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HEADER    DNA BINDING PROTEIN/DNA                 07-OCT-18   6IIQ              
TITLE     COMPLEX STRUCTURE OF THE HRP3 PWWP DOMAIN WITH A 16-BP TA-RICH DNA    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOMA-DERIVED GROWTH FACTOR-RELATED PROTEIN 3;          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HRP-3,HEPATOMA-DERIVED GROWTH FACTOR 2,HDGF-2;              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 16-BP TA-RICH DNA;                                         
COMPND   8 CHAIN: D, E, F, G;                                                   
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: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
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 6IIQ    0                                                
JRNL        AUTH   Z.WANG,W.TIAN                                                
JRNL        TITL   COMPLEX STRUCTURE OF THE HRP3 PWWP DOMAIN WITH A 16-BP       
JRNL        TITL 2 TA-RICH DNA                                                  
JRNL        REF    NUCLEIC ACIDS RES.                         2019              
JRNL        REFN                   ESSN 1362-4962                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 31477                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1576                            
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 28.9759 -  4.0961    0.96     2934   163  0.1745 0.1985        
REMARK   3     2  4.0961 -  3.2526    0.94     2794   128  0.1791 0.2297        
REMARK   3     3  3.2526 -  2.8419    0.92     2695   159  0.2303 0.2974        
REMARK   3     4  2.8419 -  2.5822    0.93     2674   139  0.2431 0.3075        
REMARK   3     5  2.5822 -  2.3972    0.93     2707   126  0.2325 0.2541        
REMARK   3     6  2.3972 -  2.2560    0.94     2766   133  0.2281 0.2937        
REMARK   3     7  2.2560 -  2.1430    0.94     2756   143  0.2267 0.2949        
REMARK   3     8  2.1430 -  2.0498    0.94     2699   138  0.2101 0.2851        
REMARK   3     9  2.0498 -  1.9709    0.94     2682   145  0.2347 0.2906        
REMARK   3    10  1.9709 -  1.9029    0.95     2787   163  0.2542 0.2867        
REMARK   3    11  1.9029 -  1.8434    0.86     2407   139  0.2740 0.3551        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.210           
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      :  0.008           3250                                  
REMARK   3   ANGLE     :  1.119           4503                                  
REMARK   3   CHIRALITY :  0.051            427                                  
REMARK   3   PLANARITY :  0.005            487                                  
REMARK   3   DIHEDRAL  : 20.226           1276                                  
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):  14.2097   7.9591  50.1795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1913 T22:   0.2183                                     
REMARK   3      T33:   0.2020 T12:   0.0925                                     
REMARK   3      T13:  -0.0054 T23:   0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0564 L22:   0.1062                                     
REMARK   3      L33:   0.4642 L12:   0.0720                                     
REMARK   3      L13:  -0.1928 L23:  -0.0675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:   0.0984 S13:   0.0072                       
REMARK   3      S21:   0.0505 S22:  -0.0176 S23:  -0.0306                       
REMARK   3      S31:   0.0637 S32:  -0.0611 S33:   0.0002                       
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 6IIQ 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_1300009272.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-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   : 31501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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   (%): 31.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78                     
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: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       28.71300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       16.77800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       28.71300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       16.77800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G                   
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     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465      DA D    16                                                      
REMARK 465      DT D    17                                                      
REMARK 465      DA D    18                                                      
REMARK 465      DT D    19                                                      
REMARK 465      DA D    20                                                      
REMARK 465      DT D    21                                                      
REMARK 465      DA D    22                                                      
REMARK 465      DT D    23                                                      
REMARK 465      DA D    24                                                      
REMARK 465      DT D    25                                                      
REMARK 465      DA D    26                                                      
REMARK 465      DT E    10                                                      
REMARK 465      DT E    16                                                      
REMARK 465      DA E    17                                                      
REMARK 465      DT E    18                                                      
REMARK 465      DA E    19                                                      
REMARK 465      DT E    20                                                      
REMARK 465      DA E    21                                                      
REMARK 465      DT E    22                                                      
REMARK 465      DA E    23                                                      
REMARK 465      DT E    24                                                      
REMARK 465      DA E    25                                                      
REMARK 465      DT F    11                                                      
REMARK 465      DA F    12                                                      
REMARK 465      DT F    13                                                      
REMARK 465      DA F    14                                                      
REMARK 465      DT F    15                                                      
REMARK 465      DA F    16                                                      
REMARK 465      DT G    11                                                      
REMARK 465      DA G    12                                                      
REMARK 465      DT G    13                                                      
REMARK 465      DA G    14                                                      
REMARK 465      DT G    15                                                      
REMARK 465      DA G    16                                                      
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   O    HOH F   104     O    HOH F   118              2.15            
REMARK 500   OP2   DA G     6     O    HOH G   101              2.16            
REMARK 500   OE2  GLU A    31     OG1  THR A    97              2.18            
REMARK 500   N7    DA F     8     O    HOH F   101              2.19            
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     DT D  15   O3'    DT D  15   C3'    -0.056                       
REMARK 500     DA E  13   O3'    DA E  13   C3'    -0.038                       
REMARK 500     DA F  10   O3'    DA F  10   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     DA E  13   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT E  14   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DA F   2   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DT F   7   O4' -  C1' -  N1  ANGL. DEV. =   2.6 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       56.46   -144.90                                   
REMARK 500    LYS A  95       15.59     58.56                                   
REMARK 500    ASN B  91       55.17   -146.26                                   
REMARK 500    ASN C  91       55.77   -147.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLA A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLA B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLA C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS C 102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6IIP   RELATED DB: PDB                                   
REMARK 900 APO-FORM HRP3 PWWP                                                   
REMARK 900 RELATED ID: 6IIR   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH A BOUND GC-RICH DNA COMPLEX                           
REMARK 900 RELATED ID: 6IIS   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH BOTH A BOUND DNA AND AN H3K36ME3 PEPTIDE              
REMARK 900 RELATED ID: 6IIT   RELATED DB: PDB                                   
REMARK 900 HRP3 PWWP WITH BOTH A BOUND DNA AND AN H3K36ME2 PEPTIDE              
DBREF  6IIQ A    1    99  UNP    Q9Y3E1   HDGR3_HUMAN      1     99             
DBREF  6IIQ B    1    99  UNP    Q9Y3E1   HDGR3_HUMAN      1     99             
DBREF  6IIQ C    1    99  UNP    Q9Y3E1   HDGR3_HUMAN      1     99             
DBREF  6IIQ D   11    26  PDB    6IIQ     6IIQ            11     26             
DBREF  6IIQ E   10    25  PDB    6IIQ     6IIQ            10     25             
DBREF  6IIQ F    1    16  PDB    6IIQ     6IIQ             1     16             
DBREF  6IIQ G    1    16  PDB    6IIQ     6IIQ             1     16             
SEQADV 6IIQ SER A    0  UNP  Q9Y3E1              EXPRESSION TAG                 
SEQADV 6IIQ SER B    0  UNP  Q9Y3E1              EXPRESSION TAG                 
SEQADV 6IIQ SER C    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  100  SER MET ALA ARG PRO ARG PRO ARG GLU TYR LYS ALA GLY          
SEQRES   2 C  100  ASP LEU VAL PHE ALA LYS MET LYS GLY TYR PRO HIS TRP          
SEQRES   3 C  100  PRO ALA ARG ILE ASP GLU LEU PRO GLU GLY ALA VAL LYS          
SEQRES   4 C  100  PRO PRO ALA ASN LYS TYR PRO ILE PHE PHE PHE GLY THR          
SEQRES   5 C  100  HIS GLU THR ALA PHE LEU GLY PRO LYS ASP LEU PHE PRO          
SEQRES   6 C  100  TYR LYS GLU TYR LYS ASP LYS PHE GLY LYS SER ASN LYS          
SEQRES   7 C  100  ARG LYS GLY PHE ASN GLU GLY LEU TRP GLU ILE GLU ASN          
SEQRES   8 C  100  ASN PRO GLY VAL LYS PHE THR GLY TYR                          
SEQRES   1 D   16   DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT          
SEQRES   2 D   16   DA  DT  DA                                                  
SEQRES   1 E   16   DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT          
SEQRES   2 E   16   DA  DT  DA                                                  
SEQRES   1 F   16   DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT          
SEQRES   2 F   16   DA  DT  DA                                                  
SEQRES   1 G   16   DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT  DA  DT          
SEQRES   2 G   16   DA  DT  DA                                                  
HET    MLA  A 101       7                                                       
HET    TRS  A 102       8                                                       
HET    MLA  B 101       7                                                       
HET    TRS  B 102       8                                                       
HET    MLA  C 101       7                                                       
HET    TRS  C 102       8                                                       
HETNAM     MLA MALONIC ACID                                                     
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;                        
HETSYN   2 MLA  METHANEDICARBOXYLIC ACID                                        
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   8  MLA    3(C3 H4 O4)                                                  
FORMUL   9  TRS    3(C4 H12 N O3 1+)                                            
FORMUL  14  HOH   *186(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    
HELIX    7 AA7 GLY C   58  LYS C   60  5                                   3    
HELIX    8 AA8 TYR C   65  GLY C   73  1                                   9    
HELIX    9 AA9 GLY C   80  ASN C   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  VAL A  15   O  ALA A  27           
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           
SHEET    1 AA3 5 THR C  54  LEU C  57  0                                        
SHEET    2 AA3 5 TYR C  44  PHE C  48 -1  N  ILE C  46   O  ALA C  55           
SHEET    3 AA3 5 TRP C  25  ILE C  29 -1  N  ARG C  28   O  PHE C  47           
SHEET    4 AA3 5 LEU C  14  ALA C  17 -1  N  VAL C  15   O  ALA C  27           
SHEET    5 AA3 5 LEU C  62  PRO C  64 -1  O  PHE C  63   N  PHE C  16           
SITE     1 AC1  6 MET A  19  TYR A  22  TRP A  25  PHE A  48                    
SITE     2 AC1  6 THR A  51  GLU A  53                                          
SITE     1 AC2  5 ARG A   5  PRO A   6  PRO A  59  LYS A  60                    
SITE     2 AC2  5 HOH A 221                                                     
SITE     1 AC3  6 MET B  19  TYR B  22  TRP B  25  PHE B  48                    
SITE     2 AC3  6 THR B  51  GLU B  53                                          
SITE     1 AC4  4 ARG B   5  PRO B   6  ARG B   7  LYS B  60                    
SITE     1 AC5  6 MET C  19  TYR C  22  TRP C  25  PHE C  48                    
SITE     2 AC5  6 THR C  51  GLU C  53                                          
SITE     1 AC6  4 ARG C   5  PRO C   6  ARG C   7  PRO C  59                    
CRYST1   57.426   33.556  201.151  90.00  90.06  90.00 C 1 2 1      16          
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      0.017414  0.000000  0.000019        0.00000                         
SCALE2      0.000000  0.029801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004971        0.00000                         
ATOM      1  N   MET A   1      -4.611 -19.585  91.000  1.00 52.29           N  
ANISOU    1  N   MET A   1     8337   5490   6040   -216    -36   -422       N  
ATOM      2  CA  MET A   1      -4.853 -19.352  89.576  1.00 61.78           C  
ANISOU    2  CA  MET A   1     9529   6713   7232   -220    -29   -440       C  
ATOM      3  C   MET A   1      -4.846 -17.858  89.250  1.00 61.06           C  
ANISOU    3  C   MET A   1     9403   6631   7166   -204    -41   -434       C  
ATOM      4  O   MET A   1      -5.626 -17.095  89.819  1.00 67.72           O  
ANISOU    4  O   MET A   1    10228   7485   8019   -226    -37   -432       O  
ATOM      5  CB  MET A   1      -6.182 -19.977  89.152  1.00 60.58           C  
ANISOU    5  CB  MET A   1     9383   6589   7045   -275     -2   -468       C  
ATOM      6  CG  MET A   1      -6.442 -19.885  87.670  1.00 60.71           C  
ANISOU    6  CG  MET A   1     9391   6633   7042   -284      6   -490       C  
ATOM      7  SD  MET A   1      -7.928 -20.771  87.172  1.00 71.34           S  
ANISOU    7  SD  MET A   1    10745   8019   8342   -354     38   -524       S  
ATOM      8  CE  MET A   1      -7.447 -22.477  87.442  1.00 51.48           C  
ANISOU    8  CE  MET A   1     8276   5476   5807   -354     50   -522       C  
ATOM      9  N   ALA A   2      -3.980 -17.449  88.324  1.00 53.72           N  
ANISOU    9  N   ALA A   2     8466   5697   6248   -165    -55   -429       N  
ATOM     10  CA  ALA A   2      -3.767 -16.028  88.054  1.00 45.61           C  
ANISOU   10  CA  ALA A   2     7408   4672   5248   -141    -68   -418       C  
ATOM     11  C   ALA A   2      -3.816 -15.657  86.567  1.00 47.10           C  
ANISOU   11  C   ALA A   2     7588   4880   5427   -132    -66   -434       C  
ATOM     12  O   ALA A   2      -3.169 -16.297  85.730  1.00 40.01           O  
ANISOU   12  O   ALA A   2     6699   3984   4520   -110    -68   -438       O  
ATOM     13  CB  ALA A   2      -2.447 -15.604  88.637  1.00 44.20           C  
ANISOU   13  CB  ALA A   2     7224   4466   5102    -94    -94   -387       C  
ATOM     14  N   ARG A   3      -4.569 -14.611  86.235  1.00 45.14           N  
ANISOU   14  N   ARG A   3     7271   4686   5192   -140    -58   -422       N  
ATOM     15  CA  ARG A   3      -4.656 -14.160  84.843  1.00 41.83           C  
ANISOU   15  CA  ARG A   3     6780   4335   4777   -124    -53   -411       C  
ATOM     16  C   ARG A   3      -3.359 -13.608  84.326  1.00 32.75           C  
ANISOU   16  C   ARG A   3     5597   3186   3661    -66    -73   -382       C  
ATOM     17  O   ARG A   3      -2.887 -12.594  84.819  1.00 41.85           O  
ANISOU   17  O   ARG A   3     6724   4331   4848    -39    -86   -355       O  
ATOM     18  CB  ARG A   3      -5.721 -13.072  84.662  1.00 50.21           C  
ANISOU   18  CB  ARG A   3     7774   5456   5848   -140    -39   -398       C  
ATOM     19  CG  ARG A   3      -6.944 -13.555  83.900  1.00 56.05           C  
ANISOU   19  CG  ARG A   3     8496   6252   6550   -186    -16   -422       C  
ATOM     20  CD  ARG A   3      -6.666 -13.628  82.389  1.00 66.52           C  
ANISOU   20  CD  ARG A   3     9774   7631   7870   -167    -15   -417       C  
ATOM     21  NE  ARG A   3      -6.806 -12.392  81.627  1.00 76.68           N  
ANISOU   21  NE  ARG A   3    10974   8981   9182   -139    -15   -387       N  
ATOM     22  CZ  ARG A   3      -6.254 -12.183  80.427  1.00 84.21           C  
ANISOU   22  CZ  ARG A   3    11882   9971  10143   -108    -20   -374       C  
ATOM     23  NH1 ARG A   3      -5.511 -13.122  79.843  1.00 84.48           N  
ANISOU   23  NH1 ARG A   3    11948   9986  10163    -99    -25   -388       N  
ATOM     24  NH2 ARG A   3      -6.440 -11.026  79.800  1.00 85.84           N  
ANISOU   24  NH2 ARG A   3    12012  10233  10371    -84    -18   -346       N  
ATOM     25  N   PRO A   4      -2.797 -14.231  83.283  1.00 29.62           N  
ANISOU   25  N   PRO A   4     5197   2803   3253    -47    -74   -387       N  
ATOM     26  CA  PRO A   4      -1.540 -13.662  82.793  1.00 35.69           C  
ANISOU   26  CA  PRO A   4     5930   3575   4054      9    -93   -358       C  
ATOM     27  C   PRO A   4      -1.771 -12.300  82.143  1.00 39.98           C  
ANISOU   27  C   PRO A   4     6387   4178   4624     26    -92   -332       C  
ATOM     28  O   PRO A   4      -2.868 -12.033  81.649  1.00 38.91           O  
ANISOU   28  O   PRO A   4     6216   4094   4476     -2    -74   -338       O  
ATOM     29  CB  PRO A   4      -1.072 -14.691  81.778  1.00 34.52           C  
ANISOU   29  CB  PRO A   4     5801   3431   3884     19    -89   -372       C  
ATOM     30  CG  PRO A   4      -2.334 -15.352  81.331  1.00 37.65           C  
ANISOU   30  CG  PRO A   4     6208   3857   4240    -34    -64   -403       C  
ATOM     31  CD  PRO A   4      -3.234 -15.401  82.501  1.00 31.43           C  
ANISOU   31  CD  PRO A   4     5455   3046   3441    -76    -57   -417       C  
ATOM     32  N   ARG A   5      -0.764 -11.439  82.185  1.00 36.54           N  
ANISOU   32  N   ARG A   5     5921   3737   4225     70   -110   -302       N  
ATOM     33  CA  ARG A   5      -0.820 -10.185  81.442  1.00 37.29           C  
ANISOU   33  CA  ARG A   5     5938   3887   4345     92   -108   -276       C  
ATOM     34  C   ARG A   5      -0.545 -10.481  79.966  1.00 32.73           C  
ANISOU   34  C   ARG A   5     5324   3352   3758    110   -105   -277       C  
ATOM     35  O   ARG A   5       0.016 -11.527  79.649  1.00 40.78           O  
ANISOU   35  O   ARG A   5     6382   4351   4762    116   -109   -292       O  
ATOM     36  CB  ARG A   5       0.185  -9.180  82.016  1.00 34.44           C  
ANISOU   36  CB  ARG A   5     5561   3503   4022    129   -127   -245       C  
ATOM     37  CG  ARG A   5      -0.234  -8.593  83.367  1.00 35.34           C  
ANISOU   37  CG  ARG A   5     5697   3585   4146    109   -126   -240       C  
ATOM     38  CD  ARG A   5       0.807  -7.611  83.900  1.00 35.54           C  
ANISOU   38  CD  ARG A   5     5708   3589   4205    141   -144   -211       C  
ATOM     39  NE  ARG A   5       1.934  -8.286  84.546  1.00 38.30           N  
ANISOU   39  NE  ARG A   5     6109   3888   4557    157   -167   -212       N  
ATOM     40  CZ  ARG A   5       3.211  -8.150  84.186  1.00 40.35           C  
ANISOU   40  CZ  ARG A   5     6353   4146   4834    197   -186   -194       C  
ATOM     41  NH1 ARG A   5       3.550  -7.366  83.182  1.00 35.62           N  
ANISOU   41  NH1 ARG A   5     5691   3590   4251    224   -185   -175       N  
ATOM     42  NH2 ARG A   5       4.161  -8.805  84.835  1.00 41.67           N  
ANISOU   42  NH2 ARG A   5     6565   4268   4999    211   -205   -194       N  
ATOM     43  N   PRO A   6      -0.947  -9.575  79.059  1.00 32.68           N  
ANISOU   43  N   PRO A   6     5248   3407   3763    119    -97   -261       N  
ATOM     44  CA  PRO A   6      -0.757  -9.831  77.625  1.00 35.14           C  
ANISOU   44  CA  PRO A   6     5524   3764   4065    133    -93   -262       C  
ATOM     45  C   PRO A   6       0.705 -10.069  77.237  1.00 32.56           C  
ANISOU   45  C   PRO A   6     5204   3413   3755    178   -111   -252       C  
ATOM     46  O   PRO A   6       1.604  -9.542  77.889  1.00 29.61           O  
ANISOU   46  O   PRO A   6     4834   3007   3409    207   -128   -232       O  
ATOM     47  CB  PRO A   6      -1.277  -8.551  76.977  1.00 30.22           C  
ANISOU   47  CB  PRO A   6     4823   3202   3459    144    -84   -238       C  
ATOM     48  CG  PRO A   6      -2.291  -8.036  77.923  1.00 33.04           C  
ANISOU   48  CG  PRO A   6     5182   3557   3815    116    -73   -238       C  
ATOM     49  CD  PRO A   6      -1.760  -8.371  79.296  1.00 31.80           C  
ANISOU   49  CD  PRO A   6     5090   3328   3666    112    -86   -243       C  
ATOM     50  N   ARG A   7       0.937 -10.859  76.194  1.00 29.15           N  
ANISOU   50  N   ARG A   7     4774   2997   3304    182   -106   -264       N  
ATOM     51  CA  ARG A   7       2.287 -11.043  75.666  1.00 34.86           C  
ANISOU   51  CA  ARG A   7     5496   3706   4042    228   -121   -253       C  
ATOM     52  C   ARG A   7       2.471 -10.240  74.377  1.00 34.06           C  
ANISOU   52  C   ARG A   7     5321   3663   3956    253   -119   -234       C  
ATOM     53  O   ARG A   7       3.558 -10.204  73.802  1.00 39.41           O  
ANISOU   53  O   ARG A   7     5984   4339   4649    292   -130   -221       O  
ATOM     54  CB  ARG A   7       2.566 -12.525  75.426  1.00 39.28           C  
ANISOU   54  CB  ARG A   7     6117   4236   4571    220   -115   -278       C  
ATOM     55  CG  ARG A   7       2.197 -13.375  76.639  1.00 50.76           C  
ANISOU   55  CG  ARG A   7     7647   5636   6005    189   -113   -300       C  
ATOM     56  CD  ARG A   7       2.736 -14.784  76.531  1.00 54.84           C  
ANISOU   56  CD  ARG A   7     8232   6111   6495    193   -108   -320       C  
ATOM     57  NE  ARG A   7       4.187 -14.818  76.660  1.00 59.99           N  
ANISOU   57  NE  ARG A   7     8892   6731   7169    247   -127   -300       N  
ATOM     58  CZ  ARG A   7       4.842 -15.348  77.689  1.00 54.47           C  
ANISOU   58  CZ  ARG A   7     8251   5974   6472    261   -138   -300       C  
ATOM     59  NH1 ARG A   7       4.182 -15.900  78.697  1.00 45.43           N  
ANISOU   59  NH1 ARG A   7     7164   4792   5307    225   -132   -319       N  
ATOM     60  NH2 ARG A   7       6.167 -15.325  77.708  1.00 55.05           N  
ANISOU   60  NH2 ARG A   7     8323   6028   6565    312   -156   -278       N  
ATOM     61  N   GLU A   8       1.391  -9.605  73.935  1.00 31.70           N  
ANISOU   61  N   GLU A   8     4975   3417   3651    231   -105   -232       N  
ATOM     62  CA  GLU A   8       1.415  -8.748  72.743  1.00 29.16           C  
ANISOU   62  CA  GLU A   8     4582   3156   3343    253   -101   -212       C  
ATOM     63  C   GLU A   8       0.515  -7.549  72.937  1.00 36.81           C  
ANISOU   63  C   GLU A   8     5501   4161   4323    245    -92   -195       C  
ATOM     64  O   GLU A   8      -0.556  -7.661  73.542  1.00 37.83           O  
ANISOU   64  O   GLU A   8     5645   4293   4435    208    -80   -207       O  
ATOM     65  CB  GLU A   8       0.955  -9.521  71.502  1.00 32.89           C  
ANISOU   65  CB  GLU A   8     5045   3669   3783    235    -87   -231       C  
ATOM     66  CG  GLU A   8       1.815 -10.707  71.161  1.00 45.89           C  
ANISOU   66  CG  GLU A   8     6740   5281   5416    245    -91   -248       C  
ATOM     67  CD  GLU A   8       1.227 -11.518  70.042  1.00 63.83           C  
ANISOU   67  CD  GLU A   8     9012   7591   7651    217    -74   -270       C  
ATOM     68  OE1 GLU A   8       0.009 -11.375  69.801  1.00 69.08           O  
ANISOU   68  OE1 GLU A   8     9652   8301   8294    179    -60   -278       O  
ATOM     69  OE2 GLU A   8       1.977 -12.292  69.410  1.00 74.92           O  
ANISOU   69  OE2 GLU A   8    10440   8980   9046    233    -74   -278       O  
ATOM     70  N   TYR A   9       0.928  -6.404  72.403  1.00 37.65           N  
ANISOU   70  N   TYR A   9     5551   4297   4457    280    -94   -167       N  
ATOM     71  CA  TYR A   9       0.118  -5.203  72.517  1.00 27.74           C  
ANISOU   71  CA  TYR A   9     4250   3077   3213    278    -82   -147       C  
ATOM     72  C   TYR A   9      -0.129  -4.613  71.152  1.00 27.15           C  
ANISOU   72  C   TYR A   9     4108   3069   3137    294    -72   -132       C  
ATOM     73  O   TYR A   9       0.562  -4.955  70.197  1.00 27.75           O  
ANISOU   73  O   TYR A   9     4173   3158   3213    313    -79   -134       O  
ATOM     74  CB  TYR A   9       0.783  -4.162  73.416  1.00 30.23           C  
ANISOU   74  CB  TYR A   9     4565   3358   3564    303    -91   -122       C  
ATOM     75  CG  TYR A   9       0.649  -4.501  74.885  1.00 35.52           C  
ANISOU   75  CG  TYR A   9     5293   3972   4232    280    -96   -133       C  
ATOM     76  CD1 TYR A   9      -0.481  -4.125  75.607  1.00 30.12           C  
ANISOU   76  CD1 TYR A   9     4612   3293   3542    252    -81   -134       C  
ATOM     77  CD2 TYR A   9       1.645  -5.216  75.542  1.00 35.31           C  
ANISOU   77  CD2 TYR A   9     5319   3888   4210    286   -115   -142       C  
ATOM     78  CE1 TYR A   9      -0.605  -4.446  76.958  1.00 34.21           C  
ANISOU   78  CE1 TYR A   9     5185   3757   4057    229    -85   -145       C  
ATOM     79  CE2 TYR A   9       1.528  -5.540  76.890  1.00 34.18           C  
ANISOU   79  CE2 TYR A   9     5230   3694   4064    265   -120   -152       C  
ATOM     80  CZ  TYR A   9       0.406  -5.156  77.588  1.00 33.02           C  
ANISOU   80  CZ  TYR A   9     5086   3550   3910    235   -105   -154       C  
ATOM     81  OH  TYR A   9       0.287  -5.476  78.927  1.00 34.32           O  
ANISOU   81  OH  TYR A   9     5306   3662   4072    213   -109   -164       O  
ATOM     82  N   LYS A  10      -1.119  -3.732  71.087  1.00 34.01           N  
ANISOU   82  N   LYS A  10     4934   3981   4005    288    -56   -118       N  
ATOM     83  CA  LYS A  10      -1.479  -3.042  69.859  1.00 36.87           C  
ANISOU   83  CA  LYS A  10     5230   4411   4367    305    -45   -100       C  
ATOM     84  C   LYS A  10      -1.432  -1.530  70.071  1.00 32.48           C  
ANISOU   84  C   LYS A  10     4635   3864   3841    336    -37    -66       C  
ATOM     85  O   LYS A  10      -1.690  -1.034  71.174  1.00 28.89           O  
ANISOU   85  O   LYS A  10     4200   3379   3397    330    -33    -59       O  
ATOM     86  CB  LYS A  10      -2.864  -3.487  69.393  1.00 42.79           C  
ANISOU   86  CB  LYS A  10     5961   5218   5080    267    -28   -114       C  
ATOM     87  CG  LYS A  10      -2.827  -4.683  68.454  1.00 55.50           C  
ANISOU   87  CG  LYS A  10     7582   6847   6659    246    -30   -140       C  
ATOM     88  CD  LYS A  10      -3.990  -5.632  68.687  1.00 67.15           C  
ANISOU   88  CD  LYS A  10     9082   8339   8093    191    -19   -168       C  
ATOM     89  CE  LYS A  10      -3.776  -6.470  69.941  1.00 75.72           C  
ANISOU   89  CE  LYS A  10    10243   9352   9175    168    -26   -192       C  
ATOM     90  NZ  LYS A  10      -4.688  -7.653  69.990  1.00 78.39           N  
ANISOU   90  NZ  LYS A  10    10616   9700   9468    112    -16   -225       N  
ATOM     91  N   ALA A  11      -1.063  -0.817  69.013  1.00 28.86           N  
ANISOU   91  N   ALA A  11     4127   3445   3395    369    -35    -45       N  
ATOM     92  CA  ALA A  11      -1.046   0.631  69.016  1.00 33.23           C  
ANISOU   92  CA  ALA A  11     4641   4012   3972    400    -24    -12       C  
ATOM     93  C   ALA A  11      -2.349   1.131  69.555  1.00 28.75           C  
ANISOU   93  C   ALA A  11     4061   3468   3394    382     -2     -4       C  
ATOM     94  O   ALA A  11      -3.404   0.702  69.111  1.00 32.89           O  
ANISOU   94  O   ALA A  11     4566   4040   3890    359      9    -14       O  
ATOM     95  CB  ALA A  11      -0.815   1.177  67.605  1.00 35.46           C  
ANISOU   95  CB  ALA A  11     4866   4349   4259    430    -19      6       C  
ATOM     96  N   GLY A  12      -2.276   2.037  70.518  1.00 28.18           N  
ANISOU   96  N   GLY A  12     4002   3362   3344    393      5     14       N  
ATOM     97  CA  GLY A  12      -3.475   2.598  71.093  1.00 26.87           C  
ANISOU   97  CA  GLY A  12     3826   3214   3171    381     28     24       C  
ATOM     98  C   GLY A  12      -3.780   2.062  72.468  1.00 30.87           C  
ANISOU   98  C   GLY A  12     4388   3668   3672    347     25      5       C  
ATOM     99  O   GLY A  12      -4.499   2.705  73.207  1.00 30.03           O  
ANISOU   99  O   GLY A  12     4284   3558   3568    343     43     18       O  
ATOM    100  N   ASP A  13      -3.229   0.899  72.818  1.00 30.58           N  
ANISOU  100  N   ASP A  13     4399   3591   3628    326      3    -23       N  
ATOM    101  CA  ASP A  13      -3.525   0.274  74.119  1.00 27.49           C  
ANISOU  101  CA  ASP A  13     4066   3150   3229    292      0    -43       C  
ATOM    102  C   ASP A  13      -3.054   1.191  75.250  1.00 25.87           C  
ANISOU  102  C   ASP A  13     3885   2891   3052    304      1    -25       C  
ATOM    103  O   ASP A  13      -1.967   1.771  75.172  1.00 29.10           O  
ANISOU  103  O   ASP A  13     4292   3280   3487    333     -9    -10       O  
ATOM    104  CB  ASP A  13      -2.845  -1.108  74.259  1.00 28.61           C  
ANISOU  104  CB  ASP A  13     4258   3253   3360    273    -23    -74       C  
ATOM    105  CG  ASP A  13      -3.584  -2.233  73.519  1.00 40.92           C  
ANISOU  105  CG  ASP A  13     5814   4852   4882    242    -20   -100       C  
ATOM    106  OD1 ASP A  13      -4.787  -2.085  73.205  1.00 37.78           O  
ANISOU  106  OD1 ASP A  13     5384   4507   4464    224     -1    -99       O  
ATOM    107  OD2 ASP A  13      -2.949  -3.287  73.271  1.00 35.39           O  
ANISOU  107  OD2 ASP A  13     5146   4129   4171    235    -35   -122       O  
ATOM    108  N   LEU A  14      -3.861   1.301  76.300  1.00 25.75           N  
ANISOU  108  N   LEU A  14     3896   2858   3032    280     14    -28       N  
ATOM    109  CA  LEU A  14      -3.477   2.083  77.471  1.00 28.31           C  
ANISOU  109  CA  LEU A  14     4250   3127   3378    285     16    -15       C  
ATOM    110  C   LEU A  14      -2.972   1.163  78.584  1.00 29.80           C  
ANISOU  110  C   LEU A  14     4507   3251   3566    259     -5    -39       C  
ATOM    111  O   LEU A  14      -3.576   0.121  78.875  1.00 22.85           O  
ANISOU  111  O   LEU A  14     3654   2366   2662    226     -7    -65       O  
ATOM    112  CB  LEU A  14      -4.652   2.929  77.957  1.00 29.62           C  
ANISOU  112  CB  LEU A  14     4402   3311   3543    280     47      2       C  
ATOM    113  CG  LEU A  14      -5.193   3.953  76.952  1.00 28.59           C  
ANISOU  113  CG  LEU A  14     4206   3244   3414    311     71     30       C  
ATOM    114  CD1 LEU A  14      -6.365   4.695  77.544  1.00 31.04           C  
ANISOU  114  CD1 LEU A  14     4507   3566   3719    306    103     46       C  
ATOM    115  CD2 LEU A  14      -4.090   4.936  76.551  1.00 26.27           C  
ANISOU  115  CD2 LEU A  14     3896   2939   3147    350     68     55       C  
ATOM    116  N   VAL A  15      -1.857   1.547  79.195  1.00 22.17           N  
ANISOU  116  N   VAL A  15     3567   2236   2622    272    -20    -29       N  
ATOM    117  CA  VAL A  15      -1.176   0.680  80.159  1.00 20.14           C  
ANISOU  117  CA  VAL A  15     3369   1918   2363    254    -43    -49       C  
ATOM    118  C   VAL A  15      -0.623   1.472  81.322  1.00 27.40           C  
ANISOU  118  C   VAL A  15     4319   2787   3304    255    -46    -34       C  
ATOM    119  O   VAL A  15      -0.665   2.698  81.323  1.00 26.75           O  
ANISOU  119  O   VAL A  15     4213   2714   3237    271    -29     -9       O  
ATOM    120  CB  VAL A  15       0.002  -0.072  79.534  1.00 26.13           C  
ANISOU  120  CB  VAL A  15     4133   2672   3125    272    -70    -57       C  
ATOM    121  CG1 VAL A  15      -0.478  -1.088  78.492  1.00 26.61           C  
ANISOU  121  CG1 VAL A  15     4178   2773   3160    264    -69    -78       C  
ATOM    122  CG2 VAL A  15       1.020   0.917  78.935  1.00 26.68           C  
ANISOU  122  CG2 VAL A  15     4165   2753   3219    310    -75    -31       C  
ATOM    123  N   PHE A  16      -0.112   0.747  82.311  1.00 22.66           N  
ANISOU  123  N   PHE A  16     3775   2135   2701    237    -66    -50       N  
ATOM    124  CA  PHE A  16       0.916   1.279  83.185  1.00 28.64           C  
ANISOU  124  CA  PHE A  16     4559   2845   3477    242    -80    -37       C  
ATOM    125  C   PHE A  16       2.231   0.668  82.723  1.00 22.09           C  
ANISOU  125  C   PHE A  16     3731   2009   2652    263   -109    -40       C  
ATOM    126  O   PHE A  16       2.284  -0.516  82.430  1.00 28.21           O  
ANISOU  126  O   PHE A  16     4523   2785   3412    259   -122    -61       O  
ATOM    127  CB  PHE A  16       0.647   0.948  84.658  1.00 28.02           C  
ANISOU  127  CB  PHE A  16     4541   2712   3393    209    -83    -49       C  
ATOM    128  CG  PHE A  16      -0.505   1.714  85.253  1.00 26.74           C  
ANISOU  128  CG  PHE A  16     4380   2550   3230    191    -53    -42       C  
ATOM    129  CD1 PHE A  16      -0.309   2.959  85.830  1.00 26.82           C  
ANISOU  129  CD1 PHE A  16     4391   2541   3257    196    -40    -19       C  
ATOM    130  CD2 PHE A  16      -1.777   1.183  85.241  1.00 30.89           C  
ANISOU  130  CD2 PHE A  16     4907   3094   3735    168    -36    -59       C  
ATOM    131  CE1 PHE A  16      -1.364   3.655  86.382  1.00 30.85           C  
ANISOU  131  CE1 PHE A  16     4905   3049   3766    181     -9    -11       C  
ATOM    132  CE2 PHE A  16      -2.832   1.880  85.792  1.00 29.13           C  
ANISOU  132  CE2 PHE A  16     4684   2873   3511    154     -7    -51       C  
ATOM    133  CZ  PHE A  16      -2.621   3.112  86.360  1.00 25.61           C  
ANISOU  133  CZ  PHE A  16     4240   2406   3084    162      7    -27       C  
ATOM    134  N   ALA A  17       3.270   1.483  82.614  1.00 24.06           N  
ANISOU  134  N   ALA A  17     3963   2256   2922    286   -118    -18       N  
ATOM    135  CA  ALA A  17       4.567   0.977  82.180  1.00 23.86           C  
ANISOU  135  CA  ALA A  17     3935   2229   2902    309   -146    -18       C  
ATOM    136  C   ALA A  17       5.580   1.156  83.302  1.00 26.60           C  
ANISOU  136  C   ALA A  17     4318   2529   3258    304   -166    -10       C  
ATOM    137  O   ALA A  17       5.606   2.209  83.956  1.00 24.75           O  
ANISOU  137  O   ALA A  17     4087   2280   3036    295   -157      6       O  
ATOM    138  CB  ALA A  17       5.024   1.696  80.920  1.00 29.94           C  
ANISOU  138  CB  ALA A  17     4647   3044   3686    342   -141      0       C  
ATOM    139  N   LYS A  18       6.397   0.130  83.521  1.00 25.23           N  
ANISOU  139  N   LYS A  18     4173   2335   3079    309   -193    -21       N  
ATOM    140  CA  LYS A  18       7.343   0.132  84.628  1.00 26.71           C  
ANISOU  140  CA  LYS A  18     4397   2481   3271    303   -215    -15       C  
ATOM    141  C   LYS A  18       8.776   0.285  84.163  1.00 24.34           C  
ANISOU  141  C   LYS A  18     4072   2194   2983    333   -237      1       C  
ATOM    142  O   LYS A  18       9.269  -0.523  83.383  1.00 31.70           O  
ANISOU  142  O   LYS A  18     4993   3142   3910    357   -249     -5       O  
ATOM    143  CB  LYS A  18       7.226  -1.160  85.443  1.00 24.97           C  
