ANISOU  814  CB  MET B   1    17515  16343  11035  -7748   3886  -3708       C  
ATOM    815  CG  MET B   1      91.767 -10.112-240.817  1.00120.67           C  
ANISOU  815  CG  MET B   1    17534  17026  11288  -7600   3410  -3562       C  
ATOM    816  SD  MET B   1      93.415 -10.053-241.569  1.00151.39           S  
ANISOU  816  SD  MET B   1    21243  21209  15069  -7780   3468  -3663       S  
ATOM    817  CE  MET B   1      93.076  -9.512-243.234  1.00119.84           C  
ANISOU  817  CE  MET B   1    17725  16519  11290  -7533   3597  -3581       C  
ATOM    818  N   ALA B   2      88.199 -10.074-241.232  1.00123.90           N  
ANISOU  818  N   ALA B   2    18703  16218  12156  -6902   3281  -3209       N  
ATOM    819  CA  ALA B   2      87.327 -11.241-241.394  1.00105.50           C  
ANISOU  819  CA  ALA B   2    16384  13764   9938  -6571   2855  -2975       C  
ATOM    820  C   ALA B   2      87.090 -11.564-242.872  1.00103.19           C  
ANISOU  820  C   ALA B   2    16333  13060   9815  -6254   2708  -2806       C  
ATOM    821  O   ALA B   2      86.760 -10.677-243.653  1.00106.77           O  
ANISOU  821  O   ALA B   2    17086  13100  10383  -6171   2971  -2811       O  
ATOM    822  CB  ALA B   2      86.004 -10.997-240.686  1.00 98.65           C  
ANISOU  822  CB  ALA B   2    15651  12674   9159  -6491   2905  -2933       C  
ATOM    823  N   ARG B   3      87.258 -12.829-243.255  1.00101.53           N  
ANISOU  823  N   ARG B   3    15990  12977   9611  -6072   2305  -2653       N  
ATOM    824  CA  ARG B   3      87.161 -13.237-244.666  1.00 95.47           C  
ANISOU  824  CA  ARG B   3    15411  11879   8982  -5794   2150  -2504       C  
ATOM    825  C   ARG B   3      85.766 -13.077-245.248  1.00 96.76           C  
ANISOU  825  C   ARG B   3    15887  11518   9359  -5500   2148  -2348       C  
ATOM    826  O   ARG B   3      84.786 -13.558-244.687  1.00107.47           O  
ANISOU  826  O   ARG B   3    17236  12821  10775  -5386   1983  -2248       O  
ATOM    827  CB  ARG B   3      87.614 -14.693-244.844  1.00105.42           C  
ANISOU  827  CB  ARG B   3    16450  13416  10188  -5673   1728  -2377       C  
ATOM    828  CG  ARG B   3      87.692 -15.179-246.298  1.00107.87           C  
ANISOU  828  CG  ARG B   3    16921  13450  10616  -5421   1568  -2244       C  
ATOM    829  CD  ARG B   3      88.370 -16.554-246.403  1.00112.51           C  
ANISOU  829  CD  ARG B   3    17268  14375  11107  -5348   1203  -2150       C  
ATOM    830  NE  ARG B   3      89.824 -16.384-246.474  1.00128.51           N  
ANISOU  830  NE  ARG B   3    19095  16770  12963  -5547   1289  -2279       N  
ATOM    831  CZ  ARG B   3      90.641 -16.466-245.423  1.00139.27           C  
ANISOU  831  CZ  ARG B   3    20131  18669  14117  -5779   1308  -2381       C  
ATOM    832  NH1 ARG B   3      90.148 -16.750-244.222  1.00144.55           N  
ANISOU  832  NH1 ARG B   3    20638  19566  14717  -5834   1237  -2366       N  
ATOM    833  NH2 ARG B   3      91.950 -16.274-245.566  1.00135.69           N  
ANISOU  833  NH2 ARG B   3    19492  18545  13519  -5952   1398  -2492       N  
ATOM    834  N   PRO B   4      85.675 -12.410-246.396  1.00 97.27           N  
ANISOU  834  N   PRO B   4    16215  11212   9531  -5366   2332  -2317       N  
ATOM    835  CA  PRO B   4      84.388 -12.271-247.076  1.00 94.62           C  
ANISOU  835  CA  PRO B   4    16154  10414   9384  -5054   2329  -2145       C  
ATOM    836  C   PRO B   4      83.860 -13.582-247.628  1.00 89.83           C  
ANISOU  836  C   PRO B   4    15518   9741   8871  -4780   1910  -1939       C  
ATOM    837  O   PRO B   4      84.579 -14.332-248.295  1.00 93.08           O  
ANISOU  837  O   PRO B   4    15842  10267   9257  -4735   1701  -1901       O  
ATOM    838  CB  PRO B   4      84.691 -11.305-248.230  1.00 91.81           C  
ANISOU  838  CB  PRO B   4    16038   9770   9078  -4991   2624  -2164       C  
ATOM    839  CG  PRO B   4      86.040 -10.724-247.937  1.00 94.97           C  
ANISOU  839  CG  PRO B   4    16311  10453   9320  -5325   2854  -2381       C  
ATOM    840  CD  PRO B   4      86.763 -11.717-247.106  1.00 97.11           C  
ANISOU  840  CD  PRO B   4    16239  11205   9452  -5499   2569  -2435       C  
ATOM    841  N   ARG B   5      82.592 -13.847-247.363  1.00 95.77           N  
ANISOU  841  N   ARG B   5    16349  10307   9733  -4600   1804  -1807       N  
ATOM    842  CA  ARG B   5      81.883 -14.856-248.123  1.00 96.70           C  
ANISOU  842  CA  ARG B   5    16516  10255   9971  -4308   1489  -1600       C  
ATOM    843  C   ARG B   5      81.890 -14.433-249.574  1.00 93.97           C  
ANISOU  843  C   ARG B   5    16384   9612   9709  -4110   1595  -1525       C  
ATOM    844  O   ARG B   5      81.863 -13.246-249.866  1.00105.63           O  
ANISOU  844  O   ARG B   5    18038  10899  11197  -4121   1938  -1579       O  
ATOM    845  CB  ARG B   5      80.448 -15.016-247.637  1.00 93.43           C  
ANISOU  845  CB  ARG B   5    16170   9668   9661  -4151   1417  -1476       C  
ATOM    846  CG  ARG B   5      80.320 -15.635-246.284  1.00 86.51           C  
ANISOU  846  CG  ARG B   5    15081   9076   8715  -4303   1256  -1513       C  
ATOM    847  CD  ARG B   5      78.871 -15.941-246.024  1.00 75.82           C  
ANISOU  847  CD  ARG B   5    13805   7521   7482  -4108   1143  -1361       C  
ATOM    848  NE  ARG B   5      78.250 -14.907-245.209  1.00 84.22           N  
ANISOU  848  NE  ARG B   5    14953   8500   8548  -4190   1423  -1434       N  
ATOM    849  CZ  ARG B   5      77.002 -14.488-245.371  1.00 84.61           C  
ANISOU  849  CZ  ARG B   5    15184   8251   8714  -3988   1515  -1318       C  
ATOM    850  NH1 ARG B   5      76.258 -15.011-246.334  1.00 74.48           N  
ANISOU  850  NH1 ARG B   5    14004   6753   7542  -3700   1345  -1127       N  
ATOM    851  NH2 ARG B   5      76.504 -13.541-244.579  1.00 91.18           N  
ANISOU  851  NH2 ARG B   5    16087   9019   9538  -4073   1786  -1394       N  
ATOM    852  N   PRO B   6      81.915 -15.401-250.490  1.00 93.93           N  
ANISOU  852  N   PRO B   6    16367   9567   9756  -3923   1315  -1396       N  
ATOM    853  CA  PRO B   6      81.909 -15.092-251.922  1.00 94.53           C  
ANISOU  853  CA  PRO B   6    16631   9387   9901  -3721   1389  -1313       C  
ATOM    854  C   PRO B   6      80.689 -14.248-252.333  1.00 97.91           C  
ANISOU  854  C   PRO B   6    17302   9470  10430  -3498   1601  -1196       C  
ATOM    855  O   PRO B   6      79.631 -14.381-251.716  1.00106.19           O  
ANISOU  855  O   PRO B   6    18359  10458  11530  -3419   1548  -1119       O  
ATOM    856  CB  PRO B   6      81.871 -16.482-252.569  1.00 91.79           C  
ANISOU  856  CB  PRO B   6    16197   9084   9595  -3557   1004  -1185       C  
ATOM    857  CG  PRO B   6      82.481 -17.388-251.533  1.00 79.22           C  
ANISOU  857  CG  PRO B   6    14318   7867   7915  -3720    789  -1238       C  
ATOM    858  CD  PRO B   6      81.984 -16.850-250.234  1.00 81.06           C  
ANISOU  858  CD  PRO B   6    14545   8141   8113  -3895    929  -1324       C  
ATOM    859  N   ARG B   7      80.843 -13.389-253.340  1.00 89.95           N  
ANISOU  859  N   ARG B   7    16483   8253   9441  -3393   1848  -1175       N  
ATOM    860  CA  ARG B   7      79.733 -12.585-253.856  1.00 89.80           C  
ANISOU  860  CA  ARG B   7    16696   7924   9501  -3139   2069  -1033       C  
ATOM    861  C   ARG B   7      79.300 -13.198-255.196  1.00 83.70           C  
ANISOU  861  C   ARG B   7    16000   7016   8785  -2838   1873   -840       C  
ATOM    862  O   ARG B   7      78.271 -12.831-255.783  1.00 82.85           O  
ANISOU  862  O   ARG B   7    16053   6693   8732  -2564   1969   -666       O  
ATOM    863  CB  ARG B   7      80.145 -11.095-253.992  1.00 80.93           C  
ANISOU  863  CB  ARG B   7    15742   6662   8346  -3217   2540  -1133       C  
ATOM    864  CG  ARG B   7      79.052 -10.142-254.519  1.00 76.53           C  
ANISOU  864  CG  ARG B   7    15429   5791   7856  -2930   2830   -974       C  
ATOM    865  CD  ARG B   7      79.237  -8.666-254.130  1.00 93.80           C  
ANISOU  865  CD  ARG B   7    17766   7858  10014  -3047   3329  -1098       C  
ATOM    866  NE  ARG B   7      79.916  -8.441-252.851  1.00105.13           N  
ANISOU  866  NE  ARG B   7    19072   9505  11370  -3422   3422  -1338       N  
ATOM    867  CZ  ARG B   7      79.622  -7.445-252.014  1.00 99.32           C  
ANISOU  867  CZ  ARG B   7    18418   8702  10615  -3537   3770  -1440       C  
ATOM    868  NH1 ARG B   7      78.647  -6.598-252.306  1.00 98.77           N  
ANISOU  868  NH1 ARG B   7    18564   8351  10612  -3287   4054  -1315       N  
ATOM    869  NH2 ARG B   7      80.282  -7.307-250.873  1.00 99.73           N  
ANISOU  869  NH2 ARG B   7    18331   8988  10575  -3892   3840  -1662       N  
ATOM    870  N   GLU B   8      80.103 -14.147-255.671  1.00 86.17           N  
ANISOU  870  N   GLU B   8    16187   7481   9074  -2887   1603   -868       N  
ATOM    871  CA  GLU B   8      79.754 -14.951-256.845  1.00 92.51           C  
ANISOU  871  CA  GLU B   8    16963   8269   9917  -2606   1353   -698       C  
ATOM    872  C   GLU B   8      79.860 -16.434-256.535  1.00 90.66           C  
ANISOU  872  C   GLU B   8    16441   8314   9692  -2602    940   -676       C  
ATOM    873  O   GLU B   8      80.770 -16.862-255.818  1.00 85.97           O  
ANISOU  873  O   GLU B   8    15699   7920   9046  -2839    852   -807       O  
ATOM    874  CB  GLU B   8      80.656 -14.628-258.036  1.00102.26           C  
ANISOU  874  CB  GLU B   8    18299   9433  11124  -2584   1457   -721       C  
ATOM    875  CG  GLU B   8      80.287 -13.371-258.812  1.00115.79           C  
ANISOU  875  CG  GLU B   8    20297  10849  12851  -2426   1829   -640       C  
ATOM    876  CD  GLU B   8      81.336 -13.006-259.859  1.00113.84           C  
ANISOU  876  CD  GLU B   8    20118  10570  12566  -2440   1951   -687       C  
ATOM    877  OE1 GLU B   8      80.978 -12.353-260.865  1.00113.84           O  
ANISOU  877  OE1 GLU B   8    20303  10372  12578  -2205   2149   -550       O  
ATOM    878  OE2 GLU B   8      82.520 -13.370-259.670  1.00107.06           O  
ANISOU  878  OE2 GLU B   8    19120   9901  11657  -2676   1856   -847       O  
ATOM    879  N   TYR B   9      78.942 -17.218-257.097  1.00 85.11           N  
ANISOU  879  N   TYR B   9    15653   7639   9044  -2329    710   -508       N  
ATOM    880  CA  TYR B   9      78.954 -18.655-256.902  1.00 77.31           C  
ANISOU  880  CA  TYR B   9    14420   6869   8085  -2303    359   -478       C  
ATOM    881  C   TYR B   9      78.908 -19.370-258.248  1.00 82.70           C  
ANISOU  881  C   TYR B   9    15052   7578   8792  -2088    184   -384       C  
ATOM    882  O   TYR B   9      78.422 -18.818-259.228  1.00 88.48           O  
ANISOU  882  O   TYR B   9    15912   8188   9519  -1898    290   -296       O  
ATOM    883  CB  TYR B   9      77.786 -19.075-256.008  1.00 79.87           C  
ANISOU  883  CB  TYR B   9    14659   7232   8457  -2241    245   -406       C  
ATOM    884  CG  TYR B   9      78.010 -18.796-254.526  1.00 81.05           C  
ANISOU  884  CG  TYR B   9    14770   7449   8576  -2490    327   -516       C  
ATOM    885  CD1 TYR B   9      78.722 -19.690-253.735  1.00 83.95           C  
ANISOU  885  CD1 TYR B   9    14929   8051   8918  -2647    147   -577       C  
ATOM    886  CD2 TYR B   9      77.501 -17.645-253.914  1.00 77.20           C  
ANISOU  886  CD2 TYR B   9    14447   6807   8077  -2559    599   -552       C  
ATOM    887  CE1 TYR B   9      78.938 -19.444-252.374  1.00 80.33           C  
ANISOU  887  CE1 TYR B   9    14406   7711   8404  -2875    217   -677       C  
ATOM    888  CE2 TYR B   9      77.714 -17.388-252.544  1.00 64.88           C  
ANISOU  888  CE2 TYR B   9    12840   5335   6477  -2812    680   -675       C  
ATOM    889  CZ  TYR B   9      78.431 -18.302-251.790  1.00 69.09           C  
ANISOU  889  CZ  TYR B   9    13142   6143   6967  -2970    475   -738       C  
ATOM    890  OH  TYR B   9      78.647 -18.096-250.454  1.00 75.26           O  
ANISOU  890  OH  TYR B   9    13844   7069   7684  -3212    541   -853       O  
ATOM    891  N   LYS B  10      79.432 -20.589-258.301  1.00 81.34           N  
ANISOU  891  N   LYS B  10    14692   7574   8638  -2114    -65   -398       N  
ATOM    892  CA  LYS B  10      79.504 -21.329-259.560  1.00 79.11           C  
ANISOU  892  CA  LYS B  10    14355   7325   8378  -1950   -219   -341       C  
ATOM    893  C   LYS B  10      78.639 -22.600-259.509  1.00 85.73           C  
ANISOU  893  C   LYS B  10    15027   8261   9285  -1830   -466   -269       C  
ATOM    894  O   LYS B  10      78.587 -23.280-258.468  1.00 71.10           O  
ANISOU  894  O   LYS B  10    13051   6497   7467  -1920   -571   -281       O  
ATOM    895  CB  LYS B  10      80.957 -21.694-259.867  1.00 85.18           C  
ANISOU  895  CB  LYS B  10    15065   8183   9115  -2079   -260   -428       C  
ATOM    896  CG  LYS B  10      81.117 -23.119-260.346  1.00 94.69           C  
ANISOU  896  CG  LYS B  10    16100   9507  10372  -1997   -509   -393       C  
ATOM    897  CD  LYS B  10      82.356 -23.804-259.792  1.00 97.86           C  
ANISOU  897  CD  LYS B  10    16363  10066  10753  -2151   -586   -453       C  
ATOM    898  CE  LYS B  10      82.053 -25.280-259.515  1.00106.81           C  
ANISOU  898  CE  LYS B  10    17320  11296  11968  -2077   -796   -388       C  
ATOM    899  NZ  LYS B  10      83.256 -26.075-259.159  1.00116.25           N  
ANISOU  899  NZ  LYS B  10    18372  12655  13144  -2161   -866   -402       N  
ATOM    900  N   ALA B  11      77.960 -22.912-260.619  1.00 81.18           N  
ANISOU  900  N   ALA B  11    14442   7684   8719  -1636   -542   -200       N  
ATOM    901  CA  ALA B  11      77.135 -24.120-260.694  1.00 71.26           C  
ANISOU  901  CA  ALA B  11    13032   6524   7520  -1548   -747   -164       C  
ATOM    902  C   ALA B  11      77.908 -25.288-260.132  1.00 64.91           C  
ANISOU  902  C   ALA B  11    12085   5801   6775  -1671   -886   -213       C  
ATOM    903  O   ALA B  11      79.053 -25.517-260.507  1.00 71.88           O  
ANISOU  903  O   ALA B  11    12954   6711   7648  -1734   -895   -258       O  
ATOM    904  CB  ALA B  11      76.713 -24.414-262.121  1.00 73.46           C  
ANISOU  904  CB  ALA B  11    13290   6849   7775  -1379   -809   -131       C  
ATOM    905  N   GLY B  12      77.305 -26.008-259.200  1.00 63.69           N  
ANISOU  905  N   GLY B  12    11827   5691   6680  -1696   -979   -192       N  
ATOM    906  CA  GLY B  12      77.989 -27.142-258.627  1.00 66.85           C  
ANISOU  906  CA  GLY B  12    12094   6168   7137  -1777  -1082   -204       C  
ATOM    907  C   GLY B  12      78.521 -26.898-257.244  1.00 82.42           C  
ANISOU  907  C   GLY B  12    14031   8202   9083  -1920  -1036   -210       C  
ATOM    908  O   GLY B  12      78.806 -27.854-256.522  1.00 91.47           O  
ANISOU  908  O   GLY B  12    15047   9435  10271  -1953  -1115   -181       O  
ATOM    909  N   ASP B  13      78.656 -25.632-256.862  1.00 69.75           N  
ANISOU  909  N   ASP B  13    12537   6563   7404  -2004   -889   -248       N  
ATOM    910  CA  ASP B  13      79.205 -25.310-255.551  1.00 70.50           C  
ANISOU  910  CA  ASP B  13    12586   6757   7445  -2176   -827   -285       C  
ATOM    911  C   ASP B  13      78.282 -25.817-254.429  1.00 73.01           C  
ANISOU  911  C   ASP B  13    12813   7114   7813  -2169   -900   -229       C  
ATOM    912  O   ASP B  13      77.056 -25.794-254.573  1.00 74.64           O  
ANISOU  912  O   ASP B  13    13061   7226   8071  -2060   -923   -185       O  
ATOM    913  CB  ASP B  13      79.428 -23.795-255.426  1.00 82.49           C  
ANISOU  913  CB  ASP B  13    14265   8199   8879  -2291   -610   -365       C  
ATOM    914  CG  ASP B  13      80.786 -23.348-255.971  1.00 80.65           C  
ANISOU  914  CG  ASP B  13    14073   8004   8568  -2400   -517   -453       C  
ATOM    915  OD1 ASP B  13      81.800 -24.029-255.680  1.00 83.32           O  
ANISOU  915  OD1 ASP B  13    14266   8522   8871  -2482   -598   -473       O  
ATOM    916  OD2 ASP B  13      80.831 -22.314-256.685  1.00 77.28           O  
ANISOU  916  OD2 ASP B  13    13820   7432   8110  -2393   -349   -491       O  
ATOM    917  N   LEU B  14      78.871 -26.273-253.321  1.00 63.09           N  
ANISOU  917  N   LEU B  14    11420   6023   6528  -2276   -932   -224       N  
ATOM    918  CA  LEU B  14      78.104 -26.738-252.172  1.00 65.46           C  
ANISOU  918  CA  LEU B  14    11628   6377   6867  -2278   -989   -167       C  
ATOM    919  C   LEU B  14      78.119 -25.695-251.059  1.00 72.83           C  
ANISOU  919  C   LEU B  14    12589   7374   7710  -2446   -862   -233       C  
ATOM    920  O   LEU B  14      79.152 -25.100-250.735  1.00 67.67           O  
ANISOU  920  O   LEU B  14    11922   6845   6944  -2610   -763   -320       O  
ATOM    921  CB  LEU B  14      78.645 -28.079-251.649  1.00 64.97           C  
ANISOU  921  CB  LEU B  14    11378   6470   6835  -2250  -1100    -85       C  
ATOM    922  CG  LEU B  14      78.729 -29.235-252.657  1.00 66.64           C  
ANISOU  922  CG  LEU B  14    11560   6613   7147  -2106  -1192    -32       C  
ATOM    923  CD1 LEU B  14      79.378 -30.493-252.050  1.00 62.95           C  
ANISOU  923  CD1 LEU B  14    10923   6286   6708  -2067  -1243     69       C  
ATOM    924  CD2 LEU B  14      77.360 -29.546-253.223  1.00 52.34           C  
ANISOU  924  CD2 LEU B  14     9811   4635   5442  -1993  -1243    -20       C  
ATOM    925  N   VAL B  15      76.954 -25.483-250.466  1.00 69.74           N  
ANISOU  925  N   VAL B  15    12230   6908   7359  -2418   -855   -204       N  
ATOM    926  CA  VAL B  15      76.762 -24.391-249.527  1.00 67.65           C  
ANISOU  926  CA  VAL B  15    12028   6653   7023  -2568   -705   -277       C  
ATOM    927  C   VAL B  15      75.777 -24.782-248.427  1.00 78.16           C  
ANISOU  927  C   VAL B  15    13278   8023   8397  -2552   -771   -216       C  
ATOM    928  O   VAL B  15      75.084 -25.807-248.529  1.00 71.80           O  
ANISOU  928  O   VAL B  15    12399   7195   7687  -2409   -917   -117       O  
ATOM    929  CB  VAL B  15      76.195 -23.173-250.232  1.00 64.78           C  
ANISOU  929  CB  VAL B  15    11886   6067   6661  -2531   -537   -317       C  
ATOM    930  CG1 VAL B  15      77.145 -22.660-251.345  1.00 60.74           C  
ANISOU  930  CG1 VAL B  15    11476   5496   6105  -2547   -441   -378       C  
ATOM    931  CG2 VAL B  15      74.846 -23.554-250.840  1.00 56.76           C  
ANISOU  931  CG2 VAL B  15    10907   4918   5742  -2308   -630   -210       C  
ATOM    932  N   PHE B  16      75.721 -23.953-247.384  1.00 63.96           N  
ANISOU  932  N   PHE B  16    11498   6280   6526  -2715   -646   -288       N  
ATOM    933  CA  PHE B  16      74.556 -23.882-246.518  1.00 60.99           C  
ANISOU  933  CA  PHE B  16    11119   5864   6190  -2694   -652   -248       C  
ATOM    934  C   PHE B  16      73.726 -22.706-246.984  1.00 63.05           C  
ANISOU  934  C   PHE B  16    11598   5890   6470  -2650   -484   -277       C  
ATOM    935  O   PHE B  16      74.239 -21.605-247.078  1.00 71.09           O  
ANISOU  935  O   PHE B  16    12746   6845   7420  -2776   -278   -382       O  
ATOM    936  CB  PHE B  16      74.947 -23.708-245.046  1.00 68.94           C  
ANISOU  936  CB  PHE B  16    12004   7092   7100  -2897   -606   -306       C  
ATOM    937  CG  PHE B  16      75.581 -24.916-244.451  1.00 74.63           C  
ANISOU  937  CG  PHE B  16    12489   8070   7795  -2890   -762   -227       C  
ATOM    938  CD1 PHE B  16      74.807 -25.882-243.836  1.00 70.31           C  
ANISOU  938  CD1 PHE B  16    11833   7556   7327  -2777   -895   -103       C  
ATOM    939  CD2 PHE B  16      76.943 -25.103-244.522  1.00 74.17           C  
ANISOU  939  CD2 PHE B  16    12322   8228   7633  -2979   -760   -264       C  
ATOM    940  CE1 PHE B  16      75.387 -27.005-243.286  1.00 54.04           C  
ANISOU  940  CE1 PHE B  16     9566   5718   5247  -2739  -1003     -1       C  
ATOM    941  CE2 PHE B  16      77.531 -26.230-243.978  1.00 64.64           C  
ANISOU  941  CE2 PHE B  16    10893   7273   6393  -2932   -882   -155       C  
ATOM    942  CZ  PHE B  16      76.755 -27.182-243.364  1.00 62.20           C  
ANISOU  942  CZ  PHE B  16    10488   6974   6171  -2803   -994    -16       C  
ATOM    943  N   ALA B  17      72.450 -22.917-247.275  1.00 56.84           N  
ANISOU  943  N   ALA B  17    10851   4980   5767  -2468   -549   -182       N  
ATOM    944  CA  ALA B  17      71.599 -21.798-247.671  1.00 62.63           C  
ANISOU  944  CA  ALA B  17    11777   5516   6502  -2385   -374   -173       C  
ATOM    945  C   ALA B  17      70.641 -21.440-246.554  1.00 65.40           C  
ANISOU  945  C   ALA B  17    12136   5851   6863  -2420   -318   -161       C  
ATOM    946  O   ALA B  17      70.054 -22.324-245.920  1.00 65.44           O  
ANISOU  946  O   ALA B  17    12000   5952   6912  -2387   -486   -103       O  
ATOM    947  CB  ALA B  17      70.828 -22.126-248.942  1.00 68.82           C  
ANISOU  947  CB  ALA B  17    12598   6212   7338  -2137   -459    -72       C  
ATOM    948  N   LYS B  18      70.484 -20.141-246.314  1.00 63.13           N  
ANISOU  948  N   LYS B  18    12022   5428   6538  -2488    -59   -218       N  
ATOM    949  CA  LYS B  18      69.597 -19.683-245.258  1.00 67.90           C  
ANISOU  949  CA  LYS B  18    12653   5997   7147  -2530     29   -217       C  
ATOM    950  C   LYS B  18      68.290 -19.189-245.835  1.00 67.54           C  
ANISOU  950  C   LYS B  18    12739   5781   7144  -2288    106    -96       C  
ATOM    951  O   LYS B  18      68.285 -18.394-246.759  1.00 74.97           O  
ANISOU  951  O   LYS B  18    13846   6566   8071  -2176    282    -67       O  
ATOM    952  CB  LYS B  18      70.251 -18.571-244.438  1.00 65.57           C  
ANISOU  952  CB  LYS B  18    12458   5676   6779  -2794    301   -376       C  
ATOM    953  CG  LYS B  18      69.344 -18.004-243.367  1.00 72.34           C  
ANISOU  953  CG  LYS B  18    13364   6479   7644  -2848    427   -388       C  
ATOM    954  CD  LYS B  18      69.156 -18.943-242.187  1.00 66.57           C  
ANISOU  954  CD  LYS B  18    12408   5976   6908  -2933    211   -380       C  
ATOM    955  CE  LYS B  18      68.133 -18.374-241.207  1.00 68.66           C  
ANISOU  955  CE  LYS B  18    12729   6171   7187  -2961    331   -381       C  
ATOM    956  NZ  LYS B  18      66.747 -18.521-241.766  1.00 83.06           N  
ANISOU  956  NZ  LYS B  18    14610   7854   9094  -2667    262   -212       N  
ATOM    957  N   MET B  19      67.183 -19.673-245.297  1.00 75.76           N  
ANISOU  957  N   MET B  19    13693   6868   8224  -2196    -20    -16       N  
ATOM    958  CA  MET B  19      65.881 -19.160-245.668  1.00 75.99           C  
ANISOU  958  CA  MET B  19    13821   6784   8268  -1972     63    103       C  
ATOM    959  C   MET B  19      65.126 -18.764-244.415  1.00 83.79           C  
ANISOU  959  C   MET B  19    14821   7751   9264  -2044    149     94       C  
ATOM    960  O   MET B  19      65.294 -19.373-243.354  1.00 77.91           O  
ANISOU  960  O   MET B  19    13937   7137   8529  -2207     23     36       O  
ATOM    961  CB  MET B  19      65.091 -20.188-246.473  1.00 74.39           C  
ANISOU  961  CB  MET B  19    13487   6685   8093  -1755   -183    215       C  
ATOM    962  CG  MET B  19      65.585 -20.334-247.899  1.00 85.86           C  
ANISOU  962  CG  MET B  19    14962   8135   9526  -1636   -215    240       C  
ATOM    963  SD  MET B  19      64.270 -20.227-249.144  1.00 90.61           S  
ANISOU  963  SD  MET B  19    15571   8769  10087  -1300   -230    399       S  
ATOM    964  CE  MET B  19      63.947 -18.464-249.168  1.00122.32           C  
ANISOU  964  CE  MET B  19    19845  12575  14055  -1185    154    476       C  
ATOM    965  N   LYS B  20      64.318 -17.719-244.544  1.00 76.71           N  
ANISOU  965  N   LYS B  20    14094   6693   8358  -1909    382    163       N  
ATOM    966  CA  LYS B  20      63.473 -17.240-243.463  1.00 76.93           C  
ANISOU  966  CA  LYS B  20    14159   6675   8397  -1943    494    170       C  
ATOM    967  C   LYS B  20      62.685 -18.379-242.804  1.00 78.47           C  
ANISOU  967  C   LYS B  20    14141   7048   8625  -1920    201    217       C  
ATOM    968  O   LYS B  20      61.879 -19.055-243.452  1.00 72.80           O  
ANISOU  968  O   LYS B  20    13330   6411   7920  -1714     22    329       O  
ATOM    969  CB  LYS B  20      62.521 -16.170-244.001  1.00 92.52           C  
ANISOU  969  CB  LYS B  20    16325   8469  10360  -1696    752    303       C  
ATOM    970  CG  LYS B  20      63.174 -15.245-245.045  1.00 97.11           C  
ANISOU  970  CG  LYS B  20    17108   8873  10914  -1623   1017    314       C  
ATOM    971  CD  LYS B  20      62.383 -13.969-245.256  1.00 94.91           C  
ANISOU  971  CD  LYS B  20    17059   8377  10627  -1417   1378    439       C  
ATOM    972  CE  LYS B  20      63.189 -12.929-246.025  1.00 96.53           C  
ANISOU  972  CE  LYS B  20    17499   8360  10818  -1409   1718    419       C  
ATOM    973  NZ  LYS B  20      64.416 -12.482-245.299  1.00 96.90           N  
ANISOU  973  NZ  LYS B  20    17634   8311  10874  -1790   1898    176       N  
ATOM    974  N   GLY B  21      62.945 -18.607-241.520  1.00 70.68           N  
ANISOU  974  N   GLY B  21    13069   6143   7643  -2144    164    122       N  
ATOM    975  CA  GLY B  21      62.182 -19.580-240.763  1.00 66.48           C  
ANISOU  975  CA  GLY B  21    12358   5755   7147  -2130    -67    169       C  
ATOM    976  C   GLY B  21      62.841 -20.941-240.684  1.00 89.53           C  
ANISOU  976  C   GLY B  21    15075   8854  10089  -2207   -335    149       C  
ATOM    977  O   GLY B  21      62.417 -21.808-239.916  1.00 95.62           O  
ANISOU  977  O   GLY B  21    15695   9743  10893  -2233   -503    176       O  
ATOM    978  N   TYR B  22      63.882 -21.137-241.483  1.00 85.67           N  
ANISOU  978  N   TYR B  22    14588   8377   9585  -2231   -358    112       N  
ATOM    979  CA  TYR B  22      64.587 -22.406-241.494  1.00 75.19           C  
ANISOU  979  CA  TYR B  22    13085   7202   8281  -2280   -577    109       C  
ATOM    980  C   TYR B  22      66.020 -22.243-241.010  1.00 70.35           C  
ANISOU  980  C   TYR B  22    12438   6687   7604  -2501   -515      1       C  
ATOM    981  O   TYR B  22      66.636 -21.209-241.223  1.00 55.89           O  
ANISOU  981  O   TYR B  22    10742   4777   5717  -2596   -313    -87       O  
ATOM    982  CB  TYR B  22      64.592 -23.005-242.890  1.00 72.46           C  
ANISOU  982  CB  TYR B  22    12731   6835   7967  -2112   -690    163       C  
ATOM    983  CG  TYR B  22      63.234 -23.342-243.454  1.00 74.25           C  
ANISOU  983  CG  TYR B  22    12938   7045   8227  -1908   -777    255       C  
ATOM    984  CD1 TYR B  22      62.455 -22.376-244.077  1.00 79.20           C  
ANISOU  984  CD1 TYR B  22    13698   7579   8816  -1750   -637    309       C  
ATOM    985  CD2 TYR B  22      62.742 -24.631-243.394  1.00 68.95           C  
ANISOU  985  CD2 TYR B  22    12111   6471   7616  -1870   -977    287       C  
ATOM    986  CE1 TYR B  22      61.211 -22.694-244.621  1.00 79.00           C  
ANISOU  986  CE1 TYR B  22    13620   7608   8788  -1559   -721    394       C  
ATOM    987  CE2 TYR B  22      61.497 -24.955-243.925  1.00 79.51           C  
ANISOU  987  CE2 TYR B  22    13410   7836   8964  -1714  -1051    343       C  
ATOM    988  CZ  TYR B  22      60.737 -23.982-244.534  1.00 82.34           C  
ANISOU  988  CZ  TYR B  22    13872   8152   9260  -1560   -934    395       C  
ATOM    989  OH  TYR B  22      59.506 -24.300-245.064  1.00 85.20           O  
ANISOU  989  OH  TYR B  22    14164   8609   9600  -1403  -1010    451       O  
ATOM    990  N   PRO B  23      66.561 -23.272-240.347  1.00 72.20           N  
ANISOU  990  N   PRO B  23    12485   7110   7838  -2580   -672     11       N  
ATOM    991  CA  PRO B  23      68.001 -23.260-240.051  1.00 72.90           C  
ANISOU  991  CA  PRO B  23    12499   7358   7839  -2760   -638    -73       C  
ATOM    992  C   PRO B  23      68.866 -23.119-241.319  1.00 62.66           C  
ANISOU  992  C   PRO B  23    11281   5996   6532  -2722   -608   -102       C  
ATOM    993  O   PRO B  23      68.411 -23.498-242.401  1.00 67.51           O  
ANISOU  993  O   PRO B  23    11942   6490   7217  -2537   -686    -31       O  
ATOM    994  CB  PRO B  23      68.229 -24.626-239.382  1.00 62.19           C  
ANISOU  994  CB  PRO B  23    10921   6208   6503  -2746   -833     13       C  
ATOM    995  CG  PRO B  23      67.054 -25.474-239.807  1.00 70.13           C  
ANISOU  995  CG  PRO B  23    11916   7097   7632  -2546   -972    125       C  
ATOM    996  CD  PRO B  23      65.908 -24.508-239.887  1.00 71.85           C  
ANISOU  996  CD  PRO B  23    12284   7150   7864  -2497   -868    109       C  
ATOM    997  N   HIS B  24      70.071 -22.574-241.186  1.00 57.90           N  
ANISOU  997  N   HIS B  24    10681   5489   5829  -2906   -491   -217       N  
ATOM    998  CA  HIS B  24      71.066 -22.657-242.256  1.00 62.14           C  
ANISOU  998  CA  HIS B  24    11246   6017   6347  -2888   -493   -241       C  
ATOM    999  C   HIS B  24      71.054 -24.091-242.769  1.00 60.75           C  
ANISOU  999  C   HIS B  24    10937   5893   6251  -2717   -725   -116       C  
ATOM   1000  O   HIS B  24      71.069 -25.018-241.976  1.00 66.26           O  
ANISOU 1000  O   HIS B  24    11465   6752   6959  -2718   -848    -50       O  
ATOM   1001  CB  HIS B  24      72.461 -22.309-241.759  1.00 61.07           C  
ANISOU 1001  CB  HIS B  24    11035   6094   6076  -3129   -400   -370       C  
ATOM   1002  CG  HIS B  24      72.620 -20.892-241.325  1.00 69.01           C  
ANISOU 1002  CG  HIS B  24    12180   7042   6998  -3345   -127   -536       C  
ATOM   1003  ND1 HIS B  24      73.168 -20.552-240.103  1.00 82.49           N  
ANISOU 1003  ND1 HIS B  24    13775   8990   8576  -3607    -37   -664       N  
ATOM   1004  CD2 HIS B  24      72.370 -19.723-241.955  1.00 67.96           C  
ANISOU 1004  CD2 HIS B  24    12291   6648   6884  -3349    106   -604       C  
ATOM   1005  CE1 HIS B  24      73.218 -19.243-239.994  1.00 87.93           C  
ANISOU 1005  CE1 HIS B  24    14642   9550   9219  -3786    246   -825       C  
ATOM   1006  NE2 HIS B  24      72.735 -18.709-241.105  1.00 81.65           N  
ANISOU 1006  NE2 HIS B  24    14075   8427   8519  -3622    349   -781       N  
ATOM   1007  N   TRP B  25      71.031 -24.281-244.082  1.00 58.59           N  
ANISOU 1007  N   TRP B  25    10742   5486   6033  -2571   -764    -83       N  
ATOM   1008  CA  TRP B  25      70.671 -25.598-244.621  1.00 55.14           C  
ANISOU 1008  CA  TRP B  25    10211   5047   5694  -2405   -951     20       C  
ATOM   1009  C   TRP B  25      71.548 -26.075-245.772  1.00 62.61           C  
ANISOU 1009  C   TRP B  25    11154   5985   6650  -2348   -999     20       C  
ATOM   1010  O   TRP B  25      71.799 -25.331-246.721  1.00 63.01           O  
ANISOU 1010  O   TRP B  25    11335   5932   6673  -2328   -911    -29       O  
ATOM   1011  CB  TRP B  25      69.224 -25.540-245.064  1.00 59.56           C  
ANISOU 1011  CB  TRP B  25    10847   5458   6325  -2253   -977     70       C  
ATOM   1012  CG  TRP B  25      68.569 -26.837-245.348  1.00 68.47           C  
ANISOU 1012  CG  TRP B  25    11873   6593   7550  -2129  -1139    144       C  
ATOM   1013  CD1 TRP B  25      68.841 -27.690-246.374  1.00 70.31           C  
ANISOU 1013  CD1 TRP B  25    12074   6809   7833  -2044  -1224    158       C  
ATOM   1014  CD2 TRP B  25      67.474 -27.407-244.627  1.00 50.30           C  
ANISOU 1014  CD2 TRP B  25     9499   4306   5308  -2092  -1212    197       C  
ATOM   1015  NE1 TRP B  25      67.992 -28.777-246.324  1.00 67.34           N  
ANISOU 1015  NE1 TRP B  25    11611   6430   7545  -1972  -1328    202       N  
ATOM   1016  CE2 TRP B  25      67.143 -28.620-245.261  1.00 51.55           C  
ANISOU 1016  CE2 TRP B  25     9586   4450   5552  -1998  -1325    229       C  
ATOM   1017  CE3 TRP B  25      66.754 -27.016-243.496  1.00 61.01           C  
ANISOU 1017  CE3 TRP B  25    10845   5683   6652  -2142  -1180    209       C  
ATOM   1018  CZ2 TRP B  25      66.122 -29.442-244.805  1.00 50.57           C  
ANISOU 1018  CZ2 TRP B  25     9384   4330   5502  -1961  -1398    268       C  
ATOM   1019  CZ3 TRP B  25      65.733 -27.833-243.046  1.00 57.54           C  
ANISOU 1019  CZ3 TRP B  25    10323   5254   6285  -2086  -1274    264       C  
ATOM   1020  CH2 TRP B  25      65.427 -29.033-243.704  1.00 60.34           C  
ANISOU 1020  CH2 TRP B  25    10610   5591   6724  -2000  -1377    290       C  
ATOM   1021  N   PRO B  26      71.987 -27.342-245.708  1.00 61.43           N  
ANISOU 1021  N   PRO B  26    10861   5935   6547  -2306  -1123     85       N  
ATOM   1022  CA  PRO B  26      72.847 -27.980-246.713  1.00 55.53           C  
ANISOU 1022  CA  PRO B  26    10092   5189   5820  -2247  -1171     94       C  
ATOM   1023  C   PRO B  26      72.282 -27.892-248.109  1.00 57.45           C  
ANISOU 1023  C   PRO B  26    10448   5265   6115  -2124  -1185     77       C  
ATOM   1024  O   PRO B  26      71.199 -28.395-248.342  1.00 68.65           O  
ANISOU 1024  O   PRO B  26    11859   6616   7608  -2026  -1250    111       O  
ATOM   1025  CB  PRO B  26      72.890 -29.435-246.262  1.00 51.77           C  
ANISOU 1025  CB  PRO B  26     9461   4790   5420  -2181  -1273    195       C  
ATOM   1026  CG  PRO B  26      71.730 -29.585-245.326  1.00 59.46           C  
ANISOU 1026  CG  PRO B  26    10404   5749   6439  -2172  -1298    237       C  
ATOM   1027  CD  PRO B  26      71.622 -28.280-244.640  1.00 51.01           C  
ANISOU 1027  CD  PRO B  26     9396   4716   5270  -2295  -1205    168       C  
ATOM   1028  N   ALA B  27      73.026 -27.307-249.037  1.00 54.09           N  
ANISOU 1028  N   ALA B  27    10109   4802   5640  -2133  -1124     23       N  
ATOM   1029  CA  ALA B  27      72.467 -27.028-250.341  1.00 57.56           C  
ANISOU 1029  CA  ALA B  27    10655   5116   6099  -2011  -1118     13       C  
ATOM   1030  C   ALA B  27      73.530 -26.892-251.424  1.00 66.19           C  
ANISOU 1030  C   ALA B  27    11795   6196   7158  -2007  -1091    -27       C  
ATOM   1031  O   ALA B  27      74.731 -27.018-251.161  1.00 58.95           O  
ANISOU 1031  O   ALA B  27    10827   5369   6201  -2104  -1078    -52       O  
ATOM   1032  CB  ALA B  27      71.620 -25.773-250.267  1.00 63.10           C  
ANISOU 1032  CB  ALA B  27    11490   5727   6756  -1989   -997      5       C  
ATOM   1033  N   ARG B  28      73.076 -26.616-252.641  1.00 70.19           N  
ANISOU 1033  N   ARG B  28    12387   6618   7665  -1889  -1081    -29       N  
ATOM   1034  CA  ARG B  28      73.941 -26.643-253.817  1.00 62.41           C  
ANISOU 1034  CA  ARG B  28    11437   5617   6659  -1860  -1076    -61       C  
ATOM   1035  C   ARG B  28      73.527 -25.604-254.859  1.00 56.79           C  
ANISOU 1035  C   ARG B  28    10868   4818   5891  -1756   -974    -58       C  
ATOM   1036  O   ARG B  28      72.339 -25.388-255.077  1.00 63.50           O  
ANISOU 1036  O   ARG B  28    11740   5650   6739  -1638   -973    -12       O  
ATOM   1037  CB  ARG B  28      73.910 -28.044-254.433  1.00 62.06           C  
ANISOU 1037  CB  ARG B  28    11282   5604   6694  -1793  -1213    -49       C  
ATOM   1038  CG  ARG B  28      74.540 -28.145-255.795  1.00 72.13           C  
ANISOU 1038  CG  ARG B  28    12591   6863   7954  -1741  -1219    -83       C  
ATOM   1039  CD  ARG B  28      74.272 -29.511-256.435  1.00 68.68           C  
ANISOU 1039  CD  ARG B  28    12055   6439   7599  -1685  -1326    -93       C  
ATOM   1040  NE  ARG B  28      72.980 -29.613-257.124  1.00 54.62           N  
ANISOU 1040  NE  ARG B  28    10266   4669   5816  -1592  -1363   -106       N  
ATOM   1041  CZ  ARG B  28      72.219 -30.704-257.103  1.00 75.38           C  
ANISOU 1041  CZ  ARG B  28    12801   7322   8520  -1586  -1431   -128       C  
ATOM   1042  NH1 ARG B  28      72.611 -31.786-256.426  1.00 72.23           N  
ANISOU 1042  NH1 ARG B  28    12328   6895   8220  -1647  -1453   -118       N  
ATOM   1043  NH2 ARG B  28      71.070 -30.720-257.759  1.00 86.56           N  
ANISOU 1043  NH2 ARG B  28    14187   8801   9900  -1519  -1459   -157       N  
ATOM   1044  N   ILE B  29      74.509 -24.976-255.504  1.00 54.71           N  
ANISOU 1044  N   ILE B  29    10694   4519   5575  -1787   -879    -98       N  
ATOM   1045  CA  ILE B  29      74.250 -24.120-256.665  1.00 52.25           C  
ANISOU 1045  CA  ILE B  29    10512   4129   5211  -1658   -774    -75       C  
ATOM   1046  C   ILE B  29      74.019 -24.923-257.931  1.00 65.00           C  
ANISOU 1046  C   ILE B  29    12057   5800   6839  -1526   -901    -59       C  
ATOM   1047  O   ILE B  29      74.914 -25.641-258.413  1.00 66.29           O  
ANISOU 1047  O   ILE B  29    12163   6000   7026  -1569   -978   -103       O  
ATOM   1048  CB  ILE B  29      75.411 -23.148-256.907  1.00 52.84           C  
ANISOU 1048  CB  ILE B  29    10717   4134   5227  -1752   -603   -132       C  
ATOM   1049  CG1 ILE B  29      75.936 -22.666-255.556  1.00 54.42           C  
ANISOU 1049  CG1 ILE B  29    10930   4342   5406  -1959   -501   -199       C  
ATOM   1050  CG2 ILE B  29      74.962 -21.974-257.792  1.00 71.02           C  
ANISOU 1050  CG2 ILE B  29    13193   6317   7474  -1607   -419    -78       C  
ATOM   1051  CD1 ILE B  29      74.885 -21.948-254.744  1.00 65.20           C  
ANISOU 1051  CD1 ILE B  29    12367   5634   6771  -1945   -391   -166       C  
ATOM   1052  N   ASP B  30      72.810 -24.816-258.471  1.00 57.61           N  
ANISOU 1052  N   ASP B  30    11116   4897   5877  -1367   -915      1       N  
ATOM   1053  CA  ASP B  30      72.511 -25.440-259.760  1.00 63.46           C  
ANISOU 1053  CA  ASP B  30    11781   5734   6595  -1251  -1012     -2       C  
ATOM   1054  C   ASP B  30      72.907 -24.551-260.939  1.00 72.48           C  
ANISOU 1054  C   ASP B  30    13034   6853   7650  -1140   -897     30       C  
ATOM   1055  O   ASP B  30      73.232 -23.360-260.780  1.00 63.88           O  
ANISOU 1055  O   ASP B  30    12102   5649   6522  -1131   -713     67       O  
ATOM   1056  CB  ASP B  30      71.030 -25.772-259.875  1.00 64.43           C  
ANISOU 1056  CB  ASP B  30    11811   5976   6696  -1137  -1084     38       C  
ATOM   1057  CG  ASP B  30      70.661 -27.041-259.144  1.00 72.96           C  
ANISOU 1057  CG  ASP B  30    12752   7099   7870  -1239  -1223    -17       C  
ATOM   1058  OD1 ASP B  30      71.550 -27.901-258.942  1.00 67.57           O  
ANISOU 1058  OD1 ASP B  30    12024   6380   7269  -1354  -1283    -75       O  
ATOM   1059  OD2 ASP B  30      69.471 -27.184-258.794  1.00 75.73           O  
ANISOU 1059  OD2 ASP B  30    13039   7524   8212  -1192  -1259      8       O  
ATOM   1060  N   GLU B  31      72.871 -25.138-262.123  1.00 66.00           N  
ANISOU 1060  N   GLU B  31    12135   6141   6799  -1062   -985     10       N  
ATOM   1061  CA  GLU B  31      73.150 -24.396-263.328  1.00 71.74           C  
ANISOU 1061  CA  GLU B  31    12945   6880   7434   -932   -889     54       C  
ATOM   1062  C   GLU B  31      71.965 -23.500-263.642  1.00 71.56           C  
ANISOU 1062  C   GLU B  31    12960   6924   7307   -720   -783    183       C  
ATOM   1063  O   GLU B  31      70.829 -23.810-263.265  1.00 67.15           O  
ANISOU 1063  O   GLU B  31    12303   6476   6735   -669   -851    212       O  
ATOM   1064  CB  GLU B  31      73.421 -25.347-264.500  1.00 94.02           C  
ANISOU 1064  CB  GLU B  31    15651   9831  10243   -918  -1019    -13       C  
ATOM   1065  CG  GLU B  31      72.247 -26.264-264.875  1.00108.66           C  
ANISOU 1065  CG  GLU B  31    17328  11888  12069   -866  -1154    -42       C  
ATOM   1066  CD  GLU B  31      72.133 -26.484-266.382  1.00130.86           C  
ANISOU 1066  CD  GLU B  31    20059  14886  14776   -762  -1192    -63       C  
ATOM   1067  OE1 GLU B  31      73.036 -26.031-267.121  1.00143.43           O  
ANISOU 1067  OE1 GLU B  31    21735  16426  16337   -729  -1130    -52       O  
ATOM   1068  OE2 GLU B  31      71.152 -27.121-266.831  1.00133.12           O  
ANISOU 1068  OE2 GLU B  31    20188  15389  15002   -727  -1280   -104       O  
ATOM   1069  N   LEU B  32      72.226 -22.397-264.335  1.00 66.62           N  
ANISOU 1069  N   LEU B  32    12473   6239   6601   -586   -603    271       N  
ATOM   1070  CA  LEU B  32      71.146 -21.639-264.936  1.00 76.14           C  
ANISOU 1070  CA  LEU B  32    13692   7556   7682   -324   -495    427       C  
ATOM   1071  C   LEU B  32      71.342 -21.650-266.441  1.00101.85           C  
ANISOU 1071  C   LEU B  32    16904  10965  10831   -176   -505    462       C  
ATOM   1072  O   LEU B  32      72.007 -20.763-266.981  1.00117.20           O  
ANISOU 1072  O   LEU B  32    19002  12789  12741   -100   -326    525       O  
ATOM   1073  CB  LEU B  32      71.117 -20.215-264.408  1.00 62.29           C  
ANISOU 1073  CB  LEU B  32    12157   5591   5920   -248   -212    539       C  
ATOM   1074  CG  LEU B  32      69.805 -19.431-264.570  1.00 86.91           C  
ANISOU 1074  CG  LEU B  32    15292   8800   8930     32    -73    732       C  
ATOM   1075  CD1 LEU B  32      69.469 -19.063-266.032  1.00 99.24           C  
ANISOU 1075  CD1 LEU B  32    16818  10555  10334    318    -11    877       C  
ATOM   1076  CD2 LEU B  32      68.647 -20.165-263.915  1.00 83.55           C  
ANISOU 1076  CD2 LEU B  32    14691   8548   8507     24   -249    721       C  
ATOM   1077  N   PRO B  33      70.754 -22.641-267.132  1.00105.95           N  
ANISOU 1077  N   PRO B  33    17211  11756  11289   -144   -697    413       N  
ATOM   1078  CA  PRO B  33      71.052 -22.750-268.559  1.00111.26           C  
ANISOU 1078  CA  PRO B  33    17822  12596  11855    -39   -721    418       C  
ATOM   1079  C   PRO B  33      70.316 -21.695-269.362  1.00112.97           C  
ANISOU 1079  C   PRO B  33    18063  12967  11894    275   -558    625       C  
ATOM   1080  O   PRO B  33      69.195 -21.300-269.023  1.00105.92           O  
ANISOU 1080  O   PRO B  33    17133  12186  10927    430   -505    747       O  
ATOM   1081  CB  PRO B  33      70.550 -24.144-268.913  1.00102.83           C  
ANISOU 1081  CB  PRO B  33    16514  11783  10775   -136   -951    277       C  
ATOM   1082  CG  PRO B  33      69.393 -24.313-268.039  1.00 97.29           C  
ANISOU 1082  CG  PRO B  33    15732  11158  10075   -130   -991    300       C  
ATOM   1083  CD  PRO B  33      69.706 -23.594-266.736  1.00102.64           C  
ANISOU 1083  CD  PRO B  33    16600  11528  10872   -191   -869    354       C  
ATOM   1084  N   GLU B  34      70.960 -21.245-270.429  1.00111.86           N  
ANISOU 1084  N   GLU B  34    17982  12838  11680    384   -470    677       N  
ATOM   1085  CA  GLU B  34      70.343 -20.314-271.344  1.00113.93           C  
ANISOU 1085  CA  GLU B  34    18251  13279  11756    713   -306    895       C  
ATOM   1086  C   GLU B  34      69.096 -20.998-271.894  1.00105.19           C  
ANISOU 1086  C   GLU B  34    16859  12625  10483    830   -473    907       C  
ATOM   1087  O   GLU B  34      68.944 -22.215-271.772  1.00 97.86           O  
ANISOU 1087  O   GLU B  34    15754  11831   9597    623   -699    714       O  
ATOM   1088  CB  GLU B  34      71.329 -19.917-272.450  1.00128.26           C  
ANISOU 1088  CB  GLU B  34    20155  15053  13526    782   -212    924       C  
ATOM   1089  CG  GLU B  34      72.507 -19.040-271.969  1.00133.59           C  
ANISOU 1089  CG  GLU B  34    21122  15303  14334    684      8    923       C  
ATOM   1090  CD  GLU B  34      73.725 -19.065-272.909  1.00131.64           C  
ANISOU 1090  CD  GLU B  34    20932  14997  14089    630     20    858       C  
ATOM   1091  OE1 GLU B  34      73.540 -19.071-274.147  1.00129.99           O  
ANISOU 1091  OE1 GLU B  34    20621  15037  13730    821      5    940       O  
ATOM   1092  OE2 GLU B  34      74.872 -19.077-272.403  1.00126.32           O  
ANISOU 1092  OE2 GLU B  34    20391  14053  13552    394     46    725       O  
ATOM   1093  N   GLY B  35      68.189 -20.222-272.468  1.00105.83           N  
ANISOU 1093  N   GLY B  35    16891  12952  10369   1157   -341   1134       N  
ATOM   1094  CA  GLY B  35      66.961 -20.787-272.993  1.00 95.70           C  
ANISOU 1094  CA  GLY B  35    15310  12165   8886   1274   -485   1150       C  
ATOM   1095  C   GLY B  35      65.800 -20.672-272.027  1.00 89.38           C  
ANISOU 1095  C   GLY B  35    14459  11428   8075   1330   -478   1221       C  
ATOM   1096  O   GLY B  35      64.660 -20.924-272.407  1.00 77.88           O  
ANISOU 1096  O   GLY B  35    12759  10410   6421   1469   -555   1273       O  
ATOM   1097  N   ALA B  36      66.088 -20.288-270.782  1.00 84.23           N  
ANISOU 1097  N   ALA B  36    14022  10366   7616   1214   -385   1216       N  
ATOM   1098  CA  ALA B  36      65.047 -20.091-269.770  1.00 80.04           C  
ANISOU 1098  CA  ALA B  36    13473   9845   7092   1264   -357   1290       C  
ATOM   1099  C   ALA B  36      64.696 -18.610-269.554  1.00 84.70           C  
ANISOU 1099  C   ALA B  36    14266  10285   7632   1573    -37   1576       C  
ATOM   1100  O   ALA B  36      65.357 -17.722-270.072  1.00 82.67           O  
ANISOU 1100  O   ALA B  36    14195   9851   7365   1719    185   1704       O  
ATOM   1101  CB  ALA B  36      65.479 -20.714-268.453  1.00 65.90           C  
ANISOU 1101  CB  ALA B  36    11764   7737   5540    927   -464   1091       C  
ATOM   1102  N   VAL B  37      63.635 -18.357-268.798  1.00 90.78           N  
ANISOU 1102  N   VAL B  37    15002  11120   8372   1677      7   1678       N  
ATOM   1103  CA  VAL B  37      63.390 -17.026-268.252  1.00 90.35           C  
ANISOU 1103  CA  VAL B  37    15186  10806   8337   1899    334   1910       C  
ATOM   1104  C   VAL B  37      64.580 -16.650-267.382  1.00 83.35           C  
ANISOU 1104  C   VAL B  37    14597   9379   7693   1639    465   1786       C  
ATOM   1105  O   VAL B  37      64.977 -17.426-266.494  1.00 75.35           O  
ANISOU 1105  O   VAL B  37    13569   8220   6841   1304    281   1558       O  
ATOM   1106  CB  VAL B  37      62.101 -16.965-267.389  1.00 76.77           C  
ANISOU 1106  CB  VAL B  37    13379   9214   6577   1991    330   1996       C  
ATOM   1107  CG1 VAL B  37      61.976 -15.605-266.708  1.00 73.51           C  
ANISOU 1107  CG1 VAL B  37    13252   8454   6224   2177    700   2207       C  
ATOM   1108  CG2 VAL B  37      60.871 -17.273-268.222  1.00 74.33           C  
ANISOU 1108  CG2 VAL B  37    12752   9495   5994   2252    218   2122       C  
ATOM   1109  N   LYS B  38      65.136 -15.468-267.626  1.00 71.73           N  
ANISOU 1109  N   LYS B  38    13386   7633   6237   1792    798   1936       N  
ATOM   1110  CA  LYS B  38      66.327 -15.015-266.913  1.00 81.82           C  
ANISOU 1110  CA  LYS B  38    14941   8434   7713   1535    959   1804       C  
ATOM   1111  C   LYS B  38      66.019 -14.877-265.422  1.00 87.47           C  
ANISOU 1111  C   LYS B  38    15748   8924   8563   1361   1005   1733       C  
ATOM   1112  O   LYS B  38      64.912 -14.502-265.052  1.00 92.76           O  
ANISOU 1112  O   LYS B  38    16393   9681   9170   1560   1096   1891       O  
ATOM   1113  CB  LYS B  38      66.811 -13.689-267.496  1.00 98.82           C  
ANISOU 1113  CB  LYS B  38    17360  10347   9839   1756   1363   1991       C  
ATOM   1114  CG  LYS B  38      68.263 -13.676-267.971  1.00105.42           C  
ANISOU 1114  CG  LYS B  38    18324  10975  10754   1559   1394   1845       C  
ATOM   1115  CD  LYS B  38      68.416 -12.731-269.164  1.00114.73           C  
ANISOU 1115  CD  LYS B  38    19629  12149  11815   1891   1688   2079       C  
ATOM   1116  CE  LYS B  38      69.877 -12.489-269.560  1.00107.98           C  
ANISOU 1116  CE  LYS B  38    18953  11026  11047   1702   1795   1948       C  
ATOM   1117  NZ  LYS B  38      70.718 -11.989-268.428  1.00 95.53           N  
ANISOU 1117  NZ  LYS B  38    17630   9011   9655   1381   1991   1771       N  
ATOM   1118  N   PRO B  39      66.988 -15.210-264.559  1.00 82.36           N  
ANISOU 1118  N   PRO B  39    15187   8019   8086    992    937   1498       N  
ATOM   1119  CA  PRO B  39      66.730 -15.108-263.126  1.00 80.12           C  
ANISOU 1119  CA  PRO B  39    14971   7552   7917    812    974   1421       C  
ATOM   1120  C   PRO B  39      66.688 -13.655-262.694  1.00 83.29           C  
ANISOU 1120  C   PRO B  39    15666   7632   8347    924   1413   1552       C  
ATOM   1121  O   PRO B  39      67.094 -12.770-263.453  1.00 70.23           O  
ANISOU 1121  O   PRO B  39    14189   5843   6654   1091   1698   1672       O  
ATOM   1122  CB  PRO B  39      67.927 -15.825-262.511  1.00 77.89           C  
ANISOU 1122  CB  PRO B  39    14685   7135   7774    414    802   1152       C  
ATOM   1123  CG  PRO B  39      69.020 -15.538-263.472  1.00 83.51           C  