ANISOU  143  CB  LYS A  18     4233   2222   3032    286   -229    -36       C  
ATOM    144  CG  LYS A  18       8.151  -1.165  86.662  1.00 31.56           C  
ANISOU  144  CG  LYS A  18     5106   3015   3869    279   -253    -28       C  
ATOM    145  CD  LYS A  18       7.735  -0.090  87.627  1.00 29.75           C  
ANISOU  145  CD  LYS A  18     4890   2766   3648    251   -240    -18       C  
ATOM    146  CE  LYS A  18       8.512  -0.177  88.944  1.00 35.51           C  
ANISOU  146  CE  LYS A  18     5663   3453   4376    236   -262    -13       C  
ATOM    147  NZ  LYS A  18       9.959   0.072  88.727  1.00 36.04           N  
ANISOU  147  NZ  LYS A  18     5708   3534   4452    260   -287      6       N  
ATOM    148  N   MET A  19       9.441   1.330  84.643  1.00 24.23           N  
ANISOU  148  N   MET A  19     4050   2173   2983    331   -241     22       N  
ATOM    149  CA  MET A  19      10.860   1.514  84.403  1.00 23.94           C  
ANISOU  149  CA  MET A  19     3994   2148   2956    354   -265     38       C  
ATOM    150  C   MET A  19      11.541   1.577  85.752  1.00 35.64           C  
ANISOU  150  C   MET A  19     5514   3592   4435    335   -284     44       C  
ATOM    151  O   MET A  19      10.960   2.087  86.709  1.00 31.71           O  
ANISOU  151  O   MET A  19     5045   3068   3937    304   -273     44       O  
ATOM    152  CB  MET A  19      11.120   2.769  83.601  1.00 27.05           C  
ANISOU  152  CB  MET A  19     4337   2576   3366    368   -251     57       C  
ATOM    153  CG  MET A  19      10.312   2.800  82.315  1.00 41.12           C  
ANISOU  153  CG  MET A  19     6080   4396   5148    384   -229     53       C  
ATOM    154  SD  MET A  19      11.283   3.346  80.908  1.00 44.16           S  
ANISOU  154  SD  MET A  19     6404   4828   5547    422   -232     69       S  
ATOM    155  CE  MET A  19      12.552   2.092  80.886  1.00 69.52           C  
ANISOU  155  CE  MET A  19     9628   8033   8753    443   -268     64       C  
ATOM    156  N   LYS A  20      12.749   1.027  85.835  1.00 32.33           N  
ANISOU  156  N   LYS A  20     5096   3172   4014    353   -314     50       N  
ATOM    157  CA  LYS A  20      13.475   0.986  87.101  1.00 34.77           C  
ANISOU  157  CA  LYS A  20     5441   3451   4318    336   -336     57       C  
ATOM    158  C   LYS A  20      13.644   2.384  87.652  1.00 32.42           C  
ANISOU  158  C   LYS A  20     5136   3151   4030    312   -328     74       C  
ATOM    159  O   LYS A  20      14.001   3.301  86.919  1.00 30.79           O  
ANISOU  159  O   LYS A  20     4888   2975   3836    323   -319     89       O  
ATOM    160  CB  LYS A  20      14.841   0.320  86.928  1.00 37.16           C  
ANISOU  160  CB  LYS A  20     5734   3766   4619    366   -368     66       C  
ATOM    161  CG  LYS A  20      15.673   0.293  88.208  1.00 41.45           C  
ANISOU  161  CG  LYS A  20     6308   4285   5155    351   -393     77       C  
ATOM    162  CD  LYS A  20      16.935  -0.547  88.022  1.00 48.95           C  
ANISOU  162  CD  LYS A  20     7250   5250   6100    385   -424     86       C  
ATOM    163  CE  LYS A  20      17.940  -0.321  89.140  1.00 57.72           C  
ANISOU  163  CE  LYS A  20     8375   6352   7204    372   -451    103       C  
ATOM    164  NZ  LYS A  20      19.183  -1.107  88.887  1.00 63.19           N  
ANISOU  164  NZ  LYS A  20     9053   7065   7891    411   -479    115       N  
ATOM    165  N   GLY A  21      13.351   2.547  88.939  1.00 32.43           N  
ANISOU  165  N   GLY A  21     5183   3115   4025    277   -328     72       N  
ATOM    166  CA  GLY A  21      13.445   3.844  89.586  1.00 30.29           C  
ANISOU  166  CA  GLY A  21     4915   2834   3759    248   -317     87       C  
ATOM    167  C   GLY A  21      12.193   4.701  89.542  1.00 34.94           C  
ANISOU  167  C   GLY A  21     5507   3416   4354    230   -278     85       C  
ATOM    168  O   GLY A  21      12.188   5.802  90.090  1.00 37.53           O  
ANISOU  168  O   GLY A  21     5843   3732   4685    205   -263     97       O  
ATOM    169  N   TYR A  22      11.136   4.209  88.892  1.00 28.23           N  
ANISOU  169  N   TYR A  22     4649   2575   3503    242   -260     70       N  
ATOM    170  CA  TYR A  22       9.896   4.965  88.767  1.00 25.28           C  
ANISOU  170  CA  TYR A  22     4271   2200   3132    229   -222     69       C  
ATOM    171  C   TYR A  22       8.712   4.121  89.206  1.00 20.65           C  
ANISOU  171  C   TYR A  22     3719   1593   2535    214   -213     48       C  
ATOM    172  O   TYR A  22       8.729   2.901  89.077  1.00 24.39           O  
ANISOU  172  O   TYR A  22     4204   2063   2998    223   -230     31       O  
ATOM    173  CB  TYR A  22       9.678   5.429  87.317  1.00 24.77           C  
ANISOU  173  CB  TYR A  22     4152   2183   3078    260   -203     76       C  
ATOM    174  CG  TYR A  22      10.684   6.450  86.828  1.00 29.06           C  
ANISOU  174  CG  TYR A  22     4660   2748   3633    273   -205     98       C  
ATOM    175  CD1 TYR A  22      11.880   6.046  86.243  1.00 32.17           C  
ANISOU  175  CD1 TYR A  22     5028   3165   4029    296   -233    102       C  
ATOM    176  CD2 TYR A  22      10.429   7.808  86.926  1.00 33.53           C  
ANISOU  176  CD2 TYR A  22     5222   3313   4206    261   -175    113       C  
ATOM    177  CE1 TYR A  22      12.802   6.978  85.774  1.00 38.62           C  
ANISOU  177  CE1 TYR A  22     5813   4006   4856    306   -233    121       C  
ATOM    178  CE2 TYR A  22      11.346   8.750  86.449  1.00 35.07           C  
ANISOU  178  CE2 TYR A  22     5388   3528   4409    270   -174    132       C  
ATOM    179  CZ  TYR A  22      12.529   8.328  85.886  1.00 40.29           C  
ANISOU  179  CZ  TYR A  22     6022   4214   5073    291   -204    135       C  
ATOM    180  OH  TYR A  22      13.439   9.262  85.429  1.00 43.84           O  
ANISOU  180  OH  TYR A  22     6442   4684   5529    297   -203    153       O  
ATOM    181  N   PRO A  23       7.660   4.776  89.703  1.00 23.12           N  
ANISOU  181  N   PRO A  23     4048   1889   2848    191   -182     48       N  
ATOM    182  CA  PRO A  23       6.403   4.051  89.922  1.00 20.53           C  
ANISOU  182  CA  PRO A  23     3742   1550   2508    178   -169     27       C  
ATOM    183  C   PRO A  23       5.839   3.568  88.600  1.00 22.89           C  
ANISOU  183  C   PRO A  23     4000   1893   2805    203   -160     19       C  
ATOM    184  O   PRO A  23       6.152   4.176  87.577  1.00 24.63           O  
ANISOU  184  O   PRO A  23     4172   2150   3035    229   -153     33       O  
ATOM    185  CB  PRO A  23       5.484   5.115  90.546  1.00 24.03           C  
ANISOU  185  CB  PRO A  23     4199   1976   2954    155   -134     35       C  
ATOM    186  CG  PRO A  23       6.061   6.429  90.078  1.00 27.87           C  
ANISOU  186  CG  PRO A  23     4653   2481   3455    168   -121     60       C  
ATOM    187  CD  PRO A  23       7.555   6.204  90.041  1.00 25.06           C  
ANISOU  187  CD  PRO A  23     4293   2128   3102    178   -157     66       C  
ATOM    188  N   HIS A  24       5.038   2.511  88.619  1.00 23.47           N  
ANISOU  188  N   HIS A  24     4092   1963   2864    194   -159     -4       N  
ATOM    189  CA  HIS A  24       4.271   2.125  87.433  1.00 27.12           C  
ANISOU  189  CA  HIS A  24     4516   2467   3320    210   -145    -13       C  
ATOM    190  C   HIS A  24       3.531   3.357  86.910  1.00 28.22           C  
ANISOU  190  C   HIS A  24     4616   2637   3469    217   -111      5       C  
ATOM    191  O   HIS A  24       2.838   4.029  87.675  1.00 24.10           O  
ANISOU  191  O   HIS A  24     4113   2096   2949    197    -89     10       O  
ATOM    192  CB  HIS A  24       3.300   0.996  87.769  1.00 24.19           C  
ANISOU  192  CB  HIS A  24     4178   2083   2928    187   -142    -39       C  
ATOM    193  CG  HIS A  24       3.974  -0.258  88.214  1.00 31.59           C  
ANISOU  193  CG  HIS A  24     5158   2991   3855    183   -171    -56       C  
ATOM    194  ND1 HIS A  24       4.570  -0.384  89.458  1.00 28.34           N  
ANISOU  194  ND1 HIS A  24     4794   2531   3442    168   -189    -56       N  
ATOM    195  CD2 HIS A  24       4.170  -1.441  87.589  1.00 34.10           C  
ANISOU  195  CD2 HIS A  24     5479   3318   4159    195   -184    -73       C  
ATOM    196  CE1 HIS A  24       5.089  -1.591  89.574  1.00 29.78           C  
ANISOU  196  CE1 HIS A  24     5007   2697   3613    172   -212    -70       C  
ATOM    197  NE2 HIS A  24       4.862  -2.253  88.449  1.00 37.96           N  
ANISOU  197  NE2 HIS A  24     6018   3765   4641    189   -209    -81       N  
ATOM    198  N   TRP A  25       3.693   3.653  85.620  1.00 23.06           N  
ANISOU  198  N   TRP A  25     3910   2031   2822    246   -106     14       N  
ATOM    199  CA  TRP A  25       3.377   4.968  85.081  1.00 20.41           C  
ANISOU  199  CA  TRP A  25     3535   1722   2498    261    -78     37       C  
ATOM    200  C   TRP A  25       2.337   4.909  83.974  1.00 24.48           C  
ANISOU  200  C   TRP A  25     4007   2289   3006    275    -56     36       C  
ATOM    201  O   TRP A  25       2.472   4.099  83.062  1.00 22.98           O  
ANISOU  201  O   TRP A  25     3794   2128   2809    288    -69     24       O  
ATOM    202  CB  TRP A  25       4.655   5.617  84.532  1.00 20.30           C  
ANISOU  202  CB  TRP A  25     3494   1720   2499    286    -90     56       C  
ATOM    203  CG  TRP A  25       4.619   7.104  84.444  1.00 17.78           C  
ANISOU  203  CG  TRP A  25     3156   1408   2193    294    -63     81       C  
ATOM    204  CD1 TRP A  25       3.949   7.862  83.531  1.00 21.71           C  
ANISOU  204  CD1 TRP A  25     3611   1944   2693    315    -33     95       C  
ATOM    205  CD2 TRP A  25       5.301   8.031  85.310  1.00 21.40           C  
ANISOU  205  CD2 TRP A  25     3641   1832   2660    280    -61     96       C  
ATOM    206  NE1 TRP A  25       4.158   9.201  83.784  1.00 23.30           N  
ANISOU  206  NE1 TRP A  25     3814   2134   2905    317    -11    118       N  
ATOM    207  CE2 TRP A  25       4.984   9.323  84.867  1.00 23.65           C  
ANISOU  207  CE2 TRP A  25     3900   2133   2952    294    -27    118       C  
ATOM    208  CE3 TRP A  25       6.139   7.880  86.417  1.00 28.10           C  
ANISOU  208  CE3 TRP A  25     4531   2638   3507    257    -84     94       C  
ATOM    209  CZ2 TRP A  25       5.491  10.465  85.486  1.00 25.39           C  
ANISOU  209  CZ2 TRP A  25     4140   2327   3179    282    -14    136       C  
ATOM    210  CZ3 TRP A  25       6.650   9.011  87.018  1.00 27.87           C  
ANISOU  210  CZ3 TRP A  25     4517   2587   3485    244    -73    111       C  
ATOM    211  CH2 TRP A  25       6.315  10.286  86.555  1.00 25.90           C  
ANISOU  211  CH2 TRP A  25     4246   2353   3243    256    -37    131       C  
ATOM    212  N   PRO A  26       1.328   5.795  84.034  1.00 25.43           N  
ANISOU  212  N   PRO A  26     4113   2422   3127    274    -22     48       N  
ATOM    213  CA  PRO A  26       0.280   5.848  83.011  1.00 27.78           C  
ANISOU  213  CA  PRO A  26     4365   2775   3416    287      1     51       C  
ATOM    214  C   PRO A  26       0.888   6.059  81.634  1.00 26.61           C  
ANISOU  214  C   PRO A  26     4166   2671   3275    321     -5     61       C  
ATOM    215  O   PRO A  26       1.646   7.001  81.454  1.00 22.57           O  
ANISOU  215  O   PRO A  26     3641   2156   2779    340     -2     82       O  
ATOM    216  CB  PRO A  26      -0.578   7.049  83.440  1.00 24.16           C  
ANISOU  216  CB  PRO A  26     3903   2314   2961    287     39     71       C  
ATOM    217  CG  PRO A  26       0.302   7.856  84.354  1.00 20.59           C  
ANISOU  217  CG  PRO A  26     3486   1813   2525    281     37     84       C  
ATOM    218  CD  PRO A  26       1.119   6.815  85.081  1.00 21.45           C  
ANISOU  218  CD  PRO A  26     3637   1882   2630    259      0     63       C  
ATOM    219  N   ALA A  27       0.559   5.196  80.680  1.00 24.37           N  
ANISOU  219  N   ALA A  27     3855   2426   2978    327    -12     47       N  
ATOM    220  CA  ALA A  27       1.256   5.199  79.402  1.00 21.43           C  
ANISOU  220  CA  ALA A  27     3441   2092   2611    357    -23     54       C  
ATOM    221  C   ALA A  27       0.408   4.633  78.281  1.00 27.00           C  
ANISOU  221  C   ALA A  27     4107   2853   3299    361    -15     45       C  
ATOM    222  O   ALA A  27      -0.674   4.103  78.502  1.00 22.29           O  
ANISOU  222  O   ALA A  27     3519   2268   2684    339     -4     31       O  
ATOM    223  CB  ALA A  27       2.549   4.390  79.498  1.00 18.01           C  
ANISOU  223  CB  ALA A  27     3031   1631   2182    358    -58     41       C  
ATOM    224  N   ARG A  28       0.946   4.716  77.074  1.00 23.98           N  
ANISOU  224  N   ARG A  28     3683   2507   2920    388    -21     52       N  
ATOM    225  CA  ARG A  28       0.232   4.241  75.894  1.00 29.13           C  
ANISOU  225  CA  ARG A  28     4296   3218   3556    393    -14     45       C  
ATOM    226  C   ARG A  28       1.205   3.527  74.961  1.00 21.04           C  
ANISOU  226  C   ARG A  28     3259   2204   2531    408    -37     35       C  
ATOM    227  O   ARG A  28       2.358   3.932  74.846  1.00 22.94           O  
ANISOU  227  O   ARG A  28     3497   2429   2791    430    -50     47       O  
ATOM    228  CB  ARG A  28      -0.436   5.415  75.175  1.00 28.39           C  
ANISOU  228  CB  ARG A  28     4151   3172   3466    416     16     72       C  
ATOM    229  CG  ARG A  28      -1.088   5.064  73.848  1.00 28.59           C  
ANISOU  229  CG  ARG A  28     4126   3264   3473    425     23     70       C  
ATOM    230  CD  ARG A  28      -1.554   6.329  73.122  1.00 30.80           C  
ANISOU  230  CD  ARG A  28     4354   3590   3758    455     50    101       C  
ATOM    231  NE  ARG A  28      -0.411   7.144  72.721  1.00 27.76           N  
ANISOU  231  NE  ARG A  28     3958   3194   3397    486     46    120       N  
ATOM    232  CZ  ARG A  28      -0.322   8.463  72.860  1.00 29.39           C  
ANISOU  232  CZ  ARG A  28     4154   3394   3618    508     68    148       C  
ATOM    233  NH1 ARG A  28      -1.316   9.169  73.398  1.00 25.49           N  
ANISOU  233  NH1 ARG A  28     3661   2903   3120    507     98    163       N  
ATOM    234  NH2 ARG A  28       0.772   9.085  72.434  1.00 33.41           N  
ANISOU  234  NH2 ARG A  28     4654   3895   4145    532     63    161       N  
ATOM    235  N   ILE A  29       0.729   2.473  74.307  1.00 22.92           N  
ANISOU  235  N   ILE A  29     3491   2471   2748    396    -42     15       N  
ATOM    236  CA  ILE A  29       1.466   1.799  73.248  1.00 28.18           C  
ANISOU  236  CA  ILE A  29     4141   3155   3410    411    -58      6       C  
ATOM    237  C   ILE A  29       1.373   2.619  71.953  1.00 26.90           C  
ANISOU  237  C   ILE A  29     3918   3051   3253    440    -44     27       C  
ATOM    238  O   ILE A  29       0.293   2.761  71.395  1.00 29.51           O  
ANISOU  238  O   ILE A  29     4216   3430   3568    434    -25     30       O  
ATOM    239  CB  ILE A  29       0.907   0.375  72.986  1.00 26.34           C  
ANISOU  239  CB  ILE A  29     3928   2932   3147    383    -63    -25       C  
ATOM    240  CG1 ILE A  29       0.848  -0.443  74.286  1.00 29.96           C  
ANISOU  240  CG1 ILE A  29     4451   3335   3598    353    -72    -46       C  
ATOM    241  CG2 ILE A  29       1.726  -0.345  71.922  1.00 31.83           C  
ANISOU  241  CG2 ILE A  29     4613   3641   3838    399    -77    -34       C  
ATOM    242  CD1 ILE A  29       2.192  -0.689  74.904  1.00 30.59           C  
ANISOU  242  CD1 ILE A  29     4568   3361   3694    366    -97    -46       C  
ATOM    243  N   ASP A  30       2.483   3.175  71.482  1.00 25.89           N  
ANISOU  243  N   ASP A  30     3771   2919   3145    470    -53     42       N  
ATOM    244  CA  ASP A  30       2.429   3.959  70.249  1.00 31.73           C  
ANISOU  244  CA  ASP A  30     4455   3712   3890    498    -40     62       C  
ATOM    245  C   ASP A  30       2.529   3.019  69.041  1.00 30.91           C  
ANISOU  245  C   ASP A  30     4332   3644   3770    501    -49     46       C  
ATOM    246  O   ASP A  30       2.775   1.824  69.192  1.00 32.80           O  
ANISOU  246  O   ASP A  30     4604   3862   3997    484    -65     22       O  
ATOM    247  CB  ASP A  30       3.532   5.029  70.228  1.00 31.55           C  
ANISOU  247  CB  ASP A  30     4421   3672   3894    528    -42     85       C  
ATOM    248  CG  ASP A  30       3.063   6.369  70.822  1.00 28.44           C  
ANISOU  248  CG  ASP A  30     4023   3273   3512    533    -18    110       C  
ATOM    249  OD1 ASP A  30       1.835   6.553  71.003  1.00 35.02           O  
ANISOU  249  OD1 ASP A  30     4848   4126   4332    522      4    113       O  
ATOM    250  OD2 ASP A  30       3.922   7.243  71.087  1.00 33.07           O  
ANISOU  250  OD2 ASP A  30     4612   3835   4118    548    -18    127       O  
ATOM    251  N   GLU A  31       2.310   3.518  67.835  1.00 35.39           N  
ANISOU  251  N   GLU A  31     4847   4265   4335    521    -37     60       N  
ATOM    252  CA  GLU A  31       2.411   2.588  66.716  1.00 35.46           C  
ANISOU  252  CA  GLU A  31     4841   4305   4326    520    -46     44       C  
ATOM    253  C   GLU A  31       3.863   2.520  66.300  1.00 37.35           C  
ANISOU  253  C   GLU A  31     5082   4524   4585    546    -64     46       C  
ATOM    254  O   GLU A  31       4.619   3.453  66.540  1.00 38.07           O  
ANISOU  254  O   GLU A  31     5168   4598   4701    568    -65     66       O  
ATOM    255  CB  GLU A  31       1.516   3.011  65.546  1.00 47.34           C  
ANISOU  255  CB  GLU A  31     6290   5881   5816    527    -27     56       C  
ATOM    256  CG  GLU A  31       2.075   4.118  64.692  1.00 48.34           C  
ANISOU  256  CG  GLU A  31     6373   6033   5963    566    -20     83       C  
ATOM    257  CD  GLU A  31       1.967   5.479  65.346  1.00 61.31           C  
ANISOU  257  CD  GLU A  31     8009   7662   7625    583     -3    110       C  
ATOM    258  OE1 GLU A  31       1.580   5.553  66.535  1.00 61.12           O  
ANISOU  258  OE1 GLU A  31     8017   7603   7602    565      0    108       O  
ATOM    259  OE2 GLU A  31       2.262   6.480  64.659  1.00 65.31           O  
ANISOU  259  OE2 GLU A  31     8481   8192   8144    614      7    134       O  
ATOM    260  N   LEU A  32       4.272   1.409  65.706  1.00 43.12           N  
ANISOU  260  N   LEU A  32     5824   5256   5302    541    -77     26       N  
ATOM    261  CA  LEU A  32       5.586   1.367  65.089  1.00 47.40           C  
ANISOU  261  CA  LEU A  32     6359   5790   5861    570    -91     30       C  
ATOM    262  C   LEU A  32       5.385   1.607  63.613  1.00 49.24           C  
ANISOU  262  C   LEU A  32     6541   6081   6087    585    -81     37       C  
ATOM    263  O   LEU A  32       4.863   0.740  62.921  1.00 54.08           O  
ANISOU  263  O   LEU A  32     7153   6722   6675    569    -78     20       O  
ATOM    264  CB  LEU A  32       6.286   0.035  65.335  1.00 49.43           C  
ANISOU  264  CB  LEU A  32     6661   6009   6110    562   -109      6       C  
ATOM    265  CG  LEU A  32       7.815   0.027  65.245  1.00 54.94           C  
ANISOU  265  CG  LEU A  32     7364   6681   6829    592   -127     13       C  
ATOM    266  CD1 LEU A  32       8.314   0.100  63.799  1.00 59.60           C  
ANISOU  266  CD1 LEU A  32     7914   7310   7421    617   -126     19       C  
ATOM    267  CD2 LEU A  32       8.427   1.146  66.084  1.00 50.08           C  
ANISOU  267  CD2 LEU A  32     6747   6041   6241    606   -132     35       C  
ATOM    268  N   PRO A  33       5.786   2.792  63.124  1.00 53.97           N  
ANISOU  268  N   PRO A  33     7101   6699   6706    615    -74     63       N  
ATOM    269  CA  PRO A  33       5.553   3.107  61.711  1.00 56.97           C  
ANISOU  269  CA  PRO A  33     7431   7136   7078    631    -64     72       C  
ATOM    270  C   PRO A  33       6.272   2.145  60.764  1.00 61.59           C  
ANISOU  270  C   PRO A  33     8018   7728   7656    636    -76     56       C  
ATOM    271  O   PRO A  33       7.454   1.833  60.925  1.00 55.14           O  
ANISOU  271  O   PRO A  33     7222   6876   6855    651    -92     52       O  
ATOM    272  CB  PRO A  33       6.105   4.531  61.564  1.00 49.92           C  
ANISOU  272  CB  PRO A  33     6509   6247   6211    663    -56    102       C  
ATOM    273  CG  PRO A  33       7.054   4.689  62.694  1.00 54.06           C  
ANISOU  273  CG  PRO A  33     7069   6713   6757    665    -70    103       C  
ATOM    274  CD  PRO A  33       6.481   3.885  63.822  1.00 52.89           C  
ANISOU  274  CD  PRO A  33     6966   6532   6596    633    -75     84       C  
ATOM    275  N   GLU A  34       5.507   1.655  59.793  1.00 70.23           N  
ANISOU  275  N   GLU A  34     9091   8869   8725    623    -67     47       N  
ATOM    276  CA  GLU A  34       6.030   0.942  58.637  1.00 71.22           C  
ANISOU  276  CA  GLU A  34     9208   9013   8841    630    -72     35       C  
ATOM    277  C   GLU A  34       7.070   1.826  57.988  1.00 54.30           C  
ANISOU  277  C   GLU A  34     7032   6875   6723    669    -75     56       C  
ATOM    278  O   GLU A  34       6.906   3.043  57.940  1.00 56.46           O  
ANISOU  278  O   GLU A  34     7274   7168   7011    687    -65     81       O  
ATOM    279  CB  GLU A  34       4.926   0.641  57.648  1.00 84.07           C  
ANISOU  279  CB  GLU A  34    10806  10701  10437    610    -59     29       C  
ATOM    280  CG  GLU A  34       3.902   1.753  57.528  1.00 91.55           C  
ANISOU  280  CG  GLU A  34    11708  11695  11381    613    -42     52       C  
ATOM    281  CD  GLU A  34       2.820   1.679  58.602  1.00 95.76           C  
ANISOU  281  CD  GLU A  34    12260  12221  11902    584    -35     47       C  
ATOM    282  OE1 GLU A  34       2.958   0.849  59.525  1.00 97.56           O  
ANISOU  282  OE1 GLU A  34    12539  12403  12127    562    -45     26       O  
ATOM    283  OE2 GLU A  34       1.850   2.469  58.537  1.00 95.46           O  
ANISOU  283  OE2 GLU A  34    12188  12225  11857    585    -19     65       O  
ATOM    284  N   GLY A  35       8.163   1.242  57.526  1.00 54.02           N  
ANISOU  284  N   GLY A  35     7007   6822   6694    684    -87     48       N  
ATOM    285  CA  GLY A  35       9.216   2.043  56.923  1.00 53.25           C  
ANISOU  285  CA  GLY A  35     6880   6730   6622    720    -90     67       C  
ATOM    286  C   GLY A  35       9.992   2.836  57.953  1.00 48.93           C  
ANISOU  286  C   GLY A  35     6345   6143   6103    735    -98     82       C  
ATOM    287  O   GLY A  35      10.403   3.969  57.705  1.00 42.18           O  
ANISOU  287  O   GLY A  35     5460   5299   5267    757    -93    104       O  
ATOM    288  N   ALA A  36      10.162   2.249  59.133  1.00 43.89           N  
ANISOU  288  N   ALA A  36     5751   5458   5465    720   -110     71       N  
ATOM    289  CA  ALA A  36      11.099   2.784  60.104  1.00 38.51           C  
ANISOU  289  CA  ALA A  36     5086   4736   4808    732   -121     82       C  
ATOM    290  C   ALA A  36      12.078   1.677  60.470  1.00 40.63           C  
ANISOU  290  C   ALA A  36     5392   4967   5077    735   -141     67       C  
ATOM    291  O   ALA A  36      11.818   0.511  60.191  1.00 47.74           O  
ANISOU  291  O   ALA A  36     6315   5866   5958    724   -142     46       O  
ATOM    292  CB  ALA A  36      10.375   3.311  61.342  1.00 31.70           C  
ANISOU  292  CB  ALA A  36     4243   3853   3948    712   -116     88       C  
ATOM    293  N   VAL A  37      13.204   2.041  61.072  1.00 29.02           N  
ANISOU  293  N   VAL A  37     3929   3469   3628    751   -155     78       N  
ATOM    294  CA  VAL A  37      14.109   1.050  61.634  1.00 29.15           C  
ANISOU  294  CA  VAL A  37     3983   3449   3646    757   -174     67       C  
ATOM    295  C   VAL A  37      13.276   0.174  62.573  1.00 37.09           C  
ANISOU  295  C   VAL A  37     5035   4426   4633    727   -175     49       C  
ATOM    296  O   VAL A  37      12.485   0.693  63.357  1.00 31.21           O  
ANISOU  296  O   VAL A  37     4298   3674   3887    706   -168     52       O  
ATOM    297  CB  VAL A  37      15.287   1.705  62.391  1.00 30.43           C  
ANISOU  297  CB  VAL A  37     4144   3588   3830    771   -189     84       C  
ATOM    298  CG1 VAL A  37      16.112   0.656  63.113  1.00 28.77           C  
ANISOU  298  CG1 VAL A  37     3973   3340   3617    777   -209     75       C  
ATOM    299  CG2 VAL A  37      16.174   2.490  61.426  1.00 40.59           C  
ANISOU  299  CG2 VAL A  37     5386   4903   5133    799   -188    101       C  
ATOM    300  N   LYS A  38      13.409  -1.145  62.477  1.00 40.27           N  
ANISOU  300  N   LYS A  38     5471   4812   5018    725   -180     29       N  
ATOM    301  CA  LYS A  38      12.535  -1.991  63.279  1.00 45.22           C  
ANISOU  301  CA  LYS A  38     6144   5413   5624    694   -177      9       C  
ATOM    302  C   LYS A  38      13.108  -2.136  64.676  1.00 44.87           C  
ANISOU  302  C   LYS A  38     6138   5320   5589    693   -194     12       C  
ATOM    303  O   LYS A  38      14.319  -2.233  64.850  1.00 42.63           O  
ANISOU  303  O   LYS A  38     5859   5021   5319    718   -209     21       O  
ATOM    304  CB  LYS A  38      12.314  -3.356  62.619  1.00 53.33           C  
ANISOU  304  CB  LYS A  38     7198   6441   6626    686   -171    -14       C  
ATOM    305  CG  LYS A  38      11.060  -3.396  61.747  1.00 58.17           C  
ANISOU  305  CG  LYS A  38     7790   7096   7216    662   -152    -25       C  
ATOM    306  CD  LYS A  38      10.025  -4.377  62.296  1.00 66.79           C  
ANISOU  306  CD  LYS A  38     8927   8171   8278    623   -145    -50       C  
ATOM    307  CE  LYS A  38       8.661  -4.219  61.621  1.00 72.40           C  
ANISOU  307  CE  LYS A  38     9612   8931   8967    594   -127    -57       C  
ATOM    308  NZ  LYS A  38       7.870  -3.071  62.166  1.00 74.85           N  
ANISOU  308  NZ  LYS A  38     9894   9258   9287    584   -122    -41       N  
ATOM    309  N   PRO A  39      12.234  -2.114  65.688  1.00 49.39           N  
ANISOU  309  N   PRO A  39     6738   5873   6153    663   -191      5       N  
ATOM    310  CA  PRO A  39      12.656  -2.194  67.087  1.00 46.80           C  
ANISOU  310  CA  PRO A  39     6449   5501   5833    657   -206      8       C  
ATOM    311  C   PRO A  39      13.166  -3.577  67.448  1.00 44.97           C  
ANISOU  311  C   PRO A  39     6267   5233   5587    662   -217     -8       C  
ATOM    312  O   PRO A  39      12.955  -4.522  66.689  1.00 38.66           O  
ANISOU  312  O   PRO A  39     5479   4441   4769    662   -208    -25       O  
ATOM    313  CB  PRO A  39      11.375  -1.876  67.849  1.00 55.52           C  
ANISOU  313  CB  PRO A  39     7567   6600   6929    622   -194      2       C  
ATOM    314  CG  PRO A  39      10.296  -2.308  66.930  1.00 57.96           C  
ANISOU  314  CG  PRO A  39     7865   6942   7216    606   -176    -13       C  
ATOM    315  CD  PRO A  39      10.773  -2.000  65.557  1.00 55.31           C  
ANISOU  315  CD  PRO A  39     7483   6646   6887    633   -173     -4       C  
ATOM    316  N   PRO A  40      13.829  -3.701  68.606  1.00 60.02           N  
ANISOU  316  N   PRO A  40     8204   7101   7501    665   -234     -3       N  
ATOM    317  CA  PRO A  40      14.134  -5.040  69.113  1.00 56.97           C  
ANISOU  317  CA  PRO A  40     7872   6676   7097    668   -241    -18       C  
ATOM    318  C   PRO A  40      12.864  -5.876  69.207  1.00 49.65           C  
ANISOU  318  C   PRO A  40     6983   5740   6143    633   -225    -44       C  
ATOM    319  O   PRO A  40      11.793  -5.327  69.461  1.00 53.82           O  
ANISOU  319  O   PRO A  40     7502   6279   6668    603   -215    -48       O  
ATOM    320  CB  PRO A  40      14.721  -4.767  70.498  1.00 64.52           C  
ANISOU  320  CB  PRO A  40     8852   7599   8065    667   -260     -6       C  
ATOM    321  CG  PRO A  40      15.261  -3.392  70.411  1.00 66.53           C  
ANISOU  321  CG  PRO A  40     9058   7877   8345    678   -266     18       C  
ATOM    322  CD  PRO A  40      14.343  -2.643  69.491  1.00 64.62           C  
ANISOU  322  CD  PRO A  40     8775   7674   8105    667   -246     18       C  
ATOM    323  N   ALA A  41      12.977  -7.179  68.987  1.00 37.71           N  
ANISOU  323  N   ALA A  41     5512   4208   4609    636   -222    -62       N  
ATOM    324  CA  ALA A  41      11.814  -8.049  68.999  1.00 33.51           C  
ANISOU  324  CA  ALA A  41     5018   3667   4047    600   -205    -89       C  
ATOM    325  C   ALA A  41      11.086  -7.970  70.336  1.00 39.99           C  
ANISOU  325  C   ALA A  41     5873   4458   4863    568   -207    -96       C  
ATOM    326  O   ALA A  41      11.721  -7.828  71.375  1.00 31.02           O  
ANISOU  326  O   ALA A  41     4756   3290   3739    578   -224    -85       O  
ATOM    327  CB  ALA A  41      12.223  -9.469  68.715  1.00 40.50           C  
ANISOU  327  CB  ALA A  41     5951   4526   4909    611   -200   -106       C  
ATOM    328  N   ASN A  42       9.762  -8.075  70.282  1.00 37.36           N  
ANISOU  328  N   ASN A  42     5545   4139   4510    529   -191   -113       N  
ATOM    329  CA  ASN A  42       8.897  -8.053  71.462  1.00 44.41           C  
ANISOU  329  CA  ASN A  42     6471   5007   5396    493   -189   -122       C  
ATOM    330  C   ASN A  42       9.073  -6.822  72.342  1.00 39.56           C  
ANISOU  330  C   ASN A  42     5835   4388   4810    497   -200   -100       C  
ATOM    331  O   ASN A  42       8.853  -6.887  73.547  1.00 43.72           O  
ANISOU  331  O   ASN A  42     6398   4879   5335    479   -205   -103       O  
ATOM    332  CB  ASN A  42       9.115  -9.318  72.288  1.00 47.29           C  
ANISOU  332  CB  ASN A  42     6908   5318   5741    486   -193   -140       C  
ATOM    333  CG  ASN A  42       8.615 -10.556  71.578  1.00 60.39           C  
ANISOU  333  CG  ASN A  42     8601   6978   7366    469   -175   -167       C  
ATOM    334  OD1 ASN A  42       7.554 -10.534  70.952  1.00 58.72           O  
ANISOU  334  OD1 ASN A  42     8372   6801   7137    439   -158   -181       O  
ATOM    335  ND2 ASN A  42       9.381 -11.641  71.657  1.00 61.90           N  
ANISOU  335  ND2 ASN A  42     8841   7133   7545    488   -178   -175       N  
ATOM    336  N   LYS A  43       9.478  -5.708  71.738  1.00 32.70           N  
ANISOU  336  N   LYS A  43     4908   3552   3963    519   -202    -77       N  
ATOM    337  CA  LYS A  43       9.524  -4.430  72.440  1.00 34.30           C  
ANISOU  337  CA  LYS A  43     5088   3755   4189    518   -206    -56       C  
ATOM    338  C   LYS A  43       8.600  -3.446  71.735  1.00 35.61           C  
ANISOU  338  C   LYS A  43     5203   3968   4359    510   -187    -48       C  
ATOM    339  O   LYS A  43       8.550  -3.402  70.503  1.00 32.61           O  
ANISOU  339  O   LYS A  43     4787   3628   3976    522   -179    -47       O  
ATOM    340  CB  LYS A  43      10.949  -3.868  72.500  1.00 35.73           C  
ANISOU  340  CB  LYS A  43     5250   3931   4396    553   -225    -33       C  
ATOM    341  CG  LYS A  43      11.916  -4.675  73.352  1.00 42.05           C  
ANISOU  341  CG  LYS A  43     6095   4687   5193    565   -245    -35       C  
ATOM    342  CD  LYS A  43      12.629  -3.783  74.355  1.00 47.38           C  
ANISOU  342  CD  LYS A  43     6768   5345   5890    569   -261    -14       C  
ATOM    343  CE  LYS A  43      13.566  -4.578  75.245  1.00 47.64           C  
ANISOU  343  CE  LYS A  43     6844   5339   5918    581   -283    -13       C  
ATOM    344  NZ  LYS A  43      14.257  -3.683  76.206  1.00 59.29           N  
ANISOU  344  NZ  LYS A  43     8314   6803   7411    580   -299      7       N  
ATOM    345  N   TYR A  44       7.875  -2.658  72.522  1.00 28.26           N  
ANISOU  345  N   TYR A  44     4272   3032   3434    489   -179    -42       N  
ATOM    346  CA  TYR A  44       6.892  -1.706  71.995  1.00 33.14           C  
ANISOU  346  CA  TYR A  44     4845   3693   4053    482   -159    -32       C  
ATOM    347  C   TYR A  44       7.274  -0.280  72.314  1.00 30.75           C  
ANISOU  347  C   TYR A  44     4516   3392   3777    497   -157     -5       C  
ATOM    348  O   TYR A  44       7.881  -0.017  73.356  1.00 30.01           O  
ANISOU  348  O   TYR A  44     4449   3260   3695    495   -169      2       O  
ATOM    349  CB  TYR A  44       5.506  -2.003  72.563  1.00 35.56           C  
ANISOU  349  CB  TYR A  44     5175   3999   4340    444   -144    -47       C  
ATOM    350  CG  TYR A  44       5.014  -3.365  72.166  1.00 37.38           C  
ANISOU  350  CG  TYR A  44     5431   4232   4540    424   -141    -76       C  
ATOM    351  CD1 TYR A  44       5.429  -4.506  72.851  1.00 41.65           C  
ANISOU  351  CD1 TYR A  44     6031   4726   5069    415   -153    -95       C  
ATOM    352  CD2 TYR A  44       4.172  -3.522  71.081  1.00 32.11           C  
ANISOU  352  CD2 TYR A  44     4732   3616   3854    414   -125    -83       C  
ATOM    353  CE1 TYR A  44       4.995  -5.760  72.474  1.00 40.96           C  
ANISOU  353  CE1 TYR A  44     5973   4639   4952    395   -148   -121       C  
ATOM    354  CE2 TYR A  44       3.727  -4.764  70.707  1.00 39.38           C  
ANISOU  354  CE2 TYR A  44     5679   4540   4744    391   -121   -110       C  
ATOM    355  CZ  TYR A  44       4.142  -5.880  71.396  1.00 39.39           C  
ANISOU  355  CZ  TYR A  44     5742   4490   4733    381   -131   -130       C  
ATOM    356  OH  TYR A  44       3.691  -7.119  71.005  1.00 41.30           O  
ANISOU  356  OH  TYR A  44     6017   4734   4943    356   -123   -157       O  
ATOM    357  N   PRO A  45       6.939   0.651  71.407  1.00 32.08           N  
ANISOU  357  N   PRO A  45     4633   3605   3952    510   -142     11       N  
ATOM    358  CA  PRO A  45       7.212   2.061  71.678  1.00 30.21           C  
ANISOU  358  CA  PRO A  45     4373   3369   3737    522   -135     37       C  
ATOM    359  C   PRO A  45       6.182   2.555  72.678  1.00 27.88           C  
ANISOU  359  C   PRO A  45     4096   3058   3438    497   -119     39       C  
ATOM    360  O   PRO A  45       4.988   2.348  72.462  1.00 31.49           O  
ANISOU  360  O   PRO A  45     4547   3540   3879    481   -102     31       O  
ATOM    361  CB  PRO A  45       7.042   2.735  70.313  1.00 30.07           C  
ANISOU  361  CB  PRO A  45     4299   3405   3723    545   -120     51       C  
ATOM    362  CG  PRO A  45       6.067   1.865  69.590  1.00 32.66           C  
ANISOU  362  CG  PRO A  45     4619   3765   4026    531   -111     32       C  
ATOM    363  CD  PRO A  45       6.279   0.452  70.101  1.00 35.99           C  
ANISOU  363  CD  PRO A  45     5091   4152   4433    513   -128      6       C  
ATOM    364  N   ILE A  46       6.652   3.175  73.754  1.00 25.91           N  
ANISOU  364  N   ILE A  46     3871   2771   3203    492   -123     50       N  
ATOM    365  CA  ILE A  46       5.797   3.585  74.859  1.00 26.91           C  
ANISOU  365  CA  ILE A  46     4023   2873   3327    467   -109     51       C  
ATOM    366  C   ILE A  46       5.767   5.100  74.937  1.00 27.13           C  
ANISOU  366  C   ILE A  46     4028   2908   3371    477    -89     78       C  
ATOM    367  O   ILE A  46       6.790   5.757  74.735  1.00 33.60           O  
ANISOU  367  O   ILE A  46     4835   3725   4207    496    -96     93       O  
ATOM    368  CB  ILE A  46       6.298   3.020  76.210  1.00 26.91           C  
ANISOU  368  CB  ILE A  46     4079   2817   3327    447   -129     40       C  
ATOM    369  CG1 ILE A  46       6.604   1.532  76.102  1.00 29.78           C  
ANISOU  369  CG1 ILE A  46     4470   3170   3676    443   -150     17       C  
ATOM    370  CG2 ILE A  46       5.272   3.273  77.302  1.00 28.73           C  
ANISOU  370  CG2 ILE A  46     4341   3025   3552    418   -113     38       C  
ATOM    371  CD1 ILE A  46       5.377   0.681  75.835  1.00 30.83           C  
ANISOU  371  CD1 ILE A  46     4610   3319   3784    422   -137     -5       C  
ATOM    372  N   PHE A  47       4.588   5.646  75.205  1.00 25.34           N  
ANISOU  372  N   PHE A  47     3799   2691   3139    466    -63     84       N  
ATOM    373  CA  PHE A  47       4.420   7.081  75.410  1.00 23.71           C  
ANISOU  373  CA  PHE A  47     3579   2484   2944    475    -38    110       C  
ATOM    374  C   PHE A  47       3.959   7.252  76.842  1.00 25.14           C  
ANISOU  374  C   PHE A  47     3807   2620   3124    447    -31    107       C  
ATOM    375  O   PHE A  47       2.943   6.694  77.215  1.00 24.57           O  