ANISOU 1123  CG  PRO B  39    15497   7762   8471    409    897   1130       C  
ATOM   1124  CD  PRO B  39      68.379 -15.605-264.831  1.00 88.88           C  
ANISOU 1124  CD  PRO B  39    16054   8723   8994    738    852   1308       C  
ATOM   1125  N   PRO B  40      66.187 -13.400-261.484  1.00 80.64           N  
ANISOU 1125  N   PRO B  40    15391   7165   8082    833   1493   1529       N  
ATOM   1126  CA  PRO B  40      66.357 -12.040-260.970  1.00 80.40           C  
ANISOU 1126  CA  PRO B  40    15671   6768   8108    857   1947   1594       C  
ATOM   1127  C   PRO B  40      67.847 -11.760-260.809  1.00 84.40           C  
ANISOU 1127  C   PRO B  40    16354   7000   8714    541   2076   1385       C  
ATOM   1128  O   PRO B  40      68.634 -12.712-260.686  1.00 77.43           O  
ANISOU 1128  O   PRO B  40    15331   6214   7876    266   1775   1178       O  
ATOM   1129  CB  PRO B  40      65.631 -12.067-259.621  1.00 80.33           C  
ANISOU 1129  CB  PRO B  40    15650   6709   8165    746   1934   1550       C  
ATOM   1130  CG  PRO B  40      65.578 -13.522-259.230  1.00 80.69           C  
ANISOU 1130  CG  PRO B  40    15412   7013   8235    529   1462   1379       C  
ATOM   1131  CD  PRO B  40      65.513 -14.296-260.526  1.00 84.23           C  
ANISOU 1131  CD  PRO B  40    15657   7771   8577    688   1211   1433       C  
ATOM   1132  N   ALA B  41      68.218 -10.486-260.832  1.00 77.52           N  
ANISOU 1132  N   ALA B  41    15780   5804   7871    584   2534   1441       N  
ATOM   1133  CA  ALA B  41      69.609 -10.053-260.723  1.00 84.44           C  
ANISOU 1133  CA  ALA B  41    16842   6419   8821    284   2724   1240       C  
ATOM   1134  C   ALA B  41      70.311 -10.663-259.510  1.00 91.67           C  
ANISOU 1134  C   ALA B  41    17679   7326   9826   -168   2527    941       C  
ATOM   1135  O   ALA B  41      69.712 -10.758-258.446  1.00 95.33           O  
ANISOU 1135  O   ALA B  41    18103   7791  10327   -257   2490    903       O  
ATOM   1136  CB  ALA B  41      69.663  -8.541-260.649  1.00 74.66           C  
ANISOU 1136  CB  ALA B  41    15881   4865   7619    375   3275   1298       C  
ATOM   1137  N   ASN B  42      71.566 -11.088-259.680  1.00 83.02           N  
ANISOU 1137  N   ASN B  42    16546   6248   8750   -434   2401    744       N  
ATOM   1138  CA  ASN B  42      72.416 -11.552-258.572  1.00 82.03           C  
ANISOU 1138  CA  ASN B  42    16350   6134   8682   -858   2267    470       C  
ATOM   1139  C   ASN B  42      71.804 -12.554-257.607  1.00 89.34           C  
ANISOU 1139  C   ASN B  42    17044   7269   9633   -951   1923    422       C  
ATOM   1140  O   ASN B  42      72.168 -12.576-256.431  1.00 97.22           O  
ANISOU 1140  O   ASN B  42    18033   8238  10670  -1248   1934    248       O  
ATOM   1141  CB  ASN B  42      72.901 -10.366-257.744  1.00 89.12           C  
ANISOU 1141  CB  ASN B  42    17485   6756   9622  -1091   2700    327       C  
ATOM   1142  CG  ASN B  42      74.165  -9.766-258.291  1.00103.96           C  
ANISOU 1142  CG  ASN B  42    19434   8578  11487  -1226   2909    184       C  
ATOM   1143  OD1 ASN B  42      75.235 -10.369-258.199  1.00115.13           O  
ANISOU 1143  OD1 ASN B  42    20751  10102  12892  -1498   2720      2       O  
ATOM   1144  ND2 ASN B  42      74.057  -8.572-258.862  1.00 93.29           N  
ANISOU 1144  ND2 ASN B  42    18245   7071  10131  -1029   3309    269       N  
ATOM   1145  N   LYS B  43      70.866 -13.361-258.090  1.00 84.75           N  
ANISOU 1145  N   LYS B  43    16272   6909   9018   -705   1637    571       N  
ATOM   1146  CA  LYS B  43      70.353 -14.485-257.312  1.00 76.42           C  
ANISOU 1146  CA  LYS B  43    14981   6064   7990   -795   1286    518       C  
ATOM   1147  C   LYS B  43      70.758 -15.769-258.008  1.00 78.30           C  
ANISOU 1147  C   LYS B  43    14997   6535   8218   -809    917    474       C  
ATOM   1148  O   LYS B  43      70.893 -15.793-259.230  1.00 81.59           O  
ANISOU 1148  O   LYS B  43    15412   7007   8582   -634    902    554       O  
ATOM   1149  CB  LYS B  43      68.834 -14.428-257.164  1.00 77.38           C  
ANISOU 1149  CB  LYS B  43    15054   6262   8085   -535   1272    699       C  
ATOM   1150  CG  LYS B  43      68.323 -13.475-256.099  1.00 83.91           C  
ANISOU 1150  CG  LYS B  43    16047   6888   8946   -574   1564    713       C  
ATOM   1151  CD  LYS B  43      66.937 -13.904-255.652  1.00 92.41           C  
ANISOU 1151  CD  LYS B  43    16981   8123  10009   -411   1404    831       C  
ATOM   1152  CE  LYS B  43      66.063 -12.724-255.261  1.00 90.75           C  
ANISOU 1152  CE  LYS B  43    16963   7727   9791   -234   1764    977       C  
ATOM   1153  NZ  LYS B  43      64.815 -13.270-254.662  1.00 96.58           N  
ANISOU 1153  NZ  LYS B  43    17533   8646  10517   -135   1566   1053       N  
ATOM   1154  N   TYR B  44      70.946 -16.837-257.235  1.00 86.75           N  
ANISOU 1154  N   TYR B  44    15885   7741   9337  -1009    638    353       N  
ATOM   1155  CA  TYR B  44      71.374 -18.117-257.794  1.00 75.41           C  
ANISOU 1155  CA  TYR B  44    14250   6495   7908  -1042    320    301       C  
ATOM   1156  C   TYR B  44      70.301 -19.178-257.548  1.00 76.04           C  
ANISOU 1156  C   TYR B  44    14124   6764   8003   -964     52    344       C  
ATOM   1157  O   TYR B  44      69.528 -19.082-256.588  1.00 74.49           O  
ANISOU 1157  O   TYR B  44    13915   6558   7829   -980     66    366       O  
ATOM   1158  CB  TYR B  44      72.721 -18.541-257.194  1.00 73.40           C  
ANISOU 1158  CB  TYR B  44    13956   6239   7694  -1343    252    124       C  
ATOM   1159  CG  TYR B  44      73.881 -17.631-257.532  1.00 86.04           C  
ANISOU 1159  CG  TYR B  44    15730   7694   9267  -1455    494     48       C  
ATOM   1160  CD1 TYR B  44      73.877 -16.287-257.165  1.00 97.84           C  
ANISOU 1160  CD1 TYR B  44    17448   8980  10749  -1496    848     40       C  
ATOM   1161  CD2 TYR B  44      74.983 -18.111-258.222  1.00 90.16           C  
ANISOU 1161  CD2 TYR B  44    16201   8278   9779  -1530    394    -25       C  
ATOM   1162  CE1 TYR B  44      74.936 -15.445-257.490  1.00100.30           C  
ANISOU 1162  CE1 TYR B  44    17928   9146  11035  -1621   1101    -50       C  
ATOM   1163  CE2 TYR B  44      76.045 -17.277-258.546  1.00 95.57           C  
ANISOU 1163  CE2 TYR B  44    17041   8839  10431  -1645    621   -106       C  
ATOM   1164  CZ  TYR B  44      76.019 -15.950-258.173  1.00 99.16           C  
ANISOU 1164  CZ  TYR B  44    17717   9087  10873  -1699    977   -125       C  
ATOM   1165  OH  TYR B  44      77.071 -15.125-258.494  1.00105.84           O  
ANISOU 1165  OH  TYR B  44    18724   9800  11689  -1837   1230   -225       O  
ATOM   1166  N   PRO B  45      70.220 -20.174-258.437  1.00 72.16           N  
ANISOU 1166  N   PRO B  45    13476   6444   7496   -886   -173    348       N  
ATOM   1167  CA  PRO B  45      69.267 -21.267-258.229  1.00 78.66           C  
ANISOU 1167  CA  PRO B  45    14103   7448   8338   -853   -409    353       C  
ATOM   1168  C   PRO B  45      69.764 -22.235-257.177  1.00 70.44           C  
ANISOU 1168  C   PRO B  45    12958   6414   7394  -1087   -568    236       C  
ATOM   1169  O   PRO B  45      70.845 -22.809-257.303  1.00 76.18           O  
ANISOU 1169  O   PRO B  45    13647   7140   8157  -1218   -644    150       O  
ATOM   1170  CB  PRO B  45      69.189 -21.942-259.604  1.00 84.27           C  
ANISOU 1170  CB  PRO B  45    14698   8329   8993   -729   -547    363       C  
ATOM   1171  CG  PRO B  45      70.484 -21.598-260.270  1.00 83.53           C  
ANISOU 1171  CG  PRO B  45    14707   8135   8895   -781   -463    319       C  
ATOM   1172  CD  PRO B  45      70.849 -20.228-259.767  1.00 75.53           C  
ANISOU 1172  CD  PRO B  45    13912   6909   7876   -802   -182    353       C  
ATOM   1173  N   ILE B  46      68.975 -22.428-256.137  1.00 68.78           N  
ANISOU 1173  N   ILE B  46    12694   6222   7218  -1123   -609    248       N  
ATOM   1174  CA  ILE B  46      69.445 -23.229-255.021  1.00 72.20           C  
ANISOU 1174  CA  ILE B  46    13037   6664   7733  -1327   -723    164       C  
ATOM   1175  C   ILE B  46      68.735 -24.572-254.927  1.00 66.74           C  
ANISOU 1175  C   ILE B  46    12162   6103   7093  -1317   -937    154       C  
ATOM   1176  O   ILE B  46      67.504 -24.640-255.028  1.00 63.97           O  
ANISOU 1176  O   ILE B  46    11759   5830   6716  -1199   -973    207       O  
ATOM   1177  CB  ILE B  46      69.278 -22.447-253.709  1.00 65.34           C  
ANISOU 1177  CB  ILE B  46    12250   5705   6872  -1427   -586    162       C  
ATOM   1178  CG1 ILE B  46      69.928 -21.071-253.859  1.00 58.98           C  
ANISOU 1178  CG1 ILE B  46    11646   4747   6018  -1454   -322    150       C  
ATOM   1179  CG2 ILE B  46      69.940 -23.165-252.554  1.00 59.19           C  
ANISOU 1179  CG2 ILE B  46    11370   4971   6149  -1635   -683     85       C  
ATOM   1180  CD1 ILE B  46      71.378 -21.148-254.299  1.00 63.22           C  
ANISOU 1180  CD1 ILE B  46    12203   5271   6546  -1581   -310     60       C  
ATOM   1181  N   PHE B  47      69.526 -25.634-254.754  1.00 72.42           N  
ANISOU 1181  N   PHE B  47    12786   6849   7881  -1439  -1058     88       N  
ATOM   1182  CA  PHE B  47      69.012 -26.987-254.517  1.00 59.69           C  
ANISOU 1182  CA  PHE B  47    11020   5316   6343  -1464  -1216     66       C  
ATOM   1183  C   PHE B  47      69.235 -27.400-253.059  1.00 64.77           C  
ANISOU 1183  C   PHE B  47    11614   5943   7054  -1597  -1240     65       C  
ATOM   1184  O   PHE B  47      70.375 -27.471-252.593  1.00 68.75           O  
ANISOU 1184  O   PHE B  47    12117   6434   7570  -1704  -1220     45       O  
ATOM   1185  CB  PHE B  47      69.681 -28.001-255.460  1.00 65.02           C  
ANISOU 1185  CB  PHE B  47    11626   6024   7054  -1476  -1302      9       C  
ATOM   1186  CG  PHE B  47      69.238 -29.447-255.232  1.00 61.63           C  
ANISOU 1186  CG  PHE B  47    11061   5637   6718  -1520  -1413    -28       C  
ATOM   1187  CD1 PHE B  47      68.063 -29.922-255.801  1.00 64.20           C  
ANISOU 1187  CD1 PHE B  47    11309   6057   7029  -1461  -1468    -59       C  
ATOM   1188  CD2 PHE B  47      69.990 -30.315-254.446  1.00 65.24           C  
ANISOU 1188  CD2 PHE B  47    11466   6055   7268  -1619  -1439    -30       C  
ATOM   1189  CE1 PHE B  47      67.638 -31.225-255.602  1.00 58.41           C  
ANISOU 1189  CE1 PHE B  47    10467   5342   6386  -1527  -1530   -117       C  
ATOM   1190  CE2 PHE B  47      69.559 -31.654-254.229  1.00 57.36           C  
ANISOU 1190  CE2 PHE B  47    10366   5059   6370  -1649  -1494    -54       C  
ATOM   1191  CZ  PHE B  47      68.386 -32.092-254.813  1.00 56.50           C  
ANISOU 1191  CZ  PHE B  47    10201   5008   6260  -1618  -1531   -110       C  
ATOM   1192  N   PHE B  48      68.150 -27.682-252.344  1.00 57.04           N  
ANISOU 1192  N   PHE B  48    10576   4993   6104  -1585  -1282     91       N  
ATOM   1193  CA  PHE B  48      68.246 -28.067-250.934  1.00 64.84           C  
ANISOU 1193  CA  PHE B  48    11506   5984   7148  -1694  -1303    105       C  
ATOM   1194  C   PHE B  48      68.299 -29.577-250.755  1.00 63.42           C  
ANISOU 1194  C   PHE B  48    11198   5833   7066  -1725  -1407     97       C  
ATOM   1195  O   PHE B  48      67.362 -30.268-251.122  1.00 50.25           O  
ANISOU 1195  O   PHE B  48     9470   4187   5436  -1680  -1465     79       O  
ATOM   1196  CB  PHE B  48      67.056 -27.516-250.155  1.00 59.69           C  
ANISOU 1196  CB  PHE B  48    10869   5333   6477  -1667  -1273    143       C  
ATOM   1197  CG  PHE B  48      67.013 -26.038-250.131  1.00 62.24           C  
ANISOU 1197  CG  PHE B  48    11336   5594   6720  -1639  -1121    161       C  
ATOM   1198  CD1 PHE B  48      66.176 -25.350-250.983  1.00 67.14           C  
ANISOU 1198  CD1 PHE B  48    12022   6209   7277  -1481  -1061    205       C  
ATOM   1199  CD2 PHE B  48      67.841 -25.331-249.287  1.00 66.35           C  
ANISOU 1199  CD2 PHE B  48    11921   6074   7217  -1770  -1012    134       C  
ATOM   1200  CE1 PHE B  48      66.160 -23.974-250.983  1.00 66.23           C  
ANISOU 1200  CE1 PHE B  48    12063   6003   7099  -1434   -873    240       C  
ATOM   1201  CE2 PHE B  48      67.833 -23.950-249.281  1.00 64.70           C  
ANISOU 1201  CE2 PHE B  48    11868   5772   6944  -1765   -822    132       C  
ATOM   1202  CZ  PHE B  48      66.982 -23.279-250.127  1.00 66.63           C  
ANISOU 1202  CZ  PHE B  48    12202   5965   7148  -1586   -743    195       C  
ATOM   1203  N   PHE B  49      69.372 -30.092-250.174  1.00 58.00           N  
ANISOU 1203  N   PHE B  49    10465   5158   6415  -1802  -1409    113       N  
ATOM   1204  CA  PHE B  49      69.438 -31.535-249.923  1.00 69.18           C  
ANISOU 1204  CA  PHE B  49    11775   6575   7935  -1808  -1462    134       C  
ATOM   1205  C   PHE B  49      68.400 -31.995-248.898  1.00 61.52           C  
ANISOU 1205  C   PHE B  49    10742   5612   7020  -1820  -1486    171       C  
ATOM   1206  O   PHE B  49      67.923 -31.211-248.082  1.00 68.61           O  
ANISOU 1206  O   PHE B  49    11661   6535   7871  -1844  -1469    193       O  
ATOM   1207  CB  PHE B  49      70.827 -31.925-249.455  1.00 50.07           C  
ANISOU 1207  CB  PHE B  49     9307   4200   5518  -1853  -1441    180       C  
ATOM   1208  CG  PHE B  49      71.882 -31.717-250.484  1.00 50.11           C  
ANISOU 1208  CG  PHE B  49     9356   4200   5484  -1844  -1423    142       C  
ATOM   1209  CD1 PHE B  49      71.906 -32.474-251.629  1.00 62.54           C  
ANISOU 1209  CD1 PHE B  49    10931   5715   7117  -1791  -1444    103       C  
ATOM   1210  CD2 PHE B  49      72.866 -30.758-250.303  1.00 57.17           C  
ANISOU 1210  CD2 PHE B  49    10289   5156   6276  -1908  -1371    130       C  
ATOM   1211  CE1 PHE B  49      72.898 -32.274-252.583  1.00 65.90           C  
ANISOU 1211  CE1 PHE B  49    11397   6139   7504  -1782  -1429     69       C  
ATOM   1212  CE2 PHE B  49      73.848 -30.555-251.259  1.00 57.15           C  
ANISOU 1212  CE2 PHE B  49    10328   5150   6235  -1905  -1350     91       C  
ATOM   1213  CZ  PHE B  49      73.866 -31.316-252.394  1.00 60.00           C  
ANISOU 1213  CZ  PHE B  49    10691   5448   6659  -1833  -1386     70       C  
ATOM   1214  N   GLY B  50      68.037 -33.269-248.953  1.00 59.92           N  
ANISOU 1214  N   GLY B  50    10471   5373   6922  -1809  -1506    170       N  
ATOM   1215  CA  GLY B  50      67.068 -33.807-248.024  1.00 50.36           C  
ANISOU 1215  CA  GLY B  50     9203   4158   5774  -1825  -1516    200       C  
ATOM   1216  C   GLY B  50      65.623 -33.636-248.432  1.00 69.30           C  
ANISOU 1216  C   GLY B  50    11604   6571   8157  -1807  -1548    133       C  
ATOM   1217  O   GLY B  50      64.857 -34.601-248.451  1.00 62.96           O  
ANISOU 1217  O   GLY B  50    10745   5746   7432  -1827  -1549     94       O  
ATOM   1218  N   THR B  51      65.251 -32.396-248.723  1.00 67.59           N  
ANISOU 1218  N   THR B  51    11449   6399   7833  -1770  -1553    123       N  
ATOM   1219  CA  THR B  51      63.902 -32.037-249.153  1.00 61.01           C  
ANISOU 1219  CA  THR B  51    10606   5629   6944  -1718  -1577     86       C  
ATOM   1220  C   THR B  51      63.814 -32.039-250.675  1.00 57.45           C  
ANISOU 1220  C   THR B  51    10156   5235   6436  -1663  -1590     14       C  
ATOM   1221  O   THR B  51      62.764 -32.312-251.259  1.00 66.77           O  
ANISOU 1221  O   THR B  51    11271   6520   7580  -1639  -1619    -46       O  
ATOM   1222  CB  THR B  51      63.514 -30.629-248.655  1.00 63.34           C  
ANISOU 1222  CB  THR B  51    10975   5944   7146  -1673  -1539    143       C  
ATOM   1223  OG1 THR B  51      64.385 -29.684-249.268  1.00 72.26           O  
ANISOU 1223  OG1 THR B  51    12205   7044   8206  -1639  -1480    150       O  
ATOM   1224  CG2 THR B  51      63.662 -30.498-247.131  1.00 54.84           C  
ANISOU 1224  CG2 THR B  51     9894   4838   6105  -1746  -1519    200       C  
ATOM   1225  N   HIS B  52      64.936 -31.703-251.298  1.00 60.67           N  
ANISOU 1225  N   HIS B  52    10627   5604   6821  -1648  -1565     15       N  
ATOM   1226  CA  HIS B  52      65.021 -31.492-252.729  1.00 67.25           C  
ANISOU 1226  CA  HIS B  52    11474   6497   7581  -1585  -1568    -37       C  
ATOM   1227  C   HIS B  52      64.154 -30.314-253.185  1.00 67.42           C  
ANISOU 1227  C   HIS B  52    11530   6619   7467  -1462  -1546      2       C  
ATOM   1228  O   HIS B  52      63.854 -30.200-254.360  1.00 74.26           O  
ANISOU 1228  O   HIS B  52    12369   7599   8249  -1385  -1555    -30       O  
ATOM   1229  CB  HIS B  52      64.642 -32.779-253.470  1.00 69.56           C  
ANISOU 1229  CB  HIS B  52    11668   6837   7925  -1632  -1603   -145       C  
ATOM   1230  CG  HIS B  52      65.572 -33.913-253.192  1.00 68.73           C  
ANISOU 1230  CG  HIS B  52    11551   6607   7955  -1717  -1580   -164       C  
ATOM   1231  ND1 HIS B  52      66.118 -34.691-254.193  1.00 86.70           N  
ANISOU 1231  ND1 HIS B  52    13811   8863  10269  -1746  -1563   -248       N  
ATOM   1232  CD2 HIS B  52      66.075 -34.386-252.032  1.00 76.69           C  
ANISOU 1232  CD2 HIS B  52    12558   7518   9062  -1761  -1555    -93       C  
ATOM   1233  CE1 HIS B  52      66.903 -35.603-253.656  1.00 83.44           C  
ANISOU 1233  CE1 HIS B  52    13399   8324   9981  -1793  -1515   -219       C  
ATOM   1234  NE2 HIS B  52      66.904 -35.437-252.345  1.00 84.00           N  
ANISOU 1234  NE2 HIS B  52    13471   8360  10084  -1794  -1512   -116       N  
ATOM   1235  N   GLU B  53      63.765 -29.434-252.261  1.00 71.62           N  
ANISOU 1235  N   GLU B  53    12119   7121   7974  -1435  -1500     80       N  
ATOM   1236  CA  GLU B  53      63.103 -28.182-252.636  1.00 69.33           C  
ANISOU 1236  CA  GLU B  53    11893   6888   7560  -1290  -1428    151       C  
ATOM   1237  C   GLU B  53      64.054 -27.323-253.446  1.00 73.82           C  
ANISOU 1237  C   GLU B  53    12579   7397   8072  -1229  -1340    176       C  
ATOM   1238  O   GLU B  53      65.262 -27.593-253.458  1.00 62.77           O  
ANISOU 1238  O   GLU B  53    11215   5906   6729  -1323  -1341    136       O  
ATOM   1239  CB  GLU B  53      62.650 -27.402-251.402  1.00 64.20           C  
ANISOU 1239  CB  GLU B  53    11306   6175   6914  -1291  -1360    222       C  
ATOM   1240  CG  GLU B  53      61.640 -28.118-250.525  1.00 77.45           C  
ANISOU 1240  CG  GLU B  53    12876   7910   8641  -1341  -1436    210       C  
ATOM   1241  CD  GLU B  53      60.212 -27.701-250.834  1.00 97.20           C  
ANISOU 1241  CD  GLU B  53    15326  10566  11039  -1202  -1432    256       C  
ATOM   1242  OE1 GLU B  53      59.607 -26.966-250.020  1.00100.86           O  
ANISOU 1242  OE1 GLU B  53    15837  11005  11482  -1158  -1369    328       O  
ATOM   1243  OE2 GLU B  53      59.698 -28.099-251.902  1.00104.59           O  
ANISOU 1243  OE2 GLU B  53    16165  11672  11901  -1136  -1484    218       O  
ATOM   1244  N   THR B  54      63.526 -26.289-254.116  1.00 70.91           N  
ANISOU 1244  N   THR B  54    12271   7086   7587  -1060  -1250    254       N  
ATOM   1245  CA  THR B  54      64.379 -25.312-254.804  1.00 64.50           C  
ANISOU 1245  CA  THR B  54    11599   6187   6721   -990  -1123    294       C  
ATOM   1246  C   THR B  54      63.915 -23.869-254.602  1.00 77.94           C  
ANISOU 1246  C   THR B  54    13442   7823   8349   -849   -932    413       C  
ATOM   1247  O   THR B  54      62.764 -23.623-254.243  1.00 91.91           O  
ANISOU 1247  O   THR B  54    15176   9671  10076   -750   -916    483       O  
ATOM   1248  CB  THR B  54      64.445 -25.554-256.319  1.00 72.45           C  
ANISOU 1248  CB  THR B  54    12549   7331   7647   -885  -1164    281       C  
ATOM   1249  OG1 THR B  54      63.250 -25.064-256.941  1.00 75.36           O  
ANISOU 1249  OG1 THR B  54    12866   7888   7879   -680  -1131    372       O  
ATOM   1250  CG2 THR B  54      64.607 -27.035-256.636  1.00 69.29           C  
ANISOU 1250  CG2 THR B  54    12001   7015   7313  -1008  -1326    155       C  
ATOM   1251  N   ALA B  55      64.822 -22.926-254.857  1.00 61.46           N  
ANISOU 1251  N   ALA B  55    11519   5587   6246   -840   -768    435       N  
ATOM   1252  CA  ALA B  55      64.530 -21.502-254.790  1.00 60.82           C  
ANISOU 1252  CA  ALA B  55    11610   5394   6105   -704   -523    547       C  
ATOM   1253  C   ALA B  55      65.698 -20.720-255.348  1.00 73.78           C  
ANISOU 1253  C   ALA B  55    13417   6881   7736   -721   -353    535       C  
ATOM   1254  O   ALA B  55      66.724 -21.302-255.730  1.00 63.74           O  
ANISOU 1254  O   ALA B  55    12112   5609   6498   -843   -448    440       O  
ATOM   1255  CB  ALA B  55      64.236 -21.057-253.352  1.00 64.92           C  
ANISOU 1255  CB  ALA B  55    12195   5792   6679   -808   -433    542       C  
ATOM   1256  N   PHE B  56      65.517 -19.400-255.410  1.00 78.64           N  
ANISOU 1256  N   PHE B  56    14217   7358   8304   -592    -79    637       N  
ATOM   1257  CA  PHE B  56      66.584 -18.473-255.762  1.00 74.73           C  
ANISOU 1257  CA  PHE B  56    13917   6669   7807   -632    152    618       C  
ATOM   1258  C   PHE B  56      66.963 -17.645-254.550  1.00 71.30           C  
ANISOU 1258  C   PHE B  56    13644   6021   7427   -816    370    550       C  
ATOM   1259  O   PHE B  56      66.087 -17.153-253.843  1.00 83.60           O  
ANISOU 1259  O   PHE B  56    15248   7529   8986   -757    482    615       O  
ATOM   1260  CB  PHE B  56      66.162 -17.561-256.919  1.00 75.00           C  
ANISOU 1260  CB  PHE B  56    14060   6697   7741   -330    354    790       C  
ATOM   1261  CG  PHE B  56      66.332 -18.191-258.269  1.00 67.42           C  
ANISOU 1261  CG  PHE B  56    12977   5927   6714   -212    192    811       C  
ATOM   1262  CD1 PHE B  56      67.494 -18.013-258.986  1.00 66.17           C  
ANISOU 1262  CD1 PHE B  56    12904   5679   6558   -270    253    756       C  
ATOM   1263  CD2 PHE B  56      65.343 -18.992-258.803  1.00 76.95           C  
ANISOU 1263  CD2 PHE B  56    13971   7419   7847    -68    -20    863       C  
ATOM   1264  CE1 PHE B  56      67.660 -18.605-260.221  1.00 76.86           C  
ANISOU 1264  CE1 PHE B  56    14141   7213   7849   -171    106    766       C  
ATOM   1265  CE2 PHE B  56      65.502 -19.596-260.037  1.00 70.30           C  
ANISOU 1265  CE2 PHE B  56    13004   6775   6933     12   -161    856       C  
ATOM   1266  CZ  PHE B  56      66.659 -19.403-260.749  1.00 77.43           C  
ANISOU 1266  CZ  PHE B  56    13999   7575   7845    -33   -101    812       C  
ATOM   1267  N   LEU B  57      68.269 -17.509-254.313  1.00 70.70           N  
ANISOU 1267  N   LEU B  57    13638   5840   7384  -1050    434    409       N  
ATOM   1268  CA  LEU B  57      68.810 -16.743-253.186  1.00 63.60           C  
ANISOU 1268  CA  LEU B  57    12872   4778   6515  -1285    653    297       C  
ATOM   1269  C   LEU B  57      70.112 -16.068-253.579  1.00 71.67           C  
ANISOU 1269  C   LEU B  57    14045   5665   7522  -1427    859    195       C  
ATOM   1270  O   LEU B  57      70.818 -16.569-254.453  1.00 67.53           O  
ANISOU 1270  O   LEU B  57    13461   5215   6983  -1415    730    174       O  
ATOM   1271  CB  LEU B  57      69.063 -17.642-251.974  1.00 60.53           C  
ANISOU 1271  CB  LEU B  57    12315   4513   6171  -1530    438    174       C  
ATOM   1272  CG  LEU B  57      67.863 -18.272-251.260  1.00 70.77           C  
ANISOU 1272  CG  LEU B  57    13475   5919   7496  -1461    264    239       C  
ATOM   1273  CD1 LEU B  57      68.347 -19.062-250.075  1.00 81.18           C  
ANISOU 1273  CD1 LEU B  57    14649   7345   8852  -1710    100    122       C  
ATOM   1274  CD2 LEU B  57      66.881 -17.223-250.807  1.00 78.14           C  
ANISOU 1274  CD2 LEU B  57    14552   6719   8418  -1353    507    324       C  
ATOM   1275  N   GLY B  58      70.437 -14.953-252.922  1.00 73.40           N  
ANISOU 1275  N   GLY B  58    14456   5690   7742  -1580   1187    114       N  
ATOM   1276  CA  GLY B  58      71.644 -14.193-253.235  1.00 73.66           C  
ANISOU 1276  CA  GLY B  58    14650   5582   7755  -1746   1438     -7       C  
ATOM   1277  C   GLY B  58      72.773 -14.486-252.258  1.00 69.18           C  
ANISOU 1277  C   GLY B  58    13993   5116   7177  -2126   1382   -236       C  