ANISOU  375  O   PHE A  47     3750   2549   3038    427    -23     94       O  
ATOM    376  CB  PHE A  47       3.407   7.652  74.419  1.00 24.19           C  
ANISOU  376  CB  PHE A  47     3594   2599   3000    492     -9    123       C  
ATOM    377  CG  PHE A  47       3.033   9.093  74.661  1.00 25.65           C  
ANISOU  377  CG  PHE A  47     3771   2782   3193    503     23    150       C  
ATOM    378  CD1 PHE A  47       3.747  10.114  74.042  1.00 29.91           C  
ANISOU  378  CD1 PHE A  47     4286   3333   3747    529     32    171       C  
ATOM    379  CD2 PHE A  47       1.951   9.424  75.472  1.00 30.18           C  
ANISOU  379  CD2 PHE A  47     4363   3345   3760    487     47    154       C  
ATOM    380  CE1 PHE A  47       3.408  11.441  74.239  1.00 32.80           C  
ANISOU  380  CE1 PHE A  47     4648   3695   4118    540     65    197       C  
ATOM    381  CE2 PHE A  47       1.607  10.750  75.683  1.00 28.48           C  
ANISOU  381  CE2 PHE A  47     4143   3126   3552    500     80    180       C  
ATOM    382  CZ  PHE A  47       2.346  11.764  75.056  1.00 32.01           C  
ANISOU  382  CZ  PHE A  47     4569   3582   4013    527     90    201       C  
ATOM    383  N   PHE A  48       4.719   7.995  77.640  1.00 24.69           N  
ANISOU  383  N   PHE A  48     3774   2526   3081    443    -33    119       N  
ATOM    384  CA  PHE A  48       4.348   8.213  79.033  1.00 22.88           C  
ANISOU  384  CA  PHE A  48     3592   2252   2851    414    -25    118       C  
ATOM    385  C   PHE A  48       3.530   9.480  79.158  1.00 23.67           C  
ANISOU  385  C   PHE A  48     3683   2357   2954    419     15    140       C  
ATOM    386  O   PHE A  48       3.989  10.560  78.774  1.00 23.20           O  
ANISOU  386  O   PHE A  48     3605   2304   2904    438     29    161       O  
ATOM    387  CB  PHE A  48       5.585   8.307  79.927  1.00 20.60           C  
ANISOU  387  CB  PHE A  48     3337   1918   2571    402    -48    119       C  
ATOM    388  CG  PHE A  48       6.391   7.042  79.989  1.00 25.64           C  
ANISOU  388  CG  PHE A  48     3991   2545   3205    399    -86    100       C  
ATOM    389  CD1 PHE A  48       7.425   6.825  79.090  1.00 20.40           C  
ANISOU  389  CD1 PHE A  48     3299   1905   2548    424   -105    102       C  
ATOM    390  CD2 PHE A  48       6.133   6.082  80.958  1.00 26.08           C  
ANISOU  390  CD2 PHE A  48     4092   2567   3250    374   -100     80       C  
ATOM    391  CE1 PHE A  48       8.171   5.649  79.138  1.00 23.94           C  
ANISOU  391  CE1 PHE A  48     3762   2343   2991    425   -137     87       C  
ATOM    392  CE2 PHE A  48       6.879   4.909  81.019  1.00 30.81           C  
ANISOU  392  CE2 PHE A  48     4708   3154   3844    375   -132     64       C  
ATOM    393  CZ  PHE A  48       7.897   4.693  80.109  1.00 31.31           C  
ANISOU  393  CZ  PHE A  48     4741   3241   3913    401   -150     68       C  
ATOM    394  N   PHE A  49       2.322   9.357  79.705  1.00 24.18           N  
ANISOU  394  N   PHE A  49     3762   2417   3007    403     34    135       N  
ATOM    395  CA  PHE A  49       1.489  10.531  79.911  1.00 23.57           C  
ANISOU  395  CA  PHE A  49     3680   2342   2931    409     75    157       C  
ATOM    396  C   PHE A  49       2.110  11.411  80.984  1.00 23.01           C  
ANISOU  396  C   PHE A  49     3652   2220   2872    395     82    168       C  
ATOM    397  O   PHE A  49       2.874  10.925  81.823  1.00 26.66           O  
ANISOU  397  O   PHE A  49     4152   2642   3336    371     55    155       O  
ATOM    398  CB  PHE A  49       0.074  10.135  80.307  1.00 19.95           C  
ANISOU  398  CB  PHE A  49     3228   1893   2458    393     92    148       C  
ATOM    399  CG  PHE A  49      -0.678   9.437  79.228  1.00 25.96           C  
ANISOU  399  CG  PHE A  49     3946   2713   3206    404     92    140       C  
ATOM    400  CD1 PHE A  49      -1.168  10.151  78.137  1.00 28.59           C  
ANISOU  400  CD1 PHE A  49     4226   3098   3537    436    116    161       C  
ATOM    401  CD2 PHE A  49      -0.910   8.074  79.298  1.00 26.15           C  
ANISOU  401  CD2 PHE A  49     3982   2739   3215    382     68    111       C  
ATOM    402  CE1 PHE A  49      -1.879   9.510  77.137  1.00 30.32           C  
ANISOU  402  CE1 PHE A  49     4404   3376   3741    443    115    153       C  
ATOM    403  CE2 PHE A  49      -1.640   7.421  78.301  1.00 21.52           C  
ANISOU  403  CE2 PHE A  49     3357   2208   2612    386     69    102       C  
ATOM    404  CZ  PHE A  49      -2.117   8.145  77.217  1.00 28.73           C  
ANISOU  404  CZ  PHE A  49     4215   3176   3523    416     91    123       C  
ATOM    405  N   GLY A  50       1.789  12.697  80.941  1.00 23.96           N  
ANISOU  405  N   GLY A  50     3766   2341   2996    409    120    193       N  
ATOM    406  CA  GLY A  50       2.311  13.659  81.901  1.00 23.38           C  
ANISOU  406  CA  GLY A  50     3734   2219   2931    394    133    206       C  
ATOM    407  C   GLY A  50       3.658  14.225  81.516  1.00 25.66           C  
ANISOU  407  C   GLY A  50     4015   2504   3229    403    121    216       C  
ATOM    408  O   GLY A  50       3.845  15.438  81.504  1.00 30.99           O  
ANISOU  408  O   GLY A  50     4695   3170   3910    410    150    237       O  
ATOM    409  N   THR A  51       4.607  13.343  81.211  1.00 22.78           N  
ANISOU  409  N   THR A  51     3642   2147   2868    401     80    201       N  
ATOM    410  CA  THR A  51       5.958  13.772  80.868  1.00 27.89           C  
ANISOU  410  CA  THR A  51     4279   2794   3524    407     64    208       C  
ATOM    411  C   THR A  51       6.149  13.823  79.358  1.00 31.18           C  
ANISOU  411  C   THR A  51     4640   3263   3944    444     64    215       C  
ATOM    412  O   THR A  51       6.975  14.576  78.861  1.00 28.85           O  
ANISOU  412  O   THR A  51     4330   2975   3656    457     67    229       O  
ATOM    413  CB  THR A  51       7.006  12.842  81.468  1.00 28.67           C  
ANISOU  413  CB  THR A  51     4401   2870   3623    386     19    191       C  
ATOM    414  OG1 THR A  51       6.885  11.548  80.878  1.00 26.40           O  
ANISOU  414  OG1 THR A  51     4092   2607   3331    397     -8    172       O  
ATOM    415  CG2 THR A  51       6.821  12.720  82.970  1.00 27.36           C  
ANISOU  415  CG2 THR A  51     4291   2653   3452    349     17    183       C  
ATOM    416  N   HIS A  52       5.373  13.005  78.652  1.00 26.98           N  
ANISOU  416  N   HIS A  52     4079   2766   3406    458     59    205       N  
ATOM    417  CA  HIS A  52       5.481  12.806  77.191  1.00 24.81           C  
ANISOU  417  CA  HIS A  52     3751   2543   3132    490     55    207       C  
ATOM    418  C   HIS A  52       6.848  12.248  76.779  1.00 29.91           C  
ANISOU  418  C   HIS A  52     4387   3192   3784    495     17    198       C  
ATOM    419  O   HIS A  52       7.265  12.370  75.625  1.00 27.11           O  
ANISOU  419  O   HIS A  52     3992   2874   3434    521     15    204       O  
ATOM    420  CB  HIS A  52       5.174  14.103  76.442  1.00 29.53           C  
ANISOU  420  CB  HIS A  52     4321   3167   3734    518     93    234       C  
ATOM    421  CG  HIS A  52       3.751  14.549  76.590  1.00 31.13           C  
ANISOU  421  CG  HIS A  52     4521   3379   3928    523    131    245       C  
ATOM    422  ND1 HIS A  52       3.149  15.431  75.723  1.00 30.95           N  
ANISOU  422  ND1 HIS A  52     4464   3393   3904    555    165    268       N  
ATOM    423  CD2 HIS A  52       2.810  14.218  77.503  1.00 27.51           C  
ANISOU  423  CD2 HIS A  52     4090   2900   3460    502    139    237       C  
ATOM    424  CE1 HIS A  52       1.899  15.637  76.103  1.00 26.82           C  
ANISOU  424  CE1 HIS A  52     3945   2873   3371    555    194    275       C  
ATOM    425  NE2 HIS A  52       1.668  14.910  77.181  1.00 32.49           N  
ANISOU  425  NE2 HIS A  52     4701   3557   4085    522    179    256       N  
ATOM    426  N   GLU A  53       7.526  11.620  77.730  1.00 25.81           N  
ANISOU  426  N   GLU A  53     3904   2637   3265    470    -11    185       N  
ATOM    427  CA  GLU A  53       8.743  10.873  77.446  1.00 25.45           C  
ANISOU  427  CA  GLU A  53     3852   2595   3224    475    -49    175       C  
ATOM    428  C   GLU A  53       8.350   9.611  76.676  1.00 24.28           C  
ANISOU  428  C   GLU A  53     3683   2475   3068    487    -64    156       C  
ATOM    429  O   GLU A  53       7.192   9.194  76.717  1.00 29.04           O  
ANISOU  429  O   GLU A  53     4289   3085   3660    481    -52    147       O  
ATOM    430  CB  GLU A  53       9.504  10.554  78.751  1.00 30.66           C  
ANISOU  430  CB  GLU A  53     4557   3209   3883    447    -73    168       C  
ATOM    431  CG  GLU A  53      10.612   9.493  78.596  1.00 57.13           C  
ANISOU  431  CG  GLU A  53     7906   6564   7236    453   -114    156       C  
ATOM    432  CD  GLU A  53      11.554   9.378  79.787  1.00 72.80           C  
ANISOU  432  CD  GLU A  53     9929   8512   9220    429   -138    155       C  
ATOM    433  OE1 GLU A  53      11.526  10.270  80.668  1.00 77.97           O  
ANISOU  433  OE1 GLU A  53    10609   9139   9876    406   -124    165       O  
ATOM    434  OE2 GLU A  53      12.340   8.402  79.823  1.00 73.47           O  
ANISOU  434  OE2 GLU A  53    10017   8596   9304    435   -171    145       O  
ATOM    435  N   THR A  54       9.310   9.028  75.956  1.00 27.33           N  
ANISOU  435  N   THR A  54     4048   2878   3457    504    -90    151       N  
ATOM    436  CA  THR A  54       9.123   7.763  75.274  1.00 33.14           C  
ANISOU  436  CA  THR A  54     4773   3635   4184    514   -106    132       C  
ATOM    437  C   THR A  54      10.230   6.789  75.645  1.00 31.99           C  
ANISOU  437  C   THR A  54     4648   3468   4038    512   -141    121       C  
ATOM    438  O   THR A  54      11.291   7.177  76.158  1.00 36.19           O  
ANISOU  438  O   THR A  54     5189   3982   4578    510   -156    130       O  
ATOM    439  CB  THR A  54       9.113   7.924  73.744  1.00 38.87           C  
ANISOU  439  CB  THR A  54     5446   4410   4911    543    -97    139       C  
ATOM    440  OG1 THR A  54      10.376   8.449  73.323  1.00 39.86           O  
ANISOU  440  OG1 THR A  54     5553   4542   5050    561   -108    151       O  
ATOM    441  CG2 THR A  54       8.005   8.862  73.302  1.00 36.37           C  
ANISOU  441  CG2 THR A  54     5105   4120   4592    550    -62    153       C  
ATOM    442  N   ALA A  55       9.966   5.521  75.378  1.00 25.54           N  
ANISOU  442  N   ALA A  55     3839   2655   3209    513   -154    101       N  
ATOM    443  CA  ALA A  55      10.903   4.437  75.634  1.00 29.58           C  
ANISOU  443  CA  ALA A  55     4372   3148   3718    516   -185     89       C  
ATOM    444  C   ALA A  55      10.396   3.189  74.937  1.00 30.51           C  
ANISOU  444  C   ALA A  55     4490   3281   3820    521   -187     68       C  
ATOM    445  O   ALA A  55       9.257   3.152  74.469  1.00 36.82           O  
ANISOU  445  O   ALA A  55     5277   4102   4610    514   -167     61       O  
ATOM    446  CB  ALA A  55      11.052   4.189  77.113  1.00 34.16           C  
ANISOU  446  CB  ALA A  55     5003   3682   4295    491   -198     84       C  
ATOM    447  N   PHE A  56      11.242   2.167  74.849  1.00 28.37           N  
ANISOU  447  N   PHE A  56     4233   3000   3545    533   -210     59       N  
ATOM    448  CA  PHE A  56      10.807   0.889  74.326  1.00 27.69           C  
ANISOU  448  CA  PHE A  56     4160   2920   3442    534   -212     37       C  
ATOM    449  C   PHE A  56      10.799  -0.119  75.454  1.00 33.00           C  
ANISOU  449  C   PHE A  56     4889   3548   4102    515   -226     21       C  
ATOM    450  O   PHE A  56      11.786  -0.261  76.164  1.00 37.96           O  
ANISOU  450  O   PHE A  56     5538   4150   4736    522   -246     27       O  
ATOM    451  CB  PHE A  56      11.713   0.426  73.174  1.00 30.16           C  
ANISOU  451  CB  PHE A  56     4446   3258   3757    566   -222     38       C  
ATOM    452  CG  PHE A  56      11.321   1.011  71.845  1.00 30.46           C  
ANISOU  452  CG  PHE A  56     4432   3343   3798    580   -204     44       C  
ATOM    453  CD1 PHE A  56      11.658   2.312  71.520  1.00 36.73           C  
ANISOU  453  CD1 PHE A  56     5188   4158   4609    592   -196     66       C  
ATOM    454  CD2 PHE A  56      10.588   0.266  70.943  1.00 33.08           C  
ANISOU  454  CD2 PHE A  56     4756   3700   4112    577   -193     28       C  
ATOM    455  CE1 PHE A  56      11.290   2.852  70.299  1.00 37.56           C  
ANISOU  455  CE1 PHE A  56     5247   4307   4717    606   -179     74       C  
ATOM    456  CE2 PHE A  56      10.215   0.804  69.718  1.00 32.29           C  
ANISOU  456  CE2 PHE A  56     4608   3646   4013    590   -177     35       C  
ATOM    457  CZ  PHE A  56      10.570   2.090  69.400  1.00 30.37           C  
ANISOU  457  CZ  PHE A  56     4327   3423   3790    606   -171     58       C  
ATOM    458  N   LEU A  57       9.669  -0.795  75.626  1.00 27.70           N  
ANISOU  458  N   LEU A  57     4243   2871   3412    492   -214      1       N  
ATOM    459  CA  LEU A  57       9.499  -1.754  76.710  1.00 27.61           C  
ANISOU  459  CA  LEU A  57     4290   2815   3386    471   -223    -16       C  
ATOM    460  C   LEU A  57       8.845  -3.023  76.210  1.00 31.22           C  
ANISOU  460  C   LEU A  57     4768   3276   3819    461   -216    -42       C  
ATOM    461  O   LEU A  57       8.015  -2.979  75.301  1.00 36.05           O  
ANISOU  461  O   LEU A  57     5351   3924   4421    456   -199    -48       O  
ATOM    462  CB  LEU A  57       8.643  -1.166  77.845  1.00 28.53           C  
ANISOU  462  CB  LEU A  57     4428   2909   3502    439   -213    -15       C  
ATOM    463  CG  LEU A  57       9.276  -0.042  78.651  1.00 32.58           C  
ANISOU  463  CG  LEU A  57     4939   3406   4035    439   -219      7       C  
ATOM    464  CD1 LEU A  57       8.329   0.400  79.759  1.00 25.86           C  
ANISOU  464  CD1 LEU A  57     4116   2528   3181    406   -206      4       C  
ATOM    465  CD2 LEU A  57      10.599  -0.530  79.232  1.00 38.01           C  
ANISOU  465  CD2 LEU A  57     5651   4065   4726    452   -248     11       C  
ATOM    466  N   GLY A  58       9.212  -4.150  76.817  1.00 25.18           N  
ANISOU  466  N   GLY A  58     4054   2473   3040    459   -230    -56       N  
ATOM    467  CA  GLY A  58       8.544  -5.412  76.571  1.00 28.52           C  
ANISOU  467  CA  GLY A  58     4512   2890   3436    443   -221    -83       C  
ATOM    468  C   GLY A  58       7.404  -5.655  77.549  1.00 32.24           C  
ANISOU  468  C   GLY A  58     5022   3335   3891    402   -210    -99       C  
ATOM    469  O   GLY A  58       7.288  -4.959  78.561  1.00 35.36           O  
ANISOU  469  O   GLY A  58     5427   3711   4299    389   -213    -90       O  
ATOM    470  N   PRO A  59       6.556  -6.655  77.250  1.00 32.82           N  
ANISOU  470  N   PRO A  59     5122   3411   3938    379   -197   -125       N  
ATOM    471  CA  PRO A  59       5.293  -6.929  77.948  1.00 24.01           C  
ANISOU  471  CA  PRO A  59     4037   2283   2802    336   -183   -144       C  
ATOM    472  C   PRO A  59       5.462  -7.215  79.440  1.00 35.60           C  
ANISOU  472  C   PRO A  59     5562   3695   4270    321   -194   -148       C  
ATOM    473  O   PRO A  59       4.496  -7.071  80.189  1.00 33.42           O  
ANISOU  473  O   PRO A  59     5305   3408   3986    288   -184   -157       O  
ATOM    474  CB  PRO A  59       4.755  -8.169  77.233  1.00 33.02           C  
ANISOU  474  CB  PRO A  59     5201   3434   3911    319   -171   -171       C  
ATOM    475  CG  PRO A  59       5.362  -8.113  75.869  1.00 39.80           C  
ANISOU  475  CG  PRO A  59     6016   4330   4775    350   -171   -163       C  
ATOM    476  CD  PRO A  59       6.740  -7.534  76.078  1.00 37.32           C  
ANISOU  476  CD  PRO A  59     5687   4001   4491    391   -192   -138       C  
ATOM    477  N   LYS A  60       6.659  -7.619  79.858  1.00 30.86           N  
ANISOU  477  N   LYS A  60     4989   3061   3676    346   -215   -141       N  
ATOM    478  CA  LYS A  60       6.900  -7.919  81.266  1.00 35.83           C  
ANISOU  478  CA  LYS A  60     5672   3637   4303    335   -228   -143       C  
ATOM    479  C   LYS A  60       6.801  -6.652  82.102  1.00 31.61           C  
ANISOU  479  C   LYS A  60     5121   3099   3791    324   -231   -124       C  
ATOM    480  O   LYS A  60       6.559  -6.709  83.312  1.00 36.86           O  
ANISOU  480  O   LYS A  60     5827   3726   4452    301   -234   -128       O  
ATOM    481  CB  LYS A  60       8.268  -8.576  81.461  1.00 36.74           C  
ANISOU  481  CB  LYS A  60     5813   3725   4420    369   -250   -135       C  
ATOM    482  CG  LYS A  60       9.473  -7.685  81.207  1.00 39.38           C  
ANISOU  482  CG  LYS A  60     6102   4079   4783    405   -268   -106       C  
ATOM    483  CD  LYS A  60      10.742  -8.302  81.812  1.00 47.42           C  
ANISOU  483  CD  LYS A  60     7153   5064   5800    433   -291    -96       C  
ATOM    484  CE  LYS A  60      12.004  -7.493  81.481  1.00 49.52           C  
ANISOU  484  CE  LYS A  60     7371   5355   6091    468   -309    -67       C  
ATOM    485  NZ  LYS A  60      12.075  -6.165  82.173  1.00 51.98           N  
ANISOU  485  NZ  LYS A  60     7657   5670   6423    454   -316    -48       N  
ATOM    486  N   ASP A  61       6.975  -5.504  81.450  1.00 27.19           N  
ANISOU  486  N   ASP A  61     4502   2578   3253    340   -227   -103       N  
ATOM    487  CA  ASP A  61       6.946  -4.231  82.150  1.00 32.79           C  
ANISOU  487  CA  ASP A  61     5194   3283   3981    333   -226    -84       C  
ATOM    488  C   ASP A  61       5.661  -3.451  81.848  1.00 34.83           C  
ANISOU  488  C   ASP A  61     5422   3572   4240    312   -199    -84       C  
ATOM    489  O   ASP A  61       5.553  -2.272  82.188  1.00 34.11           O  
ANISOU  489  O   ASP A  61     5310   3485   4165    310   -192    -66       O  
ATOM    490  CB  ASP A  61       8.182  -3.400  81.783  1.00 36.49           C  
ANISOU  490  CB  ASP A  61     5623   3767   4473    366   -241    -57       C  
ATOM    491  CG  ASP A  61       9.468  -3.976  82.363  1.00 49.50           C  
ANISOU  491  CG  ASP A  61     7301   5385   6122    384   -269    -52       C  
ATOM    492  OD1 ASP A  61       9.451  -4.433  83.534  1.00 41.08           O  
ANISOU  492  OD1 ASP A  61     6285   4277   5047    366   -278    -59       O  
ATOM    493  OD2 ASP A  61      10.499  -3.967  81.651  1.00 50.74           O  
ANISOU  493  OD2 ASP A  61     7429   5562   6288    417   -281    -39       O  
ATOM    494  N   LEU A  62       4.685  -4.118  81.230  1.00 28.67           N  
ANISOU  494  N   LEU A  62     4641   2814   3440    297   -183   -104       N  
ATOM    495  CA  LEU A  62       3.462  -3.454  80.785  1.00 31.17           C  
ANISOU  495  CA  LEU A  62     4921   3170   3753    282   -158   -102       C  
ATOM    496  C   LEU A  62       2.211  -4.048  81.433  1.00 32.08           C  
ANISOU  496  C   LEU A  62     5072   3271   3845    241   -143   -125       C  
ATOM    497  O   LEU A  62       2.050  -5.275  81.538  1.00 31.39           O  
ANISOU  497  O   LEU A  62     5026   3166   3734    225   -147   -150       O  
ATOM    498  CB  LEU A  62       3.346  -3.517  79.257  1.00 30.50           C  
ANISOU  498  CB  LEU A  62     4786   3139   3663    300   -150   -102       C  
ATOM    499  CG  LEU A  62       4.545  -2.898  78.527  1.00 28.79           C  
ANISOU  499  CG  LEU A  62     4531   2940   3470    340   -162    -80       C  
ATOM    500  CD1 LEU A  62       4.483  -3.157  77.008  1.00 28.20           C  
ANISOU  500  CD1 LEU A  62     4414   2915   3388    357   -155    -83       C  
ATOM    501  CD2 LEU A  62       4.627  -1.415  78.813  1.00 30.68           C  
ANISOU  501  CD2 LEU A  62     4739   3186   3733    349   -155    -53       C  
ATOM    502  N   PHE A  63       1.331  -3.155  81.861  1.00 25.73           N  
ANISOU  502  N   PHE A  63     4254   2477   3046    225   -125   -116       N  
ATOM    503  CA  PHE A  63       0.171  -3.512  82.673  1.00 30.13           C  
ANISOU  503  CA  PHE A  63     4844   3019   3585    186   -111   -134       C  
ATOM    504  C   PHE A  63      -1.100  -2.862  82.150  1.00 33.22           C  
ANISOU  504  C   PHE A  63     5190   3462   3971    176    -83   -128       C  
ATOM    505  O   PHE A  63      -1.230  -1.642  82.230  1.00 31.08           O  
ANISOU  505  O   PHE A  63     4888   3204   3719    189    -71   -104       O  
ATOM    506  CB  PHE A  63       0.380  -3.072  84.124  1.00 32.18           C  
ANISOU  506  CB  PHE A  63     5144   3225   3856    174   -116   -127       C  
ATOM    507  CG  PHE A  63       1.553  -3.719  84.788  1.00 29.74           C  
ANISOU  507  CG  PHE A  63     4882   2867   3550    181   -144   -131       C  
ATOM    508  CD1 PHE A  63       2.838  -3.228  84.591  1.00 33.60           C  
ANISOU  508  CD1 PHE A  63     5353   3353   4060    214   -162   -110       C  
ATOM    509  CD2 PHE A  63       1.376  -4.810  85.620  1.00 33.93           C  
ANISOU  509  CD2 PHE A  63     5475   3356   4062    156   -150   -155       C  
ATOM    510  CE1 PHE A  63       3.924  -3.825  85.211  1.00 34.44           C  
ANISOU  510  CE1 PHE A  63     5499   3419   4167    222   -188   -112       C  
ATOM    511  CE2 PHE A  63       2.452  -5.410  86.235  1.00 32.11           C  
ANISOU  511  CE2 PHE A  63     5286   3081   3832    166   -175   -156       C  
ATOM    512  CZ  PHE A  63       3.725  -4.920  86.035  1.00 32.51           C  
ANISOU  512  CZ  PHE A  63     5316   3134   3904    200   -194   -134       C  
ATOM    513  N   PRO A  64      -2.052  -3.670  81.648  1.00 31.18           N  
ANISOU  513  N   PRO A  64     4929   3233   3684    152    -71   -150       N  
ATOM    514  CA  PRO A  64      -3.327  -3.140  81.143  1.00 36.06           C  
ANISOU  514  CA  PRO A  64     5502   3908   4292    140    -45   -145       C  
ATOM    515  C   PRO A  64      -3.959  -2.162  82.127  1.00 36.21           C  
ANISOU  515  C   PRO A  64     5523   3913   4323    132    -28   -130       C  
ATOM    516  O   PRO A  64      -4.090  -2.484  83.300  1.00 34.19           O  
ANISOU  516  O   PRO A  64     5319   3608   4064    107    -31   -142       O  
ATOM    517  CB  PRO A  64      -4.178  -4.401  80.971  1.00 34.99           C  
ANISOU  517  CB  PRO A  64     5389   3785   4119    102    -40   -178       C  
ATOM    518  CG  PRO A  64      -3.178  -5.451  80.630  1.00 30.66           C  
ANISOU  518  CG  PRO A  64     4873   3211   3564    110    -60   -194       C  
ATOM    519  CD  PRO A  64      -1.953  -5.128  81.455  1.00 30.79           C  
ANISOU  519  CD  PRO A  64     4920   3171   3609    134    -81   -180       C  
ATOM    520  N   TYR A  65      -4.315  -0.974  81.640  1.00 32.91           N  
ANISOU  520  N   TYR A  65     5051   3535   3918    154    -10   -103       N  
ATOM    521  CA  TYR A  65      -4.671   0.161  82.492  1.00 32.94           C  
ANISOU  521  CA  TYR A  65     5055   3522   3938    156      8    -82       C  
ATOM    522  C   TYR A  65      -5.897  -0.080  83.366  1.00 35.11           C  
ANISOU  522  C   TYR A  65     5355   3789   4195    119     26    -95       C  
ATOM    523  O   TYR A  65      -5.832   0.105  84.573  1.00 34.75           O  
ANISOU  523  O   TYR A  65     5354   3692   4158    104     26    -96       O  
ATOM    524  CB  TYR A  65      -4.888   1.418  81.629  1.00 32.91           C  
ANISOU  524  CB  TYR A  65     4988   3569   3949    190     28    -50       C  
ATOM    525  CG  TYR A  65      -5.515   2.590  82.356  1.00 32.32           C  
ANISOU  525  CG  TYR A  65     4909   3486   3885    193     56    -28       C  
ATOM    526  CD1 TYR A  65      -4.841   3.234  83.386  1.00 26.62           C  
ANISOU  526  CD1 TYR A  65     4225   2706   3183    195     53    -17       C  
ATOM    527  CD2 TYR A  65      -6.767   3.066  82.004  1.00 36.63           C  
ANISOU  527  CD2 TYR A  65     5415   4084   4419    194     86    -16       C  
ATOM    528  CE1 TYR A  65      -5.395   4.301  84.051  1.00 33.51           C  
ANISOU  528  CE1 TYR A  65     5100   3568   4066    197     81      4       C  
ATOM    529  CE2 TYR A  65      -7.340   4.144  82.678  1.00 40.07           C  
ANISOU  529  CE2 TYR A  65     5851   4510   4865    200    114      6       C  
ATOM    530  CZ  TYR A  65      -6.643   4.756  83.699  1.00 38.48           C  
ANISOU  530  CZ  TYR A  65     5691   4245   4683    201    113     15       C  
ATOM    531  OH  TYR A  65      -7.179   5.827  84.385  1.00 35.74           O  
ANISOU  531  OH  TYR A  65     5350   3884   4345    206    144     37       O  
ATOM    532  N   LYS A  66      -7.013  -0.493  82.784  1.00 34.84           N  
ANISOU  532  N   LYS A  66     5294   3808   4137    101     41   -106       N  
ATOM    533  CA  LYS A  66      -8.223  -0.580  83.584  1.00 38.22           C  
ANISOU  533  CA  LYS A  66     5737   4235   4548     68     61   -115       C  
ATOM    534  C   LYS A  66      -8.106  -1.739  84.568  1.00 38.35           C  
ANISOU  534  C   LYS A  66     5826   4196   4551     29     46   -148       C  
ATOM    535  O   LYS A  66      -8.577  -1.638  85.700  1.00 44.83           O  
ANISOU  535  O   LYS A  66     6682   4980   5370      7     55   -152       O  
ATOM    536  CB  LYS A  66      -9.459  -0.721  82.698  1.00 47.18           C  
ANISOU  536  CB  LYS A  66     6821   5449   5657     57     81   -117       C  
ATOM    537  CG  LYS A  66      -9.180  -1.260  81.317  1.00 62.49           C  
ANISOU  537  CG  LYS A  66     8723   7437   7583     67     70   -124       C  
ATOM    538  CD  LYS A  66     -10.310  -0.888  80.367  1.00 73.61           C  
ANISOU  538  CD  LYS A  66    10064   8932   8974     69     93   -111       C  
ATOM    539  CE  LYS A  66     -11.639  -1.460  80.843  1.00 79.43           C  
ANISOU  539  CE  LYS A  66    10810   9692   9680     23    109   -131       C  
ATOM    540  NZ  LYS A  66     -12.775  -1.036  79.975  1.00 83.14           N  
ANISOU  540  NZ  LYS A  66    11208  10251  10129     26    132   -115       N  
ATOM    541  N   GLU A  67      -7.443  -2.815  84.141  1.00 37.83           N  
ANISOU  541  N   GLU A  67     5782   4119   4474     24     23   -169       N  
ATOM    542  CA  GLU A  67      -7.208  -3.973  84.999  1.00 38.75           C  
ANISOU  542  CA  GLU A  67     5969   4179   4575     -7      8   -199       C  
ATOM    543  C   GLU A  67      -6.350  -3.610  86.208  1.00 44.80           C  
ANISOU  543  C   GLU A  67     6782   4873   5365      1     -5   -191       C  
ATOM    544  O   GLU A  67      -6.611  -4.065  87.315  1.00 46.31           O  
ANISOU  544  O   GLU A  67     7028   5019   5548    -29     -6   -207       O  
ATOM    545  CB  GLU A  67      -6.544  -5.106  84.205  1.00 50.92           C  
ANISOU  545  CB  GLU A  67     7524   5723   6102     -5    -10   -219       C  
ATOM    546  CG  GLU A  67      -6.310  -6.387  85.011  1.00 59.75           C  
ANISOU  546  CG  GLU A  67     8719   6783   7201    -35    -23   -250       C  
ATOM    547  CD  GLU A  67      -5.694  -7.518  84.188  1.00 70.48           C  
ANISOU  547  CD  GLU A  67    10094   8143   8542    -31    -37   -269       C  
ATOM    548  OE1 GLU A  67      -5.425  -7.314  82.986  1.00 70.46           O  
ANISOU  548  OE1 GLU A  67    10042   8187   8543     -7    -38   -259       O  
ATOM    549  OE2 GLU A  67      -5.470  -8.613  84.747  1.00 72.78           O  
ANISOU  549  OE2 GLU A  67    10449   8388   8816    -51    -45   -294       O  
ATOM    550  N   TYR A  68      -5.338  -2.774  85.998  1.00 39.29           N  
ANISOU  550  N   TYR A  68     6063   4168   4695     39    -16   -165       N  
ATOM    551  CA  TYR A  68      -4.394  -2.437  87.068  1.00 36.93           C  
ANISOU  551  CA  TYR A  68     5807   3807   4418     45    -31   -156       C  
ATOM    552  C   TYR A  68      -4.536  -1.019  87.613  1.00 37.60           C  
ANISOU  552  C   TYR A  68     5876   3884   4524     55    -14   -128       C  
ATOM    553  O   TYR A  68      -3.701  -0.566  88.403  1.00 37.55           O  
ANISOU  553  O   TYR A  68     5899   3833   4536     61    -26   -117       O  
ATOM    554  CB  TYR A  68      -2.959  -2.666  86.579  1.00 34.51           C  
ANISOU  554  CB  TYR A  68     5500   3488   4123     76    -59   -150       C  
ATOM    555  CG  TYR A  68      -2.594  -4.132  86.527  1.00 37.77           C  
ANISOU  555  CG  TYR A  68     5955   3880   4515     65    -78   -178       C  
ATOM    556  CD1 TYR A  68      -2.090  -4.780  87.653  1.00 38.07           C  
ANISOU  556  CD1 TYR A  68     6058   3856   4549     50    -95   -190       C  
ATOM    557  CD2 TYR A  68      -2.778  -4.876  85.371  1.00 43.44           C  
ANISOU  557  CD2 TYR A  68     6650   4638   5215     67    -77   -191       C  
ATOM    558  CE1 TYR A  68      -1.768  -6.117  87.624  1.00 35.00           C  
ANISOU  558  CE1 TYR A  68     5712   3446   4140     42   -108   -214       C  
ATOM    559  CE2 TYR A  68      -2.454  -6.226  85.333  1.00 44.27           C  
ANISOU  559  CE2 TYR A  68     6801   4721   5300     57    -90   -217       C  
ATOM    560  CZ  TYR A  68      -1.946  -6.834  86.465  1.00 38.78           C  
ANISOU  560  CZ  TYR A  68     6171   3962   4602     46   -105   -228       C  
ATOM    561  OH  TYR A  68      -1.622  -8.163  86.438  1.00 42.34           O  
ANISOU  561  OH  TYR A  68     6670   4388   5031     39   -115   -251       O  
ATOM    562  N   LYS A  69      -5.603  -0.330  87.211  1.00 37.29           N  
ANISOU  562  N   LYS A  69     5794   3891   4483     57     15   -116       N  
ATOM    563  CA  LYS A  69      -5.838   1.054  87.620  1.00 40.99           C  
ANISOU  563  CA  LYS A  69     6246   4357   4970     70     38    -88       C  
ATOM    564  C   LYS A  69      -5.979   1.225  89.129  1.00 43.60           C  
ANISOU  564  C   LYS A  69     6635   4627   5305     43     43    -91       C  
ATOM    565  O   LYS A  69      -5.465   2.172  89.715  1.00 41.69           O  
ANISOU  565  O   LYS A  69     6405   4354   5082     53     47    -71       O  
ATOM    566  CB  LYS A  69      -7.085   1.590  86.921  1.00 45.39           C  
ANISOU  566  CB  LYS A  69     6749   4978   5519     76     70    -76       C  
ATOM    567  CG  LYS A  69      -7.622   2.892  87.479  1.00 50.22           C  
ANISOU  567  CG  LYS A  69     7353   5585   6144     85    102    -49       C  
ATOM    568  CD  LYS A  69      -8.717   3.430  86.573  1.00 49.35           C  
ANISOU  568  CD  LYS A  69     7179   5546   6025    101    132    -33       C  
ATOM    569  CE  LYS A  69      -9.422   4.631  87.184  1.00 52.23           C  
ANISOU  569  CE  LYS A  69     7540   5906   6399    110    169     -7       C  
ATOM    570  NZ  LYS A  69     -10.516   5.111  86.292  1.00 59.25           N  
ANISOU  570  NZ  LYS A  69     8366   6871   7278    129    198     11       N  
ATOM    571  N   ASP A  70      -6.670   0.304  89.775  1.00 44.34           N  
ANISOU  571  N   ASP A  70     6767   4703   5378      7     43   -118       N  
ATOM    572  CA  ASP A  70      -6.924   0.493  91.186  1.00 42.74           C  
ANISOU  572  CA  ASP A  70     6616   4445   5177    -20     50   -121       C  
ATOM    573  C   ASP A  70      -5.687   0.139  91.998  1.00 43.52           C  
ANISOU  573  C   ASP A  70     6770   4481   5285    -24     19   -126       C  
ATOM    574  O   ASP A  70      -5.590   0.480  93.172  1.00 52.51           O  
ANISOU  574  O   ASP A  70     7952   5570   6430    -41     22   -124       O  
ATOM    575  CB  ASP A  70      -8.144  -0.323  91.606  1.00 56.69           C  
ANISOU  575  CB  ASP A  70     8405   6217   6918    -58     64   -147       C  
ATOM    576  CG  ASP A  70      -9.447   0.358  91.204  1.00 65.53           C  
ANISOU  576  CG  ASP A  70     9476   7391   8032    -56    100   -133       C  
ATOM    577  OD1 ASP A  70      -9.768   1.424  91.787  1.00 69.54           O  
ANISOU  577  OD1 ASP A  70     9983   7886   8554    -50    124   -112       O  
ATOM    578  OD2 ASP A  70     -10.119  -0.138  90.271  1.00 61.95           O  
ANISOU  578  OD2 ASP A  70     8984   6997   7560    -59    106   -143       O  
ATOM    579  N   LYS A  71      -4.729  -0.535  91.370  1.00 37.63           N  
ANISOU  579  N   LYS A  71     6020   3739   4538     -8     -9   -133       N  
ATOM    580  CA  LYS A  71      -3.475  -0.845  92.050  1.00 39.76           C  
ANISOU  580  CA  LYS A  71     6333   3956   4815     -6    -39   -134       C  
ATOM    581  C   LYS A  71      -2.432   0.265  91.855  1.00 41.04           C  
ANISOU  581  C   LYS A  71     6471   4120   5004     24    -46   -105       C  
ATOM    582  O   LYS A  71      -1.707   0.623  92.784  1.00 43.81           O  
ANISOU  582  O   LYS A  71     6856   4426   5365     18    -58    -96       O  
ATOM    583  CB  LYS A  71      -2.921  -2.181  91.561  1.00 44.29           C  
ANISOU  583  CB  LYS A  71     6923   4531   5375     -2    -66   -156       C  
ATOM    584  CG  LYS A  71      -1.667  -2.650  92.285  1.00 53.73           C  
ANISOU  584  CG  LYS A  71     8165   5676   6575      1    -97   -157       C  
ATOM    585  CD  LYS A  71      -1.263  -4.048  91.813  1.00 59.25           C  
ANISOU  585  CD  LYS A  71     8884   6373   7255      6   -117   -179       C  
ATOM    586  CE  LYS A  71      -0.021  -4.562  92.526  1.00 62.29           C  
ANISOU  586  CE  LYS A  71     9314   6710   7642     14   -148   -178       C  
ATOM    587  NZ  LYS A  71       0.341  -5.935  92.066  1.00 65.44           N  
ANISOU  587  NZ  LYS A  71     9733   7109   8022     22   -163   -198       N  
ATOM    588  N   PHE A  72      -2.365   0.820  90.652  1.00 34.15           N  
ANISOU  588  N   PHE A  72     5538   3298   4140     55    -38    -89       N  
ATOM    589  CA  PHE A  72      -1.267   1.735  90.314  1.00 30.76           C  
ANISOU  589  CA  PHE A  72     5084   2872   3732     84    -47    -63       C  
ATOM    590  C   PHE A  72      -1.723   3.170  90.082  1.00 37.16           C  
ANISOU  590  C   PHE A  72     5858   3704   4556     97    -14    -37       C  
ATOM    591  O   PHE A  72      -0.901   4.069  89.890  1.00 37.59           O  
ANISOU  591  O   PHE A  72     5897   3759   4628    117    -16    -15       O  
ATOM    592  CB  PHE A  72      -0.536   1.223  89.067  1.00 26.38           C  
ANISOU  592  CB  PHE A  72     4493   2354   3178    113    -66    -65       C  
ATOM    593  CG  PHE A  72       0.147  -0.103  89.259  1.00 31.85           C  
ANISOU  593  CG  PHE A  72     5222   3021   3859    108    -98    -86       C  
ATOM    594  CD1 PHE A  72       0.861  -0.375  90.415  1.00 34.96           C  
ANISOU  594  CD1 PHE A  72     5669   3362   4254     94   -118    -89       C  
ATOM    595  CD2 PHE A  72       0.064  -1.079  88.288  1.00 31.30           C  
ANISOU  595  CD2 PHE A  72     5136   2981   3775    117   -105   -102       C  
ATOM    596  CE1 PHE A  72       1.487  -1.592  90.586  1.00 30.24           C  
ANISOU  596  CE1 PHE A  72     5105   2740   3643     94   -145   -106       C  
ATOM    597  CE2 PHE A  72       0.688  -2.295  88.447  1.00 33.11           C  
ANISOU  597  CE2 PHE A  72     5403   3186   3992    115   -129   -120       C  
ATOM    598  CZ  PHE A  72       1.391  -2.561  89.598  1.00 36.52           C  
ANISOU  598  CZ  PHE A  72     5887   3564   4425    105   -149   -122       C  
ATOM    599  N   GLY A  73      -3.032   3.394  90.109  1.00 37.64           N  
ANISOU  599  N   GLY A  73     5908   3784   4608     86     17    -38       N  
ATOM    600  CA  GLY A  73      -3.574   4.693  89.767  1.00 31.71           C  
ANISOU  600  CA  GLY A  73     5121   3060   3868    105     51    -11       C  
ATOM    601  C   GLY A  73      -3.646   5.690  90.906  1.00 36.18           C  
ANISOU  601  C   GLY A  73     5722   3581   4444     91     72      4       C  
ATOM    602  O   GLY A  73      -4.409   6.649  90.844  1.00 38.94           O  
ANISOU  602  O   GLY A  73     6053   3946   4797    101    108     23       O  
ATOM    603  N   LYS A  74      -2.855   5.474  91.946  1.00 42.69           N  
ANISOU  603  N   LYS A  74     6599   4351   5272     70     50     -3       N  
ATOM    604  CA  LYS A  74      -2.872   6.369  93.100  1.00 44.57           C  
ANISOU  604  CA  LYS A  74     6877   4541   5516     52     69      9       C  
ATOM    605  C   LYS A  74      -1.983   7.587  92.845  1.00 43.82           C  
ANISOU  605  C   LYS A  74     6766   4445   5438     72     75     37       C  
ATOM    606  O   LYS A  74      -1.025   7.509  92.070  1.00 41.28           O  
ANISOU  606  O   LYS A  74     6418   4145   5123     94     52     41       O  
ATOM    607  CB  LYS A  74      -2.416   5.628  94.365  1.00 52.57           C  
ANISOU  607  CB  LYS A  74     7954   5496   6523     17     42    -10       C  
ATOM    608  CG  LYS A  74      -3.158   4.312  94.665  1.00 63.38           C  
ANISOU  608  CG  LYS A  74     9347   6861   7873     -6     33    -40       C  
ATOM    609  CD  LYS A  74      -4.640   4.376  94.286  1.00 72.02           C  
ANISOU  609  CD  LYS A  74    10414   7991   8958     -7     67    -43       C  
ATOM    610  CE  LYS A  74      -5.469   3.285  94.964  1.00 76.68           C  
ANISOU  610  CE  LYS A  74    11043   8564   9528    -42     65    -72       C  
ATOM    611  NZ  LYS A  74      -5.124   3.098  96.401  1.00 76.51           N  
ANISOU  611  NZ  LYS A  74    11072   8493   9506    -73     53    -79       N  
ATOM    612  N   SER A  75      -2.307   8.710  93.485  1.00 31.65           N  
ANISOU  612  N   SER A  75     5245   2880   3903     65    109     54       N  
ATOM    613  CA  SER A  75      -1.517   9.931  93.342  1.00 35.04           C  
ANISOU  613  CA  SER A  75     5667   3302   4345     79    120     80       C  
ATOM    614  C   SER A  75      -0.080   9.720  93.799  1.00 33.59           C  
ANISOU  614  C   SER A  75     5510   3089   4165     65     82     76       C  
ATOM    615  O   SER A  75       0.189   8.897  94.665  1.00 35.64           O  
ANISOU  615  O   SER A  75     5811   3315   4417     38     55     58       O  
ATOM    616  CB  SER A  75      -2.141  11.088  94.121  1.00 46.07           C  
ANISOU  616  CB  SER A  75     7094   4669   5744     68    165     97       C  
ATOM    617  OG  SER A  75      -3.064  11.795  93.307  1.00 62.29           O  
ANISOU  617  OG  SER A  75     9106   6763   7800     99    206    116       O  
ATOM    618  N   ASN A  76       0.835  10.474  93.197  1.00 32.31           N  
ANISOU  618  N   ASN A  76     5323   2941   4012     84     79     94       N  
ATOM    619  CA  ASN A  76       2.262  10.298  93.400  1.00 31.13           C  
ANISOU  619  CA  ASN A  76     5185   2778   3866     76     42     94       C  
ATOM    620  C   ASN A  76       2.910  11.641  93.112  1.00 32.57           C  
ANISOU  620  C   ASN A  76     5355   2963   4056     85     61    119       C  
ATOM    621  O   ASN A  76       2.486  12.357  92.199  1.00 33.18           O  
ANISOU  621  O   ASN A  76     5394   3072   4139    114     91    134       O  
ATOM    622  CB  ASN A  76       2.796   9.176  92.483  1.00 30.25           C  
ANISOU  622  CB  ASN A  76     5038   2702   3753     98      4     81       C  
ATOM    623  CG  ASN A  76       4.231   8.788  92.782  1.00 36.24           C  
ANISOU  623  CG  ASN A  76     5810   3448   4513     92    -38     79       C  
ATOM    624  OD1 ASN A  76       5.138   9.623  92.738  1.00 39.43           O  
ANISOU  624  OD1 ASN A  76     6207   3851   4923     93    -40     96       O  
ATOM    625  ND2 ASN A  76       4.450   7.501  93.055  1.00 30.92           N  
ANISOU  625  ND2 ASN A  76     5153   2764   3830     85    -72     59       N  
ATOM    626  N   LYS A  77       3.907  12.025  93.901  1.00 24.87           N  
ANISOU  626  N   LYS A  77     4414   1955   3081     60     47    124       N  
ATOM    627  CA  LYS A  77       4.485  13.353  93.719  1.00 26.32           C  
ANISOU  627  CA  LYS A  77     4594   2139   3270     61     70    147       C  
ATOM    628  C   LYS A  77       5.560  13.436  92.625  1.00 28.36           C  
ANISOU  628  C   LYS A  77     4804   2437   3535     88     47    155       C  
ATOM    629  O   LYS A  77       6.036  14.524  92.312  1.00 34.00           O  
ANISOU  629  O   LYS A  77     5510   3156   4252     92     67    173       O  
ATOM    630  CB  LYS A  77       5.046  13.865  95.045  1.00 39.82           C  
ANISOU  630  CB  LYS A  77     6323   3833   4972     16     67    145       C  
ATOM    631  CG  LYS A  77       4.047  14.764  95.772  1.00 56.32           C  
ANISOU  631  CG  LYS A  77     8419   5920   7059     -1    114    150       C  
ATOM    632  CD  LYS A  77       3.368  15.722  94.787  1.00 62.51           C  
ANISOU  632  CD  LYS A  77     9192   6708   7849     34    161    171       C  
ATOM    633  CE  LYS A  77       1.964  16.140  95.230  1.00 67.42           C  
ANISOU  633  CE  LYS A  77     9818   7329   8468     33    205    172       C  
ATOM    634  NZ  LYS A  77       1.908  16.636  96.631  1.00 68.87           N  
ANISOU  634  NZ  LYS A  77    10018   7506   8644     -9    215    166       N  
ATOM    635  N   ARG A  78       5.935  12.303  92.039  1.00 27.40           N  
ANISOU  635  N   ARG A  78     4653   2343   3414    106      9    141       N  
ATOM    636  CA  ARG A  78       6.935  12.315  90.963  1.00 30.64           C  
ANISOU  636  CA  ARG A  78     5017   2793   3831    133    -12    148       C  
ATOM    637  C   ARG A  78       6.474  13.254  89.866  1.00 33.89           C  
ANISOU  637  C   ARG A  78     5388   3237   4250    164     26    165       C  
ATOM    638  O   ARG A  78       5.296  13.264  89.516  1.00 29.12           O  
ANISOU  638  O   ARG A  78     4772   2646   3646    179     53    165       O  
ATOM    639  CB  ARG A  78       7.169  10.914  90.390  1.00 35.16           C  
ANISOU  639  CB  ARG A  78     5565   3392   4403    153    -50    131       C  
ATOM    640  CG  ARG A  78       8.024  10.014  91.264  1.00 43.95           C  
ANISOU  640  CG  ARG A  78     6710   4480   5509    132    -93    119       C  
ATOM    641  CD  ARG A  78       9.378  10.636  91.569  1.00 44.29           C  
ANISOU  641  CD  ARG A  78     6756   4520   5552    118   -110    133       C  
ATOM    642  NE  ARG A  78      10.373  10.491  90.503  1.00 44.56           N  
ANISOU  642  NE  ARG A  78     6743   4596   5593    149   -132    139       N  
ATOM    643  CZ  ARG A  78      11.109   9.397  90.306  1.00 37.10           C  
ANISOU  643  CZ  ARG A  78     5786   3665   4646    163   -172    130       C  
ATOM    644  NH1 ARG A  78      10.946   8.319  91.068  1.00 39.37           N  
ANISOU  644  NH1 ARG A  78     6108   3928   4924    151   -194    115       N  
ATOM    645  NH2 ARG A  78      11.997   9.370  89.331  1.00 46.62           N  
ANISOU  645  NH2 ARG A  78     6948   4909   5858    191   -188    138       N  
ATOM    646  N   LYS A  79       7.401  14.069  89.367  1.00 27.00           N  
ANISOU  646  N   LYS A  79     4497   2378   3382    172     27    181       N  
ATOM    647  CA  LYS A  79       7.072  15.133  88.448  1.00 30.38           C  
ANISOU  647  CA  LYS A  79     4896   2831   3817    198     66    199       C  
ATOM    648  C   LYS A  79       6.369  14.572  87.225  1.00 30.26           C  
ANISOU  648  C   LYS A  79     4829   2862   3806    239     68    195       C  
ATOM    649  O   LYS A  79       6.860  13.648  86.588  1.00 31.32           O  
ANISOU  649  O   LYS A  79     4934   3025   3943    254     33    184       O  
ATOM    650  CB  LYS A  79       8.327  15.906  88.028  1.00 40.85           C  
ANISOU  650  CB  LYS A  79     6207   4169   5146    200     60    213       C  
ATOM    651  CG  LYS A  79       8.747  16.994  89.012  1.00 45.69           C  
ANISOU  651  CG  LYS A  79     6867   4740   5752    162     81    225       C  
ATOM    652  CD  LYS A  79      10.077  17.615  88.601  1.00 49.31           C  
ANISOU  652  CD  LYS A  79     7309   5214   6211    158     70    235       C  
ATOM    653  CE  LYS A  79      10.526  18.683  89.580  1.00 51.08           C  
ANISOU  653  CE  LYS A  79     7584   5400   6425    115     91    245       C  
ATOM    654  NZ  LYS A  79      11.801  19.303  89.131  1.00 54.94           N  
ANISOU  654  NZ  LYS A  79     8056   5908   6912    108     82    255       N  
ATOM    655  N   GLY A  80       5.208  15.136  86.921  1.00 29.35           N  
ANISOU  655  N   GLY A  80     4705   2757   3691    255    110    205       N  
ATOM    656  CA  GLY A  80       4.439  14.705  85.770  1.00 28.99           C  
ANISOU  656  CA  GLY A  80     4610   2759   3646    290    115    204       C  
ATOM    657  C   GLY A  80       3.454  13.587  86.055  1.00 28.63           C  
ANISOU  657  C   GLY A  80     4569   2716   3593    283    106    184       C  
ATOM    658  O   GLY A  80       2.574  13.336  85.243  1.00 25.78           O  
ANISOU  658  O   GLY A  80     4171   2393   3228    306    118    184       O  
ATOM    659  N   PHE A  81       3.598  12.891  87.184  1.00 24.03           N  
ANISOU  659  N   PHE A  81     4031   2094   3005    249     83    167       N  
ATOM    660  CA  PHE A  81       2.743  11.726  87.411  1.00 23.30           C  
ANISOU  660  CA  PHE A  81     3945   2004   2903    240     72    145       C  
ATOM    661  C   PHE A  81       1.247  12.055  87.484  1.00 26.23           C  
ANISOU  661  C   PHE A  81     4314   2384   3269    244    113    150       C  
ATOM    662  O   PHE A  81       0.436  11.435  86.781  1.00 24.46           O  
ANISOU  662  O   PHE A  81     4057   2199   3039    258    114    142       O  
ATOM    663  CB  PHE A  81       3.146  10.979  88.680  1.00 27.52           C  
ANISOU  663  CB  PHE A  81     4532   2491   3432    204     43    127       C  
ATOM    664  CG  PHE A  81       2.527   9.617  88.777  1.00 21.48           C  
ANISOU  664  CG  PHE A  81     3774   1731   2657    196     24    102       C  
ATOM    665  CD1 PHE A  81       1.267   9.454  89.332  1.00 25.88           C  
ANISOU  665  CD1 PHE A  81     4351   2276   3205    180     48     95       C  
ATOM    666  CD2 PHE A  81       3.200   8.497  88.292  1.00 24.17           C  
ANISOU  666  CD2 PHE A  81     4102   2087   2995    204    -14     87       C  
ATOM    667  CE1 PHE A  81       0.687   8.208  89.409  1.00 28.16           C  
ANISOU  667  CE1 PHE A  81     4647   2570   3482    169     32     70       C  
ATOM    668  CE2 PHE A  81       2.633   7.250  88.362  1.00 21.21           C  
ANISOU  668  CE2 PHE A  81     3737   1713   2608    195    -28     63       C  
ATOM    669  CZ  PHE A  81       1.368   7.096  88.918  1.00 28.57           C  
ANISOU  669  CZ  PHE A  81     4689   2634   3530    176     -5     54       C  
ATOM    670  N   ASN A  82       0.872  13.022  88.322  1.00 23.41           N  
ANISOU  670  N   ASN A  82     3990   1992   2912    230    146    164       N  
ATOM    671  CA  ASN A  82      -0.544  13.348  88.471  1.00 26.11           C  
ANISOU  671  CA  ASN A  82     4332   2341   3249    234    187    171       C  
ATOM    672  C   ASN A  82      -1.121  13.957  87.198  1.00 33.12           C  
ANISOU  672  C   ASN A  82     5163   3284   4138    277    216    191       C  
ATOM    673  O   ASN A  82      -2.305  13.787  86.904  1.00 31.44           O  
ANISOU  673  O   ASN A  82     4926   3102   3917    288    237    192       O  
ATOM    674  CB  ASN A  82      -0.758  14.272  89.675  1.00 26.35           C  
ANISOU  674  CB  ASN A  82     4415   2318   3279    211    219    182       C  
ATOM    675  CG  ASN A  82      -0.440  13.565  90.985  1.00 28.78           C  
ANISOU  675  CG  ASN A  82     4778   2574   3581    167    192    161       C  
ATOM    676  OD1 ASN A  82      -0.575  12.343  91.078  1.00 28.54           O  
ANISOU  676  OD1 ASN A  82     4749   2550   3545    156    161    138       O  
ATOM    677  ND2 ASN A  82      -0.011  14.318  91.994  1.00 34.76           N  
ANISOU  677  ND2 ASN A  82     5585   3282   4340    141    205    169       N  
ATOM    678  N   GLU A  83      -0.280  14.629  86.420  1.00 26.39           N  
ANISOU  678  N   GLU A  83     4286   2448   3295    299    216    206       N  
ATOM    679  CA  GLU A  83      -0.714  15.105  85.111  1.00 24.84           C  
ANISOU  679  CA  GLU A  83     4032   2306   3098    342    238    224       C  
ATOM    680  C   GLU A  83      -0.920  13.934  84.166  1.00 27.34           C  
ANISOU  680  C   GLU A  83     4305   2674   3411    353    208    207       C  
ATOM    681  O   GLU A  83      -1.796  13.966  83.308  1.00 26.92           O  
ANISOU  681  O   GLU A  83     4207   2670   3351    378    227    215       O  
ATOM    682  CB  GLU A  83       0.307  16.076  84.511  1.00 29.36           C  
ANISOU  682  CB  GLU A  83     4594   2882   3681    361    244    244       C  
ATOM    683  CG  GLU A  83       0.356  17.433  85.207  1.00 31.76           C  
ANISOU  683  CG  GLU A  83     4937   3144   3987    355    286    266       C  
ATOM    684  CD  GLU A  83       1.193  17.410  86.476  1.00 38.46           C  
ANISOU  684  CD  GLU A  83     5844   3932   4836    311    268    255       C  
ATOM    685  OE1 GLU A  83       1.455  16.310  87.011  1.00 38.61           O  
ANISOU  685  OE1 GLU A  83     5879   3939   4854    285    228    231       O  
ATOM    686  OE2 GLU A  83       1.595  18.496  86.940  1.00 38.69           O  
ANISOU  686  OE2 GLU A  83     5906   3927   4866    301    295    271       O  
ATOM    687  N   GLY A  84      -0.092  12.905  84.310  1.00 26.78           N  
ANISOU  687  N   GLY A  84     4244   2590   3339    335    163    184       N  
ATOM    688  CA  GLY A  84      -0.254  11.695  83.519  1.00 21.01           C  
ANISOU  688  CA  GLY A  84     3482   1900   2601    341    135    164       C  
ATOM    689  C   GLY A  84      -1.568  11.005  83.836  1.00 25.53           C  
ANISOU  689  C   GLY A  84     4058   2484   3160    325    145    150       C  
ATOM    690  O   GLY A  84      -2.265  10.527  82.938  1.00 24.38           O  
ANISOU  690  O   GLY A  84     3871   2389   3004    339    147    146       O  
ATOM    691  N   LEU A  85      -1.917  10.938  85.121  1.00 22.90           N  
ANISOU  691  N   LEU A  85     3775   2104   2823    295    151    142       N  
ATOM    692  CA  LEU A  85      -3.182  10.324  85.496  1.00 27.58           C  
ANISOU  692  CA  LEU A  85     4373   2705   3400    277    163    129       C  
ATOM    693  C   LEU A  85      -4.332  11.091  84.854  1.00 28.26           C  
ANISOU  693  C   LEU A  85     4417   2839   3482    304    205    151       C  
ATOM    694  O   LEU A  85      -5.305  10.485  84.403  1.00 29.68           O  
ANISOU  694  O   LEU A  85     4568   3063   3647    304    209    143       O  
ATOM    695  CB  LEU A  85      -3.361  10.294  87.009  1.00 28.88           C  
ANISOU  695  CB  LEU A  85     4600   2809   3564    242    167    120       C  
ATOM    696  CG  LEU A  85      -2.428   9.394  87.804  1.00 27.90           C  
ANISOU  696  CG  LEU A  85     4522   2639   3440    212    126     97       C  
ATOM    697  CD1 LEU A  85      -2.775   9.535  89.292  1.00 30.79           C  
ANISOU  697  CD1 LEU A  85     4948   2948   3804    178    138     92       C  
ATOM    698  CD2 LEU A  85      -2.528   7.946  87.350  1.00 25.13           C  
ANISOU  698  CD2 LEU A  85     4161   2311   3077    204     95     69       C  
ATOM    699  N   TRP A  86      -4.212  12.417  84.813  1.00 26.72           N  
ANISOU  699  N   TRP A  86     4218   2637   3297    327    237    181       N  
ATOM    700  CA  TRP A  86      -5.255  13.251  84.199  1.00 29.94           C  
ANISOU  700  CA  TRP A  86     4586   3089   3700    359    280    207       C  
ATOM    701  C   TRP A  86      -5.379  12.935  82.716  1.00 32.08           C  
ANISOU  701  C   TRP A  86     4792   3430   3965    388    271    210       C  
ATOM    702  O   TRP A  86      -6.489  12.731  82.201  1.00 33.66           O  
ANISOU  702  O   TRP A  86     4954   3683   4152    398    287    213       O  
ATOM    703  CB  TRP A  86      -4.980  14.748  84.375  1.00 32.37           C  
ANISOU  703  CB  TRP A  86     4907   3372   4019    380    318    238       C  
ATOM    704  CG  TRP A  86      -6.151  15.590  83.833  1.00 32.21           C  
ANISOU  704  CG  TRP A  86     4850   3396   3992    416    367    268       C  
ATOM    705  CD1 TRP A  86      -7.253  16.015  84.530  1.00 40.85           C  
ANISOU  705  CD1 TRP A  86     5959   4481   5079    415    406    280       C  
ATOM    706  CD2 TRP A  86      -6.331  16.044  82.481  1.00 33.54           C  
ANISOU  706  CD2 TRP A  86     4959   3627   4160    460    380    289       C  
ATOM    707  NE1 TRP A  86      -8.101  16.722  83.694  1.00 34.75           N  
ANISOU  707  NE1 TRP A  86     5139   3763   4300    458    443    309       N  
ATOM    708  CE2 TRP A  86      -7.559  16.761  82.439  1.00 36.76           C  
ANISOU  708  CE2 TRP A  86     5348   4062   4558    486    429    315       C  
ATOM    709  CE3 TRP A  86      -5.583  15.937  81.309  1.00 34.57           C  
ANISOU  709  CE3 TRP A  86     5050   3792   4294    481    358    290       C  
ATOM    710  CZ2 TRP A  86      -8.047  17.330  81.268  1.00 42.52           C  
ANISOU  710  CZ2 TRP A  86     6020   4854   5282    531    453    342       C  
ATOM    711  CZ3 TRP A  86      -6.065  16.528  80.139  1.00 37.97           C  
ANISOU  711  CZ3 TRP A  86     5424   4282   4720    524    383    316       C  
ATOM    712  CH2 TRP A  86      -7.279  17.221  80.135  1.00 35.95           C  
ANISOU  712  CH2 TRP A  86     5151   4054   4455    550    429    342       C  
ATOM    713  N   GLU A  87      -4.234  12.872  82.039  1.00 23.81           N  
ANISOU  713  N   GLU A  87     3732   2386   2928    399    245    208       N  
ATOM    714  CA  GLU A  87      -4.217  12.653  80.587  1.00 23.38           C  
ANISOU  714  CA  GLU A  87     3617   2396   2869    427    236    212       C  
ATOM    715  C   GLU A  87      -4.744  11.279  80.172  1.00 25.02           C  
ANISOU  715  C   GLU A  87     3805   2641   3060    410    211    185       C  
ATOM    716  O   GLU A  87      -5.483  11.177  79.183  1.00 29.40           O  
ANISOU  716  O   GLU A  87     4309   3259   3603    428    221    191       O  
ATOM    717  CB  GLU A  87      -2.804  12.836  80.019  1.00 26.42           C  
ANISOU  717  CB  GLU A  87     3998   2772   3269    441    213    214       C  
ATOM    718  CG  GLU A  87      -2.352  14.283  79.867  1.00 29.92           C  
ANISOU  718  CG  GLU A  87     4440   3204   3726    467    242    244       C  
ATOM    719  CD  GLU A  87      -1.057  14.426  79.084  1.00 32.81           C  
ANISOU  719  CD  GLU A  87     4789   3574   4102    482    220    246       C  
ATOM    720  OE1 GLU A  87      -0.249  13.471  79.062  1.00 27.99           O  
ANISOU  720  OE1 GLU A  87     4186   2955   3495    466    179    223       O  
ATOM    721  OE2 GLU A  87      -0.835  15.504  78.492  1.00 30.71           O  
ANISOU  721  OE2 GLU A  87     4505   3321   3843    512    245    272       O  
ATOM    722  N   ILE A  88      -4.388  10.222  80.911  1.00 26.71           N  
ANISOU  722  N   ILE A  88     4060   2818   3271    375    180    155       N  
ATOM    723  CA  ILE A  88      -4.771   8.868  80.493  1.00 26.92           C  
ANISOU  723  CA  ILE A  88     4073   2874   3279    356    156    127       C  
ATOM    724  C   ILE A  88      -6.294   8.727  80.585  1.00 36.84           C  
ANISOU  724  C   ILE A  88     5313   4168   4517    345    182    127       C  
ATOM    725  O   ILE A  88      -6.913   7.994  79.808  1.00 30.32           O  
ANISOU  725  O   ILE A  88     4452   3396   3672    341    177    115       O  
ATOM    726  CB  ILE A  88      -4.036   7.751  81.332  1.00 29.60           C  
ANISOU  726  CB  ILE A  88     4467   3160   3619    321    119     96       C  
ATOM    727  CG1 ILE A  88      -4.061   6.404  80.583  1.00 25.27           C  
ANISOU  727  CG1 ILE A  88     3905   2644   3054    311     93     69       C  
ATOM    728  CG2 ILE A  88      -4.585   7.648  82.754  1.00 30.13           C  
ANISOU  728  CG2 ILE A  88     4586   3179   3682    289    129     87       C  
ATOM    729  CD1 ILE A  88      -3.019   5.387  81.041  1.00 22.92           C  
ANISOU  729  CD1 ILE A  88     3651   2301   2758    292     56     45       C  
ATOM    730  N   GLU A  89      -6.902   9.481  81.497  1.00 32.70           N  
ANISOU  730  N   GLU A  89     4810   3618   3995    342    212    141       N  
ATOM    731  CA  GLU A  89      -8.359   9.509  81.608  1.00 33.50           C  
ANISOU  731  CA  GLU A  89     4892   3757   4079    337    241    146       C  
ATOM    732  C   GLU A  89      -8.997  10.460  80.589  1.00 39.76           C  
ANISOU  732  C   GLU A  89     5623   4614   4868    380    274    180       C  
ATOM    733  O   GLU A  89      -9.998  10.117  79.958  1.00 39.75           O  
ANISOU  733  O   GLU A  89     5578   4679   4848    381    282    180       O  
ATOM    734  CB  GLU A  89      -8.779   9.913  83.022  1.00 32.70           C  
ANISOU  734  CB  GLU A  89     4840   3602   3981    317    262    149       C  
ATOM    735  CG  GLU A  89      -8.684   8.776  84.034  1.00 47.95           C  
ANISOU  735  CG  GLU A  89     6826   5487   5906    270    236    114       C  
ATOM    736  CD  GLU A  89      -9.663   7.641  83.738  1.00 58.32           C  
ANISOU  736  CD  GLU A  89     8120   6846   7192    245    229     90       C  
ATOM    737  OE1 GLU A  89     -10.733   7.915  83.147  1.00 62.50           O  
ANISOU  737  OE1 GLU A  89     8601   7438   7708    259    254    104       O  
ATOM    738  OE2 GLU A  89      -9.362   6.476  84.095  1.00 50.37           O  
ANISOU  738  OE2 GLU A  89     7147   5813   6177    212    199     57       O  
ATOM    739  N   ASN A  90      -8.403  11.640  80.423  1.00 31.32           N  
ANISOU  739  N   ASN A  90     4553   3531   3819    413    291    208       N  
ATOM    740  CA  ASN A  90      -9.074  12.751  79.746  1.00 36.81           C  
ANISOU  740  CA  ASN A  90     5202   4272   4511    456    332    245       C  
ATOM    741  C   ASN A  90      -8.563  13.090  78.355  1.00 43.79           C  
ANISOU  741  C   ASN A  90     6036   5203   5399    492    326    260       C  
ATOM    742  O   ASN A  90      -9.288  13.665  77.545  1.00 42.50           O  
ANISOU  742  O   ASN A  90     5822   5099   5227    526    353    286       O  
ATOM    743  CB  ASN A  90      -8.982  14.001  80.612  1.00 37.47           C  
ANISOU  743  CB  ASN A  90     5323   4303   4609    470    367    270       C  
ATOM    744  CG  ASN A  90      -9.680  13.830  81.942  1.00 46.82           C  
ANISOU  744  CG  ASN A  90     6552   5448   5789    439    381    261       C  
ATOM    745  OD1 ASN A  90     -10.907  13.914  82.023  1.00 53.07           O  
ANISOU  745  OD1 ASN A  90     7322   6275   6565    444    409    271       O  
ATOM    746  ND2 ASN A  90      -8.907  13.554  82.989  1.00 37.85           N  
ANISOU  746  ND2 ASN A  90     5477   4240   4663    406    361    241       N  
ATOM    747  N   ASN A  91      -7.309  12.767  78.081  1.00 32.66           N  
ANISOU  747  N   ASN A  91     4639   3767   4002    488    293    246       N  
ATOM    748  CA  ASN A  91      -6.769  13.038  76.756  1.00 31.98           C  
ANISOU  748  CA  ASN A  91     4507   3724   3919    520    287    259       C  
ATOM    749  C   ASN A  91      -5.789  11.957  76.326  1.00 31.22           C  
ANISOU  749  C   ASN A  91     4414   3622   3825    502    241    229       C  
ATOM    750  O   ASN A  91      -4.646  12.267  76.027  1.00 28.39           O  
ANISOU  750  O   ASN A  91     4061   3242   3483    515    227    233       O  
ATOM    751  CB  ASN A  91      -6.091  14.412  76.751  1.00 34.44           C  
ANISOU  751  CB  ASN A  91     4829   4006   4249    552    311    288       C  
ATOM    752  CG  ASN A  91      -5.804  14.914  75.362  1.00 38.37           C  
ANISOU  752  CG  ASN A  91     5275   4555   4749    592    316    308       C  
ATOM    753  OD1 ASN A  91      -6.422  14.478  74.393  1.00 38.00           O  
ANISOU  753  OD1 ASN A  91     5177   4574   4687    603    313    308       O  
ATOM    754  ND2 ASN A  91      -4.861  15.841  75.253  1.00 32.68           N  
ANISOU  754  ND2 ASN A  91     4568   3804   4045    612    325    324       N  
ATOM    755  N   PRO A  92      -6.234  10.679  76.312  1.00 33.64           N  
ANISOU  755  N   PRO A  92     4720   3948   4115    471    218    200       N  
ATOM    756  CA  PRO A  92      -5.340   9.536  76.085  1.00 29.59           C  
ANISOU  756  CA  PRO A  92     4221   3420   3601    451    176    170       C  
ATOM    757  C   PRO A  92      -4.784   9.500  74.675  1.00 27.45           C  
ANISOU  757  C   PRO A  92     3904   3194   3331    477    164    175       C  
ATOM    758  O   PRO A  92      -3.814   8.791  74.407  1.00 27.53           O  
ANISOU  758  O   PRO A  92     3926   3188   3346    470    133    156       O  
ATOM    759  CB  PRO A  92      -6.244   8.317  76.348  1.00 27.83           C  
ANISOU  759  CB  PRO A  92     4005   3214   3354    413    166    142       C  
ATOM    760  CG  PRO A  92      -7.608   8.805  76.118  1.00 34.01           C  
ANISOU  760  CG  PRO A  92     4750   4052   4121    423    200    160       C  
ATOM    761  CD  PRO A  92      -7.620  10.242  76.538  1.00 28.94           C  
ANISOU  761  CD  PRO A  92     4111   3387   3496    453    233    194       C  
ATOM    762  N   GLY A  93      -5.385  10.278  73.782  1.00 28.70           N  
ANISOU  762  N   GLY A  93     4011   3408   3484    509    190    202       N  
ATOM    763  CA  GLY A  93      -4.904  10.330  72.419  1.00 31.81           C  
ANISOU  763  CA  GLY A  93     4361   3847   3879    535    181    209       C  
ATOM    764  C   GLY A  93      -3.895  11.422  72.122  1.00 33.08           C  
ANISOU  764  C   GLY A  93     4519   3987   4062    569    188    232       C  
ATOM    765  O   GLY A  93      -3.520  11.609  70.962  1.00 30.85           O  
ANISOU  765  O   GLY A  93     4197   3742   3781    594    185    241       O  
ATOM    766  N   VAL A  94      -3.420  12.127  73.148  1.00 33.84           N  
ANISOU  766  N   VAL A  94     4658   4023   4176    567    198    240       N  
ATOM    767  CA  VAL A  94      -2.503  13.242  72.907  1.00 28.06           C  
ANISOU  767  CA  VAL A  94     3927   3271   3463    595    209    263       C  
ATOM    768  C   VAL A  94      -1.239  12.773  72.170  1.00 30.89           C  
ANISOU  768  C   VAL A  94     4277   3629   3831    599    175    250       C  
ATOM    769  O   VAL A  94      -0.614  11.787  72.549  1.00 35.03           O  
ANISOU  769  O   VAL A  94     4828   4125   4357    573    142    223       O  
ATOM    770  CB  VAL A  94      -2.140  13.991  74.241  1.00 28.04           C  
ANISOU  770  CB  VAL A  94     3980   3199   3474    583    223    270       C  
ATOM    771  CG1 VAL A  94      -1.569  13.037  75.296  1.00 27.11           C  
ANISOU  771  CG1 VAL A  94     3912   3028   3360    543    190    240       C  
ATOM    772  CG2 VAL A  94      -1.172  15.148  73.952  1.00 29.89           C  
ANISOU  772  CG2 VAL A  94     4217   3415   3726    608    236    292       C  
ATOM    773  N   LYS A  95      -0.911  13.443  71.062  1.00 26.52           N  
ANISOU  773  N   LYS A  95     3684   3110   3282    633    185    269       N  
ATOM    774  CA  LYS A  95       0.260  13.104  70.230  1.00 34.50           C  
ANISOU  774  CA  LYS A  95     4681   4127   4302    641    157    260       C  
ATOM    775  C   LYS A  95       0.278  11.671  69.664  1.00 28.93           C  
ANISOU  775  C   LYS A  95     3961   3447   3583    625    124    232       C  
ATOM    776  O   LYS A  95       1.315  11.191  69.215  1.00 35.04           O  
ANISOU  776  O   LYS A  95     4735   4214   4365    626     98    219       O  
ATOM    777  CB  LYS A  95       1.559  13.332  71.013  1.00 34.08           C  
ANISOU  777  CB  LYS A  95     4671   4011   4267    630    141    255       C  
ATOM    778  CG  LYS A  95       1.921  14.801  71.250  1.00 36.02           C  
ANISOU  778  CG  LYS A  95     4927   4232   4525    648    171    283       C  
ATOM    779  CD  LYS A  95       3.257  14.906  71.973  1.00 40.69           C  
ANISOU  779  CD  LYS A  95     5558   4770   5132    630    150    275       C  
ATOM    780  CE  LYS A  95       3.550  16.328  72.416  1.00 41.15           C  
ANISOU  780  CE  LYS A  95     5638   4797   5198    638    183    300       C  
ATOM    781  NZ  LYS A  95       4.751  16.381  73.303  1.00 31.40           N  
ANISOU  781  NZ  LYS A  95     4446   3511   3975    612    162    291       N  
ATOM    782  N   PHE A  96      -0.868  11.002  69.699  1.00 28.88           N  
ANISOU  782  N   PHE A  96     3945   3470   3556    608    128    221       N  
ATOM    783  CA  PHE A  96      -1.007   9.670  69.127  1.00 30.29           C  
ANISOU  783  CA  PHE A  96     4113   3677   3718    589    103    194       C  
ATOM    784  C   PHE A  96      -1.136   9.771  67.604  1.00 37.51           C  
ANISOU  784  C   PHE A  96     4971   4657   4624    615    107    205       C  
ATOM    785  O   PHE A  96      -1.914  10.580  67.103  1.00 43.85           O  
ANISOU  785  O   PHE A  96     5736   5504   5420    637    135    230       O  
ATOM    786  CB  PHE A  96      -2.229   8.972  69.711  1.00 34.22           C  
ANISOU  786  CB  PHE A  96     4621   4186   4194    559    109    180       C  
ATOM    787  CG  PHE A  96      -2.376   7.543  69.280  1.00 34.11           C  
ANISOU  787  CG  PHE A  96     4607   4193   4160    532     85    148       C  
ATOM    788  CD1 PHE A  96      -1.349   6.630  69.503  1.00 30.43           C  
ANISOU  788  CD1 PHE A  96     4176   3684   3700    517     54    124       C  
ATOM    789  CD2 PHE A  96      -3.539   7.105  68.676  1.00 29.38           C  
ANISOU  789  CD2 PHE A  96     3974   3655   3533    520     95    144       C  
ATOM    790  CE1 PHE A  96      -1.481   5.305  69.117  1.00 32.05           C  
ANISOU  790  CE1 PHE A  96     4389   3905   3885    492     36     95       C  
ATOM    791  CE2 PHE A  96      -3.685   5.779  68.291  1.00 34.50           C  
ANISOU  791  CE2 PHE A  96     4628   4321   4160    491     75    114       C  
ATOM    792  CZ  PHE A  96      -2.647   4.878  68.505  1.00 38.52           C  
ANISOU  792  CZ  PHE A  96     5177   4783   4676    477     47     89       C  
ATOM    793  N   THR A  97      -0.391   8.952  66.870  1.00 37.83           N  
ANISOU  793  N   THR A  97     5005   4705   4662    612     81    186       N  
ATOM    794  CA  THR A  97      -0.416   9.038  65.410  1.00 41.02           C  
ANISOU  794  CA  THR A  97     5358   5169   5059    634     84    195       C  
ATOM    795  C   THR A  97      -0.870   7.731  64.768  1.00 47.95           C  
ANISOU  795  C   THR A  97     6224   6084   5911    610     68    169       C  
ATOM    796  O   THR A  97      -0.973   7.636  63.544  1.00 52.01           O  
ANISOU  796  O   THR A  97     6697   6650   6414    622     69    173       O  
ATOM    797  CB  THR A  97       0.970   9.414  64.847  1.00 38.20           C  
ANISOU  797  CB  THR A  97     4997   4794   4724    659     71    201       C  
ATOM    798  OG1 THR A  97       1.955   8.517  65.366  1.00 44.68           O  
ANISOU  798  OG1 THR A  97     5858   5566   5552    640     42    176       O  
ATOM    799  CG2 THR A  97       1.347  10.834  65.239  1.00 43.55           C  
ANISOU  799  CG2 THR A  97     5678   5446   5421    684     92    230       C  
ATOM    800  N   GLY A  98      -1.141   6.730  65.598  1.00 43.82           N  
ANISOU  800  N   GLY A  98     5740   5533   5377    573     55    143       N  
ATOM    801  CA  GLY A  98      -1.480   5.399  65.120  1.00 46.51           C  
ANISOU  801  CA  GLY A  98     6082   5898   5692    544     41    114       C  
ATOM    802  C   GLY A  98      -2.793   5.367  64.366  1.00 46.92           C  
ANISOU  802  C   GLY A  98     6087   6025   5714    536     58    120       C  
ATOM    803  O   GLY A  98      -2.964   4.592  63.428  1.00 49.78           O  
ANISOU  803  O   GLY A  98     6431   6429   6055    523     51    105       O  
ATOM    804  N   TYR A  99      -3.724   6.210  64.793  1.00 38.90           N  
ANISOU  804  N   TYR A  99     5054   5029   4696    544     82    142       N  
ATOM    805  CA  TYR A  99      -5.010   6.357  64.126  1.00 37.50           C  
ANISOU  805  CA  TYR A  99     4827   4929   4491    542    101    154       C  
ATOM    806  C   TYR A  99      -5.746   7.549  64.716  1.00 41.10           C  
ANISOU  806  C   TYR A  99     5269   5392   4955    564    131    186       C  
ATOM    807  O   TYR A  99      -5.204   8.249  65.569  1.00 40.99           O  
ANISOU  807  O   TYR A  99     5287   5321   4968    578    136    197       O  
ATOM    808  CB  TYR A  99      -5.856   5.074  64.236  1.00 36.80           C  
ANISOU  808  CB  TYR A  99     4749   4864   4369    492     93    124       C  
ATOM    809  CG  TYR A  99      -6.086   4.515  65.632  1.00 36.56           C  
ANISOU  809  CG  TYR A  99     4774   4780   4339    458     89    102       C  
ATOM    810  CD1 TYR A  99      -7.117   4.996  66.447  1.00 31.51           C  
ANISOU  810  CD1 TYR A  99     4131   4147   3692    451    110    115       C  
ATOM    811  CD2 TYR A  99      -5.306   3.465  66.116  1.00 35.97           C  
ANISOU  811  CD2 TYR A  99     4753   4646   4266    433     66     70       C  
ATOM    812  CE1 TYR A  99      -7.339   4.466  67.711  1.00 31.49           C  
ANISOU  812  CE1 TYR A  99     4181   4095   3689    419    107     94       C  
ATOM    813  CE2 TYR A  99      -5.525   2.930  67.379  1.00 33.58           C  
ANISOU  813  CE2 TYR A  99     4503   4295   3962    401     62     51       C  
ATOM    814  CZ  TYR A  99      -6.537   3.433  68.169  1.00 30.77           C  
ANISOU  814  CZ  TYR A  99     4144   3946   3601    393     82     62       C  
ATOM    815  OH  TYR A  99      -6.747   2.893  69.426  1.00 33.46           O  
ANISOU  815  OH  TYR A  99     4538   4236   3940    361     78     42       O  
ATOM    816  OXT TYR A  99      -6.878   7.853  64.348  1.00 48.22           O  
ANISOU  816  OXT TYR A  99     6129   6357   5836    568    151    203       O  
TER     817      TYR A  99                                                      
ATOM    818  N   ALA B   2      -1.332  15.534  45.413  1.00 55.23           N  
ANISOU  818  N   ALA B   2     6444   7820   6722   1047    211    472       N  
ATOM    819  CA  ALA B   2      -2.509  15.140  46.174  1.00 49.55           C  
ANISOU  819  CA  ALA B   2     5720   7124   5982   1024    214    471       C  
ATOM    820  C   ALA B   2      -2.134  14.751  47.615  1.00 51.69           C  
ANISOU  820  C   ALA B   2     6047   7317   6275    998    205    447       C  
ATOM    821  O   ALA B   2      -2.250  15.570  48.523  1.00 47.29           O  
ANISOU  821  O   ALA B   2     5510   6724   5733   1018    225    465       O  
ATOM    822  CB  ALA B   2      -3.234  14.005  45.475  1.00 59.31           C  
ANISOU  822  CB  ALA B   2     6925   8429   7182    985    196    453       C  
ATOM    823  N   ARG B   3      -1.684  13.516  47.835  1.00 50.13           N  
ANISOU  823  N   ARG B   3     5877   7092   6078    954    176    408       N  
ATOM    824  CA  ARG B   3      -1.317  13.105  49.192  1.00 40.81           C  
ANISOU  824  CA  ARG B   3     4750   5840   4918    930    166    385       C  
ATOM    825  C   ARG B   3      -0.121  13.897  49.700  1.00 30.26           C  
ANISOU  825  C   ARG B   3     3448   4430   3618    954    170    391       C  
ATOM    826  O   ARG B   3       0.963  13.812  49.147  1.00 39.06           O  
ANISOU  826  O   ARG B   3     4570   5523   4748    960    158    381       O  
ATOM    827  CB  ARG B   3      -0.995  11.614  49.265  1.00 49.66           C  
ANISOU  827  CB  ARG B   3     5895   6943   6029    881    136    342       C  
ATOM    828  CG  ARG B   3      -0.579  11.202  50.660  1.00 49.59           C  
ANISOU  828  CG  ARG B   3     5942   6859   6040    859    125    321       C  
ATOM    829  CD  ARG B   3      -0.501   9.698  50.841  1.00 57.05           C  
ANISOU  829  CD  ARG B   3     6914   7791   6971    811    100    281       C  
ATOM    830  NE  ARG B   3      -0.106   9.384  52.210  1.00 63.81           N  
ANISOU  830  NE  ARG B   3     7823   8575   7846    794     91    263       N  
ATOM    831  CZ  ARG B   3      -0.935   8.905  53.133  1.00 66.78           C  
ANISOU  831  CZ  ARG B   3     8218   8946   8209    764     92    252       C  
ATOM    832  NH1 ARG B   3      -2.201   8.661  52.820  1.00 67.69           N  
ANISOU  832  NH1 ARG B   3     8301   9126   8292    747    100    256       N  
ATOM    833  NH2 ARG B   3      -0.499   8.656  54.363  1.00 65.99           N  
ANISOU  833  NH2 ARG B   3     8167   8777   8127    750     83    238       N  
ATOM    834  N   PRO B   4      -0.303  14.663  50.775  1.00 33.40           N  
ANISOU  834  N   PRO B   4     3870   4790   4031    966    188    407       N  
ATOM    835  CA  PRO B   4       0.825  15.488  51.213  1.00 36.18           C  
ANISOU  835  CA  PRO B   4     4254   5077   4414    987    195    413       C  
ATOM    836  C   PRO B   4       1.892  14.655  51.921  1.00 34.63           C  
ANISOU  836  C   PRO B   4     4104   4815   4238    956    166    379       C  
ATOM    837  O   PRO B   4       1.600  13.562  52.400  1.00 34.93           O  
ANISOU  837  O   PRO B   4     4159   4848   4267    921    146    353       O  
ATOM    838  CB  PRO B   4       0.175  16.492  52.179  1.00 35.20           C  
ANISOU  838  CB  PRO B   4     4145   4934   4295   1005    225    440       C  
ATOM    839  CG  PRO B   4      -1.038  15.804  52.679  1.00 37.42           C  
ANISOU  839  CG  PRO B   4     4418   5245   4553    979    224    433       C  