ATOM   1278  O   GLY B  58      72.515 -14.996-251.170  1.00 68.00           O  
ANISOU 1278  O   GLY B  58    13704   5096   7038  -2255   1235   -288       O  
ATOM   1279  N   PRO B  59      74.022 -14.144-252.633  1.00 77.71           N  
ANISOU 1279  N   PRO B  59    15142   6163   8221  -2302   1509   -369       N  
ATOM   1280  CA  PRO B  59      75.285 -14.425-251.923  1.00 78.57           C  
ANISOU 1280  CA  PRO B  59    15139   6434   8281  -2654   1457   -585       C  
ATOM   1281  C   PRO B  59      75.242 -14.201-250.416  1.00 78.48           C  
ANISOU 1281  C   PRO B  59    15066   6509   8244  -2912   1534   -722       C  
ATOM   1282  O   PRO B  59      75.960 -14.879-249.668  1.00 76.03           O  
ANISOU 1282  O   PRO B  59    14560   6446   7881  -3138   1355   -841       O  
ATOM   1283  CB  PRO B  59      76.266 -13.435-252.550  1.00 82.62           C  
ANISOU 1283  CB  PRO B  59    15801   6838   8753  -2744   1767   -688       C  
ATOM   1284  CG  PRO B  59      75.726 -13.153-253.889  1.00 83.67           C  
ANISOU 1284  CG  PRO B  59    16112   6757   8922  -2429   1843   -502       C  
ATOM   1285  CD  PRO B  59      74.233 -13.244-253.782  1.00 86.96           C  
ANISOU 1285  CD  PRO B  59    16536   7121   9385  -2157   1785   -307       C  
ATOM   1286  N   LYS B  60      74.423 -13.246-249.994  1.00 77.38           N  
ANISOU 1286  N   LYS B  60    15055   6215   8130  -2847   1805   -694       N  
ATOM   1287  CA  LYS B  60      74.284 -12.890-248.589  1.00 87.57           C  
ANISOU 1287  CA  LYS B  60    16275   7604   9394  -3058   1915   -820       C  
ATOM   1288  C   LYS B  60      73.642 -14.015-247.779  1.00 95.51           C  
ANISOU 1288  C   LYS B  60    17117   8751  10422  -3073   1575   -763       C  
ATOM   1289  O   LYS B  60      73.802 -14.093-246.560  1.00100.74           O  
ANISOU 1289  O   LYS B  60    17648   9591  11039  -3295   1561   -883       O  
ATOM   1290  CB  LYS B  60      73.447 -11.618-248.451  1.00 90.54           C  
ANISOU 1290  CB  LYS B  60    16849   7748   9804  -2939   2295   -780       C  
ATOM   1291  CG  LYS B  60      72.078 -11.733-249.107  1.00 95.94           C  
ANISOU 1291  CG  LYS B  60    17652   8237  10564  -2573   2241   -522       C  
ATOM   1292  CD  LYS B  60      70.998 -11.122-248.231  1.00100.61           C  
ANISOU 1292  CD  LYS B  60    18306   8734  11185  -2519   2422   -484       C  
ATOM   1293  CE  LYS B  60      69.735 -10.831-249.021  1.00104.82           C  
ANISOU 1293  CE  LYS B  60    18992   9069  11767  -2124   2503   -220       C  
ATOM   1294  NZ  LYS B  60      68.531 -10.947-248.147  1.00100.93           N  
ANISOU 1294  NZ  LYS B  60    18477   8568  11305  -2054   2455   -136       N  
ATOM   1295  N   ASP B  61      72.900 -14.881-248.457  1.00 84.68           N  
ANISOU 1295  N   ASP B  61    15687   7380   9108  -2795   1301   -570       N  
ATOM   1296  CA  ASP B  61      72.244 -15.990-247.774  1.00 84.96           C  
ANISOU 1296  CA  ASP B  61    15499   7613   9171  -2737    976   -495       C  
ATOM   1297  C   ASP B  61      72.916 -17.323-248.073  1.00 78.18           C  
ANISOU 1297  C   ASP B  61    14410   6990   8306  -2732    633   -479       C  
ATOM   1298  O   ASP B  61      72.373 -18.380-247.761  1.00 79.16           O  
ANISOU 1298  O   ASP B  61    14357   7251   8468  -2639    363   -392       O  
ATOM   1299  CB  ASP B  61      70.761 -16.047-248.150  1.00 82.55           C  
ANISOU 1299  CB  ASP B  61    15237   7200   8930  -2420    925   -296       C  
ATOM   1300  CG  ASP B  61      69.947 -15.004-247.421  1.00 96.57           C  
ANISOU 1300  CG  ASP B  61    17176   8801  10716  -2433   1210   -295       C  
ATOM   1301  OD1 ASP B  61      70.266 -14.726-246.247  1.00100.38           O  
ANISOU 1301  OD1 ASP B  61    17640   9329  11172  -2704   1310   -445       O  
ATOM   1302  OD2 ASP B  61      69.009 -14.447-248.019  1.00101.66           O  
ANISOU 1302  OD2 ASP B  61    17962   9279  11386  -2170   1351   -142       O  
ATOM   1303  N   LEU B  62      74.110 -17.269-248.655  1.00 73.75           N  
ANISOU 1303  N   LEU B  62    13856   6468   7697  -2836    667   -566       N  
ATOM   1304  CA  LEU B  62      74.852 -18.490-248.938  1.00 74.64           C  
ANISOU 1304  CA  LEU B  62    13761   6796   7801  -2832    379   -551       C  
ATOM   1305  C   LEU B  62      76.181 -18.499-248.205  1.00 75.94           C  
ANISOU 1305  C   LEU B  62    13813   7179   7862  -3132    411   -717       C  
ATOM   1306  O   LEU B  62      76.829 -17.466-248.052  1.00 77.86           O  
ANISOU 1306  O   LEU B  62    14178   7372   8034  -3344    680   -873       O  
ATOM   1307  CB  LEU B  62      75.066 -18.649-250.446  1.00 68.19           C  
ANISOU 1307  CB  LEU B  62    13010   5887   7011  -2640    333   -476       C  
ATOM   1308  CG  LEU B  62      73.770 -18.452-251.239  1.00 63.09           C  
ANISOU 1308  CG  LEU B  62    12473   5073   6427  -2345    346   -318       C  
ATOM   1309  CD1 LEU B  62      74.038 -18.522-252.712  1.00 68.90           C  
ANISOU 1309  CD1 LEU B  62    13262   5753   7163  -2172    323   -256       C  
ATOM   1310  CD2 LEU B  62      72.716 -19.459-250.821  1.00 69.39           C  
ANISOU 1310  CD2 LEU B  62    13111   5974   7281  -2218     97   -214       C  
ATOM   1311  N   PHE B  63      76.570 -19.681-247.753  1.00 69.65           N  
ANISOU 1311  N   PHE B  63    12776   6638   7050  -3147    154   -681       N  
ATOM   1312  CA  PHE B  63      77.790 -19.874-246.983  1.00 80.19           C  
ANISOU 1312  CA  PHE B  63    13940   8269   8260  -3396    144   -802       C  
ATOM   1313  C   PHE B  63      78.503 -21.102-247.525  1.00 75.13           C  
ANISOU 1313  C   PHE B  63    13125   7796   7624  -3284    -97   -713       C  
ATOM   1314  O   PHE B  63      77.920 -22.166-247.505  1.00 69.84           O  
ANISOU 1314  O   PHE B  63    12348   7149   7040  -3103   -308   -569       O  
ATOM   1315  CB  PHE B  63      77.472 -20.090-245.494  1.00 74.37           C  
ANISOU 1315  CB  PHE B  63    13049   7735   7474  -3524    104   -822       C  
ATOM   1316  CG  PHE B  63      76.563 -19.054-244.891  1.00 73.56           C  
ANISOU 1316  CG  PHE B  63    13107   7453   7389  -3600    318   -884       C  
ATOM   1317  CD1 PHE B  63      75.193 -19.095-245.104  1.00 68.84           C  
ANISOU 1317  CD1 PHE B  63    12613   6628   6916  -3372    278   -747       C  
ATOM   1318  CD2 PHE B  63      77.076 -18.059-244.081  1.00 76.88           C  
ANISOU 1318  CD2 PHE B  63    13564   7953   7692  -3910    571  -1088       C  
ATOM   1319  CE1 PHE B  63      74.356 -18.151-244.539  1.00 65.99           C  
ANISOU 1319  CE1 PHE B  63    12399   6103   6571  -3422    487   -788       C  
ATOM   1320  CE2 PHE B  63      76.246 -17.114-243.515  1.00 72.14           C  
ANISOU 1320  CE2 PHE B  63    13125   7169   7118  -3982    796  -1149       C  
ATOM   1321  CZ  PHE B  63      74.888 -17.155-243.742  1.00 72.04           C  
ANISOU 1321  CZ  PHE B  63    13223   6911   7238  -3725    755   -988       C  
ATOM   1322  N   PRO B  64      79.745 -20.959-248.017  1.00 78.53           N  
ANISOU 1322  N   PRO B  64    13535   8333   7968  -3394    -47   -802       N  
ATOM   1323  CA  PRO B  64      80.570 -22.076-248.495  1.00 74.48           C  
ANISOU 1323  CA  PRO B  64    12855   7995   7447  -3302   -245   -723       C  
ATOM   1324  C   PRO B  64      80.557 -23.274-247.540  1.00 77.15           C  
ANISOU 1324  C   PRO B  64    12943   8595   7776  -3253   -442   -610       C  
ATOM   1325  O   PRO B  64      80.745 -23.097-246.350  1.00 71.78           O  
ANISOU 1325  O   PRO B  64    12139   8145   6989  -3422   -400   -667       O  
ATOM   1326  CB  PRO B  64      81.973 -21.469-248.574  1.00 66.63           C  
ANISOU 1326  CB  PRO B  64    11839   7177   6301  -3535   -105   -887       C  
ATOM   1327  CG  PRO B  64      81.786 -19.963-248.467  1.00 84.95           C  
ANISOU 1327  CG  PRO B  64    14379   9314   8585  -3727    196  -1058       C  
ATOM   1328  CD  PRO B  64      80.319 -19.670-248.421  1.00 86.38           C  
ANISOU 1328  CD  PRO B  64    14715   9209   8895  -3572    230   -969       C  
ATOM   1329  N   TYR B  65      80.348 -24.478-248.056  1.00 71.78           N  
ANISOU 1329  N   TYR B  65    12189   7883   7202  -3029   -633   -454       N  
ATOM   1330  CA  TYR B  65      80.015 -25.610-247.189  1.00 65.02           C  
ANISOU 1330  CA  TYR B  65    11145   7182   6379  -2936   -783   -317       C  
ATOM   1331  C   TYR B  65      81.120 -26.008-246.242  1.00 67.25           C  
ANISOU 1331  C   TYR B  65    11186   7860   6505  -3049   -801   -308       C  
ATOM   1332  O   TYR B  65      80.892 -26.023-245.035  1.00 77.47           O  
ANISOU 1332  O   TYR B  65    12360   9343   7733  -3129   -798   -296       O  
ATOM   1333  CB  TYR B  65      79.607 -26.824-248.023  1.00 54.65           C  
ANISOU 1333  CB  TYR B  65     9822   5724   5219  -2690   -936   -172       C  
ATOM   1334  CG  TYR B  65      79.602 -28.148-247.279  1.00 64.34           C  
ANISOU 1334  CG  TYR B  65    10853   7112   6481  -2583  -1054    -19       C  
ATOM   1335  CD1 TYR B  65      78.772 -28.359-246.178  1.00 65.18           C  
ANISOU 1335  CD1 TYR B  65    10893   7262   6610  -2582  -1079     39       C  
ATOM   1336  CD2 TYR B  65      80.382 -29.211-247.715  1.00 66.11           C  
ANISOU 1336  CD2 TYR B  65    10971   7420   6728  -2464  -1120     81       C  
ATOM   1337  CE1 TYR B  65      78.750 -29.585-245.509  1.00 65.99           C  
ANISOU 1337  CE1 TYR B  65    10828   7494   6752  -2465  -1160    197       C  
ATOM   1338  CE2 TYR B  65      80.371 -30.440-247.053  1.00 70.89           C  
ANISOU 1338  CE2 TYR B  65    11415   8143   7376  -2339  -1184    245       C  
ATOM   1339  CZ  TYR B  65      79.550 -30.621-245.950  1.00 69.97           C  
ANISOU 1339  CZ  TYR B  65    11237   8069   7280  -2338  -1201    306       C  
ATOM   1340  OH  TYR B  65      79.530 -31.834-245.285  1.00 66.06           O  
ANISOU 1340  OH  TYR B  65    10593   7677   6831  -2200  -1237    483       O  
ATOM   1341  N   LYS B  66      82.298 -26.360-246.761  1.00 79.15           N  
ANISOU 1341  N   LYS B  66    12607   9525   7942  -3043   -821   -302       N  
ATOM   1342  CA  LYS B  66      83.388 -26.842-245.879  1.00 98.35           C  
ANISOU 1342  CA  LYS B  66    14770  12399  10198  -3112   -845   -260       C  
ATOM   1343  C   LYS B  66      83.739 -25.855-244.783  1.00100.62           C  
ANISOU 1343  C   LYS B  66    14973  12970  10286  -3398   -718   -422       C  
ATOM   1344  O   LYS B  66      83.882 -26.208-243.603  1.00107.26           O  
ANISOU 1344  O   LYS B  66    15596  14148  11010  -3441   -748   -365       O  
ATOM   1345  CB  LYS B  66      84.684 -27.146-246.645  1.00104.56           C  
ANISOU 1345  CB  LYS B  66    15485  13334  10909  -3090   -855   -256       C  
ATOM   1346  CG  LYS B  66      84.549 -27.505-248.102  1.00108.48           C  
ANISOU 1346  CG  LYS B  66    16147  13500  11569  -2916   -904   -216       C  
ATOM   1347  CD  LYS B  66      85.819 -28.238-248.551  1.00112.55           C  
ANISOU 1347  CD  LYS B  66    16518  14232  12015  -2840   -946   -141       C  
ATOM   1348  CE  LYS B  66      85.807 -28.461-250.003  1.00111.03           C  
ANISOU 1348  CE  LYS B  66    16487  13741  11959  -2711   -975   -138       C  
ATOM   1349  NZ  LYS B  66      84.802 -29.548-250.267  1.00121.15           N  
ANISOU 1349  NZ  LYS B  66    17808  14778  13447  -2479  -1072     14       N  
ATOM   1350  N   GLU B  67      83.901 -24.614-245.216  1.00 97.66           N  
ANISOU 1350  N   GLU B  67    14774  12463   9869  -3598   -557   -629       N  
ATOM   1351  CA  GLU B  67      84.309 -23.530-244.348  1.00 93.02           C  
ANISOU 1351  CA  GLU B  67    14146  12105   9092  -3923   -380   -842       C  
ATOM   1352  C   GLU B  67      83.344 -23.377-243.195  1.00 88.59           C  
ANISOU 1352  C   GLU B  67    13557  11562   8541  -3974   -367   -836       C  
ATOM   1353  O   GLU B  67      83.754 -23.215-242.050  1.00101.65           O  
ANISOU 1353  O   GLU B  67    15011  13602  10009  -4168   -323   -910       O  
ATOM   1354  CB  GLU B  67      84.403 -22.233-245.148  1.00 96.86           C  
ANISOU 1354  CB  GLU B  67    14898  12313   9592  -4091   -167  -1049       C  
ATOM   1355  CG  GLU B  67      84.805 -21.026-244.339  1.00106.39           C  
ANISOU 1355  CG  GLU B  67    16105  13699  10620  -4463     75  -1310       C  
ATOM   1356  CD  GLU B  67      84.939 -19.769-245.181  1.00112.54           C  
ANISOU 1356  CD  GLU B  67    17170  14164  11426  -4615    332  -1503       C  
ATOM   1357  OE1 GLU B  67      84.704 -19.829-246.405  1.00106.35           O  
ANISOU 1357  OE1 GLU B  67    16573  13042  10793  -4411    304  -1416       O  
ATOM   1358  OE2 GLU B  67      85.278 -18.711-244.607  1.00126.38           O  
ANISOU 1358  OE2 GLU B  67    18961  16012  13046  -4946    583  -1746       O  
ATOM   1359  N   TYR B  68      82.053 -23.460-243.491  1.00 76.43           N  
ANISOU 1359  N   TYR B  68    12199   9636   7205  -3798   -409   -745       N  
ATOM   1360  CA  TYR B  68      81.059 -23.177-242.472  1.00 83.40           C  
ANISOU 1360  CA  TYR B  68    13090  10489   8107  -3853   -375   -754       C  
ATOM   1361  C   TYR B  68      80.486 -24.463-241.924  1.00 71.78           C  
ANISOU 1361  C   TYR B  68    11456   9103   6715  -3628   -579   -527       C  
ATOM   1362  O   TYR B  68      79.526 -24.456-241.147  1.00 71.91           O  
ANISOU 1362  O   TYR B  68    11475   9067   6779  -3616   -592   -492       O  
ATOM   1363  CB  TYR B  68      79.950 -22.278-243.024  1.00 83.92           C  
ANISOU 1363  CB  TYR B  68    13461  10102   8324  -3824   -250   -812       C  
ATOM   1364  CG  TYR B  68      80.331 -20.807-243.132  1.00 89.44           C  
ANISOU 1364  CG  TYR B  68    14335  10714   8936  -4094     35  -1053       C  
ATOM   1365  CD1 TYR B  68      80.292 -19.964-242.019  1.00 89.65           C  
ANISOU 1365  CD1 TYR B  68    14343  10878   8844  -4373    219  -1226       C  
ATOM   1366  CD2 TYR B  68      80.723 -20.258-244.347  1.00 90.61           C  
ANISOU 1366  CD2 TYR B  68    14674  10631   9122  -4078    146  -1114       C  
ATOM   1367  CE1 TYR B  68      80.639 -18.612-242.124  1.00 86.62           C  
ANISOU 1367  CE1 TYR B  68    14140  10380   8390  -4641    530  -1466       C  
ATOM   1368  CE2 TYR B  68      81.071 -18.909-244.460  1.00 90.73           C  
ANISOU 1368  CE2 TYR B  68    14871  10532   9069  -4324    450  -1333       C  
ATOM   1369  CZ  TYR B  68      81.026 -18.093-243.349  1.00 93.74           C  
ANISOU 1369  CZ  TYR B  68    15246  11029   9344  -4610    652  -1513       C  
ATOM   1370  OH  TYR B  68      81.374 -16.762-243.474  1.00 95.08           O  
ANISOU 1370  OH  TYR B  68    15565  11084   9475  -4796   1002  -1700       O  
ATOM   1371  N   LYS B  69      81.103 -25.572-242.300  1.00 68.67           N  
ANISOU 1371  N   LYS B  69    10922   8839   6332  -3452   -718   -372       N  
ATOM   1372  CA  LYS B  69      80.572 -26.866-241.922  1.00 62.85           C  
ANISOU 1372  CA  LYS B  69    10062   8122   5697  -3215   -873   -145       C  
ATOM   1373  C   LYS B  69      80.361 -27.020-240.434  1.00 71.21           C  
ANISOU 1373  C   LYS B  69    10925   9484   6647  -3287   -882   -101       C  
ATOM   1374  O   LYS B  69      79.294 -27.437-239.997  1.00 79.19           O  
ANISOU 1374  O   LYS B  69    11960  10349   7779  -3174   -941      0       O  
ATOM   1375  CB  LYS B  69      81.472 -27.989-242.402  1.00 76.39           C  
ANISOU 1375  CB  LYS B  69    11635   9981   7407  -3039   -966     11       C  
ATOM   1376  CG  LYS B  69      81.034 -29.326-241.828  1.00 70.41           C  
ANISOU 1376  CG  LYS B  69    10739   9277   6738  -2811  -1071    249       C  
ATOM   1377  CD  LYS B  69      81.509 -30.485-242.669  1.00 74.60           C  
ANISOU 1377  CD  LYS B  69    11243   9735   7368  -2579  -1132    411       C  
ATOM   1378  CE  LYS B  69      81.214 -31.812-241.995  1.00 69.12           C  
ANISOU 1378  CE  LYS B  69    10405   9114   6745  -2361  -1180    654       C  
ATOM   1379  NZ  LYS B  69      81.717 -32.933-242.836  1.00 82.42           N  
ANISOU 1379  NZ  LYS B  69    12082  10700   8534  -2141  -1194    803       N  
ATOM   1380  N   ASP B  70      81.357 -26.684-239.637  1.00 74.24           N  
ANISOU 1380  N   ASP B  70    11103  10314   6790  -3481   -821   -181       N  
ATOM   1381  CA  ASP B  70      81.208 -26.987-238.235  1.00 82.53           C  
ANISOU 1381  CA  ASP B  70    11928  11708   7721  -3517   -845   -109       C  
ATOM   1382  C   ASP B  70      80.196 -26.060-237.556  1.00 85.82           C  
ANISOU 1382  C   ASP B  70    12466  11982   8160  -3692   -758   -254       C  
ATOM   1383  O   ASP B  70      79.477 -26.493-236.663  1.00 94.59           O  
ANISOU 1383  O   ASP B  70    13491  13152   9298  -3623   -815   -145       O  
ATOM   1384  CB  ASP B  70      82.550 -26.938-237.521  1.00 98.52           C  
ANISOU 1384  CB  ASP B  70    13653  14333   9446  -3672   -807   -148       C  
ATOM   1385  CG  ASP B  70      82.545 -27.764-236.246  1.00120.37           C  
ANISOU 1385  CG  ASP B  70    16127  17511  12097  -3572   -877     46       C  
ATOM   1386  OD1 ASP B  70      81.445 -28.128-235.775  1.00131.43           O  
ANISOU 1386  OD1 ASP B  70    17582  18714  13641  -3456   -928    153       O  
ATOM   1387  OD2 ASP B  70      83.635 -28.067-235.719  1.00125.89           O  
ANISOU 1387  OD2 ASP B  70    16532  18749  12552  -3597   -878    103       O  
ATOM   1388  N   LYS B  71      80.092 -24.805-237.980  1.00 79.50           N  
ANISOU 1388  N   LYS B  71    11878  10968   7359  -3902   -604   -486       N  
ATOM   1389  CA  LYS B  71      79.101 -23.919-237.353  1.00 71.14           C  
ANISOU 1389  CA  LYS B  71    10953   9744   6333  -4050   -491   -612       C  
ATOM   1390  C   LYS B  71      77.642 -24.350-237.615  1.00 89.17           C  
ANISOU 1390  C   LYS B  71    13401  11615   8863  -3805   -587   -461       C  
ATOM   1391  O   LYS B  71      76.774 -24.146-236.766  1.00 93.62           O  
ANISOU 1391  O   LYS B  71    13969  12155   9447  -3846   -568   -466       O  
ATOM   1392  CB  LYS B  71      79.295 -22.483-237.821  1.00 71.93           C  
ANISOU 1392  CB  LYS B  71    11275   9657   6398  -4302   -257   -877       C  
ATOM   1393  CG  LYS B  71      78.721 -21.442-236.879  1.00 86.53           C  
ANISOU 1393  CG  LYS B  71    13192  11495   8188  -4552    -71  -1058       C  
ATOM   1394  CD  LYS B  71      79.102 -20.027-237.307  1.00 79.48           C  
ANISOU 1394  CD  LYS B  71    12515  10438   7244  -4826    220  -1332       C  
ATOM   1395  CE  LYS B  71      79.246 -19.105-236.104  1.00 97.84           C  
ANISOU 1395  CE  LYS B  71    14774  13011   9389  -5197    437  -1578       C  
ATOM   1396  NZ  LYS B  71      80.596 -18.447-236.021  1.00 99.96           N  
ANISOU 1396  NZ  LYS B  71    14940  13612   9430  -5531    623  -1829       N  
ATOM   1397  N   PHE B  72      77.369 -24.945-238.776  1.00 83.85           N  
ANISOU 1397  N   PHE B  72    12850  10643   8364  -3566   -685   -340       N  
ATOM   1398  CA  PHE B  72      75.982 -25.236-239.171  1.00 82.86           C  
ANISOU 1398  CA  PHE B  72    12887  10144   8453  -3365   -755   -237       C  
ATOM   1399  C   PHE B  72      75.669 -26.714-239.348  1.00 81.58           C  
ANISOU 1399  C   PHE B  72    12625   9955   8416  -3101   -937    -15       C  
ATOM   1400  O   PHE B  72      74.504 -27.093-239.522  1.00 84.07           O  
ANISOU 1400  O   PHE B  72    13029  10022   8889  -2955  -1001     65       O  
ATOM   1401  CB  PHE B  72      75.637 -24.517-240.477  1.00 80.69           C  
ANISOU 1401  CB  PHE B  72    12881   9495   8284  -3318   -675   -312       C  
ATOM   1402  CG  PHE B  72      75.871 -23.048-240.433  1.00 87.59           C  
ANISOU 1402  CG  PHE B  72    13902  10310   9066  -3553   -445   -521       C  
ATOM   1403  CD1 PHE B  72      75.765 -22.347-239.244  1.00 83.79           C  
ANISOU 1403  CD1 PHE B  72    13377   9983   8476  -3777   -318   -641       C  
ATOM   1404  CD2 PHE B  72      76.194 -22.361-241.582  1.00 87.36           C  
ANISOU 1404  CD2 PHE B  72    14065  10066   9062  -3557   -330   -602       C  
ATOM   1405  CE1 PHE B  72      75.995 -20.984-239.202  1.00 83.06           C  
ANISOU 1405  CE1 PHE B  72    13441   9811   8308  -4016    -58   -855       C  
ATOM   1406  CE2 PHE B  72      76.414 -21.008-241.551  1.00 83.75           C  
ANISOU 1406  CE2 PHE B  72    13767   9521   8533  -3773    -73   -793       C  
ATOM   1407  CZ  PHE B  72      76.313 -20.313-240.359  1.00 84.78           C  
ANISOU 1407  CZ  PHE B  72    13865   9784   8562  -4011     76   -927       C  
ATOM   1408  N   GLY B  73      76.701 -27.547-239.302  1.00 82.52           N  
ANISOU 1408  N   GLY B  73    12559  10333   8463  -3044   -999     82       N  
ATOM   1409  CA  GLY B  73      76.567 -28.949-239.660  1.00 70.55           C  
ANISOU 1409  CA  GLY B  73    10981   8747   7079  -2792  -1118    285       C  
ATOM   1410  C   GLY B  73      76.056 -29.937-238.629  1.00 62.96           C  
ANISOU 1410  C   GLY B  73     9865   7903   6153  -2673  -1183    463       C  
ATOM   1411  O   GLY B  73      75.994 -31.136-238.915  1.00 76.73           O  
ANISOU 1411  O   GLY B  73    11569   9573   8014  -2468  -1240    631       O  
ATOM   1412  N   LYS B  74      75.669 -29.481-237.446  1.00 64.84           N  
ANISOU 1412  N   LYS B  74    10025   8310   6300  -2796  -1155    429       N  
ATOM   1413  CA  LYS B  74      75.234 -30.438-236.438  1.00 73.08           C  
ANISOU 1413  CA  LYS B  74    10912   9486   7370  -2673  -1208    613       C  
ATOM   1414  C   LYS B  74      73.763 -30.774-236.618  1.00 74.11           C  
ANISOU 1414  C   LYS B  74    11194   9253   7712  -2562  -1254    652       C  
ATOM   1415  O   LYS B  74      73.006 -30.027-237.242  1.00 77.35           O  
ANISOU 1415  O   LYS B  74    11802   9385   8203  -2615  -1238    522       O  
ATOM   1416  CB  LYS B  74      75.497 -29.921-235.029  1.00 88.77           C  
ANISOU 1416  CB  LYS B  74    12712  11867   9149  -2846  -1166    574       C  
ATOM   1417  CG  LYS B  74      74.683 -28.717-234.593  1.00104.31           C  
ANISOU 1417  CG  LYS B  74    14805  13727  11100  -3053  -1101    384       C  
ATOM   1418  CD  LYS B  74      74.729 -28.609-233.061  1.00111.70           C  
ANISOU 1418  CD  LYS B  74    15523  15053  11863  -3174  -1081    397       C  
ATOM   1419  CE  LYS B  74      73.822 -27.516-232.506  1.00111.30           C  
ANISOU 1419  CE  LYS B  74    15595  14883  11812  -3368  -1002    223       C  
ATOM   1420  NZ  LYS B  74      72.829 -28.083-231.544  1.00111.81           N  
ANISOU 1420  NZ  LYS B  74    15587  14955  11940  -3273  -1065    356       N  
ATOM   1421  N   SER B  75      73.367 -31.912-236.073  1.00 60.45           N  
ANISOU 1421  N   SER B  75     9363   7542   6064  -2400  -1294    839       N  
ATOM   1422  CA  SER B  75      72.041 -32.425-236.325  1.00 74.02           C  
ANISOU 1422  CA  SER B  75    11206   8933   7985  -2292  -1332    877       C  
ATOM   1423  C   SER B  75      70.968 -31.433-235.944  1.00 72.53           C  
ANISOU 1423  C   SER B  75    11124   8634   7800  -2419  -1328    746       C  
ATOM   1424  O   SER B  75      71.133 -30.612-235.055  1.00 68.80           O  
ANISOU 1424  O   SER B  75    10587   8370   7184  -2577  -1287    673       O  
ATOM   1425  CB  SER B  75      71.824 -33.740-235.589  1.00 82.48           C  
ANISOU 1425  CB  SER B  75    12145  10067   9126  -2125  -1336   1094       C  
ATOM   1426  OG  SER B  75      72.206 -34.828-236.418  1.00 89.88           O  
ANISOU 1426  OG  SER B  75    13101  10866  10182  -1954  -1318   1204       O  
ATOM   1427  N   ASN B  76      69.867 -31.529-236.666  1.00 74.37           N  
ANISOU 1427  N   ASN B  76    11515   8550   8191  -2350  -1357    714       N  
ATOM   1428  CA  ASN B  76      68.717 -30.672-236.494  1.00 72.92           C  
ANISOU 1428  CA  ASN B  76    11449   8225   8032  -2422  -1349    614       C  
ATOM   1429  C   ASN B  76      67.541 -31.543-236.869  1.00 73.56           C  
ANISOU 1429  C   ASN B  76    11583   8081   8287  -2285  -1405    677       C  
ATOM   1430  O   ASN B  76      67.674 -32.432-237.713  1.00 67.71           O  
ANISOU 1430  O   ASN B  76    10858   7225   7645  -2175  -1427    722       O  
ATOM   1431  CB  ASN B  76      68.810 -29.427-237.387  1.00 84.56           C  
ANISOU 1431  CB  ASN B  76    13093   9571   9466  -2507  -1288    455       C  