ATOM    840  CD  PRO B   4      -1.512  14.882  51.588  1.00 36.82           C  
ANISOU  840  CD  PRO B   4     4301   5238   4450    963    207    420       C  
ATOM    841  N   ARG B   5       3.111  15.169  51.979  1.00 32.96           N  
ANISOU  841  N   ARG B   5     3914   4558   4052    970    163    380       N  
ATOM    842  CA  ARG B   5       4.172  14.497  52.718  1.00 39.35           C  
ANISOU  842  CA  ARG B   5     4764   5306   4880    946    137    352       C  
ATOM    843  C   ARG B   5       4.052  14.892  54.186  1.00 33.69           C  
ANISOU  843  C   ARG B   5     4088   4536   4175    936    146    355       C  
ATOM    844  O   ARG B   5       3.433  15.912  54.493  1.00 37.18           O  
ANISOU  844  O   ARG B   5     4528   4983   4617    955    176    382       O  
ATOM    845  CB  ARG B   5       5.542  14.862  52.134  1.00 38.45           C  
ANISOU  845  CB  ARG B   5     4652   5171   4787    963    130    352       C  
ATOM    846  CG  ARG B   5       5.816  14.190  50.789  1.00 35.97           C  
ANISOU  846  CG  ARG B   5     4306   4899   4463    965    116    341       C  
ATOM    847  CD  ARG B   5       7.156  14.590  50.259  1.00 30.16           C  
ANISOU  847  CD  ARG B   5     3571   4142   3747    983    110    342       C  
ATOM    848  NE  ARG B   5       7.137  15.913  49.657  1.00 32.89           N  
ANISOU  848  NE  ARG B   5     3895   4507   4096   1018    138    373       N  
ATOM    849  CZ  ARG B   5       7.940  16.909  50.015  1.00 38.94           C  
ANISOU  849  CZ  ARG B   5     4680   5235   4882   1032    150    386       C  
ATOM    850  NH1 ARG B   5       8.837  16.735  50.977  1.00 34.46           N  
ANISOU  850  NH1 ARG B   5     4149   4611   4333   1015    136    371       N  
ATOM    851  NH2 ARG B   5       7.856  18.078  49.401  1.00 37.26           N  
ANISOU  851  NH2 ARG B   5     4449   5040   4669   1064    178    414       N  
ATOM    852  N   PRO B   6       4.615  14.082  55.099  1.00 32.92           N  
ANISOU  852  N   PRO B   6     4030   4390   4087    906    122    329       N  
ATOM    853  CA  PRO B   6       4.499  14.385  56.530  1.00 34.75           C  
ANISOU  853  CA  PRO B   6     4302   4571   4329    892    128    330       C  
ATOM    854  C   PRO B   6       5.041  15.765  56.899  1.00 31.64           C  
ANISOU  854  C   PRO B   6     3923   4144   3953    915    152    354       C  
ATOM    855  O   PRO B   6       5.993  16.234  56.279  1.00 28.32           O  
ANISOU  855  O   PRO B   6     3495   3720   3545    932    151    360       O  
ATOM    856  CB  PRO B   6       5.356  13.289  57.194  1.00 34.78           C  
ANISOU  856  CB  PRO B   6     4343   4530   4343    863     95    298       C  
ATOM    857  CG  PRO B   6       5.434  12.197  56.218  1.00 33.35           C  
ANISOU  857  CG  PRO B   6     4141   4383   4149    855     75    278       C  
ATOM    858  CD  PRO B   6       5.327  12.812  54.856  1.00 30.46           C  
ANISOU  858  CD  PRO B   6     3728   4068   3776    884     89    298       C  
ATOM    859  N   ARG B   7       4.466  16.412  57.908  1.00 25.25           N  
ANISOU  859  N   ARG B   7     3138   3311   3146    913    173    368       N  
ATOM    860  CA  ARG B   7       5.097  17.629  58.441  1.00 28.58           C  
ANISOU  860  CA  ARG B   7     3587   3690   3584    925    195    386       C  
ATOM    861  C   ARG B   7       5.843  17.346  59.749  1.00 33.25           C  
ANISOU  861  C   ARG B   7     4227   4216   4189    894    177    368       C  
ATOM    862  O   ARG B   7       6.453  18.239  60.333  1.00 36.79           O  
ANISOU  862  O   ARG B   7     4703   4624   4650    895    191    379       O  
ATOM    863  CB  ARG B   7       4.056  18.727  58.659  1.00 33.05           C  
ANISOU  863  CB  ARG B   7     4149   4266   4141    948    237    417       C  
ATOM    864  CG  ARG B   7       3.559  19.327  57.344  1.00 36.90           C  
ANISOU  864  CG  ARG B   7     4589   4813   4616    987    260    442       C  
ATOM    865  CD  ARG B   7       2.346  20.226  57.553  1.00 36.05           C  
ANISOU  865  CD  ARG B   7     4475   4725   4496   1012    302    474       C  
ATOM    866  NE  ARG B   7       1.937  20.873  56.305  1.00 31.03           N  
ANISOU  866  NE  ARG B   7     3795   4145   3848   1052    324    501       N  
ATOM    867  CZ  ARG B   7       2.419  22.038  55.876  1.00 43.09           C  
ANISOU  867  CZ  ARG B   7     5325   5663   5382   1083    352    525       C  
ATOM    868  NH1 ARG B   7       3.344  22.680  56.585  1.00 43.20           N  
ANISOU  868  NH1 ARG B   7     5385   5614   5414   1076    360    524       N  
ATOM    869  NH2 ARG B   7       1.985  22.561  54.733  1.00 35.27           N  
ANISOU  869  NH2 ARG B   7     4295   4727   4380   1121    372    550       N  
ATOM    870  N   GLU B   8       5.768  16.102  60.202  1.00 31.16           N  
ANISOU  870  N   GLU B   8     3975   3944   3921    866    147    341       N  
ATOM    871  CA  GLU B   8       6.493  15.663  61.397  1.00 27.63           C  
ANISOU  871  CA  GLU B   8     3573   3439   3485    837    126    323       C  
ATOM    872  C   GLU B   8       7.085  14.297  61.159  1.00 29.89           C  
ANISOU  872  C   GLU B   8     3859   3727   3772    820     87    294       C  
ATOM    873  O   GLU B   8       6.477  13.462  60.481  1.00 32.56           O  
ANISOU  873  O   GLU B   8     4173   4103   4094    818     79    283       O  
ATOM    874  CB  GLU B   8       5.571  15.599  62.624  1.00 32.35           C  
ANISOU  874  CB  GLU B   8     4202   4013   4077    816    136    321       C  
ATOM    875  CG  GLU B   8       5.145  16.945  63.157  1.00 49.46           C  
ANISOU  875  CG  GLU B   8     6383   6162   6246    829    175    349       C  
ATOM    876  CD  GLU B   8       4.207  16.812  64.339  1.00 66.62           C  
ANISOU  876  CD  GLU B   8     8586   8312   8413    808    185    346       C  
ATOM    877  OE1 GLU B   8       3.392  15.864  64.342  1.00 68.78           O  
ANISOU  877  OE1 GLU B   8     8849   8610   8673    795    174    332       O  
ATOM    878  OE2 GLU B   8       4.291  17.646  65.267  1.00 76.52           O  
ANISOU  878  OE2 GLU B   8     9876   9524   9674    803    206    358       O  
ATOM    879  N   TYR B   9       8.257  14.058  61.745  1.00 34.19           N  
ANISOU  879  N   TYR B   9     4431   4230   4330    807     65    282       N  
ATOM    880  CA  TYR B   9       8.921  12.770  61.628  1.00 24.48           C  
ANISOU  880  CA  TYR B   9     3207   2994   3100    794     30    256       C  
ATOM    881  C   TYR B   9       9.304  12.277  63.009  1.00 30.27           C  
ANISOU  881  C   TYR B   9     3987   3676   3839    767     12    242       C  
ATOM    882  O   TYR B   9       9.384  13.081  63.945  1.00 24.82           O  
ANISOU  882  O   TYR B   9     3322   2953   3156    759     24    253       O  
ATOM    883  CB  TYR B   9      10.158  12.876  60.742  1.00 32.99           C  
ANISOU  883  CB  TYR B   9     4265   4081   4190    812     18    257       C  
ATOM    884  CG  TYR B   9       9.818  12.988  59.266  1.00 27.90           C  
ANISOU  884  CG  TYR B   9     3575   3491   3538    837     29    265       C  
ATOM    885  CD1 TYR B   9       9.559  11.850  58.507  1.00 30.30           C  
ANISOU  885  CD1 TYR B   9     3862   3824   3829    834     14    247       C  
ATOM    886  CD2 TYR B   9       9.771  14.219  58.641  1.00 28.27           C  
ANISOU  886  CD2 TYR B   9     3597   3556   3587    861     55    289       C  
ATOM    887  CE1 TYR B   9       9.244  11.940  57.157  1.00 28.66           C  
ANISOU  887  CE1 TYR B   9     3613   3667   3612    853     23    254       C  
ATOM    888  CE2 TYR B   9       9.444  14.324  57.281  1.00 27.39           C  
ANISOU  888  CE2 TYR B   9     3444   3496   3468    884     65    297       C  
ATOM    889  CZ  TYR B   9       9.188  13.174  56.553  1.00 28.21           C  
ANISOU  889  CZ  TYR B   9     3530   3631   3559    879     48    279       C  
ATOM    890  OH  TYR B   9       8.876  13.252  55.200  1.00 33.31           O  
ANISOU  890  OH  TYR B   9     4134   4328   4194    898     56    287       O  
ATOM    891  N   LYS B  10       9.525  10.968  63.118  1.00 25.32           N  
ANISOU  891  N   LYS B  10     3372   3042   3207    753    -15    218       N  
ATOM    892  CA  LYS B  10       9.980  10.335  64.355  1.00 28.19           C  
ANISOU  892  CA  LYS B  10     3779   3358   3574    729    -37    203       C  
ATOM    893  C   LYS B  10      11.321   9.644  64.112  1.00 34.37           C  
ANISOU  893  C   LYS B  10     4564   4130   4365    735    -65    192       C  
ATOM    894  O   LYS B  10      11.541   9.095  63.034  1.00 31.65           O  
ANISOU  894  O   LYS B  10     4195   3815   4017    750    -72    185       O  
ATOM    895  CB  LYS B  10       8.949   9.318  64.859  1.00 29.06           C  
ANISOU  895  CB  LYS B  10     3910   3464   3667    706    -41    184       C  
ATOM    896  CG  LYS B  10       7.621   9.932  65.301  1.00 41.63           C  
ANISOU  896  CG  LYS B  10     5504   5063   5251    698    -13    195       C  
ATOM    897  CD  LYS B  10       6.657   8.855  65.808  1.00 50.74           C  
ANISOU  897  CD  LYS B  10     6679   6215   6387    672    -19    174       C  
ATOM    898  CE  LYS B  10       5.290   9.433  66.166  1.00 56.26           C  
ANISOU  898  CE  LYS B  10     7373   6928   7075    665      9    186       C  
ATOM    899  NZ  LYS B  10       5.355  10.411  67.282  1.00 63.77           N  
ANISOU  899  NZ  LYS B  10     8352   7839   8039    661     23    201       N  
ATOM    900  N   ALA B  11      12.211   9.698  65.104  1.00 25.78           N  
ANISOU  900  N   ALA B  11     3506   3003   3288    724    -81    191       N  
ATOM    901  CA  ALA B  11      13.468   8.958  65.054  1.00 27.40           C  
ANISOU  901  CA  ALA B  11     3716   3197   3498    730   -110    182       C  
ATOM    902  C   ALA B  11      13.242   7.561  64.521  1.00 30.07           C  
ANISOU  902  C   ALA B  11     4055   3547   3824    732   -123    161       C  
ATOM    903  O   ALA B  11      12.307   6.888  64.935  1.00 26.21           O  
ANISOU  903  O   ALA B  11     3587   3050   3322    714   -121    148       O  
ATOM    904  CB  ALA B  11      14.092   8.897  66.434  1.00 36.64           C  
ANISOU  904  CB  ALA B  11     4925   4323   4674    710   -126    180       C  
ATOM    905  N   GLY B  12      14.088   7.130  63.592  1.00 26.40           N  
ANISOU  905  N   GLY B  12     3568   3099   3362    753   -135    158       N  
ATOM    906  CA  GLY B  12      13.954   5.806  63.013  1.00 23.50           C  
ANISOU  906  CA  GLY B  12     3206   2742   2982    755   -145    138       C  
ATOM    907  C   GLY B  12      13.320   5.809  61.632  1.00 25.85           C  
ANISOU  907  C   GLY B  12     3467   3085   3270    767   -129    138       C  
ATOM    908  O   GLY B  12      13.444   4.827  60.912  1.00 26.34           O  
ANISOU  908  O   GLY B  12     3527   3159   3323    772   -136    123       O  
ATOM    909  N   ASP B  13      12.617   6.890  61.282  1.00 28.52           N  
ANISOU  909  N   ASP B  13     3778   3448   3609    770   -107    154       N  
ATOM    910  CA  ASP B  13      11.901   6.955  60.002  1.00 26.17           C  
ANISOU  910  CA  ASP B  13     3444   3199   3300    780    -91    155       C  
ATOM    911  C   ASP B  13      12.891   6.906  58.846  1.00 28.41           C  
ANISOU  911  C   ASP B  13     3699   3503   3591    805    -98    158       C  
ATOM    912  O   ASP B  13      13.953   7.548  58.897  1.00 24.82           O  
ANISOU  912  O   ASP B  13     3238   3038   3155    819   -103    170       O  
ATOM    913  CB  ASP B  13      11.042   8.229  59.893  1.00 24.32           C  
ANISOU  913  CB  ASP B  13     3187   2988   3067    784    -65    177       C  
ATOM    914  CG  ASP B  13       9.710   8.121  60.636  1.00 38.03           C  
ANISOU  914  CG  ASP B  13     4940   4721   4789    762    -53    173       C  
ATOM    915  OD1 ASP B  13       9.263   6.990  60.921  1.00 37.12           O  
ANISOU  915  OD1 ASP B  13     4847   4600   4659    741    -64    152       O  
ATOM    916  OD2 ASP B  13       9.097   9.182  60.908  1.00 40.34           O  
ANISOU  916  OD2 ASP B  13     5224   5020   5084    765    -31    192       O  
ATOM    917  N   LEU B  14      12.538   6.148  57.811  1.00 27.37           N  
ANISOU  917  N   LEU B  14     3553   3402   3444    807    -96    146       N  
ATOM    918  CA  LEU B  14      13.377   6.042  56.623  1.00 25.30           C  
ANISOU  918  CA  LEU B  14     3264   3162   3187    830   -100    147       C  
ATOM    919  C   LEU B  14      12.854   6.969  55.524  1.00 26.96           C  
ANISOU  919  C   LEU B  14     3429   3419   3395    844    -80    163       C  
ATOM    920  O   LEU B  14      11.652   7.031  55.266  1.00 23.35           O  
ANISOU  920  O   LEU B  14     2961   2991   2921    834    -65    164       O  
ATOM    921  CB  LEU B  14      13.435   4.597  56.137  1.00 30.92           C  
ANISOU  921  CB  LEU B  14     3991   3875   3883    824   -110    124       C  
ATOM    922  CG  LEU B  14      14.120   3.632  57.117  1.00 29.92           C  
ANISOU  922  CG  LEU B  14     3909   3701   3759    818   -130    109       C  
ATOM    923  CD1 LEU B  14      14.240   2.280  56.461  1.00 26.63           C  
ANISOU  923  CD1 LEU B  14     3508   3287   3325    817   -135     88       C  
ATOM    924  CD2 LEU B  14      15.494   4.164  57.551  1.00 31.30           C  
ANISOU  924  CD2 LEU B  14     4083   3854   3958    837   -143    123       C  
ATOM    925  N   VAL B  15      13.751   7.723  54.901  1.00 22.95           N  
ANISOU  925  N   VAL B  15     2897   2921   2903    868    -77    177       N  
ATOM    926  CA  VAL B  15      13.327   8.748  53.949  1.00 20.08           C  
ANISOU  926  CA  VAL B  15     2495   2597   2539    884    -56    196       C  
ATOM    927  C   VAL B  15      14.302   8.854  52.792  1.00 22.90           C  
ANISOU  927  C   VAL B  15     2824   2973   2903    907    -59    199       C  
ATOM    928  O   VAL B  15      15.378   8.232  52.809  1.00 19.95           O  
ANISOU  928  O   VAL B  15     2462   2580   2539    913    -77    189       O  
ATOM    929  CB  VAL B  15      13.223  10.135  54.614  1.00 29.52           C  
ANISOU  929  CB  VAL B  15     3689   3781   3746    889    -41    219       C  
ATOM    930  CG1 VAL B  15      12.146  10.159  55.720  1.00 25.20           C  
ANISOU  930  CG1 VAL B  15     3167   3218   3191    867    -33    218       C  
ATOM    931  CG2 VAL B  15      14.576  10.550  55.180  1.00 27.19           C  
ANISOU  931  CG2 VAL B  15     3408   3451   3472    894    -52    223       C  
ATOM    932  N   PHE B  16      13.912   9.623  51.780  1.00 20.87           N  
ANISOU  932  N   PHE B  16     2532   2756   2643    923    -41    214       N  
ATOM    933  CA  PHE B  16      14.909  10.256  50.928  1.00 25.08           C  
ANISOU  933  CA  PHE B  16     3039   3299   3189    947    -38    225       C  
ATOM    934  C   PHE B  16      15.060  11.676  51.416  1.00 21.78           C  
ANISOU  934  C   PHE B  16     2619   2870   2785    955    -23    247       C  
ATOM    935  O   PHE B  16      14.074  12.318  51.777  1.00 26.75           O  
ANISOU  935  O   PHE B  16     3250   3506   3408    951     -5    259       O  
ATOM    936  CB  PHE B  16      14.502  10.221  49.455  1.00 23.80           C  
ANISOU  936  CB  PHE B  16     2842   3186   3014    960    -28    227       C  
ATOM    937  CG  PHE B  16      14.538   8.848  48.864  1.00 26.73           C  
ANISOU  937  CG  PHE B  16     3217   3567   3372    951    -41    204       C  
ATOM    938  CD1 PHE B  16      15.705   8.354  48.311  1.00 26.31           C  
ANISOU  938  CD1 PHE B  16     3162   3505   3327    964    -53    196       C  
ATOM    939  CD2 PHE B  16      13.423   8.035  48.895  1.00 24.64           C  
ANISOU  939  CD2 PHE B  16     2960   3317   3083    929    -40    191       C  
ATOM    940  CE1 PHE B  16      15.755   7.096  47.767  1.00 27.34           C  
ANISOU  940  CE1 PHE B  16     3302   3641   3444    957    -61    175       C  
ATOM    941  CE2 PHE B  16      13.471   6.760  48.357  1.00 24.85           C  
ANISOU  941  CE2 PHE B  16     2998   3350   3095    918    -50    169       C  
ATOM    942  CZ  PHE B  16      14.646   6.291  47.797  1.00 26.90           C  
ANISOU  942  CZ  PHE B  16     3259   3598   3364    933    -59    161       C  
ATOM    943  N   ALA B  17      16.285  12.167  51.463  1.00 21.50           N  
ANISOU  943  N   ALA B  17     2584   2817   2767    964    -28    253       N  
ATOM    944  CA  ALA B  17      16.513  13.531  51.902  1.00 22.28           C  
ANISOU  944  CA  ALA B  17     2685   2904   2877    968    -11    273       C  
ATOM    945  C   ALA B  17      17.187  14.330  50.794  1.00 27.18           C  
ANISOU  945  C   ALA B  17     3276   3547   3503    991      1    285       C  
ATOM    946  O   ALA B  17      18.090  13.825  50.125  1.00 23.20           O  
ANISOU  946  O   ALA B  17     2759   3052   3006    999    -13    276       O  
ATOM    947  CB  ALA B  17      17.359  13.549  53.170  1.00 27.33           C  
ANISOU  947  CB  ALA B  17     3356   3500   3529    952    -26    269       C  
ATOM    948  N   LYS B  18      16.719  15.560  50.591  1.00 23.48           N  
ANISOU  948  N   LYS B  18     2799   3090   3034   1001     29    306       N  
ATOM    949  CA  LYS B  18      17.195  16.405  49.491  1.00 26.52           C  
ANISOU  949  CA  LYS B  18     3156   3497   3422   1023     45    320       C  
ATOM    950  C   LYS B  18      18.066  17.542  49.994  1.00 31.18           C  
ANISOU  950  C   LYS B  18     3761   4062   4025   1021     56    332       C  
ATOM    951  O   LYS B  18      17.658  18.313  50.859  1.00 30.72           O  
ANISOU  951  O   LYS B  18     3726   3982   3966   1012     73    344       O  
ATOM    952  CB  LYS B  18      16.024  16.992  48.708  1.00 24.59           C  
ANISOU  952  CB  LYS B  18     2891   3290   3164   1041     72    336       C  
ATOM    953  CG  LYS B  18      16.438  17.793  47.466  1.00 29.93           C  
ANISOU  953  CG  LYS B  18     3539   3993   3841   1065     89    350       C  
ATOM    954  CD  LYS B  18      17.116  16.856  46.464  1.00 29.69           C  
ANISOU  954  CD  LYS B  18     3486   3984   3812   1070     67    333       C  
ATOM    955  CE  LYS B  18      17.404  17.550  45.132  1.00 32.99           C  
ANISOU  955  CE  LYS B  18     3874   4432   4229   1095     84    346       C  
ATOM    956  NZ  LYS B  18      18.585  18.455  45.203  1.00 30.26           N  
ANISOU  956  NZ  LYS B  18     3534   4066   3898   1099     91    353       N  
ATOM    957  N   MET B  19      19.272  17.634  49.451  1.00 27.88           N  
ANISOU  957  N   MET B  19     3330   3647   3616   1027     47    329       N  
ATOM    958  CA  MET B  19      20.147  18.768  49.705  1.00 28.86           C  
ANISOU  958  CA  MET B  19     3463   3755   3750   1024     61    341       C  
ATOM    959  C   MET B  19      20.549  19.319  48.361  1.00 35.52           C  
ANISOU  959  C   MET B  19     4276   4626   4593   1046     75    349       C  
ATOM    960  O   MET B  19      20.692  18.546  47.407  1.00 31.48           O  
ANISOU  960  O   MET B  19     3739   4141   4080   1059     62    339       O  
ATOM    961  CB  MET B  19      21.359  18.344  50.518  1.00 36.18           C  
ANISOU  961  CB  MET B  19     4405   4656   4688   1005     34    329       C  
ATOM    962  CG  MET B  19      20.954  17.644  51.814  1.00 37.23           C  
ANISOU  962  CG  MET B  19     4566   4760   4818    983     17    319       C  
ATOM    963  SD  MET B  19      21.867  18.291  53.210  1.00 40.63           S  
ANISOU  963  SD  MET B  19     5029   5153   5256    954     12    323       S  
ATOM    964  CE  MET B  19      23.475  17.579  52.887  1.00 61.94           C  
ANISOU  964  CE  MET B  19     7708   7861   7965    957    -19    311       C  
ATOM    965  N   LYS B  20      20.716  20.639  48.276  1.00 31.42           N  
ANISOU  965  N   LYS B  20     3762   4102   4073   1050    103    366       N  
ATOM    966  CA  LYS B  20      21.071  21.269  47.001  1.00 32.66           C  
ANISOU  966  CA  LYS B  20     3894   4285   4229   1072    120    375       C  
ATOM    967  C   LYS B  20      22.331  20.658  46.431  1.00 32.57           C  
ANISOU  967  C   LYS B  20     3863   4284   4228   1072     96    361       C  
ATOM    968  O   LYS B  20      23.289  20.445  47.160  1.00 32.16           O  
ANISOU  968  O   LYS B  20     3823   4212   4186   1054     77    352       O  
ATOM    969  CB  LYS B  20      21.261  22.778  47.154  1.00 42.73           C  
ANISOU  969  CB  LYS B  20     5187   5545   5502   1072    154    394       C  
ATOM    970  CG  LYS B  20      21.176  23.532  45.819  1.00 47.15           C  
ANISOU  970  CG  LYS B  20     5724   6133   6056   1099    180    408       C  
ATOM    971  CD  LYS B  20      20.950  25.034  46.006  1.00 54.73           C  
ANISOU  971  CD  LYS B  20     6708   7076   7009   1104    223    431       C  
ATOM    972  CE  LYS B  20      22.266  25.793  46.109  1.00 64.43           C  
ANISOU  972  CE  LYS B  20     7950   8287   8244   1087    229    429       C  
ATOM    973  NZ  LYS B  20      23.131  25.657  44.887  1.00 66.22           N  
ANISOU  973  NZ  LYS B  20     8144   8541   8475   1100    221    423       N  
ATOM    974  N   GLY B  21      22.315  20.350  45.133  1.00 30.70           N  
ANISOU  974  N   GLY B  21     3596   4080   3989   1094     96    359       N  
ATOM    975  CA  GLY B  21      23.489  19.813  44.460  1.00 33.95           C  
ANISOU  975  CA  GLY B  21     3986   4502   4409   1098     77    347       C  
ATOM    976  C   GLY B  21      23.523  18.300  44.439  1.00 36.16           C  
ANISOU  976  C   GLY B  21     4260   4788   4690   1097     46    328       C  
ATOM    977  O   GLY B  21      24.352  17.697  43.761  1.00 37.78           O  
ANISOU  977  O   GLY B  21     4448   5006   4902   1105     32    318       O  
ATOM    978  N   TYR B  22      22.626  17.678  45.194  1.00 28.26           N  
ANISOU  978  N   TYR B  22     3278   3777   3685   1087     38    322       N  
ATOM    979  CA  TYR B  22      22.617  16.229  45.315  1.00 26.33           C  
ANISOU  979  CA  TYR B  22     3036   3531   3439   1082     12    303       C  
ATOM    980  C   TYR B  22      21.290  15.631  44.879  1.00 23.85           C  
ANISOU  980  C   TYR B  22     2717   3237   3109   1086     16    300       C  
ATOM    981  O   TYR B  22      20.235  16.261  45.037  1.00 27.04           O  
ANISOU  981  O   TYR B  22     3123   3647   3504   1085     35    312       O  
ATOM    982  CB  TYR B  22      22.885  15.808  46.766  1.00 28.85           C  
ANISOU  982  CB  TYR B  22     3385   3815   3764   1061     -7    296       C  
ATOM    983  CG  TYR B  22      24.267  16.106  47.244  1.00 30.14           C  
ANISOU  983  CG  TYR B  22     3551   3963   3940   1055    -18    297       C  
ATOM    984  CD1 TYR B  22      24.567  17.329  47.824  1.00 33.47           C  
ANISOU  984  CD1 TYR B  22     3984   4370   4365   1043     -4    310       C  
ATOM    985  CD2 TYR B  22      25.273  15.161  47.139  1.00 29.89           C  
ANISOU  985  CD2 TYR B  22     3511   3931   3914   1059    -43    285       C  
ATOM    986  CE1 TYR B  22      25.848  17.609  48.284  1.00 40.26           C  
ANISOU  986  CE1 TYR B  22     4845   5220   5233   1032    -14    310       C  
ATOM    987  CE2 TYR B  22      26.555  15.429  47.605  1.00 41.74           C  
ANISOU  987  CE2 TYR B  22     5011   5423   5425   1053    -54    287       C  
ATOM    988  CZ  TYR B  22      26.837  16.655  48.168  1.00 40.61           C  
ANISOU  988  CZ  TYR B  22     4876   5269   5284   1037    -41    299       C  
ATOM    989  OH  TYR B  22      28.111  16.925  48.622  1.00 48.96           O  
ANISOU  989  OH  TYR B  22     5931   6324   6349   1026    -52    301       O  
ATOM    990  N   PRO B  23      21.331  14.390  44.385  1.00 23.72           N  
ANISOU  990  N   PRO B  23     2694   3231   3088   1087     -1    283       N  
ATOM    991  CA  PRO B  23      20.095  13.644  44.176  1.00 23.50           C  
ANISOU  991  CA  PRO B  23     2667   3220   3042   1081     -1    275       C  
ATOM    992  C   PRO B  23      19.388  13.384  45.496  1.00 29.77           C  
ANISOU  992  C   PRO B  23     3490   3988   3832   1061     -6    272       C  
ATOM    993  O   PRO B  23      20.046  13.384  46.538  1.00 24.15           O  
ANISOU  993  O   PRO B  23     2801   3243   3133   1051    -18    270       O  
ATOM    994  CB  PRO B  23      20.576  12.326  43.560  1.00 25.46           C  
ANISOU  994  CB  PRO B  23     2913   3474   3288   1083    -18    256       C  
ATOM    995  CG  PRO B  23      21.983  12.190  44.011  1.00 24.95           C  
ANISOU  995  CG  PRO B  23     2855   3383   3240   1087    -34    251       C  
ATOM    996  CD  PRO B  23      22.529  13.581  44.088  1.00 25.98           C  
ANISOU  996  CD  PRO B  23     2977   3512   3384   1093    -20    269       C  
ATOM    997  N   HIS B  24      18.079  13.169  45.446  1.00 27.47           N  
ANISOU  997  N   HIS B  24     3199   3716   3524   1054      2    273       N  
ATOM    998  CA  HIS B  24      17.337  12.681  46.609  1.00 26.65           C  
ANISOU  998  CA  HIS B  24     3123   3590   3414   1033     -5    265       C  
ATOM    999  C   HIS B  24      18.029  11.419  47.146  1.00 26.64           C  
ANISOU  999  C   HIS B  24     3145   3561   3417   1022    -31    243       C  
ATOM   1000  O   HIS B  24      18.207  10.430  46.401  1.00 23.90           O  
ANISOU 1000  O   HIS B  24     2792   3226   3062   1024    -40    229       O  
ATOM   1001  CB  HIS B  24      15.888  12.408  46.228  1.00 23.59           C  
ANISOU 1001  CB  HIS B  24     2724   3235   3003   1027      5    266       C  
ATOM   1002  CG  HIS B  24      15.130  13.645  45.838  1.00 28.45           C  
ANISOU 1002  CG  HIS B  24     3318   3879   3614   1042     32    291       C  
ATOM   1003  ND1 HIS B  24      15.287  14.263  44.609  1.00 23.23           N  
ANISOU 1003  ND1 HIS B  24     2626   3250   2951   1064     46    303       N  
ATOM   1004  CD2 HIS B  24      14.240  14.396  46.521  1.00 26.85           C  
ANISOU 1004  CD2 HIS B  24     3122   3673   3407   1040     49    307       C  
ATOM   1005  CE1 HIS B  24      14.506  15.329  44.552  1.00 29.82           C  
ANISOU 1005  CE1 HIS B  24     3449   4102   3779   1076     71    326       C  
ATOM   1006  NE2 HIS B  24      13.859  15.436  45.703  1.00 30.44           N  
ANISOU 1006  NE2 HIS B  24     3550   4160   3856   1063     74    329       N  
ATOM   1007  N   TRP B  25      18.402  11.453  48.432  1.00 20.70           N  
ANISOU 1007  N   TRP B  25     2420   2770   2675   1010    -41    242       N  
ATOM   1008  CA  TRP B  25      19.355  10.506  49.002  1.00 20.00           C  
ANISOU 1008  CA  TRP B  25     2353   2653   2594   1005    -65    227       C  
ATOM   1009  C   TRP B  25      18.764   9.625  50.095  1.00 24.53           C  
ANISOU 1009  C   TRP B  25     2962   3200   3160    984    -77    214       C  
ATOM   1010  O   TRP B  25      18.096  10.151  50.974  1.00 23.64           O  
ANISOU 1010  O   TRP B  25     2863   3075   3046    970    -70    221       O  
ATOM   1011  CB  TRP B  25      20.539  11.284  49.586  1.00 17.45           C  
ANISOU 1011  CB  TRP B  25     2032   2309   2290   1009    -70    238       C  
ATOM   1012  CG  TRP B  25      21.793  10.498  49.647  1.00 19.84           C  
ANISOU 1012  CG  TRP B  25     2338   2598   2601   1016    -92    228       C  
ATOM   1013  CD1 TRP B  25      22.107   9.516  50.539  1.00 21.11           C  
ANISOU 1013  CD1 TRP B  25     2527   2731   2761   1008   -112    216       C  
ATOM   1014  CD2 TRP B  25      22.934  10.635  48.779  1.00 23.61           C  
ANISOU 1014  CD2 TRP B  25     2791   3091   3088   1036    -94    231       C  
ATOM   1015  NE1 TRP B  25      23.369   9.019  50.265  1.00 22.73           N  
ANISOU 1015  NE1 TRP B  25     2725   2936   2976   1024   -126    213       N  
ATOM   1016  CE2 TRP B  25      23.892   9.695  49.190  1.00 24.14           C  
ANISOU 1016  CE2 TRP B  25     2870   3141   3161   1040   -116    222       C  
ATOM   1017  CE3 TRP B  25      23.219  11.452  47.676  1.00 28.50           C  
ANISOU 1017  CE3 TRP B  25     3378   3737   3711   1051    -79    241       C  
ATOM   1018  CZ2 TRP B  25      25.136   9.556  48.551  1.00 25.80           C  
ANISOU 1018  CZ2 TRP B  25     3061   3362   3380   1059   -123    223       C  
ATOM   1019  CZ3 TRP B  25      24.450  11.318  47.045  1.00 31.96           C  
ANISOU 1019  CZ3 TRP B  25     3799   4185   4160   1067    -86    240       C  
ATOM   1020  CH2 TRP B  25      25.391  10.378  47.483  1.00 24.56           C  
ANISOU 1020  CH2 TRP B  25     2872   3231   3227   1072   -108    232       C  
ATOM   1021  N   PRO B  26      19.031   8.302  50.051  1.00 22.33           N  
ANISOU 1021  N   PRO B  26     2699   2912   2874    982    -93    195       N  
ATOM   1022  CA  PRO B  26      18.557   7.378  51.083  1.00 27.80           C  
ANISOU 1022  CA  PRO B  26     3428   3576   3557    962   -104    181       C  
ATOM   1023  C   PRO B  26      19.039   7.843  52.448  1.00 29.86           C  
ANISOU 1023  C   PRO B  26     3711   3802   3833    953   -114    188       C  
ATOM   1024  O   PRO B  26      20.250   8.031  52.634  1.00 20.09           O  
ANISOU 1024  O   PRO B  26     2470   2553   2610    964   -125    193       O  
ATOM   1025  CB  PRO B  26      19.199   6.038  50.693  1.00 21.79           C  
ANISOU 1025  CB  PRO B  26     2680   2808   2792    969   -117    163       C  
ATOM   1026  CG  PRO B  26      20.372   6.405  49.866  1.00 20.04           C  
ANISOU 1026  CG  PRO B  26     2431   2598   2584    994   -119    171       C  
ATOM   1027  CD  PRO B  26      19.895   7.606  49.074  1.00 19.31           C  
ANISOU 1027  CD  PRO B  26     2305   2540   2493    999   -100    187       C  
ATOM   1028  N   ALA B  27      18.106   8.051  53.379  1.00 23.60           N  
ANISOU 1028  N   ALA B  27     2938   2995   3034    933   -109    189       N  
ATOM   1029  CA  ALA B  27      18.455   8.638  54.673  1.00 19.11           C  
ANISOU 1029  CA  ALA B  27     2390   2394   2476    922   -115    197       C  
ATOM   1030  C   ALA B  27      17.568   8.154  55.807  1.00 21.17           C  
ANISOU 1030  C   ALA B  27     2687   2629   2728    898   -118    188       C  
ATOM   1031  O   ALA B  27      16.603   7.435  55.597  1.00 22.23           O  
ANISOU 1031  O   ALA B  27     2828   2773   2846    888   -114    176       O  
ATOM   1032  CB  ALA B  27      18.373  10.138  54.597  1.00 15.85           C  
ANISOU 1032  CB  ALA B  27     1960   1992   2072    925    -96    218       C  
ATOM   1033  N   ARG B  28      17.910   8.594  57.009  1.00 21.86           N  
ANISOU 1033  N   ARG B  28     2796   2685   2824    886   -125    194       N  
ATOM   1034  CA  ARG B  28      17.195   8.179  58.220  1.00 26.07           C  
ANISOU 1034  CA  ARG B  28     3367   3190   3350    862   -129    186       C  
ATOM   1035  C   ARG B  28      17.036   9.376  59.140  1.00 28.09           C  
ANISOU 1035  C   ARG B  28     3632   3427   3613    849   -118    202       C  
ATOM   1036  O   ARG B  28      17.953  10.187  59.267  1.00 24.08           O  
ANISOU 1036  O   ARG B  28     3116   2915   3118    854   -119    215       O  
ATOM   1037  CB  ARG B  28      17.948   7.054  58.941  1.00 29.23           C  
ANISOU 1037  CB  ARG B  28     3796   3559   3749    858   -155    173       C  
ATOM   1038  CG  ARG B  28      17.290   6.599  60.242  1.00 28.34           C  
ANISOU 1038  CG  ARG B  28     3725   3413   3629    833   -160    164       C  
ATOM   1039  CD  ARG B  28      18.183   5.580  60.984  1.00 31.90           C  
ANISOU 1039  CD  ARG B  28     4206   3833   4080    834   -186    154       C  
ATOM   1040  NE  ARG B  28      19.412   6.174  61.495  1.00 30.62           N  
ANISOU 1040  NE  ARG B  28     4039   3661   3933    839   -199    168       N  
ATOM   1041  CZ  ARG B  28      20.623   5.653  61.336  1.00 26.09           C  
ANISOU 1041  CZ  ARG B  28     3460   3088   3365    858   -217    168       C  
ATOM   1042  NH1 ARG B  28      20.782   4.522  60.665  1.00 23.63           N  
ANISOU 1042  NH1 ARG B  28     3151   2782   3046    875   -222    156       N  
ATOM   1043  NH2 ARG B  28      21.676   6.262  61.853  1.00 31.77           N  
ANISOU 1043  NH2 ARG B  28     4173   3803   4096    859   -228    182       N  
ATOM   1044  N   ILE B  29      15.874   9.484  59.780  1.00 19.13           N  
ANISOU 1044  N   ILE B  29     2515   2284   2469    831   -106    201       N  
ATOM   1045  CA  ILE B  29      15.690  10.455  60.850  1.00 23.71           C  
ANISOU 1045  CA  ILE B  29     3115   2838   3055    816    -96    213       C  
ATOM   1046  C   ILE B  29      16.335   9.939  62.141  1.00 22.29           C  
ANISOU 1046  C   ILE B  29     2972   2618   2878    798   -119    205       C  
ATOM   1047  O   ILE B  29      15.921   8.908  62.666  1.00 24.51           O  
ANISOU 1047  O   ILE B  29     3278   2883   3150    786   -131    190       O  
ATOM   1048  CB  ILE B  29      14.198  10.728  61.114  1.00 24.40           C  
ANISOU 1048  CB  ILE B  29     3209   2930   3131    805    -73    216       C  
ATOM   1049  CG1 ILE B  29      13.472  11.037  59.802  1.00 26.71           C  
ANISOU 1049  CG1 ILE B  29     3464   3270   3416    824    -53    223       C  
ATOM   1050  CG2 ILE B  29      14.040  11.901  62.062  1.00 26.39           C  
ANISOU 1050  CG2 ILE B  29     3480   3158   3389    793    -56    232       C  
ATOM   1051  CD1 ILE B  29      13.844  12.343  59.212  1.00 34.71           C  
ANISOU 1051  CD1 ILE B  29     4452   4298   4438    842    -34    245       C  
ATOM   1052  N   ASP B  30      17.348  10.645  62.642  1.00 27.43           N  
ANISOU 1052  N   ASP B  30     3627   3254   3541    795   -124    216       N  
ATOM   1053  CA  ASP B  30      18.018  10.239  63.881  1.00 27.42           C  
ANISOU 1053  CA  ASP B  30     3659   3219   3542    777   -147    212       C  
ATOM   1054  C   ASP B  30      17.261  10.789  65.093  1.00 28.35           C  
ANISOU 1054  C   ASP B  30     3810   3306   3656    750   -135    215       C  
ATOM   1055  O   ASP B  30      16.371  11.623  64.951  1.00 32.35           O  
ANISOU 1055  O   ASP B  30     4312   3819   4161    748   -107    225       O  
ATOM   1056  CB  ASP B  30      19.473  10.710  63.898  1.00 29.10           C  
ANISOU 1056  CB  ASP B  30     3859   3434   3765    782   -160    222       C  
ATOM   1057  CG  ASP B  30      20.436   9.674  63.304  1.00 30.75           C  
ANISOU 1057  CG  ASP B  30     4052   3656   3976    803   -184    213       C  
ATOM   1058  OD1 ASP B  30      20.012   8.519  63.103  1.00 32.79           O  
ANISOU 1058  OD1 ASP B  30     4320   3913   4226    810   -192    198       O  
ATOM   1059  OD2 ASP B  30      21.617  10.009  63.055  1.00 33.18           O  
ANISOU 1059  OD2 ASP B  30     4341   3976   4292    812   -193    222       O  
ATOM   1060  N   GLU B  31      17.588  10.311  66.287  1.00 34.52           N  
ANISOU 1060  N   GLU B  31     4626   4055   4436    731   -154    209       N  
ATOM   1061  CA  GLU B  31      16.897  10.828  67.460  1.00 37.96           C  
ANISOU 1061  CA  GLU B  31     5095   4461   4869    704   -142    212       C  
ATOM   1062  C   GLU B  31      17.546  12.133  67.881  1.00 37.65           C  
ANISOU 1062  C   GLU B  31     5058   4412   4836    692   -132    230       C  
ATOM   1063  O   GLU B  31      18.730  12.348  67.637  1.00 37.75           O  
ANISOU 1063  O   GLU B  31     5055   4435   4854    697   -145    235       O  
ATOM   1064  CB  GLU B  31      16.904   9.820  68.617  1.00 48.99           C  
ANISOU 1064  CB  GLU B  31     6531   5825   6260    685   -165    199       C  
ATOM   1065  CG  GLU B  31      18.119   9.882  69.527  1.00 54.52           C  
ANISOU 1065  CG  GLU B  31     7248   6504   6963    672   -188    203       C  
ATOM   1066  CD  GLU B  31      19.271   9.050  69.013  1.00 66.41           C  
ANISOU 1066  CD  GLU B  31     8735   8026   8472    694   -215    200       C  
ATOM   1067  OE1 GLU B  31      19.200   8.589  67.853  1.00 69.68           O  
ANISOU 1067  OE1 GLU B  31     9122   8467   8887    719   -213    194       O  
ATOM   1068  OE2 GLU B  31      20.246   8.852  69.771  1.00 68.87           O  
ANISOU 1068  OE2 GLU B  31     9058   8325   8783    686   -238    203       O  
ATOM   1069  N   LEU B  32      16.765  13.005  68.507  1.00 41.30           N  
ANISOU 1069  N   LEU B  32     5542   4856   5296    674   -106    238       N  
ATOM   1070  CA  LEU B  32      17.318  14.214  69.103  1.00 53.63           C  
ANISOU 1070  CA  LEU B  32     7117   6400   6859    656    -94    253       C  
ATOM   1071  C   LEU B  32      17.311  14.050  70.612  1.00 57.92           C  
ANISOU 1071  C   LEU B  32     7705   6903   7398    623   -105    248       C  
ATOM   1072  O   LEU B  32      16.267  14.206  71.244  1.00 67.05           O  
ANISOU 1072  O   LEU B  32     8889   8039   8550    609    -87    248       O  
ATOM   1073  CB  LEU B  32      16.523  15.454  68.685  1.00 57.15           C  
ANISOU 1073  CB  LEU B  32     7558   6852   7305    662    -52    268       C  
ATOM   1074  CG  LEU B  32      17.148  16.835  68.931  1.00 65.52           C  
ANISOU 1074  CG  LEU B  32     8628   7901   8366    648    -31    285       C  
ATOM   1075  CD1 LEU B  32      16.990  17.312  70.380  1.00 68.78           C  
ANISOU 1075  CD1 LEU B  32     9089   8271   8773    612    -23    288       C  
ATOM   1076  CD2 LEU B  32      18.619  16.845  68.516  1.00 63.69           C  
ANISOU 1076  CD2 LEU B  32     8373   7686   8139    650    -53    286       C  
ATOM   1077  N   PRO B  33      18.476  13.731  71.196  1.00 58.77           N  
ANISOU 1077  N   PRO B  33     7821   7002   7506    610   -134    246       N  
ATOM   1078  CA  PRO B  33      18.551  13.549  72.648  1.00 59.17           C  
ANISOU 1078  CA  PRO B  33     7914   7016   7551    577   -147    243       C  
ATOM   1079  C   PRO B  33      18.179  14.824  73.395  1.00 64.66           C  
ANISOU 1079  C   PRO B  33     8638   7686   8243    549   -117    254       C  
ATOM   1080  O   PRO B  33      18.777  15.865  73.134  1.00 68.01           O  
ANISOU 1080  O   PRO B  33     9054   8118   8668    544   -102    267       O  
ATOM   1081  CB  PRO B  33      20.026  13.195  72.889  1.00 55.03           C  
ANISOU 1081  CB  PRO B  33     7382   6500   7028    573   -181    244       C  
ATOM   1082  CG  PRO B  33      20.579  12.830  71.558  1.00 60.81           C  
ANISOU 1082  CG  PRO B  33     8068   7270   7766    608   -189    243       C  
ATOM   1083  CD  PRO B  33      19.795  13.612  70.556  1.00 58.84           C  
ANISOU 1083  CD  PRO B  33     7798   7037   7520    624   -155    249       C  
ATOM   1084  N   GLU B  34      17.197  14.764  74.287  1.00 68.53           N  
ANISOU 1084  N   GLU B  34     9165   8145   8728    531   -105    250       N  
ATOM   1085  CA  GLU B  34      16.998  15.878  75.197  1.00 64.40           C  
ANISOU 1085  CA  GLU B  34     8678   7592   8200    500    -79    261       C  
ATOM   1086  C   GLU B  34      18.227  15.901  76.092  1.00 48.41           C  
ANISOU 1086  C   GLU B  34     6670   5553   6170    469   -106    261       C  
ATOM   1087  O   GLU B  34      18.880  14.875  76.281  1.00 46.46           O  
ANISOU 1087  O   GLU B  34     6416   5312   5923    472   -143    252       O  
ATOM   1088  CB  GLU B  34      15.703  15.745  76.003  1.00 75.13           C  
ANISOU 1088  CB  GLU B  34    10072   8920   9554    486    -62    256       C  
ATOM   1089  CG  GLU B  34      14.503  16.393  75.335  1.00 87.59           C  
ANISOU 1089  CG  GLU B  34    11639  10507  11132    507    -21    264       C  
ATOM   1090  CD  GLU B  34      13.768  17.350  76.256  1.00 98.39           C  
ANISOU 1090  CD  GLU B  34    13049  11840  12495    484     15    274       C  
ATOM   1091  OE1 GLU B  34      13.844  17.169  77.492  1.00 99.93           O  
ANISOU 1091  OE1 GLU B  34    13285  11999  12685    451      5    268       O  
ATOM   1092  OE2 GLU B  34      13.130  18.296  75.742  1.00101.38           O  
ANISOU 1092  OE2 GLU B  34    13421  12225  12874    499     55    289       O  
ATOM   1093  N   GLY B  35      18.550  17.069  76.629  1.00 57.91           N  
ANISOU 1093  N   GLY B  35     7896   6739   7368    440    -85    273       N  
ATOM   1094  CA  GLY B  35      19.819  17.247  77.307  1.00 56.70           C  
ANISOU 1094  CA  GLY B  35     7752   6584   7208    410   -109    276       C  
ATOM   1095  C   GLY B  35      20.895  17.610  76.303  1.00 50.74           C  
ANISOU 1095  C   GLY B  35     6955   5868   6457    425   -115    283       C  
ATOM   1096  O   GLY B  35      22.083  17.582  76.606  1.00 53.36           O  
ANISOU 1096  O   GLY B  35     7279   6212   6784    407   -140    286       O  
ATOM   1097  N   ALA B  36      20.473  17.919  75.082  1.00 44.38           N  
ANISOU 1097  N   ALA B  36     6119   5084   5659    458    -92    287       N  
ATOM   1098  CA  ALA B  36      21.371  18.475  74.087  1.00 40.17           C  
ANISOU 1098  CA  ALA B  36     5549   4585   5129    471    -90    295       C  
ATOM   1099  C   ALA B  36      20.843  19.840  73.709  1.00 42.27           C  
ANISOU 1099  C   ALA B  36     5825   4842   5392    469    -41    308       C  
ATOM   1100  O   ALA B  36      19.717  20.186  74.057  1.00 50.72           O  
ANISOU 1100  O   ALA B  36     6924   5886   6461    467    -11    310       O  
ATOM   1101  CB  ALA B  36      21.472  17.575  72.859  1.00 38.10           C  
ANISOU 1101  CB  ALA B  36     5240   4359   4878    516   -108    289       C  
ATOM   1102  N   VAL B  37      21.657  20.623  73.015  1.00 30.79           N  
ANISOU 1102  N   VAL B  37     4351   3409   3938    470    -31    316       N  
ATOM   1103  CA  VAL B  37      21.182  21.872  72.453  1.00 29.22           C  
ANISOU 1103  CA  VAL B  37     4159   3206   3737    476     18    329       C  
ATOM   1104  C   VAL B  37      20.051  21.557  71.482  1.00 34.82           C  
ANISOU 1104  C   VAL B  37     4845   3930   4456    522     34    329       C  
ATOM   1105  O   VAL B  37      20.193  20.673  70.646  1.00 31.57           O  
ANISOU 1105  O   VAL B  37     4394   3550   4053    552      9    322       O  
ATOM   1106  CB  VAL B  37      22.295  22.631  71.721  1.00 29.73           C  
ANISOU 1106  CB  VAL B  37     4200   3296   3798    472     23    336       C  
ATOM   1107  CG1 VAL B  37      21.761  23.943  71.141  1.00 35.75           C  
ANISOU 1107  CG1 VAL B  37     4975   4051   4557    481     76    350       C  
ATOM   1108  CG2 VAL B  37      23.460  22.901  72.660  1.00 41.10           C  
ANISOU 1108  CG2 VAL B  37     5660   4731   5227    424      4    336       C  
ATOM   1109  N   LYS B  38      18.928  22.261  71.591  1.00 36.88           N  
ANISOU 1109  N   LYS B  38     5130   4169   4713    527     75    338       N  
ATOM   1110  CA  LYS B  38      17.820  21.997  70.680  1.00 43.10           C  
ANISOU 1110  CA  LYS B  38     5893   4977   5507    569     91    341       C  
ATOM   1111  C   LYS B  38      18.086  22.629  69.317  1.00 41.96           C  
ANISOU 1111  C   LYS B  38     5713   4864   5365    599    110    351       C  
ATOM   1112  O   LYS B  38      18.668  23.707  69.233  1.00 44.69           O  
ANISOU 1112  O   LYS B  38     6070   5203   5705    586    134    362       O  
ATOM   1113  CB  LYS B  38      16.500  22.501  71.266  1.00 49.23           C  
ANISOU 1113  CB  LYS B  38     6704   5724   6278    567    129    349       C  
ATOM   1114  CG  LYS B  38      15.986  21.644  72.422  1.00 55.96           C  
ANISOU 1114  CG  LYS B  38     7584   6549   7128    546    109    336       C  
ATOM   1115  CD  LYS B  38      14.780  20.816  71.989  1.00 70.09           C  
ANISOU 1115  CD  LYS B  38     9353   8356   8922    576    107    331       C  
ATOM   1116  CE  LYS B  38      14.150  20.048  73.149  1.00 78.13           C  
ANISOU 1116  CE  LYS B  38    10402   9346   9937    554     93    319       C  
ATOM   1117  NZ  LYS B  38      13.511  18.767  72.710  1.00 81.13           N  
ANISOU 1117  NZ  LYS B  38    10756   9750  10320    574     69    304       N  
ATOM   1118  N   PRO B  39      17.675  21.946  68.237  1.00 46.26           N  
ANISOU 1118  N   PRO B  39     6215   5444   5917    637    100    348       N  
ATOM   1119  CA  PRO B  39      17.849  22.463  66.875  1.00 50.56           C  
ANISOU 1119  CA  PRO B  39     6724   6022   6465    668    117    357       C  
ATOM   1120  C   PRO B  39      16.787  23.499  66.545  1.00 49.35           C  
ANISOU 1120  C   PRO B  39     6581   5863   6305    688    169    376       C  
ATOM   1121  O   PRO B  39      15.868  23.676  67.344  1.00 40.60           O  
ANISOU 1121  O   PRO B  39     5506   4729   5193    680    188    380       O  
ATOM   1122  CB  PRO B  39      17.684  21.214  66.012  1.00 54.16           C  
ANISOU 1122  CB  PRO B  39     7138   6514   6928    697     87    345       C  
ATOM   1123  CG  PRO B  39      16.735  20.380  66.780  1.00 52.53           C  
ANISOU 1123  CG  PRO B  39     6949   6291   6720    691     76    335       C  
ATOM   1124  CD  PRO B  39      17.062  20.607  68.235  1.00 50.60           C  
ANISOU 1124  CD  PRO B  39     6751   6005   6472    650     72    333       C  
ATOM   1125  N   PRO B  40      16.901  24.172  65.384  1.00 57.91           N  
ANISOU 1125  N   PRO B  40     7641   6973   7390    715    191    388       N  
ATOM   1126  CA  PRO B  40      15.800  25.049  64.981  1.00 50.52           C  
ANISOU 1126  CA  PRO B  40     6711   6038   6448    742    239    408       C  
ATOM   1127  C   PRO B  40      14.515  24.255  64.896  1.00 41.30           C  
ANISOU 1127  C   PRO B  40     5527   4886   5280    764    235    406       C  
ATOM   1128  O   PRO B  40      14.560  23.043  64.698  1.00 38.41           O  
ANISOU 1128  O   PRO B  40     5135   4540   4919    766    197    388       O  
ATOM   1129  CB  PRO B  40      16.223  25.550  63.598  1.00 56.58           C  
ANISOU 1129  CB  PRO B  40     7443   6839   7217    772    252    417       C  
ATOM   1130  CG  PRO B  40      17.684  25.380  63.564  1.00 58.23           C  
ANISOU 1130  CG  PRO B  40     7644   7051   7430    749    222    405       C  
ATOM   1131  CD  PRO B  40      17.989  24.173  64.393  1.00 59.28           C  
ANISOU 1131  CD  PRO B  40     7780   7177   7569    725    176    385       C  
ATOM   1132  N   ALA B  41      13.384  24.929  65.046  1.00 35.33           N  
ANISOU 1132  N   ALA B  41     4787   4121   4516    779    277    423       N  
ATOM   1133  CA  ALA B  41      12.107  24.242  65.051  1.00 40.69           C  
ANISOU 1133  CA  ALA B  41     5451   4816   5192    796    276    422       C  
ATOM   1134  C   ALA B  41      11.872  23.575  63.705  1.00 40.63           C  
ANISOU 1134  C   ALA B  41     5388   4862   5186    829    259    419       C  
ATOM   1135  O   ALA B  41      12.295  24.089  62.670  1.00 38.09           O  
ANISOU 1135  O   ALA B  41     5042   4564   4865    851    270    429       O  
ATOM   1136  CB  ALA B  41      10.983  25.205  65.372  1.00 43.95           C  
ANISOU 1136  CB  ALA B  41     5889   5215   5596    811    327    445       C  
ATOM   1137  N   ASN B  42      11.208  22.424  63.747  1.00 37.12           N  
ANISOU 1137  N   ASN B  42     4926   4436   4741    829    234    405       N  
ATOM   1138  CA  ASN B  42      10.840  21.667  62.565  1.00 41.08           C  
ANISOU 1138  CA  ASN B  42     5378   4989   5241    855    219    400       C  
ATOM   1139  C   ASN B  42      12.037  21.236  61.719  1.00 36.72           C  
ANISOU 1139  C   ASN B  42     4800   4456   4698    858    189    388       C  
ATOM   1140  O   ASN B  42      11.885  20.969  60.537  1.00 45.88           O  
ANISOU 1140  O   ASN B  42     5920   5658   5856    883    186    389       O  
ATOM   1141  CB  ASN B  42       9.868  22.469  61.702  1.00 47.08           C  
ANISOU 1141  CB  ASN B  42     6115   5782   5992    892    259    425       C  
ATOM   1142  CG  ASN B  42       8.604  22.830  62.442  1.00 56.12           C  
ANISOU 1142  CG  ASN B  42     7280   6915   7127    895    289    439       C  
ATOM   1143  OD1 ASN B  42       8.274  24.007  62.586  1.00 61.67           O  
ANISOU 1143  OD1 ASN B  42     8003   7605   7826    910    333    463       O  
ATOM   1144  ND2 ASN B  42       7.888  21.818  62.927  1.00 51.39           N  
ANISOU 1144  ND2 ASN B  42     6679   6322   6524    881    269    424       N  
ATOM   1145  N   LYS B  43      13.220  21.176  62.323  1.00 33.46           N  
ANISOU 1145  N   LYS B  43     4408   4013   4293    832    168    377       N  
ATOM   1146  CA  LYS B  43      14.380  20.588  61.651  1.00 31.32           C  
ANISOU 1146  CA  LYS B  43     4112   3759   4029    833    135    364       C  
ATOM   1147  C   LYS B  43      14.759  19.296  62.363  1.00 36.98           C  
ANISOU 1147  C   LYS B  43     4839   4463   4750    811     93    341       C  
ATOM   1148  O   LYS B  43      14.678  19.196  63.596  1.00 31.29           O  
ANISOU 1148  O   LYS B  43     4154   3706   4028    784     88    336       O  
ATOM   1149  CB  LYS B  43      15.560  21.566  61.611  1.00 29.03           C  
ANISOU 1149  CB  LYS B  43     3831   3455   3743    826    145    372       C  
ATOM   1150  CG  LYS B  43      15.353  22.726  60.654  1.00 40.57           C  
ANISOU 1150  CG  LYS B  43     5279   4935   5202    853    184    394       C  
ATOM   1151  CD  LYS B  43      16.626  23.016  59.878  1.00 48.82           C  
ANISOU 1151  CD  LYS B  43     6305   5994   6253    856    175    393       C  
ATOM   1152  CE  LYS B  43      16.411  24.058  58.793  1.00 48.59           C  
ANISOU 1152  CE  LYS B  43     6258   5985   6218    886    213    413       C  
ATOM   1153  NZ  LYS B  43      17.649  24.219  57.981  1.00 60.16           N  
ANISOU 1153  NZ  LYS B  43     7701   7466   7689    889    201    409       N  
ATOM   1154  N   TYR B  44      15.145  18.300  61.576  1.00 28.36           N  
ANISOU 1154  N   TYR B  44     3717   3398   3661    822     64    327       N  
ATOM   1155  CA  TYR B  44      15.403  16.966  62.084  1.00 31.85           C  
ANISOU 1155  CA  TYR B  44     4166   3830   4104    807     27    305       C  
ATOM   1156  C   TYR B  44      16.829  16.597  61.780  1.00 30.86           C  
ANISOU 1156  C   TYR B  44     4029   3710   3988    808     -1    298       C  
ATOM   1157  O   TYR B  44      17.356  17.014  60.755  1.00 28.88           O  
ANISOU 1157  O   TYR B  44     3749   3484   3740    827      6    304       O  
ATOM   1158  CB  TYR B  44      14.445  15.954  61.455  1.00 34.23           C  
ANISOU 1158  CB  TYR B  44     4448   4161   4398    820     20    294       C  
ATOM   1159  CG  TYR B  44      13.039  16.181  61.908  1.00 31.78           C  
ANISOU 1159  CG  TYR B  44     4150   3848   4078    816     44    301       C  
ATOM   1160  CD1 TYR B  44      12.270  17.194  61.356  1.00 32.86           C  
ANISOU 1160  CD1 TYR B  44     4271   4004   4209    836     80    322       C  
ATOM   1161  CD2 TYR B  44      12.491  15.409  62.923  1.00 34.70           C  
ANISOU 1161  CD2 TYR B  44     4549   4195   4443    794     31    287       C  
ATOM   1162  CE1 TYR B  44      10.966  17.426  61.796  1.00 41.62           C  
ANISOU 1162  CE1 TYR B  44     5391   5115   5309    835    103    330       C  
ATOM   1163  CE2 TYR B  44      11.201  15.619  63.357  1.00 36.30           C  
ANISOU 1163  CE2 TYR B  44     4761   4396   4635    789     53    293       C  
ATOM   1164  CZ  TYR B  44      10.446  16.633  62.799  1.00 36.65           C  
ANISOU 1164  CZ  TYR B  44     4787   4462   4675    811     90    315       C  
ATOM   1165  OH  TYR B  44       9.166  16.839  63.245  1.00 35.91           O  
ANISOU 1165  OH  TYR B  44     4702   4371   4571    809    113    323       O  
ATOM   1166  N   PRO B  45      17.468  15.851  62.691  1.00 33.56           N  
ANISOU 1166  N   PRO B  45     4391   4027   4331    788    -30    285       N  
ATOM   1167  CA  PRO B  45      18.815  15.356  62.425  1.00 32.36           C  
ANISOU 1167  CA  PRO B  45     4225   3883   4186    791    -59    278       C  
ATOM   1168  C   PRO B  45      18.720  14.235  61.408  1.00 29.09           C  
ANISOU 1168  C   PRO B  45     3784   3497   3771    814    -74    266       C  
ATOM   1169  O   PRO B  45      17.936  13.297  61.601  1.00 27.81           O  
ANISOU 1169  O   PRO B  45     3632   3331   3602    812    -82    253       O  
ATOM   1170  CB  PRO B  45      19.293  14.846  63.790  1.00 31.39           C  
ANISOU 1170  CB  PRO B  45     4137   3727   4064    764    -83    270       C  
ATOM   1171  CG  PRO B  45      18.028  14.502  64.523  1.00 29.29           C  
ANISOU 1171  CG  PRO B  45     3898   3440   3790    752    -76    264       C  
ATOM   1172  CD  PRO B  45      16.987  15.479  64.035  1.00 33.22           C  
ANISOU 1172  CD  PRO B  45     4387   3949   4284    762    -37    278       C  
ATOM   1173  N   ILE B  46      19.487  14.351  60.332  1.00 26.48           N  
ANISOU 1173  N   ILE B  46     3421   3194   3447    834    -76    269       N  
ATOM   1174  CA  ILE B  46      19.403  13.400  59.238  1.00 22.44           C  
ANISOU 1174  CA  ILE B  46     2883   2711   2933    857    -86    258       C  
ATOM   1175  C   ILE B  46      20.685  12.578  59.160  1.00 23.74           C  
ANISOU 1175  C   ILE B  46     3041   2876   3104    863   -116    249       C  
ATOM   1176  O   ILE B  46      21.770  13.125  59.311  1.00 27.59           O  
ANISOU 1176  O   ILE B  46     3522   3363   3598    861   -122    257       O  
ATOM   1177  CB  ILE B  46      19.192  14.108  57.886  1.00 22.70           C  
ANISOU 1177  CB  ILE B  46     2881   2778   2966    880    -63    268       C  
ATOM   1178  CG1 ILE B  46      18.021  15.092  57.952  1.00 25.02           C  
ANISOU 1178  CG1 ILE B  46     3179   3073   3253    878    -30    282       C  
ATOM   1179  CG2 ILE B  46      18.924  13.076  56.793  1.00 27.78           C  
ANISOU 1179  CG2 ILE B  46     3501   3451   3604    898    -72    256       C  
ATOM   1180  CD1 ILE B  46      16.721  14.426  58.252  1.00 24.32           C  
ANISOU 1180  CD1 ILE B  46     3103   2985   3154    872    -28    274       C  
ATOM   1181  N   PHE B  47      20.555  11.283  58.896  1.00 25.72           N  
ANISOU 1181  N   PHE B  47     3293   3130   3349    872   -133    234       N  
ATOM   1182  CA  PHE B  47      21.717  10.403  58.670  1.00 19.71           C  
ANISOU 1182  CA  PHE B  47     2524   2373   2593    886   -158    226       C  
ATOM   1183  C   PHE B  47      21.642   9.906  57.234  1.00 25.40           C  
ANISOU 1183  C   PHE B  47     3216   3125   3311    910   -153    221       C  
ATOM   1184  O   PHE B  47      20.696   9.218  56.884  1.00 19.81           O  
ANISOU 1184  O   PHE B  47     2513   2422   2592    911   -148    210       O  
ATOM   1185  CB  PHE B  47      21.706   9.238  59.663  1.00 22.02           C  
ANISOU 1185  CB  PHE B  47     2850   2638   2880    876   -180    213       C  
ATOM   1186  CG  PHE B  47      22.810   8.217  59.451  1.00 23.87           C  
ANISOU 1186  CG  PHE B  47     3079   2873   3115    894   -203    207       C  
ATOM   1187  CD1 PHE B  47      24.076   8.432  59.977  1.00 26.92           C  
ANISOU 1187  CD1 PHE B  47     3462   3257   3510    895   -220    216       C  
ATOM   1188  CD2 PHE B  47      22.572   7.048  58.735  1.00 26.37           C  
ANISOU 1188  CD2 PHE B  47     3397   3197   3424    910   -206    193       C  
ATOM   1189  CE1 PHE B  47      25.098   7.498  59.795  1.00 31.28           C  
ANISOU 1189  CE1 PHE B  47     4008   3813   4062    916   -240    213       C  
ATOM   1190  CE2 PHE B  47      23.589   6.110  58.538  1.00 29.00           C  
ANISOU 1190  CE2 PHE B  47     3729   3530   3758    931   -224    189       C  
ATOM   1191  CZ  PHE B  47      24.855   6.344  59.075  1.00 32.78           C  
ANISOU 1191  CZ  PHE B  47     4202   4007   4247    936   -241    200       C  
ATOM   1192  N   PHE B  48      22.643  10.227  56.413  1.00 31.19           N  
ANISOU 1192  N   PHE B  48     3919   3878   4052    928   -154    227       N  
ATOM   1193  CA  PHE B  48      22.643   9.774  55.017  1.00 27.89           C  
ANISOU 1193  CA  PHE B  48     3474   3490   3632    951   -149    222       C  
ATOM   1194  C   PHE B  48      23.284   8.407  54.906  1.00 23.40           C  
ANISOU 1194  C   PHE B  48     2914   2916   3062    965   -169    209       C  
ATOM   1195  O   PHE B  48      24.424   8.208  55.322  1.00 28.71           O  
ANISOU 1195  O   PHE B  48     3586   3581   3741    971   -187    212       O  
ATOM   1196  CB  PHE B  48      23.375  10.779  54.108  1.00 20.42           C  
ANISOU 1196  CB  PHE B  48     2493   2569   2695    965   -137    235       C  
ATOM   1197  CG  PHE B  48      22.698  12.107  54.029  1.00 22.25           C  
ANISOU 1197  CG  PHE B  48     2719   2807   2927    957   -112    248       C  
ATOM   1198  CD1 PHE B  48      22.953  13.096  54.982  1.00 23.94           C  
ANISOU 1198  CD1 PHE B  48     2949   3003   3146    939   -107    260       C  
ATOM   1199  CD2 PHE B  48      21.792  12.373  53.017  1.00 24.87           C  
ANISOU 1199  CD2 PHE B  48     3033   3165   3252    968    -91    251       C  
ATOM   1200  CE1 PHE B  48      22.287  14.326  54.916  1.00 29.42           C  
ANISOU 1200  CE1 PHE B  48     3642   3699   3838    934    -79    274       C  
ATOM   1201  CE2 PHE B  48      21.127  13.598  52.945  1.00 29.07           C  
ANISOU 1201  CE2 PHE B  48     3560   3702   3782    966    -65    266       C  
ATOM   1202  CZ  PHE B  48      21.377  14.571  53.889  1.00 31.49           C  
ANISOU 1202  CZ  PHE B  48     3885   3986   4094    950    -58    277       C  
ATOM   1203  N   PHE B  49      22.561   7.447  54.339  1.00 24.58           N  
ANISOU 1203  N   PHE B  49     3070   3071   3199    969   -166    194       N  
ATOM   1204  CA  PHE B  49      23.153   6.143  54.145  1.00 21.56           C  
ANISOU 1204  CA  PHE B  49     2699   2681   2813    983   -181    182       C  
ATOM   1205  C   PHE B  49      24.240   6.240  53.083  1.00 21.62           C  
ANISOU 1205  C   PHE B  49     2673   2713   2829   1010   -181    188       C  
ATOM   1206  O   PHE B  49      24.227   7.155  52.255  1.00 28.54           O  
ANISOU 1206  O   PHE B  49     3519   3615   3711   1015   -167    197       O  
ATOM   1207  CB  PHE B  49      22.105   5.104  53.746  1.00 22.25           C  
ANISOU 1207  CB  PHE B  49     2805   2769   2882    977   -174    164       C  
ATOM   1208  CG  PHE B  49      21.157   4.772  54.848  1.00 22.99           C  
ANISOU 1208  CG  PHE B  49     2934   2837   2966    952   -176    156       C  
ATOM   1209  CD1 PHE B  49      21.584   4.023  55.933  1.00 24.00           C  
ANISOU 1209  CD1 PHE B  49     3096   2931   3092    948   -194    151       C  
ATOM   1210  CD2 PHE B  49      19.849   5.225  54.813  1.00 27.31           C  
ANISOU 1210  CD2 PHE B  49     3479   3394   3503    933   -160    156       C  
ATOM   1211  CE1 PHE B  49      20.720   3.716  56.963  1.00 30.15           C  
ANISOU 1211  CE1 PHE B  49     3910   3685   3862    924   -195    143       C  
ATOM   1212  CE2 PHE B  49      18.974   4.924  55.831  1.00 22.66           C  
ANISOU 1212  CE2 PHE B  49     2923   2783   2905    909   -161    148       C  
ATOM   1213  CZ  PHE B  49      19.413   4.169  56.915  1.00 27.97           C  
ANISOU 1213  CZ  PHE B  49     3631   3418   3576    903   -179    141       C  
ATOM   1214  N   GLY B  50      25.173   5.300  53.133  1.00 22.07           N  
ANISOU 1214  N   GLY B  50     2738   2761   2887   1027   -196    183       N  
ATOM   1215  CA  GLY B  50      26.267   5.247  52.169  1.00 24.94           C  
ANISOU 1215  CA  GLY B  50     3072   3145   3258   1055   -197    188       C  
ATOM   1216  C   GLY B  50      27.451   6.111  52.555  1.00 28.04           C  
ANISOU 1216  C   GLY B  50     3442   3545   3665   1059   -207    205       C  
ATOM   1217  O   GLY B  50      28.594   5.663  52.539  1.00 27.12           O  
ANISOU 1217  O   GLY B  50     3318   3433   3555   1080   -219    209       O  
ATOM   1218  N   THR B  51      27.188   7.365  52.885  1.00 23.59           N  
ANISOU 1218  N   THR B  51     2869   2987   3108   1040   -199    215       N  
ATOM   1219  CA  THR B  51      28.265   8.296  53.217  1.00 26.39           C  
ANISOU 1219  CA  THR B  51     3204   3351   3474   1038   -206    230       C  
ATOM   1220  C   THR B  51      28.404   8.492  54.711  1.00 29.68           C  
ANISOU 1220  C   THR B  51     3644   3743   3889   1015   -220    235       C  
ATOM   1221  O   THR B  51      29.447   8.929  55.201  1.00 28.89           O  
ANISOU 1221  O   THR B  51     3533   3649   3795   1011   -232    246       O  
ATOM   1222  CB  THR B  51      28.027   9.651  52.590  1.00 28.94           C  
ANISOU 1222  CB  THR B  51     3502   3692   3801   1030   -185    239       C  
ATOM   1223  OG1 THR B  51      26.857  10.240  53.175  1.00 27.88           O  
ANISOU 1223  OG1 THR B  51     3389   3543   3661   1007   -172    240       O  
ATOM   1224  CG2 THR B  51      27.839   9.511  51.077  1.00 26.82           C  
ANISOU 1224  CG2 THR B  51     3210   3450   3532   1051   -170    235       C  
ATOM   1225  N   HIS B  52      27.322   8.186  55.421  1.00 28.01           N  
ANISOU 1225  N   HIS B  52     3465   3506   3670    998   -218    227       N  
ATOM   1226  CA  HIS B  52      27.197   8.412  56.870  1.00 27.56           C  
ANISOU 1226  CA  HIS B  52     3436   3424   3611    972   -229    231       C  
ATOM   1227  C   HIS B  52      27.419   9.872  57.264  1.00 36.13           C  
ANISOU 1227  C   HIS B  52     4512   4513   4702    950   -220    245       C  
ATOM   1228  O   HIS B  52      27.696  10.166  58.421  1.00 32.26           O  
ANISOU 1228  O   HIS B  52     4040   4006   4210    929   -230    250       O  
ATOM   1229  CB  HIS B  52      28.141   7.480  57.639  1.00 26.72           C  
ANISOU 1229  CB  HIS B  52     3343   3306   3504    981   -255    231       C  
ATOM   1230  CG  HIS B  52      27.778   6.031  57.501  1.00 28.17           C  
ANISOU 1230  CG  HIS B  52     3549   3475   3679    998   -260    216       C  
ATOM   1231  ND1 HIS B  52      28.246   5.059  58.356  1.00 30.83           N  
ANISOU 1231  ND1 HIS B  52     3911   3792   4011   1005   -280    215       N  
ATOM   1232  CD2 HIS B  52      27.003   5.397  56.595  1.00 23.65           C  
ANISOU 1232  CD2 HIS B  52     2981   2906   3100   1008   -247    203       C  
ATOM   1233  CE1 HIS B  52      27.767   3.884  57.985  1.00 29.54           C  
ANISOU 1233  CE1 HIS B  52     3768   3617   3838   1019   -277    200       C  
ATOM   1234  NE2 HIS B  52      27.014   4.057  56.916  1.00 28.59           N  
ANISOU 1234  NE2 HIS B  52     3636   3511   3716   1019   -257    193       N  
ATOM   1235  N   GLU B  53      27.249  10.786  56.306  1.00 28.24           N  
ANISOU 1235  N   GLU B  53     3489   3535   3706    954   -198    250       N  
ATOM   1236  CA  GLU B  53      27.228  12.209  56.607  1.00 25.98           C  
ANISOU 1236  CA  GLU B  53     3201   3248   3423    933   -182    262       C  
ATOM   1237  C   GLU B  53      25.969  12.523  57.396  1.00 28.26           C  
ANISOU 1237  C   GLU B  53     3521   3511   3704    911   -169    261       C  
ATOM   1238  O   GLU B  53      25.040  11.724  57.420  1.00 25.80           O  
ANISOU 1238  O   GLU B  53     3225   3189   3387    915   -170    251       O  
ATOM   1239  CB  GLU B  53      27.266  13.048  55.326  1.00 30.39           C  
ANISOU 1239  CB  GLU B  53     3729   3834   3985    946   -160    269       C  
ATOM   1240  CG  GLU B  53      28.420  12.709  54.407  1.00 45.96           C  
ANISOU 1240  CG  GLU B  53     5667   5832   5962    970   -170    269       C  
ATOM   1241  CD  GLU B  53      29.679  13.484  54.730  1.00 60.33           C  
ANISOU 1241  CD  GLU B  53     7473   7664   7787    958   -176    280       C  
ATOM   1242  OE1 GLU B  53      29.638  14.348  55.635  1.00 56.28           O  
ANISOU 1242  OE1 GLU B  53     6978   7136   7270    928   -171    287       O  
ATOM   1243  OE2 GLU B  53      30.714  13.229  54.075  1.00 70.22           O  
ANISOU 1243  OE2 GLU B  53     8696   8939   9043    976   -185    281       O  
ATOM   1244  N   THR B  54      25.944  13.677  58.055  1.00 33.26           N  
ANISOU 1244  N   THR B  54     4166   4132   4337    887   -157    272       N  
ATOM   1245  CA  THR B  54      24.745  14.117  58.758  1.00 32.94           C  
ANISOU 1245  CA  THR B  54     4157   4069   4292    868   -139    273       C  
ATOM   1246  C   THR B  54      24.423  15.562  58.411  1.00 29.34           C  
ANISOU 1246  C   THR B  54     3696   3617   3835    862   -107    286       C  
ATOM   1247  O   THR B  54      25.268  16.297  57.874  1.00 36.49           O  
ANISOU 1247  O   THR B  54     4581   4540   4744    864   -100    294       O  
ATOM   1248  CB  THR B  54      24.884  14.010  60.297  1.00 35.93           C  
ANISOU 1248  CB  THR B  54     4570   4416   4666    839   -155    272       C  
ATOM   1249  OG1 THR B  54      25.925  14.890  60.730  1.00 43.82           O  
ANISOU 1249  OG1 THR B  54     5566   5416   5667    820   -156    283       O  
ATOM   1250  CG2 THR B  54      25.202  12.581  60.733  1.00 36.85           C  
ANISOU 1250  CG2 THR B  54     4695   4524   4782    846   -186    261       C  
ATOM   1251  N   ALA B  55      23.198  15.953  58.735  1.00 23.74           N  
ANISOU 1251  N   ALA B  55     3007   2893   3120    854    -85    289       N  
ATOM   1252  CA  ALA B  55      22.697  17.305  58.505  1.00 29.89           C  
ANISOU 1252  CA  ALA B  55     3789   3671   3896    851    -50    304       C  
ATOM   1253  C   ALA B  55      21.350  17.463  59.191  1.00 29.71           C  
ANISOU 1253  C   ALA B  55     3794   3627   3867    842    -32    306       C  
ATOM   1254  O   ALA B  55      20.749  16.488  59.638  1.00 34.33           O  
ANISOU 1254  O   ALA B  55     4391   4203   4449    839    -47    295       O  
ATOM   1255  CB  ALA B  55      22.563  17.595  57.028  1.00 36.45           C  
ANISOU 1255  CB  ALA B  55     4586   4536   4729    880    -33    309       C  
ATOM   1256  N   PHE B  56      20.887  18.702  59.275  1.00 27.36           N  
ANISOU 1256  N   PHE B  56     3509   3321   3566    837      2    321       N  
ATOM   1257  CA  PHE B  56      19.550  18.991  59.776  1.00 31.45           C  
ANISOU 1257  CA  PHE B  56     4050   3823   4077    833     25    327       C  
ATOM   1258  C   PHE B  56      18.705  19.542  58.655  1.00 30.65           C  
ANISOU 1258  C   PHE B  56     3925   3748   3971    862     55    339       C  
ATOM   1259  O   PHE B  56      19.102  20.491  57.990  1.00 34.68           O  
ANISOU 1259  O   PHE B  56     4424   4269   4482    872     76    351       O  
ATOM   1260  CB  PHE B  56      19.598  19.983  60.936  1.00 34.19           C  
ANISOU 1260  CB  PHE B  56     4436   4133   4420    804     44    336       C  
ATOM   1261  CG  PHE B  56      19.921  19.343  62.257  1.00 38.41           C  
ANISOU 1261  CG  PHE B  56     5000   4639   4954    774     17    325       C  
ATOM   1262  CD1 PHE B  56      21.219  18.979  62.564  1.00 44.68           C  
ANISOU 1262  CD1 PHE B  56     5791   5433   5752    760    -13    318       C  
ATOM   1263  CD2 PHE B  56      18.924  19.091  63.178  1.00 37.30           C  
ANISOU 1263  CD2 PHE B  56     4890   4474   4809    762     21    322       C  
ATOM   1264  CE1 PHE B  56      21.520  18.384  63.780  1.00 42.74           C  
ANISOU 1264  CE1 PHE B  56     5571   5162   5505    734    -39    310       C  
ATOM   1265  CE2 PHE B  56      19.224  18.497  64.404  1.00 37.61           C  
ANISOU 1265  CE2 PHE B  56     4958   4485   4848    734     -4    312       C  
ATOM   1266  CZ  PHE B  56      20.515  18.144  64.695  1.00 31.31           C  
ANISOU 1266  CZ  PHE B  56     4156   3688   4054    721    -34    306       C  
ATOM   1267  N   LEU B  57      17.557  18.911  58.441  1.00 25.14           N  
ANISOU 1267  N   LEU B  57     3220   3064   3267    874     57    335       N  
ATOM   1268  CA  LEU B  57      16.645  19.265  57.370  1.00 29.31           C  
ANISOU 1268  CA  LEU B  57     3723   3625   3790    902     82    346       C  
ATOM   1269  C   LEU B  57      15.201  19.331  57.855  1.00 32.25           C  
ANISOU 1269  C   LEU B  57     4109   3993   4152    902    101    353       C  
ATOM   1270  O   LEU B  57      14.796  18.570  58.743  1.00 33.54           O  
ANISOU 1270  O   LEU B  57     4293   4139   4314    883     85    341       O  
ATOM   1271  CB  LEU B  57      16.743  18.246  56.234  1.00 28.67           C  
ANISOU 1271  CB  LEU B  57     3605   3580   3708    920     61    334       C  
ATOM   1272  CG  LEU B  57      18.031  18.216  55.420  1.00 36.39           C  
ANISOU 1272  CG  LEU B  57     4559   4572   4694    929     47    330       C  
ATOM   1273  CD1 LEU B  57      17.951  17.101  54.369  1.00 30.52           C  
ANISOU 1273  CD1 LEU B  57     3786   3863   3949    946     28    317       C  
ATOM   1274  CD2 LEU B  57      18.221  19.567  54.756  1.00 43.23           C  
ANISOU 1274  CD2 LEU B  57     5415   5448   5560    944     79    350       C  
ATOM   1275  N   GLY B  58      14.420  20.234  57.267  1.00 26.13           N  
ANISOU 1275  N   GLY B  58     3322   3237   3369    924    137    373       N  
ATOM   1276  CA  GLY B  58      12.991  20.268  57.505  1.00 25.72           C  
ANISOU 1276  CA  GLY B  58     3273   3194   3307    930    157    382       C  
ATOM   1277  C   GLY B  58      12.198  19.375  56.559  1.00 27.78           C  
ANISOU 1277  C   GLY B  58     3497   3502   3558    946    146    375       C  
ATOM   1278  O   GLY B  58      12.697  18.959  55.509  1.00 30.21           O  
ANISOU 1278  O   GLY B  58     3774   3837   3867    959    132    369       O  
ATOM   1279  N   PRO B  59      10.938  19.093  56.912  1.00 38.22           N  
ANISOU 1279  N   PRO B  59     4819   4833   4868    945    155    378       N  
ATOM   1280  CA  PRO B  59      10.068  18.181  56.162  1.00 29.55           C  
ANISOU 1280  CA  PRO B  59     3690   3781   3758    951    145    370       C  
ATOM   1281  C   PRO B  59       9.943  18.539  54.677  1.00 29.10           C  
ANISOU 1281  C   PRO B  59     3589   3773   3693    982    158    383       C  
ATOM   1282  O   PRO B  59       9.599  17.664  53.893  1.00 29.09           O  
ANISOU 1282  O   PRO B  59     3560   3810   3682    984    143    372       O  
ATOM   1283  CB  PRO B  59       8.716  18.336  56.865  1.00 37.31           C  
ANISOU 1283  CB  PRO B  59     4683   4765   4728    948    166    380       C  
ATOM   1284  CG  PRO B  59       9.067  18.725  58.251  1.00 41.12           C  
ANISOU 1284  CG  PRO B  59     5213   5191   5221    926    169    379       C  
ATOM   1285  CD  PRO B  59      10.267  19.620  58.115  1.00 37.79           C  
ANISOU 1285  CD  PRO B  59     4800   4746   4811    932    176    387       C  
ATOM   1286  N   LYS B  60      10.204  19.792  54.316  1.00 26.13           N  
ANISOU 1286  N   LYS B  60     3211   3397   3321   1005    187    406       N  
ATOM   1287  CA  LYS B  60      10.160  20.220  52.917  1.00 34.63           C  
ANISOU 1287  CA  LYS B  60     4249   4517   4391   1036    200    421       C  
ATOM   1288  C   LYS B  60      11.158  19.426  52.064  1.00 37.49           C  
ANISOU 1288  C   LYS B  60     4591   4894   4761   1033    170    401       C  
ATOM   1289  O   LYS B  60      10.967  19.254  50.855  1.00 36.75           O  
ANISOU 1289  O   LYS B  60     4461   4844   4658   1051    170    404       O  
ATOM   1290  CB  LYS B  60      10.441  21.724  52.817  1.00 37.63           C  
ANISOU 1290  CB  LYS B  60     4640   4883   4775   1057    237    447       C  
ATOM   1291  CG  LYS B  60      11.735  22.096  52.130  1.00 51.08           C  
ANISOU 1291  CG  LYS B  60     6338   6581   6490   1063    232    445       C  
ATOM   1292  CD  LYS B  60      12.137  23.545  52.392  1.00 56.72           C  
ANISOU 1292  CD  LYS B  60     7078   7266   7208   1072    268    466       C  
ATOM   1293  CE  LYS B  60      13.508  23.827  51.783  1.00 62.38           C  
ANISOU 1293  CE  LYS B  60     7790   7976   7934   1072    260    460       C  
ATOM   1294  NZ  LYS B  60      13.940  25.238  51.974  1.00 66.78           N  
ANISOU 1294  NZ  LYS B  60     8376   8506   8493   1077    297    479       N  
ATOM   1295  N   ASP B  61      12.210  18.928  52.703  1.00 29.96           N  
ANISOU 1295  N   ASP B  61     3660   3902   3821   1010    144    381       N  
ATOM   1296  CA  ASP B  61      13.297  18.277  51.964  1.00 32.06           C  
ANISOU 1296  CA  ASP B  61     3910   4176   4094   1010    118    365       C  
ATOM   1297  C   ASP B  61      13.322  16.779  52.213  1.00 29.23           C  
ANISOU 1297  C   ASP B  61     3556   3815   3734    990     84    338       C  
ATOM   1298  O   ASP B  61      14.267  16.092  51.808  1.00 27.42           O  
ANISOU 1298  O   ASP B  61     3321   3586   3512    988     60    323       O  
ATOM   1299  CB  ASP B  61      14.643  18.893  52.346  1.00 40.08           C  
ANISOU 1299  CB  ASP B  61     4945   5157   5127   1004    115    366       C  
ATOM   1300  CG  ASP B  61      14.857  20.266  51.727  1.00 49.03           C  
ANISOU 1300  CG  ASP B  61     6070   6299   6261   1025    148    389       C  
ATOM   1301  OD1 ASP B  61      14.570  20.432  50.516  1.00 39.93           O  
ANISOU 1301  OD1 ASP B  61     4885   5186   5102   1050    158    398       O  
ATOM   1302  OD2 ASP B  61      15.320  21.178  52.451  1.00 48.34           O  
ANISOU 1302  OD2 ASP B  61     6010   6176   6179   1016    163    398       O  
ATOM   1303  N   LEU B  62      12.290  16.280  52.893  1.00 23.98           N  
ANISOU 1303  N   LEU B  62     2903   3148   3058    975     83    333       N  