ATOM   1432  CG  ASN B  76      67.673 -28.442-237.155  1.00 85.07           C  
ANISOU 1432  CG  ASN B  76    13282   9500   9540  -2561  -1240    373       C  
ATOM   1433  OD1 ASN B  76      66.531 -28.686-237.551  1.00 75.73           O  
ANISOU 1433  OD1 ASN B  76    12172   8135   8466  -2455  -1285    399       O  
ATOM   1434  ND2 ASN B  76      67.987 -27.313-236.519  1.00 88.32           N  
ANISOU 1434  ND2 ASN B  76    13716  10012   9829  -2733  -1131    267       N  
ATOM   1435  N   LYS B  77      66.391 -31.318-236.250  1.00 74.53           N  
ANISOU 1435  N   LYS B  77    11728   8147   8442  -2302  -1417    668       N  
ATOM   1436  CA  LYS B  77      65.309 -32.279-236.391  1.00 81.50           C  
ANISOU 1436  CA  LYS B  77    12620   8875   9473  -2195  -1462    727       C  
ATOM   1437  C   LYS B  77      64.178 -31.776-237.313  1.00 83.69           C  
ANISOU 1437  C   LYS B  77    13040   8953   9806  -2172  -1481    627       C  
ATOM   1438  O   LYS B  77      63.095 -32.369-237.375  1.00 95.25           O  
ANISOU 1438  O   LYS B  77    14507  10319  11365  -2118  -1514    641       O  
ATOM   1439  CB  LYS B  77      64.803 -32.663-234.988  1.00 91.70           C  
ANISOU 1439  CB  LYS B  77    13800  10279  10765  -2206  -1467    820       C  
ATOM   1440  CG  LYS B  77      65.949 -33.164-234.063  1.00 97.41           C  
ANISOU 1440  CG  LYS B  77    14349  11263  11399  -2201  -1441    946       C  
ATOM   1441  CD  LYS B  77      67.074 -33.885-234.865  1.00116.13           C  
ANISOU 1441  CD  LYS B  77    16693  13645  13788  -2112  -1423   1009       C  
ATOM   1442  CE  LYS B  77      68.188 -34.476-234.014  1.00112.46           C  
ANISOU 1442  CE  LYS B  77    16037  13469  13223  -2061  -1387   1169       C  
ATOM   1443  NZ  LYS B  77      68.843 -35.672-234.634  1.00105.47           N  
ANISOU 1443  NZ  LYS B  77    15127  12520  12427  -1900  -1345   1300       N  
ATOM   1444  N   ARG B  78      64.447 -30.700-238.051  1.00 70.38           N  
ANISOU 1444  N   ARG B  78    11463   7226   8051  -2207  -1446    532       N  
ATOM   1445  CA  ARG B  78      63.552 -30.257-239.120  1.00 65.26           C  
ANISOU 1445  CA  ARG B  78    10936   6428   7433  -2144  -1452    467       C  
ATOM   1446  C   ARG B  78      63.531 -31.336-240.192  1.00 63.44           C  
ANISOU 1446  C   ARG B  78    10692   6118   7295  -2057  -1502    472       C  
ATOM   1447  O   ARG B  78      64.550 -31.998-240.433  1.00 64.27           O  
ANISOU 1447  O   ARG B  78    10753   6247   7421  -2049  -1501    503       O  
ATOM   1448  CB  ARG B  78      64.006 -28.920-239.718  1.00 70.29           C  
ANISOU 1448  CB  ARG B  78    11698   7031   7977  -2179  -1368    388       C  
ATOM   1449  CG  ARG B  78      63.794 -27.713-238.826  1.00 74.45           C  
ANISOU 1449  CG  ARG B  78    12279   7586   8423  -2274  -1270    349       C  
ATOM   1450  CD  ARG B  78      62.332 -27.495-238.490  1.00 76.37           C  
ANISOU 1450  CD  ARG B  78    12551   7768   8698  -2218  -1277    369       C  
ATOM   1451  NE  ARG B  78      61.603 -26.814-239.551  1.00 81.39           N  
ANISOU 1451  NE  ARG B  78    13310   8289   9325  -2104  -1233    352       N  
ATOM   1452  CZ  ARG B  78      61.640 -25.502-239.752  1.00 76.36           C  
ANISOU 1452  CZ  ARG B  78    12814   7578   8621  -2110  -1085    316       C  
ATOM   1453  NH1 ARG B  78      62.379 -24.729-238.960  1.00 71.74           N  
ANISOU 1453  NH1 ARG B  78    12268   7015   7976  -2262   -963    258       N  
ATOM   1454  NH2 ARG B  78      60.935 -24.965-240.736  1.00 71.07           N  
ANISOU 1454  NH2 ARG B  78    12241   6827   7935  -1964  -1038    337       N  
ATOM   1455  N   LYS B  79      62.374 -31.540-240.812  1.00 64.31           N  
ANISOU 1455  N   LYS B  79    10829   6155   7451  -1997  -1536    437       N  
ATOM   1456  CA  LYS B  79      62.203 -32.679-241.705  1.00 64.53           C  
ANISOU 1456  CA  LYS B  79    10827   6123   7567  -1952  -1566    414       C  
ATOM   1457  C   LYS B  79      63.169 -32.618-242.886  1.00 66.49           C  
ANISOU 1457  C   LYS B  79    11124   6345   7796  -1928  -1555    374       C  
ATOM   1458  O   LYS B  79      63.220 -31.627-243.603  1.00 64.19           O  
ANISOU 1458  O   LYS B  79    10913   6052   7424  -1904  -1541    330       O  
ATOM   1459  CB  LYS B  79      60.762 -32.757-242.226  1.00 84.72           C  
ANISOU 1459  CB  LYS B  79    13385   8669  10135  -1916  -1599    354       C  
ATOM   1460  CG  LYS B  79      59.666 -32.773-241.164  1.00100.23           C  
ANISOU 1460  CG  LYS B  79    15305  10662  12115  -1935  -1613    383       C  
ATOM   1461  CD  LYS B  79      58.353 -33.285-241.773  1.00105.04           C  
ANISOU 1461  CD  LYS B  79    15874  11291  12745  -1916  -1645    312       C  
ATOM   1462  CE  LYS B  79      57.195 -33.212-240.790  1.00104.14           C  
ANISOU 1462  CE  LYS B  79    15717  11218  12634  -1931  -1660    335       C  
ATOM   1463  NZ  LYS B  79      55.953 -33.821-241.343  1.00 98.24           N  
ANISOU 1463  NZ  LYS B  79    14905  10528  11895  -1936  -1686    249       N  
ATOM   1464  N   GLY B  80      63.936 -33.683-243.080  1.00 69.89           N  
ANISOU 1464  N   GLY B  80    11509   6747   8301  -1923  -1543    401       N  
ATOM   1465  CA  GLY B  80      64.893 -33.735-244.167  1.00 57.43           C  
ANISOU 1465  CA  GLY B  80     9968   5143   6711  -1901  -1532    366       C  
ATOM   1466  C   GLY B  80      66.245 -33.080-243.892  1.00 53.12           C  
ANISOU 1466  C   GLY B  80     9432   4668   6082  -1929  -1505    404       C  
ATOM   1467  O   GLY B  80      67.109 -33.079-244.759  1.00 61.96           O  
ANISOU 1467  O   GLY B  80    10582   5774   7186  -1914  -1494    377       O  
ATOM   1468  N   PHE B  81      66.467 -32.541-242.706  1.00 59.84           N  
ANISOU 1468  N   PHE B  81    10249   5616   6871  -1984  -1488    452       N  
ATOM   1469  CA  PHE B  81      67.766 -31.896-242.439  1.00 56.86           C  
ANISOU 1469  CA  PHE B  81     9861   5353   6389  -2045  -1450    458       C  
ATOM   1470  C   PHE B  81      68.920 -32.881-242.395  1.00 66.34           C  
ANISOU 1470  C   PHE B  81    10967   6628   7611  -2010  -1441    540       C  
ATOM   1471  O   PHE B  81      69.889 -32.781-243.156  1.00 61.50           O  
ANISOU 1471  O   PHE B  81    10376   6029   6963  -2006  -1427    515       O  
ATOM   1472  CB  PHE B  81      67.749 -31.155-241.120  1.00 57.00           C  
ANISOU 1472  CB  PHE B  81     9839   5501   6319  -2139  -1420    471       C  
ATOM   1473  CG  PHE B  81      68.944 -30.255-240.927  1.00 67.06           C  
ANISOU 1473  CG  PHE B  81    11111   6910   7457  -2247  -1358    422       C  
ATOM   1474  CD1 PHE B  81      68.951 -28.975-241.462  1.00 59.44           C  
ANISOU 1474  CD1 PHE B  81    10284   5875   6427  -2309  -1286    313       C  
ATOM   1475  CD2 PHE B  81      70.058 -30.689-240.219  1.00 77.21           C  
ANISOU 1475  CD2 PHE B  81    12253   8410   8672  -2285  -1350    487       C  
ATOM   1476  CE1 PHE B  81      70.043 -28.131-241.281  1.00 67.57           C  
ANISOU 1476  CE1 PHE B  81    11319   7022   7331  -2442  -1199    240       C  
ATOM   1477  CE2 PHE B  81      71.153 -29.858-240.032  1.00 71.49           C  
ANISOU 1477  CE2 PHE B  81    11507   7856   7801  -2414  -1286    417       C  
ATOM   1478  CZ  PHE B  81      71.148 -28.579-240.570  1.00 62.65           C  
ANISOU 1478  CZ  PHE B  81    10537   6640   6626  -2509  -1207    278       C  
ATOM   1479  N   ASN B  82      68.809 -33.826-241.470  1.00 61.69           N  
ANISOU 1479  N   ASN B  82    10272   6093   7077  -1972  -1436    653       N  
ATOM   1480  CA  ASN B  82      69.811 -34.861-241.313  1.00 64.43           C  
ANISOU 1480  CA  ASN B  82    10519   6513   7447  -1897  -1397    776       C  
ATOM   1481  C   ASN B  82      69.942 -35.696-242.573  1.00 61.43           C  
ANISOU 1481  C   ASN B  82    10201   5959   7182  -1821  -1377    752       C  
ATOM   1482  O   ASN B  82      71.032 -36.180-242.875  1.00 60.92           O  
ANISOU 1482  O   ASN B  82    10096   5943   7109  -1765  -1338    816       O  
ATOM   1483  CB  ASN B  82      69.478 -35.745-240.113  1.00 66.86           C  
ANISOU 1483  CB  ASN B  82    10717   6882   7806  -1841  -1367    922       C  
ATOM   1484  CG  ASN B  82      69.423 -34.956-238.817  1.00 64.13           C  
ANISOU 1484  CG  ASN B  82    10289   6747   7331  -1926  -1385    942       C  
ATOM   1485  OD1 ASN B  82      70.316 -34.157-238.535  1.00 75.34           O  
ANISOU 1485  OD1 ASN B  82    11658   8369   8598  -2007  -1382    914       O  
ATOM   1486  ND2 ASN B  82      68.389 -35.191-238.012  1.00 56.14           N  
ANISOU 1486  ND2 ASN B  82     9257   5701   6373  -1923  -1393    979       N  
ATOM   1487  N   GLU B  83      68.848 -35.846-243.323  1.00 57.64           N  
ANISOU 1487  N   GLU B  83     9807   5302   6792  -1823  -1397    654       N  
ATOM   1488  CA  GLU B  83      68.913 -36.521-244.628  1.00 54.56           C  
ANISOU 1488  CA  GLU B  83     9474   4766   6490  -1786  -1373    588       C  
ATOM   1489  C   GLU B  83      69.731 -35.669-245.601  1.00 62.28           C  
ANISOU 1489  C   GLU B  83    10512   5779   7375  -1805  -1403    512       C  
ATOM   1490  O   GLU B  83      70.338 -36.184-246.540  1.00 66.75           O  
ANISOU 1490  O   GLU B  83    11099   6282   7981  -1769  -1376    491       O  
ATOM   1491  CB  GLU B  83      67.510 -36.805-245.192  1.00 51.66           C  
ANISOU 1491  CB  GLU B  83     9155   4271   6202  -1809  -1389    478       C  
ATOM   1492  CG  GLU B  83      66.742 -38.008-244.459  1.00 52.38           C  
ANISOU 1492  CG  GLU B  83     9200   4277   6426  -1797  -1319    534       C  
ATOM   1493  CD  GLU B  83      66.268 -37.611-243.064  1.00 74.53           C  
ANISOU 1493  CD  GLU B  83    11951   7176   9190  -1810  -1347    619       C  
ATOM   1494  OE1 GLU B  83      66.140 -36.386-242.804  1.00 85.30           O  
ANISOU 1494  OE1 GLU B  83    13331   8642  10438  -1852  -1421    587       O  
ATOM   1495  OE2 GLU B  83      66.051 -38.501-242.216  1.00 78.35           O  
ANISOU 1495  OE2 GLU B  83    12383   7627   9759  -1778  -1278    719       O  
ATOM   1496  N   GLY B  84      69.768 -34.368-245.353  1.00 62.20           N  
ANISOU 1496  N   GLY B  84    10534   5857   7243  -1866  -1437    471       N  
ATOM   1497  CA  GLY B  84      70.517 -33.466-246.206  1.00 64.09           C  
ANISOU 1497  CA  GLY B  84    10843   6117   7392  -1892  -1438    399       C  
ATOM   1498  C   GLY B  84      72.000 -33.503-245.896  1.00 68.17           C  
ANISOU 1498  C   GLY B  84    11291   6772   7836  -1907  -1406    459       C  
ATOM   1499  O   GLY B  84      72.830 -33.628-246.799  1.00 71.81           O  
ANISOU 1499  O   GLY B  84    11776   7218   8291  -1883  -1396    436       O  
ATOM   1500  N   LEU B  85      72.332 -33.377-244.614  1.00 63.21           N  
ANISOU 1500  N   LEU B  85    10564   6313   7139  -1949  -1391    534       N  
ATOM   1501  CA  LEU B  85      73.705 -33.578-244.136  1.00 52.21           C  
ANISOU 1501  CA  LEU B  85     9053   5132   5653  -1953  -1360    616       C  
ATOM   1502  C   LEU B  85      74.335 -34.816-244.768  1.00 70.38           C  
ANISOU 1502  C   LEU B  85    11319   7379   8045  -1826  -1335    705       C  
ATOM   1503  O   LEU B  85      75.482 -34.811-245.224  1.00 61.62           O  
ANISOU 1503  O   LEU B  85    10181   6362   6872  -1813  -1316    715       O  
ATOM   1504  CB  LEU B  85      73.702 -33.729-242.623  1.00 63.78           C  
ANISOU 1504  CB  LEU B  85    10377   6801   7055  -1972  -1349    721       C  
ATOM   1505  CG  LEU B  85      73.286 -32.491-241.836  1.00 57.36           C  
ANISOU 1505  CG  LEU B  85     9580   6083   6132  -2120  -1347    629       C  
ATOM   1506  CD1 LEU B  85      73.544 -32.708-240.348  1.00 56.29           C  
ANISOU 1506  CD1 LEU B  85     9265   6219   5902  -2146  -1334    735       C  
ATOM   1507  CD2 LEU B  85      74.062 -31.296-242.369  1.00 57.28           C  
ANISOU 1507  CD2 LEU B  85     9638   6127   5997  -2247  -1309    491       C  
ATOM   1508  N   TRP B  86      73.547 -35.878-244.800  1.00 52.80           N  
ANISOU 1508  N   TRP B  86     9103   4991   5970  -1739  -1315    760       N  
ATOM   1509  CA  TRP B  86      73.974 -37.121-245.389  1.00 74.88           C  
ANISOU 1509  CA  TRP B  86    11890   7679   8880  -1623  -1247    835       C  
ATOM   1510  C   TRP B  86      74.260 -36.930-246.871  1.00 73.39           C  
ANISOU 1510  C   TRP B  86    11806   7367   8712  -1638  -1263    708       C  
ATOM   1511  O   TRP B  86      75.356 -37.234-247.338  1.00 74.05           O  
ANISOU 1511  O   TRP B  86    11865   7497   8775  -1587  -1227    750       O  
ATOM   1512  CB  TRP B  86      72.910 -38.208-245.170  1.00 67.36           C  
ANISOU 1512  CB  TRP B  86    10956   6542   8095  -1568  -1190    875       C  
ATOM   1513  CG  TRP B  86      73.392 -39.578-245.525  1.00 74.06           C  
ANISOU 1513  CG  TRP B  86    11797   7271   9072  -1447  -1060    975       C  
ATOM   1514  CD1 TRP B  86      73.862 -40.533-244.665  1.00 66.60           C  
ANISOU 1514  CD1 TRP B  86    10760   6379   8166  -1316   -943   1184       C  
ATOM   1515  CD2 TRP B  86      73.457 -40.155-246.840  1.00 68.90           C  
ANISOU 1515  CD2 TRP B  86    11235   6422   8523  -1437  -1007    878       C  
ATOM   1516  NE1 TRP B  86      74.222 -41.661-245.367  1.00 64.54           N  
ANISOU 1516  NE1 TRP B  86    10546   5937   8040  -1218   -800   1228       N  
ATOM   1517  CE2 TRP B  86      73.975 -41.457-246.698  1.00 56.86           C  
ANISOU 1517  CE2 TRP B  86     9685   4809   7111  -1307   -839   1027       C  
ATOM   1518  CE3 TRP B  86      73.124 -39.699-248.114  1.00 73.73           C  
ANISOU 1518  CE3 TRP B  86    11941   6937   9135  -1520  -1070    686       C  
ATOM   1519  CZ2 TRP B  86      74.186 -42.288-247.784  1.00 59.35           C  
ANISOU 1519  CZ2 TRP B  86    10078   4926   7548  -1280   -728    968       C  
ATOM   1520  CZ3 TRP B  86      73.319 -40.531-249.186  1.00 71.20           C  
ANISOU 1520  CZ3 TRP B  86    11677   6455   8919  -1498   -982    625       C  
ATOM   1521  CH2 TRP B  86      73.847 -41.810-249.018  1.00 64.13           C  
ANISOU 1521  CH2 TRP B  86    10767   5454   8145  -1390   -809    754       C  
ATOM   1522  N   GLU B  87      73.275 -36.419-247.604  1.00 61.76           N  
ANISOU 1522  N   GLU B  87    10436   5763   7265  -1698  -1315    562       N  
ATOM   1523  CA  GLU B  87      73.405 -36.276-249.046  1.00 64.43           C  
ANISOU 1523  CA  GLU B  87    10862   6001   7617  -1703  -1329    444       C  
ATOM   1524  C   GLU B  87      74.571 -35.363-249.451  1.00 63.70           C  
ANISOU 1524  C   GLU B  87    10786   6022   7396  -1734  -1347    419       C  
ATOM   1525  O   GLU B  87      75.253 -35.620-250.446  1.00 74.67           O  
ANISOU 1525  O   GLU B  87    12204   7369   8798  -1704  -1331    387       O  
ATOM   1526  CB  GLU B  87      72.096 -35.746-249.653  1.00 58.02           C  
ANISOU 1526  CB  GLU B  87    10129   5103   6812  -1746  -1382    314       C  
ATOM   1527  CG  GLU B  87      71.150 -36.842-250.093  1.00 67.37           C  
ANISOU 1527  CG  GLU B  87    11314   6154   8128  -1734  -1350    262       C  
ATOM   1528  CD  GLU B  87      69.904 -36.290-250.731  1.00 70.06           C  
ANISOU 1528  CD  GLU B  87    11698   6487   8437  -1769  -1407    137       C  
ATOM   1529  OE1 GLU B  87      69.731 -35.061-250.656  1.00 65.57           O  
ANISOU 1529  OE1 GLU B  87    11165   5991   7757  -1776  -1458    127       O  
ATOM   1530  OE2 GLU B  87      69.122 -37.073-251.313  1.00 78.13           O  
ANISOU 1530  OE2 GLU B  87    12711   7443   9533  -1790  -1383     49       O  
ATOM   1531  N   ILE B  88      74.816 -34.307-248.683  1.00 62.50           N  
ANISOU 1531  N   ILE B  88    10616   6014   7117  -1807  -1363    420       N  
ATOM   1532  CA  ILE B  88      75.755 -33.286-249.148  1.00 67.44           C  
ANISOU 1532  CA  ILE B  88    11282   6724   7618  -1872  -1356    352       C  
ATOM   1533  C   ILE B  88      77.156 -33.869-249.148  1.00 62.67           C  
ANISOU 1533  C   ILE B  88    10583   6252   6977  -1835  -1326    431       C  
ATOM   1534  O   ILE B  88      78.014 -33.400-249.884  1.00 66.95           O  
ANISOU 1534  O   ILE B  88    11160   6829   7451  -1865  -1317    373       O  
ATOM   1535  CB  ILE B  88      75.680 -31.987-248.297  1.00 56.40           C  
ANISOU 1535  CB  ILE B  88     9897   5440   6093  -1994  -1338    306       C  
ATOM   1536  CG1 ILE B  88      76.512 -30.866-248.918  1.00 51.40           C  
ANISOU 1536  CG1 ILE B  88     9342   4843   5345  -2080  -1293    205       C  
ATOM   1537  CG2 ILE B  88      76.111 -32.232-246.876  1.00 55.21           C  
ANISOU 1537  CG2 ILE B  88     9597   5505   5876  -2030  -1324    401       C  
ATOM   1538  CD1 ILE B  88      75.944 -29.471-248.660  1.00 60.18           C  
ANISOU 1538  CD1 ILE B  88    10563   5916   6386  -2182  -1232    113       C  
ATOM   1539  N   GLU B  89      77.363 -34.918-248.348  1.00 67.52           N  
ANISOU 1539  N   GLU B  89    11078   6941   7635  -1754  -1298    576       N  
ATOM   1540  CA  GLU B  89      78.640 -35.644-248.288  1.00 74.49           C  
ANISOU 1540  CA  GLU B  89    11851   7967   8485  -1669  -1250    697       C  
ATOM   1541  C   GLU B  89      78.737 -36.811-249.273  1.00 84.86           C  
ANISOU 1541  C   GLU B  89    13211   9083   9950  -1547  -1200    730       C  
ATOM   1542  O   GLU B  89      79.758 -36.992-249.936  1.00 94.55           O  
ANISOU 1542  O   GLU B  89    14427  10351  11148  -1507  -1175    743       O  
ATOM   1543  CB  GLU B  89      78.878 -36.199-246.881  1.00 85.18           C  
ANISOU 1543  CB  GLU B  89    13039   9533   9794  -1607  -1213    875       C  
ATOM   1544  CG  GLU B  89      79.276 -35.169-245.851  1.00 97.55           C  
ANISOU 1544  CG  GLU B  89    14502  11400  11162  -1736  -1237    853       C  
ATOM   1545  CD  GLU B  89      80.689 -34.651-246.060  1.00101.07           C  
ANISOU 1545  CD  GLU B  89    14868  12100  11434  -1795  -1224    826       C  
ATOM   1546  OE1 GLU B  89      81.414 -35.209-246.915  1.00101.45           O  
ANISOU 1546  OE1 GLU B  89    14925  12102  11519  -1701  -1202    864       O  
ATOM   1547  OE2 GLU B  89      81.070 -33.680-245.370  1.00 96.60           O  
ANISOU 1547  OE2 GLU B  89    14229  11784  10690  -1951  -1225    752       O  
ATOM   1548  N   ASN B  90      77.671 -37.604-249.350  1.00 80.32           N  
ANISOU 1548  N   ASN B  90    12687   8300   9533  -1504  -1172    731       N  
ATOM   1549  CA  ASN B  90      77.715 -38.913-249.994  1.00 73.00           C  
ANISOU 1549  CA  ASN B  90    11788   7185   8762  -1400  -1071    773       C  
ATOM   1550  C   ASN B  90      77.142 -38.968-251.406  1.00 77.98           C  
ANISOU 1550  C   ASN B  90    12545   7607   9479  -1451  -1086    594       C  
ATOM   1551  O   ASN B  90      77.571 -39.775-252.234  1.00 71.02           O  
ANISOU 1551  O   ASN B  90    11694   6608   8683  -1398  -1005    585       O  
ATOM   1552  CB  ASN B  90      76.989 -39.918-249.101  1.00 72.34           C  
ANISOU 1552  CB  ASN B  90    11669   7016   8800  -1329   -980    890       C  
ATOM   1553  CG  ASN B  90      77.460 -39.837-247.663  1.00 75.38           C  
ANISOU 1553  CG  ASN B  90    11911   7648   9081  -1270   -971   1076       C  
ATOM   1554  OD1 ASN B  90      78.607 -39.489-247.404  1.00 81.31           O  
ANISOU 1554  OD1 ASN B  90    12563   8639   9689  -1241   -983   1157       O  
ATOM   1555  ND2 ASN B  90      76.581 -40.145-246.725  1.00 79.11           N  
ANISOU 1555  ND2 ASN B  90    12357   8092   9608  -1260   -948   1139       N  
ATOM   1556  N   ASN B  91      76.182 -38.100-251.688  1.00 72.42           N  
ANISOU 1556  N   ASN B  91    11902   6875   8737  -1548  -1179    456       N  
ATOM   1557  CA  ASN B  91      75.520 -38.117-252.980  1.00 64.98           C  
ANISOU 1557  CA  ASN B  91    11047   5799   7844  -1590  -1199    292       C  
ATOM   1558  C   ASN B  91      75.217 -36.701-253.451  1.00 77.56           C  
ANISOU 1558  C   ASN B  91    12697   7463   9310  -1654  -1302    188       C  
ATOM   1559  O   ASN B  91      74.090 -36.399-253.859  1.00 76.90           O  
ANISOU 1559  O   ASN B  91    12651   7340   9227  -1687  -1343     91       O  
ATOM   1560  CB  ASN B  91      74.237 -38.962-252.881  1.00 54.76           C  
ANISOU 1560  CB  ASN B  91     9761   4369   6677  -1612  -1152    242       C  
ATOM   1561  CG  ASN B  91      73.555 -39.141-254.208  1.00 61.02           C  
ANISOU 1561  CG  ASN B  91    10607   5078   7502  -1669  -1157     61       C  
ATOM   1562  OD1 ASN B  91      74.219 -39.200-255.236  1.00 73.35           O  
ANISOU 1562  OD1 ASN B  91    12198   6621   9052  -1662  -1145      3       O  
ATOM   1563  ND2 ASN B  91      72.218 -39.210-254.201  1.00 64.03           N  
ANISOU 1563  ND2 ASN B  91    10985   5437   7905  -1730  -1175    -33       N  
ATOM   1564  N   PRO B  92      76.229 -35.813-253.402  1.00 85.13           N  
ANISOU 1564  N   PRO B  92    13658   8538  10149  -1668  -1325    212       N  
ATOM   1565  CA  PRO B  92      75.933 -34.378-253.479  1.00 69.02           C  
ANISOU 1565  CA  PRO B  92    11682   6552   7991  -1728  -1373    144       C  
ATOM   1566  C   PRO B  92      75.458 -33.913-254.856  1.00 71.59           C  
ANISOU 1566  C   PRO B  92    12096   6809   8297  -1719  -1399     29       C  
ATOM   1567  O   PRO B  92      74.921 -32.801-254.985  1.00 56.58           O  
ANISOU 1567  O   PRO B  92    10260   4922   6314  -1734  -1412    -10       O  
ATOM   1568  CB  PRO B  92      77.264 -33.721-253.103  1.00 77.15           C  
ANISOU 1568  CB  PRO B  92    12686   7722   8904  -1768  -1353    181       C  
ATOM   1569  CG  PRO B  92      78.298 -34.729-253.412  1.00 82.49           C  
ANISOU 1569  CG  PRO B  92    13302   8416   9626  -1705  -1320    244       C  
ATOM   1570  CD  PRO B  92      77.676 -36.087-253.329  1.00 90.17           C  
ANISOU 1570  CD  PRO B  92    14243   9267  10752  -1632  -1285    294       C  
ATOM   1571  N   GLY B  93      75.628 -34.768-255.859  1.00 67.05           N  
ANISOU 1571  N   GLY B  93    11519   6166   7790  -1687  -1388    -18       N  
ATOM   1572  CA  GLY B  93      75.276 -34.418-257.220  1.00 73.93           C  
ANISOU 1572  CA  GLY B  93    12447   7020   8624  -1675  -1412   -124       C  
ATOM   1573  C   GLY B  93      73.898 -34.905-257.606  1.00 63.89           C  
ANISOU 1573  C   GLY B  93    11151   5727   7396  -1677  -1430   -202       C  
ATOM   1574  O   GLY B  93      73.520 -34.904-258.788  1.00 67.62           O  
ANISOU 1574  O   GLY B  93    11632   6226   7836  -1668  -1445   -298       O  
ATOM   1575  N   VAL B  94      73.138 -35.312-256.600  1.00 62.44           N  
ANISOU 1575  N   VAL B  94    10926   5526   7272  -1697  -1425   -165       N  
ATOM   1576  CA  VAL B  94      71.827 -35.871-256.863  1.00 61.67           C  
ANISOU 1576  CA  VAL B  94    10790   5428   7215  -1722  -1431   -251       C  
ATOM   1577  C   VAL B  94      71.003 -34.844-257.637  1.00 74.70           C  
ANISOU 1577  C   VAL B  94    12458   7191   8734  -1691  -1488   -309       C  
ATOM   1578  O   VAL B  94      70.946 -33.637-257.291  1.00 67.41           O  
ANISOU 1578  O   VAL B  94    11585   6309   7718  -1648  -1506   -244       O  
ATOM   1579  CB  VAL B  94      71.130 -36.289-255.569  1.00 63.21           C  
ANISOU 1579  CB  VAL B  94    10944   5593   7480  -1746  -1417   -192       C  
ATOM   1580  CG1 VAL B  94      71.138 -35.145-254.572  1.00 58.14           C  
ANISOU 1580  CG1 VAL B  94    10325   5009   6756  -1728  -1455    -96       C  
ATOM   1581  CG2 VAL B  94      69.715 -36.769-255.853  1.00 63.42           C  
ANISOU 1581  CG2 VAL B  94    10924   5645   7527  -1791  -1420   -300       C  
ATOM   1582  N   LYS B  95      70.440 -35.326-258.738  1.00 71.07           N  
ANISOU 1582  N   LYS B  95    11955   6790   8257  -1708  -1492   -431       N  
ATOM   1583  CA  LYS B  95      69.679 -34.492-259.653  1.00 74.17           C  
ANISOU 1583  CA  LYS B  95    12334   7343   8505  -1651  -1536   -475       C  
ATOM   1584  C   LYS B  95      70.483 -33.295-260.206  1.00 73.70           C  
ANISOU 1584  C   LYS B  95    12361   7299   8341  -1564  -1538   -410       C  
ATOM   1585  O   LYS B  95      69.896 -32.309-260.665  1.00 73.59           O  
ANISOU 1585  O   LYS B  95    12362   7398   8199  -1473  -1546   -381       O  
ATOM   1586  CB  LYS B  95      68.408 -34.003-258.951  1.00 75.35           C  
ANISOU 1586  CB  LYS B  95    12450   7577   8602  -1626  -1564   -438       C  
ATOM   1587  CG  LYS B  95      67.422 -35.108-258.589  1.00 74.87           C  
ANISOU 1587  CG  LYS B  95    12295   7535   8618  -1720  -1556   -528       C  
ATOM   1588  CD  LYS B  95      66.188 -34.518-257.896  1.00 79.94           C  
ANISOU 1588  CD  LYS B  95    12902   8279   9193  -1683  -1591   -482       C  
ATOM   1589  CE  LYS B  95      65.145 -35.575-257.520  1.00 73.88           C  
ANISOU 1589  CE  LYS B  95    12037   7544   8491  -1791  -1577   -582       C  
ATOM   1590  NZ  LYS B  95      64.120 -35.017-256.569  1.00 67.33           N  
ANISOU 1590  NZ  LYS B  95    11186   6776   7621  -1754  -1609   -510       N  
ATOM   1591  N   PHE B  96      71.813 -33.370-260.185  1.00 78.43           N  
ANISOU 1591  N   PHE B  96    13016   7795   8988  -1581  -1511   -380       N  
ATOM   1592  CA  PHE B  96      72.601 -32.245-260.702  1.00 84.10           C  
ANISOU 1592  CA  PHE B  96    13823   8520   9611  -1521  -1492   -336       C  
ATOM   1593  C   PHE B  96      72.742 -32.330-262.205  1.00 76.91           C  
ANISOU 1593  C   PHE B  96    12898   7686   8636  -1482  -1502   -412       C  
ATOM   1594  O   PHE B  96      73.384 -33.243-262.737  1.00 65.96           O  
ANISOU 1594  O   PHE B  96    11483   6263   7316  -1533  -1499   -482       O  
ATOM   1595  CB  PHE B  96      73.988 -32.178-260.069  1.00 93.32           C  
ANISOU 1595  CB  PHE B  96    15041   9593  10824  -1565  -1460   -281       C  
ATOM   1596  CG  PHE B  96      74.761 -30.924-260.418  1.00 85.58           C  
ANISOU 1596  CG  PHE B  96    14162   8610   9744  -1535  -1414   -249       C  
ATOM   1597  CD1 PHE B  96      74.239 -29.665-260.148  1.00 82.83           C  
ANISOU 1597  CD1 PHE B  96    13892   8269   9311  -1491  -1363   -202       C  
ATOM   1598  CD2 PHE B  96      76.020 -31.009-260.993  1.00 72.73           C  
ANISOU 1598  CD2 PHE B  96    12560   6961   8114  -1554  -1396   -268       C  
ATOM   1599  CE1 PHE B  96      74.958 -28.521-260.464  1.00 74.70           C  
ANISOU 1599  CE1 PHE B  96    12976   7206   8202  -1477  -1276   -182       C  
ATOM   1600  CE2 PHE B  96      76.742 -29.868-261.309  1.00 63.62           C  
ANISOU 1600  CE2 PHE B  96    11506   5798   6871  -1545  -1333   -254       C  
ATOM   1601  CZ  PHE B  96      76.210 -28.625-261.048  1.00 67.28           C  
ANISOU 1601  CZ  PHE B  96    12058   6248   7257  -1512  -1263   -215       C  
ATOM   1602  N   THR B  97      72.139 -31.348-262.871  1.00 71.53           N  
ANISOU 1602  N   THR B  97    12238   7120   7822  -1380  -1497   -387       N  
ATOM   1603  CA  THR B  97      72.125 -31.263-264.315  1.00 76.38           C  
ANISOU 1603  CA  THR B  97    12822   7862   8338  -1319  -1505   -441       C  
ATOM   1604  C   THR B  97      73.251 -30.365-264.799  1.00 76.83           C  
ANISOU 1604  C   THR B  97    12996   7850   8347  -1264  -1453   -385       C  
ATOM   1605  O   THR B  97      73.589 -30.356-265.983  1.00 74.09           O  
ANISOU 1605  O   THR B  97    12637   7577   7935  -1223  -1454   -425       O  
ATOM   1606  CB  THR B  97      70.785 -30.715-264.817  1.00 79.38           C  
ANISOU 1606  CB  THR B  97    13134   8454   8571  -1205  -1516   -419       C  
ATOM   1607  OG1 THR B  97      70.689 -29.328-264.486  1.00 85.95           O  
ANISOU 1607  OG1 THR B  97    14078   9253   9327  -1079  -1446   -277       O  
ATOM   1608  CG2 THR B  97      69.626 -31.456-264.161  1.00 86.89           C  
ANISOU 1608  CG2 THR B  97    13976   9479   9561  -1272  -1559   -473       C  
ATOM   1609  N   GLY B  98      73.819 -29.606-263.869  1.00 78.44           N  
ANISOU 1609  N   GLY B  98    13306   7925   8574  -1279  -1396   -304       N  
ATOM   1610  CA  GLY B  98      74.866 -28.649-264.180  1.00 81.47           C  
ANISOU 1610  CA  GLY B  98    13811   8234   8909  -1256  -1315   -264       C  
ATOM   1611  C   GLY B  98      76.011 -29.225-264.991  1.00 81.28           C  
ANISOU 1611  C   GLY B  98    13777   8193   8912  -1300  -1337   -330       C  
ATOM   1612  O   GLY B  98      76.441 -28.632-265.972  1.00 89.27           O  
ANISOU 1612  O   GLY B  98    14846   9227   9846  -1235  -1296   -324       O  
ATOM   1613  N   TYR B  99      76.509 -30.383-264.577  1.00 85.92           N  
ANISOU 1613  N   TYR B  99    14297   8739   9612  -1398  -1387   -379       N  
ATOM   1614  CA  TYR B  99      77.532 -31.097-265.334  1.00 79.08           C  
ANISOU 1614  CA  TYR B  99    13410   7854   8783  -1433  -1401   -439       C  
ATOM   1615  C   TYR B  99      77.646 -32.526-264.834  1.00 80.14           C  
ANISOU 1615  C   TYR B  99    13458   7939   9051  -1507  -1427   -476       C  
ATOM   1616  O   TYR B  99      76.936 -32.941-263.915  1.00 85.57           O  
ANISOU 1616  O   TYR B  99    14103   8610   9799  -1534  -1437   -457       O  
ATOM   1617  CB  TYR B  99      78.899 -30.397-265.257  1.00 66.34           C  
ANISOU 1617  CB  TYR B  99    11884   6182   7138  -1459  -1346   -406       C  
ATOM   1618  CG  TYR B  99      79.416 -30.088-263.854  1.00 72.52           C  
ANISOU 1618  CG  TYR B  99    12687   6923   7944  -1537  -1310   -351       C  
ATOM   1619  CD1 TYR B  99      79.351 -28.791-263.333  1.00 66.47           C  
ANISOU 1619  CD1 TYR B  99    12017   6136   7103  -1548  -1229   -313       C  
ATOM   1620  CD2 TYR B  99      79.990 -31.079-263.062  1.00 72.73           C  
ANISOU 1620  CD2 TYR B  99    12633   6943   8057  -1596  -1335   -334       C  
ATOM   1621  CE1 TYR B  99      79.826 -28.495-262.060  1.00 56.47           C  
ANISOU 1621  CE1 TYR B  99    10752   4867   5836  -1648  -1188   -290       C  
ATOM   1622  CE2 TYR B  99      80.473 -30.789-261.781  1.00 65.32           C  
ANISOU 1622  CE2 TYR B  99    11683   6028   7108  -1666  -1305   -282       C  
ATOM   1623  CZ  TYR B  99      80.385 -29.504-261.288  1.00 67.01           C  
ANISOU 1623  CZ  TYR B  99    11978   6246   7237  -1707  -1240   -274       C  
ATOM   1624  OH  TYR B  99      80.862 -29.224-260.018  1.00 79.57           O  
ANISOU 1624  OH  TYR B  99    13539   7895   8799  -1803  -1204   -248       O  
ATOM   1625  OXT TYR B  99      78.450 -33.290-265.357  1.00 77.74           O  
ANISOU 1625  OXT TYR B  99    13135   7603   8800  -1532  -1418   -520       O  
TER    1626      TYR B  99                                                      
ATOM   1627  P    DG C   1      55.180 -24.778-238.580  1.00 88.52           P  
ANISOU 1627  P    DG C   1    14314   9160  10158  -1666  -1114    540       P  
ATOM   1628  OP1  DG C   1      55.402 -23.454-239.206  1.00 63.48           O  
ANISOU 1628  OP1  DG C   1    11312   5889   6919  -1572   -921    564       O  
ATOM   1629  OP2  DG C   1      53.931 -25.120-237.855  1.00100.05           O  
ANISOU 1629  OP2  DG C   1    15687  10694  11633  -1641  -1179    573       O  
ATOM   1630  O5'  DG C   1      56.363 -25.022-237.556  1.00 92.58           O  
ANISOU 1630  O5'  DG C   1    14808   9657  10713  -1872  -1114    483       O  
ATOM   1631  C5'  DG C   1      57.670 -24.928-238.013  1.00 84.87           C  
ANISOU 1631  C5'  DG C   1    13873   8649   9725  -1940  -1079    438       C  
ATOM   1632  C4'  DG C   1      58.442 -26.189-237.704  1.00 72.81           C  
ANISOU 1632  C4'  DG C   1    12209   7201   8253  -2035  -1216    426       C  
ATOM   1633  O4'  DG C   1      58.429 -26.437-236.292  1.00 76.05           O  
ANISOU 1633  O4'  DG C   1    12537   7684   8676  -2151  -1233    434       O  
ATOM   1634  C3'  DG C   1      57.920 -27.454-238.330  1.00 76.27           C  
ANISOU 1634  C3'  DG C   1    12545   7675   8759  -1955  -1361    449       C  
ATOM   1635  O3'  DG C   1      59.011 -28.305-238.535  1.00 84.12           O  
ANISOU 1635  O3'  DG C   1    13481   8688   9794  -2008  -1414    440       O  
ATOM   1636  C2'  DG C   1      56.973 -27.999-237.256  1.00 78.93           C  
ANISOU 1636  C2'  DG C   1    12788   8061   9139  -1981  -1420    482       C  
ATOM   1637  C1'  DG C   1      57.702 -27.612-235.988  1.00 71.29           C  
ANISOU 1637  C1'  DG C   1    11812   7128   8147  -2116  -1362    482       C  
ATOM   1638  N9   DG C   1      56.841 -27.231-234.902  1.00 68.65           N  
ANISOU 1638  N9   DG C   1    11465   6817   7802  -2147  -1336    499       N  
ATOM   1639  C8   DG C   1      55.654 -26.556-234.994  1.00 77.02           C  
ANISOU 1639  C8   DG C   1    12588   7836   8839  -2061  -1292    510       C  
ATOM   1640  N7   DG C   1      55.137 -26.264-233.831  1.00 86.75           N  
ANISOU 1640  N7   DG C   1    13801   9097  10064  -2121  -1261    521       N  
ATOM   1641  C5   DG C   1      56.062 -26.747-232.913  1.00 68.04           C  
ANISOU 1641  C5   DG C   1    11342   6809   7700  -2259  -1288    514       C  
ATOM   1642  C6   DG C   1      56.046 -26.719-231.501  1.00 63.32           C  
ANISOU 1642  C6   DG C   1    10672   6304   7083  -2375  -1274    520       C  
ATOM   1643  O6   DG C   1      55.180 -26.244-230.744  1.00 68.17           O  
ANISOU 1643  O6   DG C   1    11299   6917   7685  -2390  -1234    522       O  
ATOM   1644  N1   DG C   1      57.174 -27.322-230.961  1.00 66.73           N  
ANISOU 1644  N1   DG C   1    10994   6863   7497  -2471  -1308    532       N  
ATOM   1645  C2   DG C   1      58.199 -27.873-231.690  1.00 68.52           C  
ANISOU 1645  C2   DG C   1    11195   7107   7734  -2453  -1343    540       C  
ATOM   1646  N2   DG C   1      59.219 -28.398-230.972  1.00 71.46           N  
ANISOU 1646  N2   DG C   1    11440   7646   8066  -2532  -1360    575       N  
ATOM   1647  N3   DG C   1      58.226 -27.910-233.017  1.00 59.56           N  
ANISOU 1647  N3   DG C   1    10141   5857   6631  -2357  -1355    524       N  
ATOM   1648  C4   DG C   1      57.128 -27.327-233.558  1.00 66.31           C  
ANISOU 1648  C4   DG C   1    11094   6606   7494  -2267  -1329    509       C  
ATOM   1649  P    DC C   2      58.826 -29.658-239.345  1.00 73.85           P  
ANISOU 1649  P    DC C   2    12099   7388   8574  -1955  -1516    437       P  
ATOM   1650  OP1  DC C   2      59.981 -29.808-240.255  1.00 66.78           O  
ANISOU 1650  OP1  DC C   2    11232   6467   7674  -1953  -1508    412       O  
ATOM   1651  OP2  DC C   2      57.447 -29.609-239.850  1.00 85.94           O  
ANISOU 1651  OP2  DC C   2    13624   8937  10092  -1867  -1544    424       O  
ATOM   1652  O5'  DC C   2      58.901 -30.755-238.210  1.00 67.93           O  
ANISOU 1652  O5'  DC C   2    11234   6674   7903  -2022  -1559    486       O  
ATOM   1653  C5'  DC C   2      59.918 -30.657-237.247  1.00 60.45           C  
ANISOU 1653  C5'  DC C   2    10250   5787   6930  -2102  -1528    526       C  
ATOM   1654  C4'  DC C   2      59.662 -31.597-236.103  1.00 63.88           C  
ANISOU 1654  C4'  DC C   2    10570   6274   7425  -2127  -1557    601       C  
ATOM   1655  O4'  DC C   2      58.846 -30.962-235.096  1.00 70.49           O  
ANISOU 1655  O4'  DC C   2    11404   7152   8226  -2166  -1546    607       O  
ATOM   1656  C3'  DC C   2      58.941 -32.896-236.465  1.00 71.94           C  
ANISOU 1656  C3'  DC C   2    11545   7226   8565  -2075  -1595    614       C  
ATOM   1657  O3'  DC C   2      59.759 -33.991-236.032  1.00 90.31           O  
ANISOU 1657  O3'  DC C   2    13792   9567  10956  -2069  -1572    701       O  
ATOM   1658  C2'  DC C   2      57.617 -32.809-235.668  1.00 70.19           C  
ANISOU 1658  C2'  DC C   2    11296   7018   8356  -2086  -1614    619       C  
ATOM   1659  C1'  DC C   2      58.041 -31.951-234.494  1.00 69.61           C  
ANISOU 1659  C1'  DC C   2    11211   7039   8199  -2149  -1586    659       C  
ATOM   1660  N1   DC C   2      56.915 -31.260-233.771  1.00 68.45           N  
ANISOU 1660  N1   DC C   2    11078   6910   8020  -2167  -1585    647       N  
ATOM   1661  C2   DC C   2      56.982 -31.072-232.367  1.00 66.26           C  
ANISOU 1661  C2   DC C   2    10736   6730   7708  -2239  -1567    695       C  
ATOM   1662  O2   DC C   2      57.955 -31.510-231.723  1.00 62.20           O  
ANISOU 1662  O2   DC C   2    10137   6318   7178  -2277  -1557    757       O  
ATOM   1663  N3   DC C   2      55.974 -30.409-231.744  1.00 59.92           N  
ANISOU 1663  N3   DC C   2     9956   5933   6879  -2256  -1555    678       N  
ATOM   1664  C4   DC C   2      54.945 -29.926-232.456  1.00 73.72           C  
ANISOU 1664  C4   DC C   2    11780   7607   8624  -2189  -1557    634       C  
ATOM   1665  N4   DC C   2      53.974 -29.283-231.780  1.00 63.70           N  
ANISOU 1665  N4   DC C   2    10529   6350   7325  -2193  -1534    633       N  
ATOM   1666  C5   DC C   2      54.864 -30.084-233.889  1.00 68.69           C  
ANISOU 1666  C5   DC C   2    11191   6906   8000  -2105  -1577    594       C  
ATOM   1667  C6   DC C   2      55.862 -30.742-234.497  1.00 66.61           C  
ANISOU 1667  C6   DC C   2    10912   6624   7771  -2108  -1592    593       C  
ATOM   1668  P    DG C   3      59.405 -35.511-236.419  1.00 88.01           P  
ANISOU 1668  P    DG C   3    13467   9164  10807  -2029  -1546    717       P  
ATOM   1669  OP1  DG C   3      60.469 -36.090-237.267  1.00 87.75           O  
ANISOU 1669  OP1  DG C   3    13449   9081  10811  -1993  -1507    725       O  
ATOM   1670  OP2  DG C   3      58.013 -35.519-236.910  1.00 79.43           O  
ANISOU 1670  OP2  DG C   3    12406   8026   9748  -2042  -1576    616       O  
ATOM   1671  O5'  DG C   3      59.508 -36.257-235.024  1.00 63.32           O  
ANISOU 1671  O5'  DG C   3    10246   6087   7727  -2018  -1503    858       O  
ATOM   1672  C5'  DG C   3      60.678 -36.120-234.238  1.00 56.62           C  
ANISOU 1672  C5'  DG C   3     9325   5382   6805  -2005  -1481    973       C  
ATOM   1673  C4'  DG C   3      60.414 -36.470-232.768  1.00 75.20           C  
ANISOU 1673  C4'  DG C   3    11576   7839   9157  -1998  -1460   1099       C  
ATOM   1674  O4'  DG C   3      59.465 -35.532-232.188  1.00 83.78           O  
ANISOU 1674  O4'  DG C   3    12678   8971  10184  -2073  -1515   1031       O  
ATOM   1675  C3'  DG C   3      59.826 -37.848-232.503  1.00 86.00           C  
ANISOU 1675  C3'  DG C   3    12920   9082  10676  -1936  -1384   1182       C  
ATOM   1676  O3'  DG C   3      60.251 -38.301-231.201  1.00109.52           O  
ANISOU 1676  O3'  DG C   3    15779  12204  13629  -1880  -1332   1366       O  
ATOM   1677  C2'  DG C   3      58.337 -37.553-232.518  1.00 74.32           C  
ANISOU 1677  C2'  DG C   3    11486   7523   9228  -2002  -1433   1066       C  
ATOM   1678  C1'  DG C   3      58.314 -36.227-231.771  1.00 80.25           C  
ANISOU 1678  C1'  DG C   3    12216   8438   9836  -2061  -1505   1050       C  
ATOM   1679  N9   DG C   3      57.144 -35.425-232.079  1.00 78.69           N  
ANISOU 1679  N9   DG C   3    12087   8195   9616  -2111  -1563    924       N  
ATOM   1680  C8   DG C   3      56.599 -35.219-233.322  1.00 81.17           C  
ANISOU 1680  C8   DG C   3    12482   8413   9946  -2106  -1589    801       C  
ATOM   1681  N7   DG C   3      55.524 -34.480-233.304  1.00 78.68           N  
ANISOU 1681  N7   DG C   3    12197   8111   9587  -2125  -1628    734       N  
ATOM   1682  C5   DG C   3      55.340 -34.180-231.961  1.00 70.86           C  
ANISOU 1682  C5   DG C   3    11156   7204   8564  -2157  -1628    803       C  
ATOM   1683  C6   DG C   3      54.338 -33.411-231.342  1.00 63.71           C  
ANISOU 1683  C6   DG C   3    10259   6340   7610  -2183  -1650    779       C  
ATOM   1684  O6   DG C   3      53.383 -32.826-231.883  1.00 73.60           O  
ANISOU 1684  O6   DG C   3    11563   7571   8833  -2161  -1671    706       O  
ATOM   1685  N1   DG C   3      54.501 -33.365-229.957  1.00 57.55           N  
ANISOU 1685  N1   DG C   3     9407   5655   6804  -2225  -1637    860       N  
ATOM   1686  C2   DG C   3      55.514 -33.994-229.258  1.00 65.25           C  
ANISOU 1686  C2   DG C   3    10294   6714   7783  -2226  -1608    967       C  
ATOM   1687  N2   DG C   3      55.511 -33.824-227.916  1.00 56.45           N  
ANISOU 1687  N2   DG C   3     9095   5737   6615  -2268  -1600   1038       N  
ATOM   1688  N3   DG C   3      56.478 -34.716-229.839  1.00 62.39           N  
ANISOU 1688  N3   DG C   3     9919   6325   7460  -2179  -1581   1011       N  
ATOM   1689  C4   DG C   3      56.327 -34.759-231.188  1.00 69.61           C  
ANISOU 1689  C4   DG C   3    10921   7111   8416  -2154  -1592    917       C  
ATOM   1690  P    DC C   4      60.069 -39.838-230.735  1.00136.95           P  
ANISOU 1690  P    DC C   4    19217  15565  17252  -1772  -1191   1525       P  
ATOM   1691  OP1  DC C   4      61.431 -40.384-230.544  1.00135.50           O  
ANISOU 1691  OP1  DC C   4    18954  15496  17035  -1646  -1104   1709       O  
ATOM   1692  OP2  DC C   4      59.128 -40.534-231.644  1.00125.49           O  
ANISOU 1692  OP2  DC C   4    17874  13848  15958  -1805  -1137   1399       O  
ATOM   1693  O5'  DC C   4      59.374 -39.711-229.293  1.00128.66           O  
ANISOU 1693  O5'  DC C   4    18079  14641  16164  -1786  -1208   1612       O  
ATOM   1694  C5'  DC C   4      58.792 -38.464-228.896  1.00125.71           C  
ANISOU 1694  C5'  DC C   4    17704  14382  15679  -1902  -1332   1497       C  
ATOM   1695  C4'  DC C   4      58.332 -38.490-227.446  1.00120.58           C  
ANISOU 1695  C4'  DC C   4    16950  13874  14989  -1903  -1329   1606       C  
ATOM   1696  O4'  DC C   4      57.150 -37.666-227.299  1.00110.34           O  
ANISOU 1696  O4'  DC C   4    15705  12543  13675  -2010  -1413   1464       O  
ATOM   1697  C3'  DC C   4      57.895 -39.845-226.938  1.00121.17           C  
ANISOU 1697  C3'  DC C   4    16998  13835  15206  -1804  -1207   1754       C  
ATOM   1698  O3'  DC C   4      57.919 -39.840-225.510  1.00127.79           O  
ANISOU 1698  O3'  DC C   4    17703  14888  15964  -1772  -1197   1908       O  
ATOM   1699  C2'  DC C   4      56.473 -39.938-227.485  1.00104.69           C  
ANISOU 1699  C2'  DC C   4    15021  11523  13235  -1889  -1227   1585       C  
ATOM   1700  C1'  DC C   4      55.994 -38.479-227.431  1.00 93.98           C  
ANISOU 1700  C1'  DC C   4    13681  10278  11750  -2002  -1374   1439       C  
ATOM   1701  N1   DC C   4      55.249 -38.047-228.663  1.00 85.08           N  
ANISOU 1701  N1   DC C   4    12667   9005  10652  -2066  -1431   1241       N  
ATOM   1702  C2   DC C   4      54.207 -37.117-228.550  1.00 70.73           C  
ANISOU 1702  C2   DC C   4    10879   7217   8780  -2136  -1514   1131       C  
ATOM   1703  O2   DC C   4      53.914 -36.675-227.426  1.00 67.53           O  
ANISOU 1703  O2   DC C   4    10417   6927   8315  -2162  -1538   1182       O  
ATOM   1704  N3   DC C   4      53.543 -36.733-229.679  1.00 64.74           N  
ANISOU 1704  N3   DC C   4    10200   6374   8022  -2163  -1557    978       N  
ATOM   1705  C4   DC C   4      53.888 -37.246-230.868  1.00 73.88           C  
ANISOU 1705  C4   DC C   4    11405   7431   9235  -2145  -1528    918       C  
ATOM   1706  N4   DC C   4      53.208 -36.845-231.948  1.00 78.31           N  
ANISOU 1706  N4   DC C   4    12019   7962   9771  -2167  -1572    775       N  
ATOM   1707  C5   DC C   4      54.942 -38.197-230.999  1.00 72.29           C  
ANISOU 1707  C5   DC C   4    11190   7171   9107  -2093  -1441   1010       C  
ATOM   1708  C6   DC C   4      55.589 -38.563-229.885  1.00 78.11           C  
ANISOU 1708  C6   DC C   4    11851   7987   9841  -2044  -1391   1179       C  
ATOM   1709  P    DG C   5      57.548 -41.158-224.671  1.00106.85           P  
ANISOU 1709  P    DG C   5    15001  12167  13432  -1647  -1047   2112       P  
ATOM   1710  OP1  DG C   5      58.303 -41.095-223.399  1.00110.26           O  
ANISOU 1710  OP1  DG C   5    15250  12932  13713  -1562  -1033   2323       O  
ATOM   1711  OP2  DG C   5      57.665 -42.346-225.548  1.00 98.46           O  
ANISOU 1711  OP2  DG C   5    14036  10828  12547  -1559   -890   2144       O  
ATOM   1712  O5'  DG C   5      56.000 -40.959-224.337  1.00118.03           O  
ANISOU 1712  O5'  DG C   5    16470  13464  14913  -1758  -1099   1986       O  
ATOM   1713  C5'  DG C   5      55.581 -39.863-223.531  1.00105.47           C  
ANISOU 1713  C5'  DG C   5    14818  12068  13186  -1856  -1227   1927       C  
ATOM   1714  C4'  DG C   5      54.065 -39.802-223.460  1.00 93.95           C  
ANISOU 1714  C4'  DG C   5    13428  10457  11812  -1944  -1261   1802       C  
ATOM   1715  O4'  DG C   5      53.535 -39.351-224.735  1.00 86.11           O  
ANISOU 1715  O4'  DG C   5    12560   9302  10856  -2026  -1325   1588       O  
ATOM   1716  C3'  DG C   5      53.381 -41.137-223.176  1.00 87.56           C  
ANISOU 1716  C3'  DG C   5    12634   9464  11171  -1883  -1119   1894       C  
ATOM   1717  O3'  DG C   5      52.281 -40.933-222.338  1.00 86.89           O  
ANISOU 1717  O3'  DG C   5    12521   9408  11084  -1944  -1160   1870       O  
ATOM   1718  C2'  DG C   5      52.928 -41.580-224.558  1.00 89.44           C  
ANISOU 1718  C2'  DG C   5    13004   9440  11538  -1933  -1079   1723       C  
ATOM   1719  C1'  DG C   5      52.531 -40.242-225.150  1.00 81.12           C  
ANISOU 1719  C1'  DG C   5    11990   8455  10375  -2043  -1254   1525       C  
ATOM   1720  N9   DG C   5      52.471 -40.242-226.602  1.00 68.81           N  
ANISOU 1720  N9   DG C   5    10528   6757   8858  -2082  -1264   1361       N  
ATOM   1721  C8   DG C   5      53.334 -40.871-227.467  1.00 75.48           C  
ANISOU 1721  C8   DG C   5    11415   7498   9765  -2031  -1180   1375       C  
ATOM   1722  N7   DG C   5      53.034 -40.689-228.730  1.00 75.45           N  
ANISOU 1722  N7   DG C   5    11487   7405   9775  -2093  -1215   1196       N  
ATOM   1723  C5   DG C   5      51.893 -39.897-228.698  1.00 65.66           C  
ANISOU 1723  C5   DG C   5    10249   6227   8472  -2173  -1326   1069       C  
ATOM   1724  C6   DG C   5      51.102 -39.384-229.769  1.00 74.84           C  
ANISOU 1724  C6   DG C   5    11455   7385   9595  -2238  -1400    879       C  
ATOM   1725  O6   DG C   5      51.268 -39.549-230.991  1.00 74.25           O  
ANISOU 1725  O6   DG C   5    11425   7252   9534  -2254  -1389    769       O  
ATOM   1726  N1   DG C   5      50.021 -38.609-229.299  1.00 63.25           N  
ANISOU 1726  N1   DG C   5     9963   6016   8053  -2275  -1489    830       N  
ATOM   1727  C2   DG C   5      49.745 -38.385-227.960  1.00 70.69           C  
ANISOU 1727  C2   DG C   5    10854   7030   8975  -2271  -1505    934       C  
ATOM   1728  N2   DG C   5      48.662 -37.644-227.694  1.00 63.72           N  
ANISOU 1728  N2   DG C   5     9959   6226   8024  -2305  -1580    869       N  
ATOM   1729  N3   DG C   5      50.483 -38.870-226.947  1.00 77.48           N  
ANISOU 1729  N3   DG C   5    11666   7904   9868  -2224  -1442   1101       N  
ATOM   1730  C4   DG C   5      51.533 -39.611-227.391  1.00 70.33           C  
ANISOU 1730  C4   DG C   5    10776   6922   9024  -2169  -1354   1167       C  
ATOM   1731  P    DC C   6      52.096 -41.837-221.028  1.00 84.09           P  
ANISOU 1731  P    DC C   6    12077   9097  10778  -1850  -1038   2089       P  
ATOM   1732  OP1  DC C   6      52.881 -41.176-219.962  1.00 78.21           O  
ANISOU 1732  OP1  DC C   6    11182   8685   9850  -1813  -1103   2225       O  
ATOM   1733  OP2  DC C   6      52.312 -43.254-221.399  1.00 95.38           O  
ANISOU 1733  OP2  DC C   6    13561  10300  12377  -1743   -826   2199       O  
ATOM   1734  O5'  DC C   6      50.565 -41.646-220.669  1.00 81.71           O  
ANISOU 1734  O5'  DC C   6    11805   8721  10521  -1963  -1090   1963       O  
ATOM   1735  C5'  DC C   6      50.043 -40.344-220.618  1.00 77.93           C  
ANISOU 1735  C5'  DC C   6    11325   8361   9923  -2076  -1260   1811       C  
ATOM   1736  C4'  DC C   6      48.798 -40.238-221.461  1.00 74.46           C  
ANISOU 1736  C4'  DC C   6    10984   7754   9555  -2175  -1301   1601       C  
ATOM   1737  O4'  DC C   6      49.120 -40.411-222.852  1.00 72.36           O  
ANISOU 1737  O4'  DC C   6    10804   7354   9335  -2184  -1285   1487       O  
ATOM   1738  C3'  DC C   6      47.732 -41.277-221.154  1.00 78.38           C  
ANISOU 1738  C3'  DC C   6    11491   8100  10189  -2198  -1195   1602       C  
ATOM   1739  O3'  DC C   6      46.554 -40.596-220.793  1.00 80.57           O  
ANISOU 1739  O3'  DC C   6    11756   8441  10416  -2284  -1298   1494       O  
ATOM   1740  C2'  DC C   6      47.581 -42.072-222.479  1.00 75.46           C  
ANISOU 1740  C2'  DC C   6    11218   7512   9943  -2234  -1099   1470       C  
ATOM   1741  C1'  DC C   6      48.025 -41.030-223.476  1.00 69.63           C  