ATOM   1304  CA  LEU B  62      12.209  14.881  53.303  1.00 24.17           C  
ANISOU 1304  CA  LEU B  62     2941   3165   3078    953     54    307       C  
ATOM   1305  C   LEU B  62      11.051  14.160  52.630  1.00 27.09           C  
ANISOU 1305  C   LEU B  62     3288   3579   3427    952     56    302       C  
ATOM   1306  O   LEU B  62       9.940  14.713  52.491  1.00 27.96           O  
ANISOU 1306  O   LEU B  62     3383   3716   3524    960     79    318       O  
ATOM   1307  CB  LEU B  62      12.049  14.777  54.823  1.00 29.69           C  
ANISOU 1307  CB  LEU B  62     3681   3820   3782    929     49    302       C  
ATOM   1308  CG  LEU B  62      13.155  15.466  55.607  1.00 28.16           C  
ANISOU 1308  CG  LEU B  62     3512   3583   3605    923     47    307       C  
ATOM   1309  CD1 LEU B  62      12.759  15.547  57.101  1.00 25.46           C  
ANISOU 1309  CD1 LEU B  62     3210   3200   3264    899     49    305       C  
ATOM   1310  CD2 LEU B  62      14.442  14.672  55.414  1.00 24.57           C  
ANISOU 1310  CD2 LEU B  62     3057   3118   3160    920     17    289       C  
ATOM   1311  N   PHE B  63      11.313  12.925  52.230  1.00 24.08           N  
ANISOU 1311  N   PHE B  63     2904   3205   3040    941     32    279       N  
ATOM   1312  CA  PHE B  63      10.374  12.120  51.443  1.00 23.59           C  
ANISOU 1312  CA  PHE B  63     2822   3188   2956    935     31    270       C  
ATOM   1313  C   PHE B  63      10.304  10.702  51.979  1.00 25.28           C  
ANISOU 1313  C   PHE B  63     3062   3383   3161    907      8    241       C  
ATOM   1314  O   PHE B  63      11.307   9.989  51.931  1.00 30.20           O  
ANISOU 1314  O   PHE B  63     3699   3983   3792    904    -11    225       O  
ATOM   1315  CB  PHE B  63      10.808  12.073  49.970  1.00 26.37           C  
ANISOU 1315  CB  PHE B  63     3138   3576   3303    953     31    271       C  
ATOM   1316  CG  PHE B  63      10.876  13.415  49.308  1.00 25.37           C  
ANISOU 1316  CG  PHE B  63     2985   3471   3183    982     54    298       C  
ATOM   1317  CD1 PHE B  63      11.952  14.270  49.532  1.00 26.40           C  
ANISOU 1317  CD1 PHE B  63     3125   3571   3335    996     58    308       C  
ATOM   1318  CD2 PHE B  63       9.876  13.821  48.439  1.00 29.36           C  
ANISOU 1318  CD2 PHE B  63     3456   4029   3670    996     73    315       C  
ATOM   1319  CE1 PHE B  63      12.015  15.512  48.917  1.00 28.00           C  
ANISOU 1319  CE1 PHE B  63     3307   3790   3541   1022     82    333       C  
ATOM   1320  CE2 PHE B  63       9.930  15.065  47.825  1.00 31.65           C  
ANISOU 1320  CE2 PHE B  63     3724   4338   3964   1026     97    341       C  
ATOM   1321  CZ  PHE B  63      11.001  15.908  48.062  1.00 29.59           C  
ANISOU 1321  CZ  PHE B  63     3477   4041   3725   1038    102    350       C  
ATOM   1322  N   PRO B  64       9.127  10.263  52.474  1.00 23.41           N  
ANISOU 1322  N   PRO B  64     2833   3156   2905    886     12    235       N  
ATOM   1323  CA  PRO B  64       9.045   8.894  53.013  1.00 29.57           C  
ANISOU 1323  CA  PRO B  64     3644   3914   3675    857     -8    207       C  
ATOM   1324  C   PRO B  64       9.561   7.820  52.045  1.00 29.93           C  
ANISOU 1324  C   PRO B  64     3686   3974   3712    854    -22    187       C  
ATOM   1325  O   PRO B  64       9.165   7.795  50.882  1.00 30.41           O  
ANISOU 1325  O   PRO B  64     3714   4082   3758    860    -14    190       O  
ATOM   1326  CB  PRO B  64       7.545   8.720  53.283  1.00 29.50           C  
ANISOU 1326  CB  PRO B  64     3632   3934   3643    837      4    207       C  
ATOM   1327  CG  PRO B  64       7.072  10.114  53.565  1.00 28.97           C  
ANISOU 1327  CG  PRO B  64     3549   3875   3583    856     28    237       C  
ATOM   1328  CD  PRO B  64       7.854  11.001  52.647  1.00 26.72           C  
ANISOU 1328  CD  PRO B  64     3237   3603   3312    888     35    255       C  
ATOM   1329  N   TYR B  65      10.446   6.955  52.531  1.00 23.27           N  
ANISOU 1329  N   TYR B  65     2876   3090   2877    847    -42    168       N  
ATOM   1330  CA  TYR B  65      11.227   6.064  51.662  1.00 25.80           C  
ANISOU 1330  CA  TYR B  65     3196   3413   3194    852    -53    153       C  
ATOM   1331  C   TYR B  65      10.363   5.128  50.822  1.00 27.69           C  
ANISOU 1331  C   TYR B  65     3428   3691   3403    832    -50    136       C  
ATOM   1332  O   TYR B  65      10.530   5.052  49.605  1.00 31.19           O  
ANISOU 1332  O   TYR B  65     3845   4167   3839    842    -46    137       O  
ATOM   1333  CB  TYR B  65      12.219   5.245  52.504  1.00 28.43           C  
ANISOU 1333  CB  TYR B  65     3571   3693   3539    847    -73    137       C  
ATOM   1334  CG  TYR B  65      12.888   4.099  51.761  1.00 30.81           C  
ANISOU 1334  CG  TYR B  65     3882   3993   3833    850    -83    118       C  
ATOM   1335  CD1 TYR B  65      13.786   4.345  50.730  1.00 28.70           C  
ANISOU 1335  CD1 TYR B  65     3589   3741   3576    876    -83    124       C  
ATOM   1336  CD2 TYR B  65      12.624   2.773  52.090  1.00 38.97           C  
ANISOU 1336  CD2 TYR B  65     4953   5007   4848    828    -90     94       C  
ATOM   1337  CE1 TYR B  65      14.404   3.310  50.045  1.00 29.63           C  
ANISOU 1337  CE1 TYR B  65     3717   3855   3686    880    -89    108       C  
ATOM   1338  CE2 TYR B  65      13.243   1.722  51.397  1.00 39.06           C  
ANISOU 1338  CE2 TYR B  65     4978   5013   4850    832    -95     77       C  
ATOM   1339  CZ  TYR B  65      14.134   2.005  50.380  1.00 38.80           C  
ANISOU 1339  CZ  TYR B  65     4918   4996   4829    859    -95     85       C  
ATOM   1340  OH  TYR B  65      14.765   0.989  49.680  1.00 38.27           O  
ANISOU 1340  OH  TYR B  65     4865   4923   4753    865    -97     70       O  
ATOM   1341  N   LYS B  66       9.422   4.440  51.463  1.00 34.19           N  
ANISOU 1341  N   LYS B  66     4275   4511   4207    802    -50    122       N  
ATOM   1342  CA  LYS B  66       8.592   3.460  50.768  1.00 40.22           C  
ANISOU 1342  CA  LYS B  66     5037   5309   4937    775    -46    104       C  
ATOM   1343  C   LYS B  66       7.752   4.111  49.662  1.00 35.26           C  
ANISOU 1343  C   LYS B  66     4358   4747   4292    780    -31    119       C  
ATOM   1344  O   LYS B  66       7.720   3.628  48.523  1.00 33.04           O  
ANISOU 1344  O   LYS B  66     4060   4500   3994    776    -29    112       O  
ATOM   1345  CB  LYS B  66       7.694   2.731  51.773  1.00 42.38           C  
ANISOU 1345  CB  LYS B  66     5345   5566   5192    740    -48     87       C  
ATOM   1346  CG  LYS B  66       8.471   1.937  52.821  1.00 50.13           C  
ANISOU 1346  CG  LYS B  66     6380   6483   6184    734    -63     69       C  
ATOM   1347  CD  LYS B  66       7.542   1.310  53.857  1.00 56.12           C  
ANISOU 1347  CD  LYS B  66     7174   7226   6925    698    -63     54       C  
ATOM   1348  CE  LYS B  66       6.448   0.481  53.199  1.00 65.24           C  
ANISOU 1348  CE  LYS B  66     8324   8422   8040    664    -54     36       C  
ATOM   1349  NZ  LYS B  66       5.425   0.034  54.194  1.00 71.69           N  
ANISOU 1349  NZ  LYS B  66     9169   9230   8839    628    -52     23       N  
ATOM   1350  N   GLU B  67       7.097   5.220  49.993  1.00 36.21           N  
ANISOU 1350  N   GLU B  67     4454   4886   4419    791    -18    143       N  
ATOM   1351  CA  GLU B  67       6.276   5.937  49.009  1.00 38.52           C  
ANISOU 1351  CA  GLU B  67     4696   5244   4696    800     -2    163       C  
ATOM   1352  C   GLU B  67       7.076   6.472  47.823  1.00 42.20           C  
ANISOU 1352  C   GLU B  67     5132   5729   5173    831      1    176       C  
ATOM   1353  O   GLU B  67       6.578   6.495  46.700  1.00 42.89           O  
ANISOU 1353  O   GLU B  67     5185   5872   5240    831      8    181       O  
ATOM   1354  CB  GLU B  67       5.527   7.096  49.664  1.00 42.38           C  
ANISOU 1354  CB  GLU B  67     5170   5743   5191    813     14    189       C  
ATOM   1355  CG  GLU B  67       4.945   6.774  51.019  1.00 60.10           C  
ANISOU 1355  CG  GLU B  67     7448   7956   7433    788     12    180       C  
ATOM   1356  CD  GLU B  67       4.397   8.009  51.732  1.00 72.90           C  
ANISOU 1356  CD  GLU B  67     9058   9575   9064    805     29    208       C  
ATOM   1357  OE1 GLU B  67       4.077   9.014  51.040  1.00 67.89           O  
ANISOU 1357  OE1 GLU B  67     8384   8981   8429    832     47    235       O  
ATOM   1358  OE2 GLU B  67       4.260   7.960  52.980  1.00 72.85           O  
ANISOU 1358  OE2 GLU B  67     9086   9528   9066    792     27    203       O  
ATOM   1359  N   TYR B  68       8.312   6.892  48.065  1.00 31.48           N  
ANISOU 1359  N   TYR B  68     3787   4329   3846    855     -6    180       N  
ATOM   1360  CA  TYR B  68       9.084   7.559  47.019  1.00 30.41           C  
ANISOU 1360  CA  TYR B  68     3621   4209   3722    885     -2    195       C  
ATOM   1361  C   TYR B  68      10.225   6.708  46.479  1.00 32.04           C  
ANISOU 1361  C   TYR B  68     3842   4395   3935    888    -16    175       C  
ATOM   1362  O   TYR B  68      11.021   7.179  45.662  1.00 33.10           O  
ANISOU 1362  O   TYR B  68     3957   4538   4083    912    -14    184       O  
ATOM   1363  CB  TYR B  68       9.620   8.905  47.532  1.00 25.75           C  
ANISOU 1363  CB  TYR B  68     3027   3596   3161    913      7    219       C  
ATOM   1364  CG  TYR B  68       8.513   9.946  47.602  1.00 32.13           C  
ANISOU 1364  CG  TYR B  68     3810   4437   3961    922     29    245       C  
ATOM   1365  CD1 TYR B  68       8.110  10.641  46.463  1.00 33.53           C  
ANISOU 1365  CD1 TYR B  68     3944   4668   4127    943     45    265       C  
ATOM   1366  CD2 TYR B  68       7.857  10.209  48.792  1.00 38.41           C  
ANISOU 1366  CD2 TYR B  68     4625   5213   4757    912     34    250       C  
ATOM   1367  CE1 TYR B  68       7.088  11.569  46.513  1.00 32.36           C  
ANISOU 1367  CE1 TYR B  68     3773   4552   3970    956     66    291       C  
ATOM   1368  CE2 TYR B  68       6.833  11.145  48.853  1.00 35.02           C  
ANISOU 1368  CE2 TYR B  68     4172   4815   4319    923     57    275       C  
ATOM   1369  CZ  TYR B  68       6.462  11.823  47.711  1.00 35.33           C  
ANISOU 1369  CZ  TYR B  68     4169   4907   4348    947     73    296       C  
ATOM   1370  OH  TYR B  68       5.443  12.748  47.774  1.00 33.09           O  
ANISOU 1370  OH  TYR B  68     3863   4655   4054    963     97    324       O  
ATOM   1371  N   LYS B  69      10.290   5.455  46.925  1.00 33.35           N  
ANISOU 1371  N   LYS B  69     4046   4535   4092    863    -28    149       N  
ATOM   1372  CA  LYS B  69      11.338   4.543  46.488  1.00 28.58           C  
ANISOU 1372  CA  LYS B  69     3460   3907   3491    866    -40    131       C  
ATOM   1373  C   LYS B  69      11.356   4.393  44.971  1.00 33.88           C  
ANISOU 1373  C   LYS B  69     4102   4623   4148    871    -33    130       C  
ATOM   1374  O   LYS B  69      12.425   4.432  44.362  1.00 39.19           O  
ANISOU 1374  O   LYS B  69     4769   5286   4835    893    -36    131       O  
ATOM   1375  CB  LYS B  69      11.167   3.173  47.146  1.00 36.82           C  
ANISOU 1375  CB  LYS B  69     4551   4921   4519    837    -49    103       C  
ATOM   1376  CG  LYS B  69      12.167   2.126  46.676  1.00 40.84           C  
ANISOU 1376  CG  LYS B  69     5085   5406   5028    841    -57     85       C  
ATOM   1377  CD  LYS B  69      12.067   0.839  47.490  1.00 40.73           C  
ANISOU 1377  CD  LYS B  69     5123   5352   4999    816    -64     60       C  
ATOM   1378  CE  LYS B  69      12.873  -0.294  46.847  1.00 51.18           C  
ANISOU 1378  CE  LYS B  69     6473   6659   6316    819    -66     41       C  
ATOM   1379  NZ  LYS B  69      12.550  -1.622  47.456  1.00 55.70           N  
ANISOU 1379  NZ  LYS B  69     7098   7199   6865    791    -67     15       N  
ATOM   1380  N   ASP B  70      10.181   4.248  44.360  1.00 37.84           N  
ANISOU 1380  N   ASP B  70     4583   5176   4619    851    -23    129       N  
ATOM   1381  CA  ASP B  70      10.121   3.986  42.928  1.00 42.57           C  
ANISOU 1381  CA  ASP B  70     5157   5818   5199    850    -17    126       C  
ATOM   1382  C   ASP B  70      10.735   5.134  42.165  1.00 38.22           C  
ANISOU 1382  C   ASP B  70     4568   5284   4668    887    -11    150       C  
ATOM   1383  O   ASP B  70      11.446   4.936  41.185  1.00 50.66           O  
ANISOU 1383  O   ASP B  70     6135   6867   6246    899    -11    146       O  
ATOM   1384  CB  ASP B  70       8.674   3.769  42.475  1.00 61.15           C  
ANISOU 1384  CB  ASP B  70     7489   8230   7514    820     -8    124       C  
ATOM   1385  CG  ASP B  70       8.363   2.304  42.191  1.00 77.59           C  
ANISOU 1385  CG  ASP B  70     9602  10315   9564    780    -11     93       C  
ATOM   1386  OD1 ASP B  70       9.137   1.437  42.673  1.00 79.04           O  
ANISOU 1386  OD1 ASP B  70     9830  10445   9756    776    -19     73       O  
ATOM   1387  OD2 ASP B  70       7.367   2.021  41.477  1.00 83.67           O  
ANISOU 1387  OD2 ASP B  70    10351  11140  10299    753     -3     90       O  
ATOM   1388  N   LYS B  71      10.464   6.341  42.649  1.00 33.49           N  
ANISOU 1388  N   LYS B  71     3949   4690   4084    905     -4    174       N  
ATOM   1389  CA  LYS B  71      10.925   7.570  42.022  1.00 33.59           C  
ANISOU 1389  CA  LYS B  71     3929   4719   4115    940      6    199       C  
ATOM   1390  C   LYS B  71      12.416   7.817  42.254  1.00 36.60           C  
ANISOU 1390  C   LYS B  71     4325   5052   4528    963     -2    199       C  
ATOM   1391  O   LYS B  71      13.151   8.147  41.328  1.00 35.83           O  
ANISOU 1391  O   LYS B  71     4208   4965   4440    983      1    205       O  
ATOM   1392  CB  LYS B  71      10.109   8.748  42.555  1.00 40.87           C  
ANISOU 1392  CB  LYS B  71     4833   5657   5040    951     20    226       C  
ATOM   1393  CG  LYS B  71      10.324  10.069  41.847  1.00 50.28           C  
ANISOU 1393  CG  LYS B  71     5990   6873   6242    985     36    254       C  
ATOM   1394  CD  LYS B  71       9.360  11.105  42.407  1.00 53.99           C  
ANISOU 1394  CD  LYS B  71     6446   7358   6709    995     53    280       C  
ATOM   1395  CE  LYS B  71       9.404  12.418  41.653  1.00 53.35           C  
ANISOU 1395  CE  LYS B  71     6333   7305   6634   1030     73    310       C  
ATOM   1396  NZ  LYS B  71       8.448  13.387  42.255  1.00 53.24           N  
ANISOU 1396  NZ  LYS B  71     6311   7303   6616   1042     93    336       N  
ATOM   1397  N   PHE B  72      12.864   7.665  43.494  1.00 30.30           N  
ANISOU 1397  N   PHE B  72     3560   4204   3748    958    -12    193       N  
ATOM   1398  CA  PHE B  72      14.197   8.134  43.857  1.00 28.88           C  
ANISOU 1398  CA  PHE B  72     3389   3986   3599    980    -19    199       C  
ATOM   1399  C   PHE B  72      15.228   7.021  44.079  1.00 31.85           C  
ANISOU 1399  C   PHE B  72     3795   4324   3982    977    -36    177       C  
ATOM   1400  O   PHE B  72      16.406   7.295  44.299  1.00 31.71           O  
ANISOU 1400  O   PHE B  72     3782   4280   3988    994    -43    181       O  
ATOM   1401  CB  PHE B  72      14.100   8.990  45.122  1.00 22.53           C  
ANISOU 1401  CB  PHE B  72     2598   3153   2811    981    -17    213       C  
ATOM   1402  CG  PHE B  72      13.308  10.256  44.947  1.00 29.47           C  
ANISOU 1402  CG  PHE B  72     3450   4061   3687    993      4    238       C  
ATOM   1403  CD1 PHE B  72      13.353  10.974  43.761  1.00 31.37           C  
ANISOU 1403  CD1 PHE B  72     3654   4339   3924   1015     18    254       C  
ATOM   1404  CD2 PHE B  72      12.492  10.713  45.965  1.00 29.38           C  
ANISOU 1404  CD2 PHE B  72     3450   4041   3674    984     12    248       C  
ATOM   1405  CE1 PHE B  72      12.617  12.136  43.614  1.00 28.20           C  
ANISOU 1405  CE1 PHE B  72     3231   3965   3520   1029     39    280       C  
ATOM   1406  CE2 PHE B  72      11.769  11.861  45.834  1.00 29.11           C  
ANISOU 1406  CE2 PHE B  72     3393   4031   3635    999     34    273       C  
ATOM   1407  CZ  PHE B  72      11.819  12.578  44.652  1.00 36.15           C  
ANISOU 1407  CZ  PHE B  72     4250   4960   4524   1022     48    290       C  
ATOM   1408  N   GLY B  73      14.791   5.768  44.037  1.00 27.80           N  
ANISOU 1408  N   GLY B  73     3304   3810   3448    954    -42    155       N  
ATOM   1409  CA  GLY B  73      15.648   4.665  44.406  1.00 26.71           C  
ANISOU 1409  CA  GLY B  73     3202   3633   3315    952    -55    136       C  
ATOM   1410  C   GLY B  73      16.441   4.079  43.253  1.00 35.95           C  
ANISOU 1410  C   GLY B  73     4366   4811   4483    965    -55    127       C  
ATOM   1411  O   GLY B  73      16.917   2.954  43.335  1.00 42.78           O  
ANISOU 1411  O   GLY B  73     5262   5650   5342    961    -61    108       O  
ATOM   1412  N   LYS B  74      16.591   4.837  42.180  1.00 42.29           N  
ANISOU 1412  N   LYS B  74     5131   5648   5289    981    -45    140       N  
ATOM   1413  CA  LYS B  74      17.361   4.361  41.032  1.00 41.51           C  
ANISOU 1413  CA  LYS B  74     5025   5558   5189    995    -43    132       C  
ATOM   1414  C   LYS B  74      18.852   4.549  41.250  1.00 38.95           C  
ANISOU 1414  C   LYS B  74     4704   5203   4894   1022    -52    137       C  
ATOM   1415  O   LYS B  74      19.274   5.411  42.027  1.00 36.33           O  
ANISOU 1415  O   LYS B  74     4366   4855   4584   1033    -57    152       O  
ATOM   1416  CB  LYS B  74      16.913   5.073  39.756  1.00 42.36           C  
ANISOU 1416  CB  LYS B  74     5091   5717   5287   1001    -29    145       C  
ATOM   1417  CG  LYS B  74      15.518   4.662  39.317  1.00 53.60           C  
ANISOU 1417  CG  LYS B  74     6509   7180   6676    972    -21    138       C  
ATOM   1418  CD  LYS B  74      14.885   5.696  38.409  1.00 61.36           C  
ANISOU 1418  CD  LYS B  74     7448   8216   7652    980     -9    158       C  
ATOM   1419  CE  LYS B  74      13.383   5.461  38.300  1.00 70.55           C  
ANISOU 1419  CE  LYS B  74     8602   9422   8782    951     -2    156       C  
ATOM   1420  NZ  LYS B  74      12.691   6.560  37.574  1.00 73.11           N  
ANISOU 1420  NZ  LYS B  74     8881   9799   9098    963     11    180       N  
ATOM   1421  N   SER B  75      19.649   3.726  40.571  1.00 37.85           N  
ANISOU 1421  N   SER B  75     4573   5056   4753   1033    -53    126       N  
ATOM   1422  CA  SER B  75      21.098   3.778  40.708  1.00 36.42           C  
ANISOU 1422  CA  SER B  75     4392   4849   4597   1060    -61    130       C  
ATOM   1423  C   SER B  75      21.637   5.124  40.257  1.00 33.93           C  
ANISOU 1423  C   SER B  75     4036   4553   4301   1080    -56    151       C  
ATOM   1424  O   SER B  75      21.107   5.747  39.341  1.00 36.75           O  
ANISOU 1424  O   SER B  75     4365   4947   4650   1080    -44    158       O  
ATOM   1425  CB  SER B  75      21.761   2.642  39.920  1.00 44.07           C  
ANISOU 1425  CB  SER B  75     5376   5811   5558   1069    -58    115       C  
ATOM   1426  OG  SER B  75      21.960   1.511  40.754  1.00 51.43           O  
ANISOU 1426  OG  SER B  75     6352   6705   6484   1064    -66    100       O  
ATOM   1427  N   ASN B  76      22.686   5.571  40.935  1.00 29.36           N  
ANISOU 1427  N   ASN B  76     3457   3953   3747   1096    -66    160       N  
ATOM   1428  CA  ASN B  76      23.267   6.883  40.703  1.00 31.23           C  
ANISOU 1428  CA  ASN B  76     3662   4203   4002   1112    -62    179       C  
ATOM   1429  C   ASN B  76      24.752   6.744  40.978  1.00 29.96           C  
ANISOU 1429  C   ASN B  76     3502   4021   3861   1131    -73    180       C  
ATOM   1430  O   ASN B  76      25.161   6.017  41.868  1.00 30.17           O  
ANISOU 1430  O   ASN B  76     3553   4018   3890   1131    -87    174       O  
ATOM   1431  CB  ASN B  76      22.603   7.943  41.607  1.00 25.74           C  
ANISOU 1431  CB  ASN B  76     2965   3504   3311   1100    -59    193       C  
ATOM   1432  CG  ASN B  76      22.968   9.367  41.228  1.00 33.19           C  
ANISOU 1432  CG  ASN B  76     3879   4465   4268   1113    -48    212       C  
ATOM   1433  OD1 ASN B  76      24.121   9.767  41.333  1.00 44.18           O  
ANISOU 1433  OD1 ASN B  76     5262   5847   5677   1125    -53    218       O  
ATOM   1434  ND2 ASN B  76      21.980  10.144  40.803  1.00 33.22           N  
ANISOU 1434  ND2 ASN B  76     3866   4494   4262   1109    -32    223       N  
ATOM   1435  N   LYS B  77      25.572   7.418  40.197  1.00 27.25           N  
ANISOU 1435  N   LYS B  77     3130   3695   3530   1149    -67    190       N  
ATOM   1436  CA  LYS B  77      27.005   7.197  40.280  1.00 35.23           C  
ANISOU 1436  CA  LYS B  77     4136   4694   4557   1169    -77    191       C  
ATOM   1437  C   LYS B  77      27.666   8.097  41.366  1.00 32.75           C  
ANISOU 1437  C   LYS B  77     3818   4367   4260   1167    -87    205       C  
ATOM   1438  O   LYS B  77      28.843   7.927  41.696  1.00 30.16           O  
ANISOU 1438  O   LYS B  77     3486   4029   3944   1179    -98    208       O  
ATOM   1439  CB  LYS B  77      27.579   7.383  38.865  1.00 42.30           C  
ANISOU 1439  CB  LYS B  77     5003   5615   5454   1187    -65    193       C  
ATOM   1440  CG  LYS B  77      28.783   8.239  38.717  1.00 57.95           C  
ANISOU 1440  CG  LYS B  77     6965   7598   7456   1180    -66    201       C  
ATOM   1441  CD  LYS B  77      28.988   8.703  37.271  1.00 68.21           C  
ANISOU 1441  CD  LYS B  77     8240   8922   8754   1177    -50    201       C  
ATOM   1442  CE  LYS B  77      29.120   7.542  36.292  1.00 73.68           C  
ANISOU 1442  CE  LYS B  77     8937   9621   9438   1193    -46    188       C  
ATOM   1443  NZ  LYS B  77      29.322   8.006  34.883  1.00 70.72           N  
ANISOU 1443  NZ  LYS B  77     8540   9270   9062   1190    -31    189       N  
ATOM   1444  N   ARG B  78      26.894   8.996  41.987  1.00 29.62           N  
ANISOU 1444  N   ARG B  78     3423   3968   3862   1150    -82    214       N  
ATOM   1445  CA  ARG B  78      27.463   9.861  43.054  1.00 26.63           C  
ANISOU 1445  CA  ARG B  78     3046   3576   3498   1142    -89    226       C  
ATOM   1446  C   ARG B  78      28.072   8.997  44.142  1.00 29.48           C  
ANISOU 1446  C   ARG B  78     3430   3910   3862   1141   -110    220       C  
ATOM   1447  O   ARG B  78      27.548   7.919  44.432  1.00 29.07           O  
ANISOU 1447  O   ARG B  78     3403   3842   3799   1138   -117    208       O  
ATOM   1448  CB  ARG B  78      26.409  10.798  43.656  1.00 27.54           C  
ANISOU 1448  CB  ARG B  78     3169   3688   3609   1123    -79    235       C  
ATOM   1449  CG  ARG B  78      25.924  11.877  42.719  1.00 36.34           C  
ANISOU 1449  CG  ARG B  78     4260   4828   4719   1127    -57    246       C  
ATOM   1450  CD  ARG B  78      27.058  12.793  42.284  1.00 40.37           C  
ANISOU 1450  CD  ARG B  78     4748   5348   5243   1135    -51    256       C  
ATOM   1451  NE  ARG B  78      27.569  13.637  43.368  1.00 42.61           N  
ANISOU 1451  NE  ARG B  78     5041   5615   5536   1124    -54    266       N  
ATOM   1452  CZ  ARG B  78      27.021  14.798  43.724  1.00 41.24           C  
ANISOU 1452  CZ  ARG B  78     4872   5437   5360   1113    -37    279       C  
ATOM   1453  NH1 ARG B  78      25.932  15.238  43.108  1.00 37.07           N  
ANISOU 1453  NH1 ARG B  78     4339   4923   4822   1117    -17    285       N  
ATOM   1454  NH2 ARG B  78      27.553  15.515  44.700  1.00 46.16           N  
ANISOU 1454  NH2 ARG B  78     5507   6043   5990   1097    -39    286       N  
ATOM   1455  N   LYS B  79      29.211   9.434  44.687  1.00 27.27           N  
ANISOU 1455  N   LYS B  79     3141   3626   3595   1145   -121    229       N  
ATOM   1456  CA  LYS B  79      29.965   8.618  45.632  1.00 26.52           C  
ANISOU 1456  CA  LYS B  79     3062   3511   3503   1149   -142    227       C  
ATOM   1457  C   LYS B  79      29.085   8.283  46.842  1.00 25.65           C  
ANISOU 1457  C   LYS B  79     2987   3373   3386   1128   -150    222       C  
ATOM   1458  O   LYS B  79      28.481   9.171  47.435  1.00 32.62           O  
ANISOU 1458  O   LYS B  79     3876   4251   4269   1107   -144    229       O  
ATOM   1459  CB  LYS B  79      31.230   9.328  46.100  1.00 39.32           C  
ANISOU 1459  CB  LYS B  79     4664   5139   5137   1149   -151    240       C  
ATOM   1460  CG  LYS B  79      32.143   8.423  46.928  1.00 49.89           C  
ANISOU 1460  CG  LYS B  79     6014   6465   6478   1160   -173    240       C  
ATOM   1461  CD  LYS B  79      33.094   9.203  47.830  1.00 55.98           C  
ANISOU 1461  CD  LYS B  79     6773   7240   7257   1148   -186    253       C  
ATOM   1462  CE  LYS B  79      32.774   8.932  49.305  1.00 59.97           C  
ANISOU 1462  CE  LYS B  79     7311   7719   7758   1129   -202    254       C  
ATOM   1463  NZ  LYS B  79      32.432   7.499  49.571  1.00 57.28           N  
ANISOU 1463  NZ  LYS B  79     6998   7356   7409   1143   -211    243       N  
ATOM   1464  N   GLY B  80      29.005   7.002  47.168  1.00 27.49           N  
ANISOU 1464  N   GLY B  80     3245   3588   3611   1134   -160    211       N  
ATOM   1465  CA  GLY B  80      28.228   6.553  48.311  1.00 30.39           C  
ANISOU 1465  CA  GLY B  80     3648   3927   3970   1115   -168    205       C  
ATOM   1466  C   GLY B  80      26.766   6.245  48.046  1.00 26.07           C  
ANISOU 1466  C   GLY B  80     3119   3378   3409   1100   -155    193       C  
ATOM   1467  O   GLY B  80      26.139   5.610  48.873  1.00 27.32           O  
ANISOU 1467  O   GLY B  80     3309   3513   3558   1086   -162    185       O  
ATOM   1468  N   PHE B  81      26.211   6.686  46.910  1.00 23.82           N  
ANISOU 1468  N   PHE B  81     2812   3119   3119   1102   -138    193       N  
ATOM   1469  CA  PHE B  81      24.769   6.534  46.671  1.00 22.35           C  
ANISOU 1469  CA  PHE B  81     2637   2939   2917   1085   -126    185       C  
ATOM   1470  C   PHE B  81      24.300   5.085  46.597  1.00 23.76           C  
ANISOU 1470  C   PHE B  81     2845   3105   3079   1081   -129    166       C  
ATOM   1471  O   PHE B  81      23.356   4.680  47.282  1.00 24.02           O  
ANISOU 1471  O   PHE B  81     2904   3123   3099   1060   -130    158       O  
ATOM   1472  CB  PHE B  81      24.348   7.254  45.376  1.00 26.47           C  
ANISOU 1472  CB  PHE B  81     3126   3496   3435   1090   -107    191       C  
ATOM   1473  CG  PHE B  81      22.854   7.442  45.253  1.00 23.01           C  
ANISOU 1473  CG  PHE B  81     2690   3071   2981   1072    -94    189       C  
ATOM   1474  CD1 PHE B  81      22.240   8.575  45.768  1.00 24.93           C  
ANISOU 1474  CD1 PHE B  81     2928   3317   3227   1061    -85    203       C  
ATOM   1475  CD2 PHE B  81      22.070   6.479  44.631  1.00 26.04           C  
ANISOU 1475  CD2 PHE B  81     3083   3466   3344   1064    -89    174       C  
ATOM   1476  CE1 PHE B  81      20.872   8.748  45.649  1.00 20.69           C  
ANISOU 1476  CE1 PHE B  81     2391   2796   2674   1048    -73    204       C  
ATOM   1477  CE2 PHE B  81      20.722   6.637  44.510  1.00 30.14           C  
ANISOU 1477  CE2 PHE B  81     3602   4004   3847   1047    -78    173       C  
ATOM   1478  CZ  PHE B  81      20.110   7.774  45.031  1.00 32.54           C  
ANISOU 1478  CZ  PHE B  81     3897   4313   4156   1040    -70    189       C  
ATOM   1479  N   ASN B  82      24.959   4.291  45.760  1.00 24.51           N  
ANISOU 1479  N   ASN B  82     2937   3204   3170   1100   -128    159       N  
ATOM   1480  CA  ASN B  82      24.566   2.912  45.598  1.00 25.58           C  
ANISOU 1480  CA  ASN B  82     3105   3327   3288   1096   -126    140       C  
ATOM   1481  C   ASN B  82      24.785   2.125  46.879  1.00 30.90           C  
ANISOU 1481  C   ASN B  82     3818   3963   3961   1093   -141    135       C  
ATOM   1482  O   ASN B  82      24.032   1.189  47.178  1.00 28.37           O  
ANISOU 1482  O   ASN B  82     3532   3625   3621   1077   -139    119       O  
ATOM   1483  CB  ASN B  82      25.327   2.292  44.419  1.00 30.32           C  
ANISOU 1483  CB  ASN B  82     3697   3938   3887   1120   -119    135       C  
ATOM   1484  CG  ASN B  82      24.868   2.865  43.105  1.00 32.60           C  
ANISOU 1484  CG  ASN B  82     3954   4263   4170   1118   -103    136       C  
ATOM   1485  OD1 ASN B  82      23.761   3.378  43.024  1.00 28.26           O  
ANISOU 1485  OD1 ASN B  82     3397   3730   3611   1097    -96    137       O  
ATOM   1486  ND2 ASN B  82      25.703   2.782  42.068  1.00 33.21           N  
ANISOU 1486  ND2 ASN B  82     4011   4354   4253   1140    -97    138       N  
ATOM   1487  N   GLU B  83      25.806   2.514  47.643  1.00 22.43           N  
ANISOU 1487  N   GLU B  83     2739   2879   2906   1106   -155    148       N  
ATOM   1488  CA  GLU B  83      26.002   1.932  48.968  1.00 23.51           C  
ANISOU 1488  CA  GLU B  83     2909   2981   3042   1103   -171    146       C  
ATOM   1489  C   GLU B  83      24.828   2.315  49.887  1.00 22.92           C  
ANISOU 1489  C   GLU B  83     2852   2895   2961   1070   -171    143       C  
ATOM   1490  O   GLU B  83      24.379   1.519  50.709  1.00 24.74           O  
ANISOU 1490  O   GLU B  83     3122   3099   3180   1058   -177    133       O  
ATOM   1491  CB  GLU B  83      27.309   2.414  49.577  1.00 21.33           C  
ANISOU 1491  CB  GLU B  83     2617   2704   2785   1120   -187    163       C  
ATOM   1492  CG  GLU B  83      28.553   1.787  48.920  1.00 28.50           C  
ANISOU 1492  CG  GLU B  83     3514   3618   3698   1155   -189    165       C  
ATOM   1493  CD  GLU B  83      28.907   2.409  47.562  1.00 36.68           C  
ANISOU 1493  CD  GLU B  83     4508   4687   4740   1168   -176    170       C  
ATOM   1494  OE1 GLU B  83      28.171   3.295  47.079  1.00 39.91           O  
ANISOU 1494  OE1 GLU B  83     4900   5115   5150   1151   -165    171       O  
ATOM   1495  OE2 GLU B  83      29.928   2.000  46.969  1.00 41.94           O  
ANISOU 1495  OE2 GLU B  83     5163   5362   5412   1197   -176    173       O  
ATOM   1496  N   GLY B  84      24.387   3.558  49.763  1.00 24.57           N  
ANISOU 1496  N   GLY B  84     3034   3124   3177   1059   -164    154       N  
ATOM   1497  CA  GLY B  84      23.237   4.036  50.525  1.00 23.68           C  
ANISOU 1497  CA  GLY B  84     2935   3004   3058   1031   -161    154       C  
ATOM   1498  C   GLY B  84      21.988   3.229  50.227  1.00 26.29           C  
ANISOU 1498  C   GLY B  84     3286   3337   3366   1013   -151    137       C  
ATOM   1499  O   GLY B  84      21.234   2.885  51.145  1.00 26.49           O  
ANISOU 1499  O   GLY B  84     3341   3341   3381    992   -154    129       O  
ATOM   1500  N   LEU B  85      21.742   2.934  48.948  1.00 22.99           N  
ANISOU 1500  N   LEU B  85     2853   2945   2938   1019   -138    130       N  
ATOM   1501  CA  LEU B  85      20.577   2.128  48.601  1.00 27.62           C  
ANISOU 1501  CA  LEU B  85     3458   3537   3499    998   -128    113       C  
ATOM   1502  C   LEU B  85      20.653   0.758  49.260  1.00 29.05           C  
ANISOU 1502  C   LEU B  85     3687   3682   3667    992   -136     95       C  
ATOM   1503  O   LEU B  85      19.640   0.200  49.670  1.00 34.08           O  
ANISOU 1503  O   LEU B  85     4353   4312   4286    966   -132     82       O  
ATOM   1504  CB  LEU B  85      20.465   1.955  47.088  1.00 23.90           C  
ANISOU 1504  CB  LEU B  85     2964   3100   3017   1005   -115    108       C  
ATOM   1505  CG  LEU B  85      20.134   3.189  46.257  1.00 22.91           C  
ANISOU 1505  CG  LEU B  85     2793   3014   2897   1009   -103    123       C  
ATOM   1506  CD1 LEU B  85      19.972   2.784  44.775  1.00 26.61           C  
ANISOU 1506  CD1 LEU B  85     3245   3514   3350   1012    -91    115       C  
ATOM   1507  CD2 LEU B  85      18.896   3.956  46.765  1.00 27.01           C  
ANISOU 1507  CD2 LEU B  85     3306   3546   3410    987    -97    131       C  
ATOM   1508  N   TRP B  86      21.862   0.206  49.329  1.00 30.96           N  
ANISOU 1508  N   TRP B  86     3939   3905   3918   1017   -145     96       N  
ATOM   1509  CA  TRP B  86      22.056  -1.104  49.932  1.00 33.76           C  
ANISOU 1509  CA  TRP B  86     4343   4224   4261   1018   -150     82       C  
ATOM   1510  C   TRP B  86      21.745  -1.041  51.414  1.00 31.17           C  
ANISOU 1510  C   TRP B  86     4041   3866   3935   1001   -163     83       C  
ATOM   1511  O   TRP B  86      20.993  -1.867  51.944  1.00 30.50           O  
ANISOU 1511  O   TRP B  86     3997   3760   3832    980   -160     68       O  
ATOM   1512  CB  TRP B  86      23.480  -1.606  49.705  1.00 31.41           C  
ANISOU 1512  CB  TRP B  86     4046   3915   3975   1054   -156     88       C  
ATOM   1513  CG  TRP B  86      23.713  -3.010  50.214  1.00 35.04           C  
ANISOU 1513  CG  TRP B  86     4558   4337   4420   1061   -158     75       C  
ATOM   1514  CD1 TRP B  86      23.645  -4.167  49.490  1.00 37.21           C  
ANISOU 1514  CD1 TRP B  86     4861   4603   4674   1066   -143     58       C  
ATOM   1515  CD2 TRP B  86      24.047  -3.396  51.557  1.00 31.00           C  
ANISOU 1515  CD2 TRP B  86     4078   3790   3910   1064   -173     77       C  
ATOM   1516  NE1 TRP B  86      23.907  -5.246  50.303  1.00 34.93           N  
ANISOU 1516  NE1 TRP B  86     4623   4274   4375   1073   -146     51       N  
ATOM   1517  CE2 TRP B  86      24.160  -4.800  51.574  1.00 33.36           C  
ANISOU 1517  CE2 TRP B  86     4425   4059   4190   1073   -166     63       C  
ATOM   1518  CE3 TRP B  86      24.247  -2.692  52.747  1.00 31.40           C  
ANISOU 1518  CE3 TRP B  86     4123   3831   3976   1059   -190     91       C  
ATOM   1519  CZ2 TRP B  86      24.472  -5.511  52.730  1.00 37.04           C  
ANISOU 1519  CZ2 TRP B  86     4933   4487   4652   1080   -176     63       C  
ATOM   1520  CZ3 TRP B  86      24.573  -3.404  53.903  1.00 34.53           C  
ANISOU 1520  CZ3 TRP B  86     4560   4192   4369   1064   -203     90       C  
ATOM   1521  CH2 TRP B  86      24.677  -4.795  53.881  1.00 36.16           C  
ANISOU 1521  CH2 TRP B  86     4812   4370   4556   1075   -196     77       C  
ATOM   1522  N   GLU B  87      22.299  -0.042  52.089  1.00 22.81           N  
ANISOU 1522  N   GLU B  87     2962   2808   2899   1008   -174    101       N  
ATOM   1523  CA  GLU B  87      22.096   0.084  53.533  1.00 24.60           C  
ANISOU 1523  CA  GLU B  87     3213   3005   3127    992   -187    104       C  
ATOM   1524  C   GLU B  87      20.642   0.350  53.964  1.00 25.67           C  
ANISOU 1524  C   GLU B  87     3361   3142   3251    957   -179     97       C  
ATOM   1525  O   GLU B  87      20.195  -0.177  54.987  1.00 27.08           O  
ANISOU 1525  O   GLU B  87     3577   3292   3421    939   -184     88       O  
ATOM   1526  CB  GLU B  87      22.972   1.201  54.099  1.00 25.28           C  
ANISOU 1526  CB  GLU B  87     3273   3095   3237   1002   -199    125       C  
ATOM   1527  CG  GLU B  87      24.429   0.833  54.252  1.00 31.43           C  
ANISOU 1527  CG  GLU B  87     4049   3865   4026   1031   -214    134       C  
ATOM   1528  CD  GLU B  87      25.184   1.881  55.013  1.00 29.07           C  
ANISOU 1528  CD  GLU B  87     3730   3568   3746   1031   -227    153       C  
ATOM   1529  OE1 GLU B  87      24.765   3.048  54.938  1.00 25.49           O  
ANISOU 1529  OE1 GLU B  87     3255   3132   3300   1016   -219    161       O  
ATOM   1530  OE2 GLU B  87      26.182   1.543  55.686  1.00 30.00           O  
ANISOU 1530  OE2 GLU B  87     3857   3674   3869   1046   -244    160       O  
ATOM   1531  N   ILE B  88      19.908   1.162  53.211  1.00 22.86           N  
ANISOU 1531  N   ILE B  88     2972   2819   2894    948   -165    101       N  
ATOM   1532  CA  ILE B  88      18.552   1.503  53.644  1.00 22.15           C  
ANISOU 1532  CA  ILE B  88     2888   2734   2793    918   -156     98       C  
ATOM   1533  C   ILE B  88      17.695   0.242  53.560  1.00 28.92           C  
ANISOU 1533  C   ILE B  88     3781   3584   3623    897   -150     74       C  
ATOM   1534  O   ILE B  88      16.750   0.070  54.327  1.00 28.81           O  
ANISOU 1534  O   ILE B  88     3791   3559   3598    871   -149     67       O  
ATOM   1535  CB  ILE B  88      17.956   2.676  52.821  1.00 24.43           C  
ANISOU 1535  CB  ILE B  88     3134   3065   3085    918   -141    111       C  