ANISOU 1741  C1'  DC C   6    10514   6846   9097  -2256  -1235   1348       C  
ATOM   1742  N1   DC C   6      48.479 -41.516-224.829  1.00 74.08           N  
ANISOU 1742  N1   DC C   6    11152   7270   9725  -2261  -1173   1252       N  
ATOM   1743  C2   DC C   6      47.769 -41.130-225.982  1.00 70.67           C  
ANISOU 1743  C2   DC C   6    10765   6822   9266  -2349  -1243   1037       C  
ATOM   1744  O2   DC C   6      46.732 -40.470-225.863  1.00 78.17           O  
ANISOU 1744  O2   DC C   6    11692   7864  10146  -2406  -1342    943       O  
ATOM   1745  N3   DC C   6      48.228 -41.506-227.198  1.00 61.49           N  
ANISOU 1745  N3   DC C   6     9657   5563   8143  -2361  -1194    946       N  
ATOM   1746  C4   DC C   6      49.349 -42.223-227.290  1.00 69.96           C  
ANISOU 1746  C4   DC C   6    10755   6534   9292  -2286  -1074   1062       C  
ATOM   1747  N4   DC C   6      49.764 -42.586-228.518  1.00 63.51           N  
ANISOU 1747  N4   DC C   6     9997   5617   8517  -2306  -1021    958       N  
ATOM   1748  C5   DC C   6      50.094 -42.603-226.134  1.00 69.41           C  
ANISOU 1748  C5   DC C   6    10640   6485   9247  -2176   -997   1298       C  
ATOM   1749  C6   DC C   6      49.636 -42.220-224.939  1.00 68.21           C  
ANISOU 1749  C6   DC C   6    10420   6455   9041  -2169  -1055   1384       C  
ATOM   1750  P    DG C   7      45.473 -41.305-219.859  1.00 74.10           P  
ANISOU 1750  P    DG C   7    10901   7575   9678  -2313  -1226   1536       P  
ATOM   1751  OP1  DG C   7      44.843 -40.260-219.032  1.00 74.92           O  
ANISOU 1751  OP1  DG C   7    10950   7848   9666  -2354  -1358   1516       O  
ATOM   1752  OP2  DG C   7      46.110 -42.482-219.247  1.00 78.26           O  
ANISOU 1752  OP2  DG C   7    11404   8027  10306  -2211  -1047   1741       O  
ATOM   1753  O5'  DG C   7      44.380 -41.751-220.899  1.00 72.39           O  
ANISOU 1753  O5'  DG C   7    10752   7207   9546  -2420  -1194   1323       O  
ATOM   1754  C5'  DG C   7      43.851 -40.769-221.757  1.00 75.80           C  
ANISOU 1754  C5'  DG C   7    11205   7717   9879  -2480  -1335   1143       C  
ATOM   1755  C4'  DG C   7      43.083 -41.417-222.859  1.00 81.85           C  
ANISOU 1755  C4'  DG C   7    12007   8381  10712  -2576  -1275    953       C  
ATOM   1756  O4'  DG C   7      44.001 -41.829-223.896  1.00 75.67           O  
ANISOU 1756  O4'  DG C   7    11282   7495   9975  -2555  -1209    925       O  
ATOM   1757  C3'  DG C   7      42.332 -42.681-222.436  1.00 85.40           C  
ANISOU 1757  C3'  DG C   7    12453   8696  11300  -2651  -1108    936       C  
ATOM   1758  O3'  DG C   7      41.047 -42.673-223.030  1.00 96.29           O  
ANISOU 1758  O3'  DG C   7    13809  10128  12649  -2781  -1137    721       O  
ATOM   1759  C2'  DG C   7      43.210 -43.798-222.995  1.00 79.63           C  
ANISOU 1759  C2'  DG C   7    11789   7762  10704  -2630   -916    970       C  
ATOM   1760  C1'  DG C   7      43.692 -43.150-224.265  1.00 79.85           C  
ANISOU 1760  C1'  DG C   7    11844   7845  10649  -2632  -1021    852       C  
ATOM   1761  N9   DG C   7      44.878 -43.766-224.819  1.00 81.95           N  
ANISOU 1761  N9   DG C   7    12170   7971  10995  -2570   -902    917       N  
ATOM   1762  C8   DG C   7      45.875 -44.422-224.138  1.00 84.52           C  
ANISOU 1762  C8   DG C   7    12510   8198  11405  -2448   -765   1140       C  
ATOM   1763  N7   DG C   7      46.833 -44.855-224.908  1.00 81.57           N  
ANISOU 1763  N7   DG C   7    12192   7717  11084  -2401   -673   1157       N  
ATOM   1764  C5   DG C   7      46.444 -44.452-226.182  1.00 84.80           C  
ANISOU 1764  C5   DG C   7    12626   8154  11441  -2510   -761    920       C  
ATOM   1765  C6   DG C   7      47.080 -44.638-227.432  1.00 77.74           C  
ANISOU 1765  C6   DG C   7    11788   7186  10565  -2525   -723    822       C  
ATOM   1766  O6   DG C   7      48.154 -45.217-227.671  1.00 77.54           O  
ANISOU 1766  O6   DG C   7    11812   7036  10616  -2441   -596    926       O  
ATOM   1767  N1   DG C   7      46.339 -44.070-228.477  1.00 76.66           N  
ANISOU 1767  N1   DG C   7    11637   7158  10334  -2639   -844    586       N  
ATOM   1768  C2   DG C   7      45.142 -43.393-228.325  1.00 75.13           C  
ANISOU 1768  C2   DG C   7    11378   7130  10036  -2711   -980    477       C  
ATOM   1769  N2   DG C   7      44.574 -42.908-229.454  1.00 68.80           N  
ANISOU 1769  N2   DG C   7    10550   6462   9129  -2786  -1074    277       N  
ATOM   1770  N3   DG C   7      44.542 -43.212-227.153  1.00 69.15           N  
ANISOU 1770  N3   DG C   7    10577   6426   9270  -2697  -1013    567       N  
ATOM   1771  C4   DG C   7      45.241 -43.779-226.136  1.00 80.51           C  
ANISOU 1771  C4   DG C   7    12033   7751  10805  -2605   -900    780       C  
ATOM   1772  P    DC C   8      39.968 -43.813-222.692  1.00 88.60           P  
ANISOU 1772  P    DC C   8    12823   9053  11789  -2916   -972    629       P  
ATOM   1773  OP1  DC C   8      38.954 -43.282-221.753  1.00 86.60           O  
ANISOU 1773  OP1  DC C   8    12498   8939  11466  -2933  -1073    645       O  
ATOM   1774  OP2  DC C   8      40.703 -45.032-222.305  1.00 76.04           O  
ANISOU 1774  OP2  DC C   8    11297   7223  10372  -2880   -737    761       O  
ATOM   1775  O5'  DC C   8      39.251 -44.015-224.101  1.00 66.19           O  
ANISOU 1775  O5'  DC C   8     9971   6266   8912  -3069   -959    346       O  
ATOM   1776  C5'  DC C   8      39.181 -42.918-225.005  1.00 67.47           C  
ANISOU 1776  C5'  DC C   8    10098   6629   8909  -3038  -1146    257       C  
ATOM   1777  C4'  DC C   8      39.032 -43.395-226.451  1.00 77.37           C  
ANISOU 1777  C4'  DC C   8    11347   7900  10149  -3158  -1082     29       C  
ATOM   1778  O4'  DC C   8      40.328 -43.770-226.996  1.00 84.92           O  
ANISOU 1778  O4'  DC C   8    12392   8683  11191  -3102   -998     88       O  
ATOM   1779  C3'  DC C   8      38.140 -44.605-226.670  1.00 80.69           C  
ANISOU 1779  C3'  DC C   8    11745   8259  10654  -3371   -890   -175       C  
ATOM   1780  O3'  DC C   8      37.485 -44.455-227.933  1.00105.80           O  
ANISOU 1780  O3'  DC C   8    14843  11655  13700  -3493   -937   -425       O  
ATOM   1781  C2'  DC C   8      39.159 -45.742-226.708  1.00 74.41           C  
ANISOU 1781  C2'  DC C   8    11068   7147  10057  -3377   -653   -114       C  
ATOM   1782  C1'  DC C   8      40.247 -45.075-227.520  1.00 86.47           C  
ANISOU 1782  C1'  DC C   8    12629   8708  11520  -3252   -768    -58       C  
ATOM   1783  N1   DC C   8      41.591 -45.717-227.403  1.00 94.31           N  
ANISOU 1783  N1   DC C   8    13728   9443  12661  -3153   -617    106       N  
ATOM   1784  C2   DC C   8      42.395 -45.846-228.545  1.00 84.79           C  
ANISOU 1784  C2   DC C   8    12570   8183  11462  -3152   -583     35       C  
ATOM   1785  O2   DC C   8      41.966 -45.443-229.635  1.00 78.81           O  
ANISOU 1785  O2   DC C   8    11761   7596  10585  -3239   -678   -167       O  
ATOM   1786  N3   DC C   8      43.620 -46.419-228.424  1.00 76.96           N  
ANISOU 1786  N3   DC C   8    11669   6974  10597  -3044   -442    199       N  
ATOM   1787  C4   DC C   8      44.039 -46.852-227.233  1.00 76.29           C  
ANISOU 1787  C4   DC C   8    11615   6756  10617  -2930   -334    436       C  
ATOM   1788  N4   DC C   8      45.246 -47.409-227.164  1.00 75.22           N  
ANISOU 1788  N4   DC C   8    11551   6447  10584  -2800   -187    613       N  
ATOM   1789  C5   DC C   8      43.235 -46.731-226.061  1.00 79.34           C  
ANISOU 1789  C5   DC C   8    11948   7203  10992  -2931   -368    511       C  
ATOM   1790  C6   DC C   8      42.031 -46.160-226.189  1.00 89.82           C  
ANISOU 1790  C6   DC C   8    13200   8722  12208  -3050   -512    336       C  
ATOM   1791  P    DG C   9      36.202 -45.343-228.345  1.00131.64           P  
ANISOU 1791  P    DG C   9    18026  15032  16957  -3761   -796   -721       P  
ATOM   1792  OP1  DG C   9      35.028 -44.443-228.355  1.00126.85           O  
ANISOU 1792  OP1  DG C   9    17270  14788  16140  -3757   -987   -787       O  
ATOM   1793  OP2  DG C   9      36.170 -46.569-227.518  1.00133.15           O  
ANISOU 1793  OP2  DG C   9    18301  14928  17361  -3867   -540   -705       O  
ATOM   1794  O5'  DG C   9      36.522 -45.769-229.857  1.00121.07           O  
ANISOU 1794  O5'  DG C   9    16680  13734  15587  -3885   -714   -944       O  
ATOM   1795  C5'  DG C   9      37.879 -45.842-230.282  1.00115.94           C  
ANISOU 1795  C5'  DG C   9    16148  12875  15028  -3774   -677   -833       C  
ATOM   1796  C4'  DG C   9      38.002 -46.248-231.739  1.00114.28           C  
ANISOU 1796  C4'  DG C   9    15911  12739  14770  -3919   -599  -1078       C  
ATOM   1797  O4'  DG C   9      39.314 -46.819-231.934  1.00113.34           O  
ANISOU 1797  O4'  DG C   9    15941  12302  14822  -3859   -454   -981       O  
ATOM   1798  C3'  DG C   9      37.066 -47.358-232.193  1.00111.20           C  
ANISOU 1798  C3'  DG C   9    15463  12386  14403  -4233   -376  -1401       C  
ATOM   1799  O3'  DG C   9      37.114 -47.456-233.621  1.00113.04           O  
ANISOU 1799  O3'  DG C   9    15629  12795  14524  -4359   -361  -1640       O  
ATOM   1800  C2'  DG C   9      37.732 -48.558-231.550  1.00104.15           C  
ANISOU 1800  C2'  DG C   9    14745  11039  13789  -4271    -76  -1321       C  
ATOM   1801  C1'  DG C   9      39.221 -48.226-231.754  1.00105.11           C  
ANISOU 1801  C1'  DG C   9    14980  10983  13976  -4042   -131  -1094       C  
ATOM   1802  N9   DG C   9      40.060 -48.610-230.623  1.00 91.41           N  
ANISOU 1802  N9   DG C   9    13378   8921  12433  -3875    -16   -803       N  
ATOM   1803  C8   DG C   9      39.753 -48.509-229.282  1.00 83.40           C  
ANISOU 1803  C8   DG C   9    12365   7860  11465  -3783    -39   -611       C  
ATOM   1804  N7   DG C   9      40.695 -48.950-228.498  1.00 79.42           N  
ANISOU 1804  N7   DG C   9    11969   7086  11119  -3625     92   -354       N  
ATOM   1805  C5   DG C   9      41.694 -49.359-229.372  1.00 75.94           C  
ANISOU 1805  C5   DG C   9    11613   6493  10748  -3604    210   -371       C  
ATOM   1806  C6   DG C   9      42.962 -49.923-229.101  1.00 79.69           C  
ANISOU 1806  C6   DG C   9    12206   6695  11377  -3437    383   -140       C  
ATOM   1807  O6   DG C   9      43.469 -50.171-227.993  1.00 87.20           O  
ANISOU 1807  O6   DG C   9    13202   7509  12423  -3264    465    140       O  
ATOM   1808  N1   DG C   9      43.662 -50.219-230.285  1.00 80.01           N  
ANISOU 1808  N1   DG C   9    12303   6653  11444  -3476    469   -255       N  
ATOM   1809  C2   DG C   9      43.186 -49.986-231.563  1.00 86.24           C  
ANISOU 1809  C2   DG C   9    13032   7619  12116  -3661    390   -559       C  
ATOM   1810  N2   DG C   9      43.995 -50.338-232.579  1.00 86.24           N  
ANISOU 1810  N2   DG C   9    13097   7509  12160  -3677    495   -633       N  
ATOM   1811  N3   DG C   9      41.998 -49.445-231.825  1.00 81.22           N  
ANISOU 1811  N3   DG C   9    12267   7276  11317  -3808    224   -767       N  
ATOM   1812  C4   DG C   9      41.311 -49.163-230.686  1.00 77.48           C  
ANISOU 1812  C4   DG C   9    11747   6868  10826  -3766    145   -655       C  
ATOM   1813  P    DC C  10      35.952 -48.183-234.465  1.00112.16           P  
ANISOU 1813  P    DC C  10    15369  12946  14300  -4710   -216  -2050       P  
ATOM   1814  OP1  DC C  10      34.916 -47.167-234.743  1.00116.82           O  
ANISOU 1814  OP1  DC C  10    15743  14045  14599  -4672   -473  -2104       O  
ATOM   1815  OP2  DC C  10      35.548 -49.458-233.822  1.00 98.10           O  
ANISOU 1815  OP2  DC C  10    13668  10886  12719  -4940    101  -2177       O  
ATOM   1816  O5'  DC C  10      36.687 -48.533-235.852  1.00122.95           O  
ANISOU 1816  O5'  DC C  10    16756  14306  15655  -4801   -125  -2223       O  
ATOM   1817  C5'  DC C  10      38.123 -48.693-235.899  1.00106.94           C  
ANISOU 1817  C5'  DC C  10    14916  11909  13808  -4638    -60  -2029       C  
ATOM   1818  C4'  DC C  10      38.517 -50.146-236.182  1.00103.17           C  
ANISOU 1818  C4'  DC C  10    14573  11074  13553  -4864    325  -2208       C  
ATOM   1819  O4'  DC C  10      39.495 -50.566-235.216  1.00 99.96           O  
ANISOU 1819  O4'  DC C  10    14368  10211  13401  -4681    463  -1913       O  
ATOM   1820  C3'  DC C  10      37.380 -51.143-236.089  1.00104.31           C  
ANISOU 1820  C3'  DC C  10    14631  11283  13719  -5092    568  -2464       C  
ATOM   1821  O3'  DC C  10      36.920 -51.443-237.391  1.00121.26           O  
ANISOU 1821  O3'  DC C  10    16627  13741  15707  -5265    630  -2781       O  
ATOM   1822  C2'  DC C  10      37.984 -52.382-235.408  1.00 93.37           C  
ANISOU 1822  C2'  DC C  10    13442   9393  12641  -5046    925  -2348       C  
ATOM   1823  C1'  DC C  10      39.356 -51.928-234.919  1.00 96.54           C  
ANISOU 1823  C1'  DC C  10    14019   9488  13175  -4797    837  -2001       C  
ATOM   1824  N1   DC C  10      39.539 -52.078-233.448  1.00 90.97           N  
ANISOU 1824  N1   DC C  10    13432   8495  12638  -4656    902  -1710       N  
ATOM   1825  C2   DC C  10      40.736 -52.596-232.955  1.00 87.22           C  
ANISOU 1825  C2   DC C  10    13135   7627  12379  -4460   1082  -1439       C  
ATOM   1826  O2   DC C  10      41.621 -52.932-233.762  1.00 86.24           O  
ANISOU 1826  O2   DC C  10    13075   7383  12311  -4414   1185  -1455       O  
ATOM   1827  N3   DC C  10      40.892 -52.724-231.606  1.00 81.43           N  
ANISOU 1827  N3   DC C  10    12487   6679  11773  -4316   1143  -1157       N  
ATOM   1828  C4   DC C  10      39.913 -52.343-230.780  1.00 81.09           C  
ANISOU 1828  C4   DC C  10    12357   6799  11656  -4350   1015  -1145       C  
ATOM   1829  N4   DC C  10      40.105 -52.487-229.464  1.00 75.30           N  
ANISOU 1829  N4   DC C  10    11685   5890  11037  -4172   1070   -853       N  
ATOM   1830  C5   DC C  10      38.685 -51.814-231.270  1.00 84.02           C  
ANISOU 1830  C5   DC C  10    12555   7552  11817  -4550    830  -1424       C  
ATOM   1831  C6   DC C  10      38.545 -51.697-232.598  1.00 83.96           C  
ANISOU 1831  C6   DC C  10    12465   7758  11676  -4705    785  -1697       C  
TER    1832       DC C  10                                                      
ATOM   1833  P    DG D   1      49.371 -58.426-224.636  1.00114.54           P  
ANISOU 1833  P    DG D   1    17396   8986  17139  -1759   3141   2017       P  
ATOM   1834  OP1  DG D   1      48.596 -58.098-223.422  1.00107.70           O  
ANISOU 1834  OP1  DG D   1    16462   8224  16235  -1758   3043   2139       O  
ATOM   1835  OP2  DG D   1      49.630 -59.840-224.966  1.00105.37           O  
ANISOU 1835  OP2  DG D   1    16340   7569  16127  -1670   3580   1985       O  
ATOM   1836  O5'  DG D   1      48.651 -57.807-225.924  1.00102.90           O  
ANISOU 1836  O5'  DG D   1    15925   7559  15613  -2140   2919   1553       O  
ATOM   1837  C5'  DG D   1      48.562 -58.596-227.120  1.00 95.48           C  
ANISOU 1837  C5'  DG D   1    15062   6464  14753  -2298   3134   1241       C  
ATOM   1838  C4'  DG D   1      48.511 -57.722-228.359  1.00 95.04           C  
ANISOU 1838  C4'  DG D   1    14973   6549  14589  -2527   2848    946       C  
ATOM   1839  O4'  DG D   1      47.194 -57.134-228.496  1.00 92.20           O  
ANISOU 1839  O4'  DG D   1    14542   6350  14142  -2829   2636    638       O  
ATOM   1840  C3'  DG D   1      49.485 -56.550-228.381  1.00 96.88           C  
ANISOU 1840  C3'  DG D   1    15165   6944  14702  -2385   2532   1161       C  
ATOM   1841  O3'  DG D   1      49.885 -56.333-229.700  1.00113.90           O  
ANISOU 1841  O3'  DG D   1    17339   9118  16820  -2499   2455    941       O  
ATOM   1842  C2'  DG D   1      48.616 -55.398-227.904  1.00 86.24           C  
ANISOU 1842  C2'  DG D   1    13737   5811  13218  -2541   2193   1090       C  
ATOM   1843  C1'  DG D   1      47.319 -55.740-228.612  1.00 85.35           C  
ANISOU 1843  C1'  DG D   1    13607   5707  13114  -2869   2236    654       C  
ATOM   1844  N9   DG D   1      46.152 -55.130-228.012  1.00 88.12           N  
ANISOU 1844  N9   DG D   1    13886   6218  13379  -3031   2044    552       N  
ATOM   1845  C8   DG D   1      45.931 -54.919-226.680  1.00 93.25           C  
ANISOU 1845  C8   DG D   1    14488   6927  14014  -2889   1984    805       C  
ATOM   1846  N7   DG D   1      44.788 -54.355-226.425  1.00 92.38           N  
ANISOU 1846  N7   DG D   1    14281   7022  13797  -3057   1772    630       N  
ATOM   1847  C5   DG D   1      44.223 -54.162-227.675  1.00 89.93           C  
ANISOU 1847  C5   DG D   1    13949   6802  13417  -3326   1691    247       C  
ATOM   1848  C6   DG D   1      42.981 -53.587-228.032  1.00 93.00           C  
ANISOU 1848  C6   DG D   1    14226   7449  13662  -3572   1477    -60       C  
ATOM   1849  O6   DG D   1      42.107 -53.112-227.284  1.00 90.91           O  
ANISOU 1849  O6   DG D   1    13868   7360  13312  -3602   1312    -56       O  
ATOM   1850  N1   DG D   1      42.793 -53.599-229.413  1.00 90.26           N  
ANISOU 1850  N1   DG D   1    13866   7170  13256  -3788   1471   -390       N  
ATOM   1851  C2   DG D   1      43.690 -54.104-230.324  1.00 85.21           C  
ANISOU 1851  C2   DG D   1    13303   6380  12693  -3754   1631   -425       C  
ATOM   1852  N2   DG D   1      43.330 -54.027-231.612  1.00 78.37           N  
ANISOU 1852  N2   DG D   1    12369   5683  11726  -3951   1574   -759       N  
ATOM   1853  N3   DG D   1      44.854 -54.649-229.998  1.00 86.26           N  
ANISOU 1853  N3   DG D   1    13543   6263  12967  -3513   1826   -140       N  
ATOM   1854  C4   DG D   1      45.051 -54.642-228.663  1.00 86.96           C  
ANISOU 1854  C4   DG D   1    13663   6262  13116  -3323   1859    189       C  
ATOM   1855  P    DC D   2      51.355 -55.801-230.032  1.00 87.98           P  
ANISOU 1855  P    DC D   2    14071   5875  13483  -2282   2341   1178       P  
ATOM   1856  OP1  DC D   2      52.143 -57.040-230.184  1.00 88.87           O  
ANISOU 1856  OP1  DC D   2    14256   5775  13735  -2088   2712   1307       O  
ATOM   1857  OP2  DC D   2      51.718 -54.716-229.084  1.00 81.37           O  
ANISOU 1857  OP2  DC D   2    13104   5335  12477  -2094   2003   1449       O  
ATOM   1858  O5'  DC D   2      51.178 -55.061-231.435  1.00 85.30           O  
ANISOU 1858  O5'  DC D   2    13720   5655  13035  -2537   2101    821       O  
ATOM   1859  C5'  DC D   2      50.261 -55.572-232.390  1.00 81.31           C  
ANISOU 1859  C5'  DC D   2    13206   5135  12553  -2813   2195    413       C  
ATOM   1860  C4'  DC D   2      49.580 -54.433-233.122  1.00 88.32           C  
ANISOU 1860  C4'  DC D   2    14016   6283  13259  -3058   1841    127       C  
ATOM   1861  O4'  DC D   2      48.417 -53.991-232.373  1.00 75.69           O  
ANISOU 1861  O4'  DC D   2    12331   4848  11582  -3164   1684     67       O  
ATOM   1862  C3'  DC D   2      50.455 -53.200-233.323  1.00 89.51           C  
ANISOU 1862  C3'  DC D   2    14077   6703  13228  -2880   1457    274       C  
ATOM   1863  O3'  DC D   2      50.381 -52.768-234.681  1.00109.94           O  
ANISOU 1863  O3'  DC D   2    16635   9426  15713  -3047   1311    -14       O  
ATOM   1864  C2'  DC D   2      49.851 -52.172-232.362  1.00 91.72           C  
ANISOU 1864  C2'  DC D   2    14226   7268  13354  -2826   1130    372       C  
ATOM   1865  C1'  DC D   2      48.396 -52.593-232.324  1.00 88.19           C  
ANISOU 1865  C1'  DC D   2    13770   6795  12941  -3090   1234    105       C  
ATOM   1866  N1   DC D   2      47.708 -52.175-231.084  1.00 78.83           N  
ANISOU 1866  N1   DC D   2    12508   5738  11704  -3037   1100    239       N  
ATOM   1867  C2   DC D   2      46.395 -51.697-231.144  1.00 81.75           C  
ANISOU 1867  C2   DC D   2    12783   6316  11961  -3239    933      0       C  
ATOM   1868  O2   DC D   2      45.816 -51.644-232.237  1.00 87.42           O  
ANISOU 1868  O2   DC D   2    13469   7137  12611  -3459    901   -317       O  
ATOM   1869  N3   DC D   2      45.791 -51.305-230.000  1.00 74.52           N  
ANISOU 1869  N3   DC D   2    11802   5512  11002  -3184    814    128       N  
ATOM   1870  C4   DC D   2      46.446 -51.385-228.839  1.00 84.18           C  
ANISOU 1870  C4   DC D   2    13042   6661  12281  -2949    855    469       C  
ATOM   1871  N4   DC D   2      45.807 -50.992-227.726  1.00 88.44           N  
ANISOU 1871  N4   DC D   2    13509   7324  12769  -2912    736    576       N  
ATOM   1872  C5   DC D   2      47.785 -51.868-228.765  1.00 84.09           C  
ANISOU 1872  C5   DC D   2    13108   6476  12366  -2736   1021    720       C  
ATOM   1873  C6   DC D   2      48.369 -52.244-229.901  1.00 74.65           C  
ANISOU 1873  C6   DC D   2    11986   5156  11222  -2783   1139    598       C  
ATOM   1874  P    DG D   3      51.222 -51.488-235.192  1.00169.80           P  
ANISOU 1874  P    DG D   3    24133  17281  23102  -2904    936     66       P  
ATOM   1875  OP1  DG D   3      52.047 -51.944-236.332  1.00169.11           O  
ANISOU 1875  OP1  DG D   3    24124  17055  23074  -2924   1079    -25       O  
ATOM   1876  OP2  DG D   3      51.905 -50.822-234.054  1.00158.29           O  
ANISOU 1876  OP2  DG D   3    22624  15939  21582  -2639    763    415       O  
ATOM   1877  O5'  DG D   3      50.089 -50.494-235.735  1.00125.33           O  
ANISOU 1877  O5'  DG D   3    18374  11974  17269  -3091    630   -206       O  
ATOM   1878  C5'  DG D   3      48.975 -51.004-236.492  1.00112.67           C  
ANISOU 1878  C5'  DG D   3    16754  10388  15669  -3385    749   -562       C  
ATOM   1879  C4'  DG D   3      47.898 -49.944-236.628  1.00101.54           C  
ANISOU 1879  C4'  DG D   3    15193   9345  14041  -3476    436   -711       C  
ATOM   1880  O4'  DG D   3      47.123 -49.890-235.404  1.00102.15           O  
ANISOU 1880  O4'  DG D   3    15236   9443  14133  -3460    414   -610       O  
ATOM   1881  C3'  DG D   3      48.440 -48.532-236.865  1.00 95.23           C  
ANISOU 1881  C3'  DG D   3    14324   8803  13055  -3298     81   -585       C  
ATOM   1882  O3'  DG D   3      47.752 -47.906-237.899  1.00 94.06           O  
ANISOU 1882  O3'  DG D   3    14072   8941  12726  -3424    -88   -825       O  
ATOM   1883  C2'  DG D   3      48.217 -47.807-235.551  1.00 94.00           C  
ANISOU 1883  C2'  DG D   3    14125   8739  12850  -3150    -89   -356       C  
ATOM   1884  C1'  DG D   3      47.050 -48.564-234.933  1.00 96.26           C  
ANISOU 1884  C1'  DG D   3    14398   8961  13217  -3311     75   -465       C  
ATOM   1885  N9   DG D   3      47.169 -48.583-233.498  1.00 86.54           N  
ANISOU 1885  N9   DG D   3    13186   7641  12056  -3163     90   -198       N  
ATOM   1886  C8   DG D   3      48.220 -49.093-232.781  1.00 86.54           C  
ANISOU 1886  C8   DG D   3    13268   7423  12190  -2982    240     74       C  
ATOM   1887  N7   DG D   3      48.101 -48.930-231.499  1.00 89.05           N  
ANISOU 1887  N7   DG D   3    13559   7760  12517  -2868    204    286       N  
ATOM   1888  C5   DG D   3      46.899 -48.253-231.354  1.00 84.03           C  
ANISOU 1888  C5   DG D   3    12831   7341  11757  -2984     16    142       C  
ATOM   1889  C6   DG D   3      46.255 -47.804-230.184  1.00 75.87           C  
ANISOU 1889  C6   DG D   3    11734   6418  10677  -2942    -95    254       C  
ATOM   1890  O6   DG D   3      46.636 -47.928-229.008  1.00 73.62           O  
ANISOU 1890  O6   DG D   3    11454   6072  10444  -2797    -53    506       O  
ATOM   1891  N1   DG D   3      45.048 -47.152-230.473  1.00 78.25           N  
ANISOU 1891  N1   DG D   3    11945   6946  10840  -3079   -268     49       N  
ATOM   1892  C2   DG D   3      44.545 -46.949-231.741  1.00 81.84           C  
ANISOU 1892  C2   DG D   3    12358   7543  11196  -3226   -329   -219       C  
ATOM   1893  N2   DG D   3      43.380 -46.286-231.813  1.00 63.92           N  
ANISOU 1893  N2   DG D   3     9979   5531   8776  -3311   -493   -356       N  
ATOM   1894  N3   DG D   3      45.144 -47.375-232.856  1.00 80.38           N  
ANISOU 1894  N3   DG D   3    12221   7273  11046  -3277   -229   -336       N  
ATOM   1895  C4   DG D   3      46.315 -48.016-232.582  1.00 86.17           C  
ANISOU 1895  C4   DG D   3    13061   7748  11932  -3155    -58   -147       C  
ATOM   1896  P    DC D   4      48.373 -46.581-238.551  1.00 84.73           P  
ANISOU 1896  P    DC D   4    12845   7985  11362  -3267   -379   -749       P  
ATOM   1897  OP1  DC D   4      48.265 -46.772-240.015  1.00 97.39           O  
ANISOU 1897  OP1  DC D   4    14411   9701  12891  -3415   -348  -1012       O  
ATOM   1898  OP2  DC D   4      49.674 -46.282-237.894  1.00 76.17           O  
ANISOU 1898  OP2  DC D   4    11843   6753  10344  -3039   -414   -450       O  
ATOM   1899  O5'  DC D   4      47.383 -45.417-238.084  1.00 91.24           O  
ANISOU 1899  O5'  DC D   4    13555   9109  12003  -3223   -633   -724       O  
ATOM   1900  C5'  DC D   4      45.975 -45.647-237.961  1.00 87.83           C  
ANISOU 1900  C5'  DC D   4    13026   8831  11515  -3392   -613   -906       C  
ATOM   1901  C4'  DC D   4      45.360 -44.559-237.104  1.00 83.99           C  
ANISOU 1901  C4'  DC D   4    12473   8535  10907  -3271   -827   -765       C  
ATOM   1902  O4'  DC D   4      45.521 -44.910-235.692  1.00 92.95           O  
ANISOU 1902  O4'  DC D   4    13671   9459  12185  -3207   -751   -570       O  
ATOM   1903  C3'  DC D   4      46.028 -43.183-237.268  1.00 89.47           C  
ANISOU 1903  C3'  DC D   4    13173   9354  11468  -3061  -1051   -598       C  
ATOM   1904  O3'  DC D   4      45.045 -42.130-237.307  1.00106.16           O  
ANISOU 1904  O3'  DC D   4    15180  11767  13387  -3018  -1230   -619       O  
ATOM   1905  C2'  DC D   4      46.894 -43.084-236.020  1.00 83.59           C  
ANISOU 1905  C2'  DC D   4    12517   8405  10839  -2916  -1043   -331       C  
ATOM   1906  C1'  DC D   4      46.003 -43.776-235.015  1.00 79.29           C  
ANISOU 1906  C1'  DC D   4    11949   7795  10383  -3008   -940   -341       C  
ATOM   1907  N1   DC D   4      46.719 -44.161-233.773  1.00 75.40           N  
ANISOU 1907  N1   DC D   4    11527   7087  10033  -2905   -853   -107       N  
ATOM   1908  C2   DC D   4      46.133 -43.892-232.533  1.00 81.49           C  
ANISOU 1908  C2   DC D   4    12264   7899  10799  -2871   -903      7       C  
ATOM   1909  O2   DC D   4      44.998 -43.382-232.504  1.00 86.81           O  
ANISOU 1909  O2   DC D   4    12859   8763  11362  -2931  -1009    -95       O  
ATOM   1910  N3   DC D   4      46.819 -44.213-231.391  1.00 61.56           N  
ANISOU 1910  N3   DC D   4     9782   5228   8379  -2764   -828    235       N  
ATOM   1911  C4   DC D   4      48.038 -44.753-231.481  1.00 63.09           C  
ANISOU 1911  C4   DC D   4    10045   5257   8671  -2678   -709    358       C  
ATOM   1912  N4   DC D   4      48.677 -45.053-230.340  1.00 59.92           N  
ANISOU 1912  N4   DC D   4     9655   4771   8342  -2553   -634    599       N  
ATOM   1913  C5   DC D   4      48.653 -45.017-232.744  1.00 67.89           C  
ANISOU 1913  C5   DC D   4    10699   5804   9294  -2707   -655    245       C  
ATOM   1914  C6   DC D   4      47.971 -44.694-233.848  1.00 78.82           C  
ANISOU 1914  C6   DC D   4    12045   7324  10580  -2826   -735     11       C  
ATOM   1915  P    DG D   5      45.452 -40.619-237.716  1.00 87.59           P  
ANISOU 1915  P    DG D   5    12831   9581  10869  -2821  -1424   -495       P  
ATOM   1916  OP1  DG D   5      45.228 -40.496-239.162  1.00 89.69           O  
ANISOU 1916  OP1  DG D   5    13021  10063  10995  -2860  -1452   -664       O  
ATOM   1917  OP2  DG D   5      46.765 -40.239-237.152  1.00 87.94           O  
ANISOU 1917  OP2  DG D   5    12993   9422  10997  -2684  -1439   -286       O  
ATOM   1918  O5'  DG D   5      44.371 -39.720-236.957  1.00 80.28           O  
ANISOU 1918  O5'  DG D   5    11833   8847   9822  -2752  -1540   -427       O  
ATOM   1919  C5'  DG D   5      43.415 -40.338-236.114  1.00 69.15           C  
ANISOU 1919  C5'  DG D   5    10371   7436   8467  -2863  -1485   -475       C  
ATOM   1920  C4'  DG D   5      42.999 -39.403-235.002  1.00 69.78           C  
ANISOU 1920  C4'  DG D   5    10450   7565   8497  -2744  -1586   -309       C  
ATOM   1921  O4'  DG D   5      43.613 -39.814-233.764  1.00 75.57           O  
ANISOU 1921  O4'  DG D   5    11267   8049   9396  -2734  -1524   -163       O  
ATOM   1922  C3'  DG D   5      43.401 -37.955-235.208  1.00 75.65           C  
ANISOU 1922  C3'  DG D   5    11231   8401   9111  -2553  -1708   -175       C  
ATOM   1923  O3'  DG D   5      42.413 -37.097-234.672  1.00 77.35           O  
ANISOU 1923  O3'  DG D   5    11391   8787   9211  -2477  -1783   -119       O  
ATOM   1924  C2'  DG D   5      44.723 -37.836-234.455  1.00 78.91           C  
ANISOU 1924  C2'  DG D   5    11769   8566   9648  -2487  -1686     -7       C  
ATOM   1925  C1'  DG D   5      44.606 -38.886-233.364  1.00 73.97           C  
ANISOU 1925  C1'  DG D   5    11144   7780   9179  -2584  -1594     20       C  
ATOM   1926  N9   DG D   5      45.837 -39.622-233.189  1.00 79.26           N  
ANISOU 1926  N9   DG D   5    11893   8228   9995  -2585  -1498     95       N  
ATOM   1927  C8   DG D   5      46.674 -40.057-234.183  1.00 88.33           C  
ANISOU 1927  C8   DG D   5    13084   9297  11183  -2598  -1443     38       C  
ATOM   1928  N7   DG D   5      47.710 -40.708-233.744  1.00 83.80           N  
ANISOU 1928  N7   DG D   5    12571   8528  10739  -2573  -1345    149       N  
ATOM   1929  C5   DG D   5      47.547 -40.709-232.371  1.00 77.48           C  
ANISOU 1929  C5   DG D   5    11760   7696   9982  -2543  -1339    289       C  
ATOM   1930  C6   DG D   5      48.360 -41.273-231.370  1.00 74.56           C  
ANISOU 1930  C6   DG D   5    11417   7188   9722  -2488  -1248    467       C  
ATOM   1931  O6   DG D   5      49.427 -41.897-231.510  1.00 79.14           O  
ANISOU 1931  O6   DG D   5    12042   7639  10389  -2441  -1145    547       O  
ATOM   1932  N1   DG D   5      47.834 -41.047-230.100  1.00 68.76           N  
ANISOU 1932  N1   DG D   5    10643   6504   8981  -2472  -1278    567       N  
ATOM   1933  C2   DG D   5      46.661 -40.368-229.840  1.00 65.20           C  
ANISOU 1933  C2   DG D   5    10144   6193   8438  -2510  -1380    498       C  
ATOM   1934  N2   DG D   5      46.314 -40.253-228.544  1.00 67.83           N  
ANISOU 1934  N2   DG D   5    10442   6550   8779  -2492  -1392    611       N  
ATOM   1935  N3   DG D   5      45.888 -39.836-230.776  1.00 62.72           N  
ANISOU 1935  N3   DG D   5     9805   6007   8020  -2547  -1460    343       N  
ATOM   1936  C4   DG D   5      46.393 -40.044-232.011  1.00 75.81           C  
ANISOU 1936  C4   DG D   5    11490   7641   9674  -2560  -1435    248       C  
ATOM   1937  P    DC D   6      42.633 -35.509-234.704  1.00 86.99           P  
ANISOU 1937  P    DC D   6    12667  10081  10303  -2274  -1859     30       P  
ATOM   1938  OP1  DC D   6      41.312 -34.861-234.863  1.00 85.15           O  
ANISOU 1938  OP1  DC D   6    12329  10124   9900  -2201  -1906     16       O  
ATOM   1939  OP2  DC D   6      43.775 -35.190-235.581  1.00 82.30           O  
ANISOU 1939  OP2  DC D   6    12154   9413   9703  -2210  -1854     51       O  
ATOM   1940  O5'  DC D   6      43.195 -35.198-233.264  1.00 80.52           O  
ANISOU 1940  O5'  DC D   6    11942   9061   9589  -2252  -1849    184       O  
ATOM   1941  C5'  DC D   6      42.551 -35.716-232.127  1.00 71.46           C  
ANISOU 1941  C5'  DC D   6    10755   7882   8515  -2330  -1835    197       C  
ATOM   1942  C4'  DC D   6      43.295 -35.264-230.898  1.00 76.68           C  
ANISOU 1942  C4'  DC D   6    11497   8394   9242  -2293  -1829    349       C  
ATOM   1943  O4'  DC D   6      44.474 -36.099-230.720  1.00 83.29           O  
ANISOU 1943  O4'  DC D   6    12381   9051  10213  -2344  -1771    384       O  
ATOM   1944  C3'  DC D   6      43.820 -33.836-230.971  1.00 73.97           C  
ANISOU 1944  C3'  DC D   6    11238   8064   8803  -2167  -1850    439       C  
ATOM   1945  O3'  DC D   6      43.873 -33.308-229.655  1.00 93.65           O  
ANISOU 1945  O3'  DC D   6    13760  10511  11311  -2165  -1843    538       O  
ATOM   1946  C2'  DC D   6      45.230 -34.052-231.515  1.00 71.28           C  
ANISOU 1946  C2'  DC D   6    10966   7599   8517  -2172  -1824    449       C  
ATOM   1947  C1'  DC D   6      45.622 -35.283-230.717  1.00 74.41           C  
ANISOU 1947  C1'  DC D   6    11338   7875   9061  -2270  -1782    473       C  
ATOM   1948  N1   DC D   6      46.787 -36.050-231.269  1.00 68.20           N  
ANISOU 1948  N1   DC D   6    10585   6968   8359  -2292  -1733    470       N  
ATOM   1949  C2   DC D   6      47.622 -36.756-230.391  1.00 70.96           C  
ANISOU 1949  C2   DC D   6    10939   7206   8816  -2313  -1675    572       C  
ATOM   1950  O2   DC D   6      47.373 -36.742-229.181  1.00 64.77           O  
ANISOU 1950  O2   DC D   6    10125   6435   8050  -2323  -1672    656       O  
ATOM   1951  N3   DC D   6      48.682 -37.432-230.889  1.00 59.25           N  
ANISOU 1951  N3   DC D   6     9486   5622   7405  -2309  -1616    588       N  
ATOM   1952  C4   DC D   6      48.908 -37.426-232.201  1.00 71.34           C  
ANISOU 1952  C4   DC D   6    11046   7149   8912  -2306  -1620    488       C  
ATOM   1953  N4   DC D   6      49.963 -38.114-232.655  1.00 86.70           N  
ANISOU 1953  N4   DC D   6    13023   8985  10932  -2300  -1553    508       N  
ATOM   1954  C5   DC D   6      48.064 -36.718-233.113  1.00 67.46           C  
ANISOU 1954  C5   DC D   6    10543   6783   8305  -2293  -1686    377       C  
ATOM   1955  C6   DC D   6      47.032 -36.045-232.605  1.00 68.15           C  
ANISOU 1955  C6   DC D   6    10596   6982   8315  -2276  -1737    381       C  
ATOM   1956  P    DG D   7      43.408 -31.809-229.319  1.00 83.90           P  
ANISOU 1956  P    DG D   7    12577   9342   9961  -2062  -1834    600       P  
ATOM   1957  OP1  DG D   7      41.968 -31.924-229.014  1.00 86.18           O  
ANISOU 1957  OP1  DG D   7    12776   9760  10208  -2055  -1863    577       O  
ATOM   1958  OP2  DG D   7      43.889 -30.869-230.366  1.00 70.82           O  
ANISOU 1958  OP2  DG D   7    11002   7692   8216  -1954  -1804    605       O  
ATOM   1959  O5'  DG D   7      44.216 -31.480-227.974  1.00 86.83           O  
ANISOU 1959  O5'  DG D   7    12997   9615  10381  -2118  -1801    682       O  
ATOM   1960  C5'  DG D   7      44.158 -32.401-226.862  1.00 81.10           C  
ANISOU 1960  C5'  DG D   7    12202   8865   9747  -2211  -1813    713       C  
ATOM   1961  C4'  DG D   7      45.527 -32.609-226.211  1.00 79.97           C  
ANISOU 1961  C4'  DG D   7    12074   8658   9652  -2263  -1783    779       C  
ATOM   1962  O4'  DG D   7      46.395 -33.395-227.083  1.00 76.72           O  
ANISOU 1962  O4'  DG D   7    11670   8181   9298  -2263  -1775    761       O  
ATOM   1963  C3'  DG D   7      46.331 -31.338-225.888  1.00 92.61           C  
ANISOU 1963  C3'  DG D   7    13752  10267  11170  -2262  -1740    803       C  
ATOM   1964  O3'  DG D   7      47.156 -31.588-224.768  1.00107.81           O  
ANISOU 1964  O3'  DG D   7    15628  12224  13110  -2335  -1722    868       O  
ATOM   1965  C2'  DG D   7      47.214 -31.235-227.113  1.00 93.72           C  
ANISOU 1965  C2'  DG D   7    13955  10358  11297  -2224  -1728    768       C  
ATOM   1966  C1'  DG D   7      47.614 -32.701-227.207  1.00 84.27           C  
ANISOU 1966  C1'  DG D   7    12686   9125  10206  -2255  -1750    787       C  
ATOM   1967  N9   DG D   7      48.270 -33.068-228.451  1.00 61.79           N  
ANISOU 1967  N9   DG D   7     9873   6223   7380  -2226  -1748    745       N  
ATOM   1968  C8   DG D   7      47.941 -32.647-229.709  1.00 55.31           C  
ANISOU 1968  C8   DG D   7     9099   5408   6509  -2168  -1761    670       C  
ATOM   1969  N7   DG D   7      48.712 -33.137-230.632  1.00 69.57           N  
ANISOU 1969  N7   DG D   7    10922   7164   8346  -2161  -1755    641       N  
ATOM   1970  C5   DG D   7      49.624 -33.920-229.941  1.00 60.95           C  
ANISOU 1970  C5   DG D   7     9798   6025   7333  -2206  -1729    711       C  
ATOM   1971  C6   DG D   7      50.706 -34.694-230.427  1.00 61.43           C  
ANISOU 1971  C6   DG D   7     9862   6020   7457  -2206  -1698    729       C  
ATOM   1972  O6   DG D   7      51.074 -34.838-231.610  1.00 68.53           O  
ANISOU 1972  O6   DG D   7    10799   6879   8360  -2184  -1695    667       O  
ATOM   1973  N1   DG D   7      51.386 -35.343-229.390  1.00 55.61           N  
ANISOU 1973  N1   DG D   7     9071   5286   6774  -2221  -1659    842       N  
ATOM   1974  C2   DG D   7      51.056 -35.246-228.050  1.00 67.39           C  
ANISOU 1974  C2   DG D   7    10505   6846   8253  -2245  -1659    919       C  
ATOM   1975  N2   DG D   7      51.822 -35.948-227.187  1.00 55.56           N  
ANISOU 1975  N2   DG D   7     8939   5383   6791  -2233  -1612   1047       N  
ATOM   1976  N3   DG D   7      50.032 -34.521-227.589  1.00 74.33           N  
ANISOU 1976  N3   DG D   7    11387   7774   9080  -2265  -1695    883       N  
ATOM   1977  C4   DG D   7      49.364 -33.894-228.594  1.00 62.45           C  
ANISOU 1977  C4   DG D   7     9942   6256   7530  -2240  -1725    782       C  
ATOM   1978  P    DC D   8      46.628 -31.418-223.261  1.00178.00           P  
ANISOU 1978  P    DC D   8    24455  21192  21983  -2393  -1717    915       P  
ATOM   1979  OP1  DC D   8      45.740 -32.561-222.935  1.00169.40           O  
ANISOU 1979  OP1  DC D   8    23287  20095  20984  -2388  -1755    946       O  
ATOM   1980  OP2  DC D   8      46.152 -30.020-223.121  1.00173.89           O  
ANISOU 1980  OP2  DC D   8    24017  20680  21374  -2391  -1669    869       O  
ATOM   1981  O5'  DC D   8      47.970 -31.569-222.401  1.00112.94           O  
ANISOU 1981  O5'  DC D   8    16153  13045  13715  -2462  -1689    981       O  
ATOM   1982  C5'  DC D   8      49.083 -30.750-222.713  1.00109.67           C  
ANISOU 1982  C5'  DC D   8    15793  12659  13220  -2499  -1641    941       C  
ATOM   1983  C4'  DC D   8      50.355 -31.563-222.874  1.00 98.30           C  
ANISOU 1983  C4'  DC D   8    14287  11267  11795  -2493  -1645   1005       C  
ATOM   1984  O4'  DC D   8      50.410 -32.127-224.194  1.00100.75           O  
ANISOU 1984  O4'  DC D   8    14654  11445  12181  -2416  -1666    983       O  
ATOM   1985  C3'  DC D   8      51.607 -30.732-222.729  1.00 84.76           C  
ANISOU 1985  C3'  DC D   8    12577   9665   9964  -2575  -1590    969       C  
ATOM   1986  O3'  DC D   8      52.109 -30.923-221.473  1.00 75.39           O  
ANISOU 1986  O3'  DC D   8    11254   8680   8709  -2642  -1579   1036       O  
ATOM   1987  C2'  DC D   8      52.579 -31.256-223.789  1.00 92.09           C  
ANISOU 1987  C2'  DC D   8    13523  10543  10923  -2519  -1598    982       C  
ATOM   1988  C1'  DC D   8      51.753 -32.219-224.623  1.00 93.58           C  
ANISOU 1988  C1'  DC D   8    13742  10569  11244  -2418  -1644    999       C  
ATOM   1989  N1   DC D   8      51.793 -31.921-226.069  1.00 73.47           N  
ANISOU 1989  N1   DC D   8    11305   7898   8712  -2370  -1648    916       N  
ATOM   1990  C2   DC D   8      52.838 -32.419-226.852  1.00 67.52           C  
ANISOU 1990  C2   DC D   8    10556   7118   7981  -2340  -1642    930       C  
ATOM   1991  O2   DC D   8      53.734 -33.078-226.314  1.00 73.82           O  
ANISOU 1991  O2   DC D   8    11265   8004   8781  -2342  -1626   1021       O  
ATOM   1992  N3   DC D   8      52.839 -32.160-228.183  1.00 64.97           N  
ANISOU 1992  N3   DC D   8    10326   6693   7665  -2297  -1647    853       N  
ATOM   1993  C4   DC D   8      51.860 -31.425-228.719  1.00 63.86           C  
ANISOU 1993  C4   DC D   8    10263   6501   7500  -2266  -1653    782       C  
ATOM   1994  N4   DC D   8      51.904 -31.182-230.034  1.00 71.03           N  
ANISOU 1994  N4   DC D   8    11245   7345   8398  -2208  -1654    723       N  
ATOM   1995  C5   DC D   8      50.792 -30.907-227.932  1.00 69.70           C  
ANISOU 1995  C5   DC D   8    10998   7272   8214  -2280  -1651    781       C  
ATOM   1996  C6   DC D   8      50.794 -31.187-226.627  1.00 69.68           C  
ANISOU 1996  C6   DC D   8    10912   7347   8216  -2340  -1652    840       C  
ATOM   1997  P    DG D   9      52.878 -29.725-220.753  1.00 86.86           P  
ANISOU 1997  P    DG D   9    12686  10318   9999  -2801  -1501    949       P  
ATOM   1998  OP1  DG D   9      52.622 -29.911-219.308  1.00 94.26           O  
ANISOU 1998  OP1  DG D   9    13481  11452  10881  -2861  -1506   1009       O  
ATOM   1999  OP2  DG D   9      52.525 -28.462-221.453  1.00 73.48           O  
ANISOU 1999  OP2  DG D   9    11169   8463   8287  -2840  -1428    808       O  
ATOM   2000  O5'  DG D   9      54.413 -30.034-221.059  1.00 80.78           O  
ANISOU 2000  O5'  DG D   9    11839   9693   9159  -2814  -1490    980       O  
ATOM   2001  C5'  DG D   9      54.863 -31.380-221.161  1.00 81.09           C  
ANISOU 2001  C5'  DG D   9    11775   9772   9262  -2690  -1538   1135       C  
ATOM   2002  C4'  DG D   9      56.182 -31.424-221.901  1.00 83.18           C  
ANISOU 2002  C4'  DG D   9    12031  10096   9475  -2683  -1518   1131       C  
ATOM   2003  O4'  DG D   9      55.948 -31.475-223.334  1.00 86.97           O  
ANISOU 2003  O4'  DG D   9    12670  10307  10068  -2606  -1535   1074       O  
ATOM   2004  C3'  DG D   9      57.072 -30.215-221.653  1.00 91.11           C  
ANISOU 2004  C3'  DG D   9    13024  11288  10306  -2856  -1450    998       C  
ATOM   2005  O3'  DG D   9      58.402 -30.641-221.434  1.00105.46           O  
ANISOU 2005  O3'  DG D   9    14684  13374  12012  -2859  -1442   1074       O  
ATOM   2006  C2'  DG D   9      56.935 -29.387-222.933  1.00 78.09           C  
ANISOU 2006  C2'  DG D   9    11583   9383   8704  -2866  -1416    858       C  
ATOM   2007  C1'  DG D   9      56.679 -30.453-223.982  1.00 77.37           C  
ANISOU 2007  C1'  DG D   9    11540   9090   8767  -2690  -1487    947       C  
ATOM   2008  N9   DG D   9      55.884 -29.963-225.095  1.00 66.82           N  
ANISOU 2008  N9   DG D   9    10384   7492   7512  -2642  -1486    858       N  
ATOM   2009  C8   DG D   9      54.742 -29.211-225.009  1.00 69.43           C  
ANISOU 2009  C8   DG D   9    10811   7711   7857  -2655  -1464    792       C  
ATOM   2010  N7   DG D   9      54.212 -28.925-226.166  1.00 68.10           N  
ANISOU 2010  N7   DG D   9    10775   7356   7743  -2573  -1464    744       N  
ATOM   2011  C5   DG D   9      55.065 -29.509-227.087  1.00 55.09           C  
ANISOU 2011  C5   DG D   9     9126   5682   6125  -2521  -1491    763       C  
ATOM   2012  C6   DG D   9      55.009 -29.502-228.492  1.00 60.30           C  
ANISOU 2012  C6   DG D   9     9886   6194   6829  -2434  -1503    725       C  
ATOM   2013  O6   DG D   9      54.148 -28.973-229.224  1.00 70.35           O  
ANISOU 2013  O6   DG D   9    11262   7353   8115  -2368  -1491    681       O  
ATOM   2014  N1   DG D   9      56.073 -30.213-229.059  1.00 69.03           N  
ANISOU 2014  N1   DG D   9    10953   7319   7955  -2411  -1524    756       N  
ATOM   2015  C2   DG D   9      57.076 -30.839-228.347  1.00 76.28           C  
ANISOU 2015  C2   DG D   9    11745   8392   8844  -2446  -1527    833       C  
ATOM   2016  N2   DG D   9      58.019 -31.472-229.081  1.00 80.36           N  
ANISOU 2016  N2   DG D   9    12245   8902   9385  -2396  -1535    866       N  
ATOM   2017  N3   DG D   9      57.149 -30.844-227.009  1.00 68.53           N  
ANISOU 2017  N3   DG D   9    10651   7584   7802  -2515  -1516    883       N  
ATOM   2018  C4   DG D   9      56.110 -30.156-226.448  1.00 67.66           C  
ANISOU 2018  C4   DG D   9    10583   7443   7680  -2560  -1502    835       C  
ATOM   2019  P    DC D  10      59.562 -29.576-221.119  1.00100.05           P  
ANISOU 2019  P    DC D  10    13932  12969  11112  -3064  -1362    931       P  
ATOM   2020  OP1  DC D  10      60.380 -30.184-220.052  1.00115.07           O  
ANISOU 2020  OP1  DC D  10    15570  15289  12863  -3065  -1371   1063       O  
ATOM   2021  OP2  DC D  10      58.956 -28.238-220.937  1.00 96.95           O  
ANISOU 2021  OP2  DC D  10    13674  12476  10686  -3238  -1277    734       O  
ATOM   2022  O5'  DC D  10      60.441 -29.590-222.445  1.00 75.55           O  
ANISOU 2022  O5'  DC D  10    10919   9751   8035  -3018  -1355    898       O  
ATOM   2023  C5'  DC D  10      60.140 -30.543-223.440  1.00 83.25           C  
ANISOU 2023  C5'  DC D  10    11977  10468   9187  -2821  -1418   1004       C  
ATOM   2024  C4'  DC D  10      61.273 -30.690-224.413  1.00 80.32           C  
ANISOU 2024  C4'  DC D  10    11619  10104   8793  -2786  -1409   1000       C  
ATOM   2025  O4'  DC D  10      60.797 -30.463-225.759  1.00 84.02           O  
ANISOU 2025  O4'  DC D  10    12298  10232   9395  -2730  -1418    918       O  
ATOM   2026  C3'  DC D  10      62.377 -29.702-224.226  1.00 79.27           C  
ANISOU 2026  C3'  DC D  10    11434  10221   8466  -2974  -1336    866       C  
ATOM   2027  O3'  DC D  10      63.510 -30.231-224.821  1.00 82.52           O  
ANISOU 2027  O3'  DC D  10    11778  10733   8842  -2904  -1346    932       O  
ATOM   2028  C2'  DC D  10      61.846 -28.497-224.998  1.00 78.62           C  
ANISOU 2028  C2'  DC D  10    11587   9856   8429  -3069  -1270    672       C  
ATOM   2029  C1'  DC D  10      61.183 -29.168-226.192  1.00 77.21           C  
ANISOU 2029  C1'  DC D  10    11548   9344   8445  -2873  -1341    741       C  
ATOM   2030  N1   DC D  10      59.960 -28.465-226.674  1.00 66.29           N  
ANISOU 2030  N1   DC D  10    10356   7677   7154  -2860  -1318    653       N  
ATOM   2031  C2   DC D  10      59.620 -28.514-228.035  1.00 65.79           C  
ANISOU 2031  C2   DC D  10    10443   7356   7199  -2745  -1339    636       C  
ATOM   2032  O2   DC D  10      60.356 -29.127-228.823  1.00 67.67           O  
ANISOU 2032  O2   DC D  10    10666   7580   7465  -2674  -1374    676       O  
ATOM   2033  N3   DC D  10      58.495 -27.874-228.461  1.00 59.10           N  
ANISOU 2033  N3   DC D  10     9744   6304   6408  -2706  -1312    581       N  
ATOM   2034  C4   DC D  10      57.730 -27.229-227.569  1.00 61.13           C  
ANISOU 2034  C4   DC D  10    10016   6578   6635  -2776  -1262    546       C  
ATOM   2035  N4   DC D  10      56.631 -26.616-228.017  1.00 65.09           N  
ANISOU 2035  N4   DC D  10    10656   6893   7184  -2708  -1225    515       N  
ATOM   2036  C5   DC D  10      58.062 -27.180-226.183  1.00 61.71           C  
ANISOU 2036  C5   DC D  10     9951   6883   6614  -2911  -1240    547       C  
ATOM   2037  C6   DC D  10      59.171 -27.805-225.782  1.00 61.32           C  
ANISOU 2037  C6   DC D  10     9741   7066   6493  -2949  -1273    601       C  
TER    2038       DC D  10                                                      
HETATM 2039  O   HOH A 101      42.041 -37.424-202.197  1.00 68.77           O  
ANISOU 2039  O   HOH A 101     8685   9653   7793  -2541  -1554   2637       O  
HETATM 2040  O   HOH B 101      66.316 -33.898-239.671  1.00 66.78           O  
ANISOU 2040  O   HOH B 101    10879   6696   7799  -2001  -1471    690       O  
HETATM 2041  O   HOH B 102      60.222 -23.364-255.426  1.00 72.38           O  
ANISOU 2041  O   HOH B 102    12498   7657   7347   -342   -937    662       O  
HETATM 2042  O   HOH C 101      58.789 -35.425-228.853  1.00 74.39           O  
ANISOU 2042  O   HOH C 101    11260   8114   8891  -2129  -1509   1235       O  
HETATM 2043  O   HOH D 101      53.972 -24.512-226.409  1.00 70.66           O  
ANISOU 2043  O   HOH D 101    11539   7449   7859  -2762  -1006    439       O  
MASTER      321    0    0    6   10    0    0    6 2039    4    0   18          
END

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Related entries of code: 6iir

Entries with 90% protein sequence similarity cutoff in PDBbind
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Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3d2w	RCSB PDB PDBbind	10-mer
3glf	RCSB PDB PDBbind	10-mer
3i5x	RCSB PDB PDBbind	10-mer
3k49	RCSB PDB PDBbind	10-mer
3k4e	RCSB PDB PDBbind	10-mer
3kde	RCSB PDB PDBbind	10-mer
3kjo	RCSB PDB PDBbind	10-mer
5ho4	RCSB PDB PDBbind	10-mer
5zva	RCSB PDB PDBbind	10-mer
6kbs	RCSB PDB PDBbind	10-mer
5zc9	RCSB PDB PDBbind	10-mer

Entry Information

PDB ID	6iir
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	HRP3 PWWP domain
Ligand Name	10-mer
EC.Number	E.C.-.-.-.-
Resolution	2.2(Å)
Affinity (Kd/Ki/IC50)	Kd=2.8uM
Release Year	2019
Protein/NA Sequence	Check fasta file
Primary Reference	(2019) Nucleic Acids Res. Vol. 47: pp. 5436-5448

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): Q9Y3E1
Entrez Gene ID	NCBI Entrez Gene ID: 50810
ASD	Information of known allosteric effects of PDB entries

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