ATOM   1536  CG1 ILE B  88      16.773   3.308  53.576  1.00 22.59           C  
ANISOU 1536  CG1 ILE B  88     2905   2833   2847    893   -133    115       C  
ATOM   1537  CG2 ILE B  88      17.623   2.251  51.371  1.00 25.94           C  
ANISOU 1537  CG2 ILE B  88     3305   3290   3260    921   -128    102       C  
ATOM   1538  CD1 ILE B  88      16.445   4.726  53.151  1.00 23.02           C  
ANISOU 1538  CD1 ILE B  88     2919   2917   2910    899   -119    136       C  
ATOM   1539  N   GLU B  89      18.078  -0.670  52.676  1.00 29.32           N  
ANISOU 1539  N   GLU B  89     3838   3639   3663    909   -147     63       N  
ATOM   1540  CA  GLU B  89      17.393  -1.957  52.578  1.00 36.27           C  
ANISOU 1540  CA  GLU B  89     4759   4508   4514    887   -139     39       C  
ATOM   1541  C   GLU B  89      17.907  -2.975  53.588  1.00 34.22           C  
ANISOU 1541  C   GLU B  89     4551   4200   4252    891   -150     29       C  
ATOM   1542  O   GLU B  89      17.121  -3.651  54.235  1.00 41.40           O  
ANISOU 1542  O   GLU B  89     5499   5090   5142    864   -147     14       O  
ATOM   1543  CB  GLU B  89      17.533  -2.528  51.167  1.00 41.84           C  
ANISOU 1543  CB  GLU B  89     5454   5236   5206    895   -127     30       C  
ATOM   1544  CG  GLU B  89      16.656  -1.813  50.139  1.00 51.98           C  
ANISOU 1544  CG  GLU B  89     6697   6572   6482    882   -114     34       C  
ATOM   1545  CD  GLU B  89      15.182  -2.116  50.332  1.00 57.00           C  
ANISOU 1545  CD  GLU B  89     7347   7222   7091    842   -105     20       C  
ATOM   1546  OE1 GLU B  89      14.882  -3.178  50.913  1.00 61.62           O  
ANISOU 1546  OE1 GLU B  89     7979   7777   7657    822   -105      1       O  
ATOM   1547  OE2 GLU B  89      14.328  -1.297  49.915  1.00 51.97           O  
ANISOU 1547  OE2 GLU B  89     6672   6625   6449    830    -97     29       O  
ATOM   1548  N   ASN B  90      19.224  -3.087  53.714  1.00 33.07           N  
ANISOU 1548  N   ASN B  90     4406   4037   4123    924   -161     39       N  
ATOM   1549  CA  ASN B  90      19.820  -4.237  54.386  1.00 34.18           C  
ANISOU 1549  CA  ASN B  90     4595   4136   4257    935   -167     31       C  
ATOM   1550  C   ASN B  90      20.338  -3.941  55.783  1.00 38.05           C  
ANISOU 1550  C   ASN B  90     5098   4597   4762    941   -187     43       C  
ATOM   1551  O   ASN B  90      20.476  -4.846  56.598  1.00 42.62           O  
ANISOU 1551  O   ASN B  90     5723   5139   5331    941   -192     35       O  
ATOM   1552  CB  ASN B  90      20.968  -4.812  53.540  1.00 36.78           C  
ANISOU 1552  CB  ASN B  90     4921   4464   4589    972   -165     33       C  
ATOM   1553  CG  ASN B  90      20.521  -5.236  52.148  1.00 44.17           C  
ANISOU 1553  CG  ASN B  90     5851   5425   5506    965   -145     20       C  
ATOM   1554  OD1 ASN B  90      19.817  -6.231  51.989  1.00 51.70           O  
ANISOU 1554  OD1 ASN B  90     6845   6367   6433    944   -132     -1       O  
ATOM   1555  ND2 ASN B  90      20.945  -4.489  51.133  1.00 38.92           N  
ANISOU 1555  ND2 ASN B  90     5138   4795   4855    982   -141     31       N  
ATOM   1556  N   ASN B  91      20.647  -2.684  56.059  1.00 32.23           N  
ANISOU 1556  N   ASN B  91     4322   3876   4048    945   -196     62       N  
ATOM   1557  CA  ASN B  91      21.183  -2.325  57.370  1.00 32.28           C  
ANISOU 1557  CA  ASN B  91     4339   3858   4068    947   -214     74       C  
ATOM   1558  C   ASN B  91      20.731  -0.931  57.824  1.00 32.13           C  
ANISOU 1558  C   ASN B  91     4291   3853   4063    928   -216     88       C  
ATOM   1559  O   ASN B  91      21.559  -0.085  58.146  1.00 30.99           O  
ANISOU 1559  O   ASN B  91     4124   3714   3938    939   -226    106       O  
ATOM   1560  CB  ASN B  91      22.709  -2.398  57.338  1.00 36.53           C  
ANISOU 1560  CB  ASN B  91     4864   4395   4622    984   -227     89       C  
ATOM   1561  CG  ASN B  91      23.325  -2.433  58.721  1.00 38.96           C  
ANISOU 1561  CG  ASN B  91     5193   4674   4936    987   -247     99       C  
ATOM   1562  OD1 ASN B  91      22.680  -2.832  59.682  1.00 38.62           O  
ANISOU 1562  OD1 ASN B  91     5189   4603   4883    966   -251     90       O  
ATOM   1563  ND2 ASN B  91      24.588  -2.018  58.826  1.00 33.70           N  
ANISOU 1563  ND2 ASN B  91     4501   4019   4287   1013   -261    118       N  
ATOM   1564  N   PRO B  92      19.403  -0.691  57.858  1.00 33.59           N  
ANISOU 1564  N   PRO B  92     4481   4045   4237    898   -203     79       N  
ATOM   1565  CA  PRO B  92      18.915   0.678  58.056  1.00 31.54           C  
ANISOU 1565  CA  PRO B  92     4191   3803   3989    885   -198     93       C  
ATOM   1566  C   PRO B  92      19.162   1.203  59.453  1.00 25.61           C  
ANISOU 1566  C   PRO B  92     3457   3025   3250    874   -211    103       C  
ATOM   1567  O   PRO B  92      18.957   2.385  59.686  1.00 27.27           O  
ANISOU 1567  O   PRO B  92     3646   3245   3471    866   -206    117       O  
ATOM   1568  CB  PRO B  92      17.417   0.556  57.780  1.00 33.39           C  
ANISOU 1568  CB  PRO B  92     4430   4052   4204    857   -181     80       C  
ATOM   1569  CG  PRO B  92      17.091  -0.846  58.084  1.00 32.91           C  
ANISOU 1569  CG  PRO B  92     4417   3966   4123    845   -183     59       C  
ATOM   1570  CD  PRO B  92      18.289  -1.640  57.667  1.00 30.23           C  
ANISOU 1570  CD  PRO B  92     4085   3615   3785    875   -191     57       C  
ATOM   1571  N   GLY B  93      19.633   0.343  60.356  1.00 30.96           N  
ANISOU 1571  N   GLY B  93     4172   3668   3922    876   -226     97       N  
ATOM   1572  CA  GLY B  93      19.882   0.756  61.726  1.00 39.97           C  
ANISOU 1572  CA  GLY B  93     5331   4783   5072    864   -240    106       C  
ATOM   1573  C   GLY B  93      21.339   1.039  62.043  1.00 35.92           C  
ANISOU 1573  C   GLY B  93     4806   4269   4575    886   -258    123       C  
ATOM   1574  O   GLY B  93      21.714   1.221  63.206  1.00 31.67           O  
ANISOU 1574  O   GLY B  93     4284   3707   4040    877   -272    130       O  
ATOM   1575  N   VAL B  94      22.170   1.103  61.008  1.00 29.29           N  
ANISOU 1575  N   VAL B  94     3933   3455   3743    913   -257    129       N  
ATOM   1576  CA  VAL B  94      23.591   1.305  61.216  1.00 28.90           C  
ANISOU 1576  CA  VAL B  94     3866   3409   3705    935   -274    145       C  
ATOM   1577  C   VAL B  94      23.836   2.618  61.959  1.00 32.66           C  
ANISOU 1577  C   VAL B  94     4327   3889   4195    917   -280    161       C  
ATOM   1578  O   VAL B  94      23.312   3.662  61.573  1.00 33.18           O  
ANISOU 1578  O   VAL B  94     4370   3971   4266    905   -264    166       O  
ATOM   1579  CB  VAL B  94      24.371   1.276  59.863  1.00 26.87           C  
ANISOU 1579  CB  VAL B  94     3571   3183   3454    967   -269    150       C  
ATOM   1580  CG1 VAL B  94      23.762   2.244  58.857  1.00 28.27           C  
ANISOU 1580  CG1 VAL B  94     3713   3390   3637    959   -250    152       C  
ATOM   1581  CG2 VAL B  94      25.829   1.601  60.106  1.00 30.81           C  
ANISOU 1581  CG2 VAL B  94     4048   3693   3966    987   -287    168       C  
ATOM   1582  N   LYS B  95      24.579   2.554  63.068  1.00 28.74           N  
ANISOU 1582  N   LYS B  95     3845   3375   3700    915   -299    170       N  
ATOM   1583  CA  LYS B  95      24.900   3.749  63.870  1.00 28.51           C  
ANISOU 1583  CA  LYS B  95     3807   3347   3680    893   -305    185       C  
ATOM   1584  C   LYS B  95      23.665   4.448  64.441  1.00 27.79           C  
ANISOU 1584  C   LYS B  95     3733   3239   3586    859   -290    181       C  
ATOM   1585  O   LYS B  95      23.737   5.600  64.882  1.00 32.87           O  
ANISOU 1585  O   LYS B  95     4368   3884   4235    840   -286    193       O  
ATOM   1586  CB  LYS B  95      25.718   4.765  63.056  1.00 30.99           C  
ANISOU 1586  CB  LYS B  95     4072   3695   4006    904   -300    199       C  
ATOM   1587  CG  LYS B  95      27.166   4.359  62.806  1.00 36.77           C  
ANISOU 1587  CG  LYS B  95     4783   4446   4742    933   -318    209       C  
ATOM   1588  CD  LYS B  95      27.886   5.409  61.957  1.00 40.48           C  
ANISOU 1588  CD  LYS B  95     5207   4951   5224    940   -311    222       C  
ATOM   1589  CE  LYS B  95      29.295   4.962  61.592  1.00 35.08           C  
ANISOU 1589  CE  LYS B  95     4496   4290   4543    971   -327    232       C  
ATOM   1590  NZ  LYS B  95      29.891   5.894  60.600  1.00 30.72           N  
ANISOU 1590  NZ  LYS B  95     3899   3772   4000    978   -318    241       N  
ATOM   1591  N   PHE B  96      22.539   3.751  64.437  1.00 28.35           N  
ANISOU 1591  N   PHE B  96     3831   3294   3646    851   -281    165       N  
ATOM   1592  CA  PHE B  96      21.318   4.316  64.986  1.00 32.99           C  
ANISOU 1592  CA  PHE B  96     4436   3869   4230    821   -266    161       C  
ATOM   1593  C   PHE B  96      21.278   4.129  66.500  1.00 34.50           C  
ANISOU 1593  C   PHE B  96     4668   4024   4417    798   -280    160       C  
ATOM   1594  O   PHE B  96      21.392   3.009  66.981  1.00 35.49           O  
ANISOU 1594  O   PHE B  96     4824   4128   4533    802   -293    150       O  
ATOM   1595  CB  PHE B  96      20.095   3.671  64.354  1.00 31.63           C  
ANISOU 1595  CB  PHE B  96     4272   3699   4045    818   -250    144       C  
ATOM   1596  CG  PHE B  96      18.800   4.284  64.799  1.00 30.41           C  
ANISOU 1596  CG  PHE B  96     4130   3539   3887    790   -232    142       C  
ATOM   1597  CD1 PHE B  96      18.542   5.623  64.566  1.00 26.83           C  
ANISOU 1597  CD1 PHE B  96     3650   3102   3442    785   -215    156       C  
ATOM   1598  CD2 PHE B  96      17.845   3.519  65.443  1.00 33.08           C  
ANISOU 1598  CD2 PHE B  96     4505   3854   4211    771   -231    126       C  
ATOM   1599  CE1 PHE B  96      17.339   6.198  64.981  1.00 28.50           C  
ANISOU 1599  CE1 PHE B  96     3872   3308   3649    764   -197    157       C  
ATOM   1600  CE2 PHE B  96      16.647   4.086  65.860  1.00 29.15           C  
ANISOU 1600  CE2 PHE B  96     4016   3352   3709    747   -214    126       C  
ATOM   1601  CZ  PHE B  96      16.397   5.423  65.627  1.00 27.92           C  
ANISOU 1601  CZ  PHE B  96     3832   3213   3562    745   -197    142       C  
ATOM   1602  N   THR B  97      21.084   5.221  67.233  1.00 41.05           N  
ANISOU 1602  N   THR B  97     5501   4845   5252    774   -274    170       N  
ATOM   1603  CA  THR B  97      21.096   5.181  68.699  1.00 39.10           C  
ANISOU 1603  CA  THR B  97     5291   4565   5001    749   -286    171       C  
ATOM   1604  C   THR B  97      19.743   5.500  69.340  1.00 45.96           C  
ANISOU 1604  C   THR B  97     6187   5411   5863    720   -269    164       C  
ATOM   1605  O   THR B  97      19.653   5.675  70.554  1.00 44.78           O  
ANISOU 1605  O   THR B  97     6069   5234   5711    695   -275    166       O  
ATOM   1606  CB  THR B  97      22.127   6.172  69.265  1.00 35.80           C  
ANISOU 1606  CB  THR B  97     4861   4150   4590    739   -296    189       C  
ATOM   1607  OG1 THR B  97      21.910   7.466  68.692  1.00 46.62           O  
ANISOU 1607  OG1 THR B  97     6205   5539   5968    733   -273    199       O  
ATOM   1608  CG2 THR B  97      23.548   5.720  68.972  1.00 44.50           C  
ANISOU 1608  CG2 THR B  97     5942   5272   5696    764   -319    197       C  
ATOM   1609  N   GLY B  98      18.693   5.573  68.530  1.00 42.94           N  
ANISOU 1609  N   GLY B  98     5793   5044   5478    722   -247    157       N  
ATOM   1610  CA  GLY B  98      17.390   6.008  69.015  1.00 47.53           C  
ANISOU 1610  CA  GLY B  98     6392   5612   6054    698   -227    154       C  
ATOM   1611  C   GLY B  98      16.630   4.926  69.761  1.00 50.94           C  
ANISOU 1611  C   GLY B  98     6866   6016   6473    682   -233    136       C  
ATOM   1612  O   GLY B  98      15.831   5.215  70.653  1.00 57.04           O  
ANISOU 1612  O   GLY B  98     7666   6767   7242    657   -224    134       O  
ATOM   1613  N   TYR B  99      16.881   3.682  69.367  1.00 41.18           N  
ANISOU 1613  N   TYR B  99     5639   4781   5229    697   -245    122       N  
ATOM   1614  CA  TYR B  99      16.299   2.488  69.973  1.00 37.55           C  
ANISOU 1614  CA  TYR B  99     5221   4293   4752    684   -251    103       C  
ATOM   1615  C   TYR B  99      16.919   1.300  69.273  1.00 41.44           C  
ANISOU 1615  C   TYR B  99     5714   4791   5238    709   -263     93       C  
ATOM   1616  O   TYR B  99      17.860   1.500  68.503  1.00 35.79           O  
ANISOU 1616  O   TYR B  99     4968   4099   4533    735   -268    103       O  
ATOM   1617  CB  TYR B  99      14.766   2.451  69.857  1.00 31.80           C  
ANISOU 1617  CB  TYR B  99     4500   3569   4013    663   -229     91       C  
ATOM   1618  CG  TYR B  99      14.182   2.549  68.451  1.00 30.29           C  
ANISOU 1618  CG  TYR B  99     4271   3420   3818    675   -211     88       C  
ATOM   1619  CD1 TYR B  99      14.055   1.425  67.633  1.00 29.59           C  
ANISOU 1619  CD1 TYR B  99     4184   3342   3715    684   -212     72       C  
ATOM   1620  CD2 TYR B  99      13.718   3.764  67.965  1.00 36.69           C  
ANISOU 1620  CD2 TYR B  99     5046   4257   4636    676   -191    103       C  
ATOM   1621  CE1 TYR B  99      13.500   1.521  66.351  1.00 25.82           C  
ANISOU 1621  CE1 TYR B  99     3673   2905   3232    692   -196     70       C  
ATOM   1622  CE2 TYR B  99      13.159   3.871  66.702  1.00 36.76           C  
ANISOU 1622  CE2 TYR B  99     5021   4307   4641    688   -175    102       C  
ATOM   1623  CZ  TYR B  99      13.056   2.754  65.902  1.00 33.45           C  
ANISOU 1623  CZ  TYR B  99     4601   3901   4207    694   -178     86       C  
ATOM   1624  OH  TYR B  99      12.494   2.897  64.652  1.00 29.53           O  
ANISOU 1624  OH  TYR B  99     4068   3447   3704    702   -163     86       O  
ATOM   1625  OXT TYR B  99      16.504   0.154  69.438  1.00 49.04           O  
ANISOU 1625  OXT TYR B  99     6711   5736   6185    704   -264     75       O  
TER    1626      TYR B  99                                                      
ATOM   1627  N   ALA C   2       1.110  19.950  21.573  1.00 42.27           N  
ANISOU 1627  N   ALA C   2     4414   6848   4798   1173    239    643       N  
ATOM   1628  CA  ALA C   2       1.700  21.141  20.977  1.00 43.68           C  
ANISOU 1628  CA  ALA C   2     4620   6989   4989   1196    257    660       C  
ATOM   1629  C   ALA C   2       1.995  20.937  19.494  1.00 43.04           C  
ANISOU 1629  C   ALA C   2     4519   6947   4888   1191    251    658       C  
ATOM   1630  O   ALA C   2       1.090  20.677  18.707  1.00 38.12           O  
ANISOU 1630  O   ALA C   2     3858   6405   4222   1184    247    673       O  
ATOM   1631  CB  ALA C   2       2.969  21.535  21.725  1.00 46.43           C  
ANISOU 1631  CB  ALA C   2     5015   7239   5387   1203    262    641       C  
ATOM   1632  N   ARG C   3       3.260  21.067  19.098  1.00 39.73           N  
ANISOU 1632  N   ARG C   3     4125   6472   4497   1193    250    640       N  
ATOM   1633  CA  ARG C   3       3.584  20.972  17.684  1.00 32.80           C  
ANISOU 1633  CA  ARG C   3     3233   5628   3603   1191    247    639       C  
ATOM   1634  C   ARG C   3       3.388  19.537  17.217  1.00 36.10           C  
ANISOU 1634  C   ARG C   3     3613   6104   3999   1164    224    617       C  
ATOM   1635  O   ARG C   3       3.908  18.612  17.824  1.00 36.47           O  
ANISOU 1635  O   ARG C   3     3665   6124   4067   1149    211    587       O  
ATOM   1636  CB  ARG C   3       5.021  21.430  17.412  1.00 38.68           C  
ANISOU 1636  CB  ARG C   3     4014   6299   4386   1199    252    624       C  
ATOM   1637  CG  ARG C   3       5.434  21.224  15.987  1.00 45.54           C  
ANISOU 1637  CG  ARG C   3     4867   7198   5240   1196    247    620       C  
ATOM   1638  CD  ARG C   3       6.813  21.778  15.697  1.00 53.05           C  
ANISOU 1638  CD  ARG C   3     5853   8079   6226   1205    254    607       C  
ATOM   1639  NE  ARG C   3       7.248  21.351  14.371  1.00 64.13           N  
ANISOU 1639  NE  ARG C   3     7239   9512   7616   1199    247    599       N  
ATOM   1640  CZ  ARG C   3       7.030  22.035  13.250  1.00 73.17           C  
ANISOU 1640  CZ  ARG C   3     8375  10691   8736   1211    258    621       C  
ATOM   1641  NH1 ARG C   3       6.387  23.192  13.290  1.00 75.83           N  
ANISOU 1641  NH1 ARG C   3     8719  11035   9058   1232    277    655       N  
ATOM   1642  NH2 ARG C   3       7.456  21.561  12.086  1.00 75.99           N  
ANISOU 1642  NH2 ARG C   3     8716  11074   9082   1203    251    611       N  
ATOM   1643  N   PRO C   4       2.605  19.336  16.153  1.00 34.62           N  
ANISOU 1643  N   PRO C   4     3386   6001   3766   1156    221    632       N  
ATOM   1644  CA  PRO C   4       2.450  17.958  15.672  1.00 30.92           C  
ANISOU 1644  CA  PRO C   4     2882   5593   3274   1126    201    610       C  
ATOM   1645  C   PRO C   4       3.733  17.416  15.037  1.00 34.41           C  
ANISOU 1645  C   PRO C   4     3335   5999   3738   1121    194    580       C  
ATOM   1646  O   PRO C   4       4.570  18.189  14.547  1.00 36.76           O  
ANISOU 1646  O   PRO C   4     3660   6249   4058   1139    204    584       O  
ATOM   1647  CB  PRO C   4       1.333  18.071  14.628  1.00 33.05           C  
ANISOU 1647  CB  PRO C   4     3108   5961   3488   1119    202    637       C  
ATOM   1648  CG  PRO C   4       1.308  19.511  14.241  1.00 41.90           C  
ANISOU 1648  CG  PRO C   4     4250   7059   4610   1152    222    670       C  
ATOM   1649  CD  PRO C   4       1.714  20.277  15.460  1.00 32.97           C  
ANISOU 1649  CD  PRO C   4     3163   5843   3522   1172    235    672       C  
ATOM   1650  N   ARG C   5       3.899  16.101  15.067  1.00 32.71           N  
ANISOU 1650  N   ARG C   5     3102   5810   3519   1097    177    550       N  
ATOM   1651  CA  ARG C   5       4.989  15.474  14.314  1.00 35.18           C  
ANISOU 1651  CA  ARG C   5     3419   6104   3844   1092    172    524       C  
ATOM   1652  C   ARG C   5       4.574  15.359  12.846  1.00 37.16           C  
ANISOU 1652  C   ARG C   5     3633   6435   4051   1080    171    535       C  
ATOM   1653  O   ARG C   5       3.379  15.334  12.555  1.00 40.80           O  
ANISOU 1653  O   ARG C   5     4058   6977   4467   1067    169    555       O  
ATOM   1654  CB  ARG C   5       5.338  14.107  14.896  1.00 33.55           C  
ANISOU 1654  CB  ARG C   5     3207   5895   3647   1073    158    488       C  
ATOM   1655  CG  ARG C   5       6.246  14.162  16.117  1.00 34.07           C  
ANISOU 1655  CG  ARG C   5     3317   5865   3764   1088    158    471       C  
ATOM   1656  CD  ARG C   5       6.484  12.766  16.658  1.00 35.17           C  
ANISOU 1656  CD  ARG C   5     3461   5996   3905   1062    144    434       C  
ATOM   1657  NE  ARG C   5       5.295  12.247  17.340  1.00 36.89           N  
ANISOU 1657  NE  ARG C   5     3669   6255   4094   1029    136    434       N  
ATOM   1658  CZ  ARG C   5       4.755  11.050  17.117  1.00 42.45           C  
ANISOU 1658  CZ  ARG C   5     4377   6992   4761    970    125    408       C  
ATOM   1659  NH1 ARG C   5       5.276  10.226  16.213  1.00 35.21           N  
ANISOU 1659  NH1 ARG C   5     3477   6072   3830    937    121    381       N  
ATOM   1660  NH2 ARG C   5       3.675  10.680  17.789  1.00 39.22           N  
ANISOU 1660  NH2 ARG C   5     3957   6620   4326    942    120    410       N  
ATOM   1661  N   PRO C   6       5.555  15.304  11.920  1.00 33.23           N  
ANISOU 1661  N   PRO C   6     3145   5917   3565   1085    172    522       N  
ATOM   1662  CA  PRO C   6       5.265  15.237  10.479  1.00 37.53           C  
ANISOU 1662  CA  PRO C   6     3657   6533   4069   1076    172    533       C  
ATOM   1663  C   PRO C   6       4.295  14.116  10.111  1.00 32.43           C  
ANISOU 1663  C   PRO C   6     2959   5992   3372   1039    160    526       C  
ATOM   1664  O   PRO C   6       4.266  13.098  10.784  1.00 33.58           O  
ANISOU 1664  O   PRO C   6     3095   6145   3518   1019    151    501       O  
ATOM   1665  CB  PRO C   6       6.645  14.971   9.860  1.00 32.14           C  
ANISOU 1665  CB  PRO C   6     2995   5801   3415   1082    174    508       C  
ATOM   1666  CG  PRO C   6       7.598  15.571  10.798  1.00 35.97           C  
ANISOU 1666  CG  PRO C   6     3530   6182   3956   1105    180    501       C  
ATOM   1667  CD  PRO C   6       6.998  15.449  12.178  1.00 36.79           C  
ANISOU 1667  CD  PRO C   6     3638   6272   4066   1102    176    501       C  
ATOM   1668  N   ARG C   7       3.504  14.304   9.062  1.00 29.47           N  
ANISOU 1668  N   ARG C   7     2548   5699   2948   1027    160    548       N  
ATOM   1669  CA  ARG C   7       2.642  13.240   8.552  1.00 32.77           C  
ANISOU 1669  CA  ARG C   7     2914   6226   3312    983    148    540       C  
ATOM   1670  C   ARG C   7       3.258  12.608   7.324  1.00 35.74           C  
ANISOU 1670  C   ARG C   7     3290   6618   3673    957    146    518       C  
ATOM   1671  O   ARG C   7       2.803  11.570   6.841  1.00 43.13           O  
ANISOU 1671  O   ARG C   7     4225   7597   4565    892    137    496       O  
ATOM   1672  CB  ARG C   7       1.266  13.773   8.194  1.00 33.28           C  
ANISOU 1672  CB  ARG C   7     2945   6372   3326    974    147    577       C  
ATOM   1673  CG  ARG C   7       0.554  14.419   9.372  1.00 44.66           C  
ANISOU 1673  CG  ARG C   7     4400   7789   4778    992    152    598       C  
ATOM   1674  CD  ARG C   7      -0.937  14.199   9.283  1.00 42.54           C  
ANISOU 1674  CD  ARG C   7     4085   7627   4451    963    145    619       C  
ATOM   1675  NE  ARG C   7      -1.589  14.272  10.592  1.00 42.28           N  
ANISOU 1675  NE  ARG C   7     4058   7580   4427    965    146    625       N  
ATOM   1676  CZ  ARG C   7      -2.388  13.321  11.062  1.00 46.68           C  
ANISOU 1676  CZ  ARG C   7     4581   8202   4954    924    134    612       C  
ATOM   1677  NH1 ARG C   7      -2.610  12.235  10.334  1.00 52.55           N  
ANISOU 1677  NH1 ARG C   7     5284   9028   5655    875    122    592       N  
ATOM   1678  NH2 ARG C   7      -2.951  13.443  12.258  1.00 38.66           N  
ANISOU 1678  NH2 ARG C   7     3572   7170   3948    930    135    618       N  
ATOM   1679  N   GLU C   8       4.251  13.286   6.784  1.00 28.94           N  
ANISOU 1679  N   GLU C   8     2443   5709   2843    997    156    524       N  
ATOM   1680  CA  GLU C   8       5.096  12.677   5.742  1.00 31.04           C  
ANISOU 1680  CA  GLU C   8     2730   5957   3106    971    156    496       C  
ATOM   1681  C   GLU C   8       6.556  13.046   5.883  1.00 40.18           C  
ANISOU 1681  C   GLU C   8     3928   7016   4322   1010    166    482       C  
ATOM   1682  O   GLU C   8       6.906  14.075   6.465  1.00 38.52           O  
ANISOU 1682  O   GLU C   8     3738   6749   4150   1053    173    500       O  
ATOM   1683  CB  GLU C   8       4.618  13.050   4.338  1.00 38.37           C  
ANISOU 1683  CB  GLU C   8     3616   6973   3990    971    159    521       C  
ATOM   1684  CG  GLU C   8       3.688  14.217   4.267  1.00 50.58           C  
ANISOU 1684  CG  GLU C   8     5144   8556   5516    997    162    567       C  
ATOM   1685  CD  GLU C   8       3.087  14.354   2.892  1.00 63.39           C  
ANISOU 1685  CD  GLU C   8     6730  10269   7086    982    161    588       C  
ATOM   1686  OE1 GLU C   8       3.864  14.477   1.920  1.00 73.64           O  
ANISOU 1686  OE1 GLU C   8     8035  11553   8390    990    166    583       O  
ATOM   1687  OE2 GLU C   8       1.845  14.321   2.782  1.00 69.97           O  
ANISOU 1687  OE2 GLU C   8     7528  11188   7870    960    154    610       O  
ATOM   1688  N   TYR C   9       7.398  12.185   5.317  1.00 36.14           N  
ANISOU 1688  N   TYR C   9     3452   6465   3815    976    164    446       N  
ATOM   1689  CA  TYR C   9       8.838  12.303   5.435  1.00 27.47           C  
ANISOU 1689  CA  TYR C   9     2395   5274   2769   1003    172    427       C  
ATOM   1690  C   TYR C   9       9.467  12.221   4.056  1.00 29.61           C  
ANISOU 1690  C   TYR C   9     2668   5553   3030    996    178    419       C  
ATOM   1691  O   TYR C   9       8.815  11.784   3.095  1.00 28.91           O  
ANISOU 1691  O   TYR C   9     2559   5533   2891    957    175    420       O  
ATOM   1692  CB  TYR C   9       9.394  11.209   6.340  1.00 27.31           C  
ANISOU 1692  CB  TYR C   9     2424   5180   2771    971    165    385       C  
ATOM   1693  CG  TYR C   9       9.111  11.439   7.813  1.00 26.49           C  
ANISOU 1693  CG  TYR C   9     2327   5046   2694    989    161    391       C  
ATOM   1694  CD1 TYR C   9       9.979  12.205   8.592  1.00 32.76           C  
ANISOU 1694  CD1 TYR C   9     3137   5770   3542   1039    167    398       C  
ATOM   1695  CD2 TYR C   9       7.991  10.892   8.420  1.00 33.02           C  
ANISOU 1695  CD2 TYR C   9     3143   5915   3489    953    152    390       C  
ATOM   1696  CE1 TYR C   9       9.728  12.422   9.940  1.00 28.76           C  
ANISOU 1696  CE1 TYR C   9     2638   5234   3057   1053    164    403       C  
ATOM   1697  CE2 TYR C   9       7.727  11.102   9.781  1.00 29.09           C  
ANISOU 1697  CE2 TYR C   9     2651   5387   3014    969    148    395       C  
ATOM   1698  CZ  TYR C   9       8.601  11.873  10.527  1.00 31.84           C  
ANISOU 1698  CZ  TYR C   9     3017   5664   3416   1019    154    402       C  
ATOM   1699  OH  TYR C   9       8.372  12.088  11.874  1.00 36.02           O  
ANISOU 1699  OH  TYR C   9     3555   6161   3968   1034    152    407       O  
ATOM   1700  N   LYS C  10      10.721  12.651   3.986  1.00 28.67           N  
ANISOU 1700  N   LYS C  10     2573   5363   2956   1032    188    413       N  
ATOM   1701  CA  LYS C  10      11.520  12.637   2.766  1.00 36.25           C  
ANISOU 1701  CA  LYS C  10     3542   6316   3917   1032    196    404       C  
ATOM   1702  C   LYS C  10      12.752  11.772   2.983  1.00 35.68           C  
ANISOU 1702  C   LYS C  10     3520   6158   3877   1017    198    363       C  
ATOM   1703  O   LYS C  10      13.279  11.714   4.095  1.00 34.86           O  
ANISOU 1703  O   LYS C  10     3441   5990   3812   1032    196    352       O  
ATOM   1704  CB  LYS C  10      11.944  14.053   2.367  1.00 41.19           C  
ANISOU 1704  CB  LYS C  10     4146   6940   4565   1094    209    436       C  
ATOM   1705  CG  LYS C  10      10.822  14.918   1.827  1.00 48.34           C  
ANISOU 1705  CG  LYS C  10     5022   7913   5431   1097    208    476       C  
ATOM   1706  CD  LYS C  10      11.340  16.274   1.371  1.00 52.25           C  
ANISOU 1706  CD  LYS C  10     5547   8359   5948   1125    218    497       C  
ATOM   1707  CE  LYS C  10      10.207  17.147   0.839  1.00 58.06           C  
ANISOU 1707  CE  LYS C  10     6261   9156   6642   1129    219    537       C  
ATOM   1708  NZ  LYS C  10      10.716  18.366   0.141  1.00 61.91           N  
ANISOU 1708  NZ  LYS C  10     6772   9609   7141   1155    232    556       N  
ATOM   1709  N   ALA C  11      13.188  11.089   1.932  1.00 28.79           N  
ANISOU 1709  N   ALA C  11     2665   5288   2988    986    202    341       N  
ATOM   1710  CA  ALA C  11      14.393  10.281   2.001  1.00 31.77           C  
ANISOU 1710  CA  ALA C  11     3090   5588   3394    975    207    305       C  
ATOM   1711  C   ALA C  11      15.538  11.149   2.509  1.00 30.78           C  
ANISOU 1711  C   ALA C  11     2972   5394   3327   1033    213    312       C  
ATOM   1712  O   ALA C  11      15.708  12.266   2.036  1.00 32.30           O  
ANISOU 1712  O   ALA C  11     3141   5603   3530   1072    221    338       O  
ATOM   1713  CB  ALA C  11      14.723   9.697   0.631  1.00 39.64           C  
ANISOU 1713  CB  ALA C  11     4097   6599   4364    944    215    288       C  
ATOM   1714  N   GLY C  12      16.296  10.641   3.478  1.00 29.38           N  
ANISOU 1714  N   GLY C  12     2831   5145   3186   1036    211    289       N  
ATOM   1715  CA  GLY C  12      17.411  11.377   4.040  1.00 32.94           C  
ANISOU 1715  CA  GLY C  12     3292   5534   3692   1084    217    293       C  
ATOM   1716  C   GLY C  12      17.099  11.947   5.413  1.00 34.38           C  
ANISOU 1716  C   GLY C  12     3468   5699   3897   1108    210    308       C  
ATOM   1717  O   GLY C  12      18.008  12.342   6.137  1.00 28.85           O  
ANISOU 1717  O   GLY C  12     2782   4939   3240   1139    212    306       O  
ATOM   1718  N   ASP C  13      15.816  11.989   5.774  1.00 28.25           N  
ANISOU 1718  N   ASP C  13     2669   4974   3090   1093    202    324       N  
ATOM   1719  CA  ASP C  13      15.416  12.588   7.049  1.00 22.39           C  
ANISOU 1719  CA  ASP C  13     1920   4220   2367   1117    197    341       C  
ATOM   1720  C   ASP C  13      15.945  11.734   8.184  1.00 25.45           C  
ANISOU 1720  C   ASP C  13     2347   4543   2782   1103    189    312       C  
ATOM   1721  O   ASP C  13      15.914  10.507   8.110  1.00 30.60           O  
ANISOU 1721  O   ASP C  13     3023   5186   3416   1061    184    284       O  
ATOM   1722  CB  ASP C  13      13.881  12.726   7.164  1.00 22.98           C  
ANISOU 1722  CB  ASP C  13     1963   4369   2401   1102    191    363       C  
ATOM   1723  CG  ASP C  13      13.319  13.901   6.369  1.00 41.83           C  
ANISOU 1723  CG  ASP C  13     4316   6809   4769   1125    199    400       C  
ATOM   1724  OD1 ASP C  13      14.091  14.813   5.983  1.00 41.24           O  
ANISOU 1724  OD1 ASP C  13     4267   6685   4719   1140    207    407       O  
ATOM   1725  OD2 ASP C  13      12.085  13.921   6.164  1.00 46.16           O  
ANISOU 1725  OD2 ASP C  13     4831   7431   5275   1112    195    419       O  
ATOM   1726  N   LEU C  14      16.417  12.389   9.236  1.00 27.26           N  
ANISOU 1726  N   LEU C  14     2583   4725   3050   1136    189    321       N  
ATOM   1727  CA  LEU C  14      16.905  11.684  10.415  1.00 26.67           C  
ANISOU 1727  CA  LEU C  14     2542   4589   3001   1127    181    298       C  
ATOM   1728  C   LEU C  14      15.838  11.702  11.504  1.00 30.08           C  
ANISOU 1728  C   LEU C  14     2968   5039   3423   1118    172    308       C  
ATOM   1729  O   LEU C  14      15.215  12.741  11.756  1.00 28.78           O  
ANISOU 1729  O   LEU C  14     2776   4903   3257   1144    175    338       O  
ATOM   1730  CB  LEU C  14      18.199  12.317  10.913  1.00 29.75           C  
ANISOU 1730  CB  LEU C  14     2946   4916   3441   1165    185    298       C  
ATOM   1731  CG  LEU C  14      19.347  12.321   9.886  1.00 28.35           C  
ANISOU 1731  CG  LEU C  14     2778   4716   3277   1172    194    287       C  
ATOM   1732  CD1 LEU C  14      20.561  12.926  10.532  1.00 30.50           C  
ANISOU 1732  CD1 LEU C  14     3085   4908   3596   1177    193    282       C  
ATOM   1733  CD2 LEU C  14      19.638  10.901   9.360  1.00 25.76           C  
ANISOU 1733  CD2 LEU C  14     2473   4380   2933   1139    193    256       C  
ATOM   1734  N   VAL C  15      15.614  10.552  12.137  1.00 25.14           N  
ANISOU 1734  N   VAL C  15     2369   4395   2789   1082    162    283       N  
ATOM   1735  CA  VAL C  15      14.491  10.409  13.072  1.00 23.78           C  
ANISOU 1735  CA  VAL C  15     2191   4245   2600   1066    153    289       C  
ATOM   1736  C   VAL C  15      14.891   9.491  14.216  1.00 30.13           C  
ANISOU 1736  C   VAL C  15     3036   4989   3423   1049    144    262       C  
ATOM   1737  O   VAL C  15      15.959   8.883  14.177  1.00 23.51           O  
ANISOU 1737  O   VAL C  15     2229   4099   2606   1048    145    239       O  
ATOM   1738  CB  VAL C  15      13.235   9.813  12.394  1.00 28.03           C  
ANISOU 1738  CB  VAL C  15     2710   4858   3083   1022    150    289       C  
ATOM   1739  CG1 VAL C  15      12.723  10.719  11.279  1.00 30.14           C  
ANISOU 1739  CG1 VAL C  15     2933   5192   3326   1039    158    319       C  
ATOM   1740  CG2 VAL C  15      13.551   8.410  11.846  1.00 26.75           C  
ANISOU 1740  CG2 VAL C  15     2581   4682   2900    976    149    253       C  
ATOM   1741  N   PHE C  16      14.028   9.397  15.223  1.00 24.29           N  
ANISOU 1741  N   PHE C  16     2295   4258   2676   1037    137    266       N  
ATOM   1742  CA  PHE C  16      13.993   8.229  16.081  1.00 27.30           C  
ANISOU 1742  CA  PHE C  16     2715   4604   3056   1004    128    238       C  
ATOM   1743  C   PHE C  16      12.794   7.413  15.634  1.00 22.38           C  
ANISOU 1743  C   PHE C  16     2085   4039   2379    953    126    230       C  
ATOM   1744  O   PHE C  16      11.738   7.978  15.328  1.00 25.95           O  
ANISOU 1744  O   PHE C  16     2498   4558   2803    951    126    253       O  
ATOM   1745  CB  PHE C  16      13.867   8.589  17.563  1.00 30.82           C  
ANISOU 1745  CB  PHE C  16     3169   5015   3527   1020    122    246       C  
ATOM   1746  CG  PHE C  16      15.087   9.250  18.144  1.00 29.14           C  
ANISOU 1746  CG  PHE C  16     2968   4740   3364   1062    123    250       C  
ATOM   1747  CD1 PHE C  16      16.108   8.488  18.721  1.00 26.65           C  
ANISOU 1747  CD1 PHE C  16     2693   4360   3075   1060    118    225       C  
ATOM   1748  CD2 PHE C  16      15.211  10.625  18.132  1.00 30.10           C  
ANISOU 1748  CD2 PHE C  16     3063   4869   3505   1102    130    279       C  
ATOM   1749  CE1 PHE C  16      17.207   9.083  19.268  1.00 29.71           C  
ANISOU 1749  CE1 PHE C  16     3088   4696   3505   1094    118    230       C  
ATOM   1750  CE2 PHE C  16      16.341  11.234  18.685  1.00 28.49           C  
ANISOU 1750  CE2 PHE C  16     2871   4610   3344   1135    132    282       C  
ATOM   1751  CZ  PHE C  16      17.337  10.453  19.238  1.00 28.60           C  
ANISOU 1751  CZ  PHE C  16     2920   4565   3382   1130    125    257       C  
ATOM   1752  N   ALA C  17      12.957   6.100  15.554  1.00 20.95           N  
ANISOU 1752  N   ALA C  17     1942   3837   2181    913    125    197       N  
ATOM   1753  CA  ALA C  17      11.860   5.242  15.121  1.00 21.19           C  
ANISOU 1753  CA  ALA C  17     1971   3921   2157    857    124    185       C  
ATOM   1754  C   ALA C  17      11.539   4.254  16.215  1.00 27.99           C  
ANISOU 1754  C   ALA C  17     2871   4751   3013    825    118    162       C  
ATOM   1755  O   ALA C  17      12.447   3.671  16.839  1.00 24.87           O  
ANISOU 1755  O   ALA C  17     2520   4285   2646    832    118    141       O  
ATOM   1756  CB  ALA C  17      12.204   4.523  13.828  1.00 25.24           C  
ANISOU 1756  CB  ALA C  17     2498   4447   2645    830    132    167       C  
ATOM   1757  N   LYS C  18      10.241   4.092  16.462  1.00 26.36           N  
ANISOU 1757  N   LYS C  18     2648   4601   2769    791    113    167       N  
ATOM   1758  CA  LYS C  18       9.768   3.263  17.563  1.00 26.45           C  
ANISOU 1758  CA  LYS C  18     2691   4588   2772    758    107    147       C  
ATOM   1759  C   LYS C  18       9.205   1.955  17.055  1.00 29.07           C  
ANISOU 1759  C   LYS C  18     3050   4945   3052    692    111    118       C  
ATOM   1760  O   LYS C  18       8.313   1.940  16.208  1.00 30.97           O  
ANISOU 1760  O   LYS C  18     3259   5261   3247    659    112    125       O  
ATOM   1761  CB  LYS C  18       8.699   4.002  18.379  1.00 24.46           C  
ANISOU 1761  CB  LYS C  18     2402   4375   2515    766    100    172       C  
ATOM   1762  CG  LYS C  18       8.290   3.263  19.655  1.00 27.74           C  
ANISOU 1762  CG  LYS C  18     2851   4759   2928    739     94    154       C  
ATOM   1763  CD  LYS C  18       9.457   3.116  20.598  1.00 28.93           C  
ANISOU 1763  CD  LYS C  18     3045   4818   3128    769     92    141       C  
ATOM   1764  CE  LYS C  18       8.994   2.502  21.912  1.00 32.89           C  
ANISOU 1764  CE  LYS C  18     3577   5291   3629    746     85    127       C  
ATOM   1765  NZ  LYS C  18       8.493   1.132  21.662  1.00 31.16           N  
ANISOU 1765  NZ  LYS C  18     3393   5083   3365    683     89     95       N  
ATOM   1766  N   MET C  19       9.765   0.857  17.550  1.00 26.17           N  
ANISOU 1766  N   MET C  19     2741   4513   2690    671    114     86       N  
ATOM   1767  CA  MET C  19       9.239  -0.468  17.281  1.00 29.99           C  
ANISOU 1767  CA  MET C  19     3262   5008   3124    605    121     55       C  
ATOM   1768  C   MET C  19       8.933  -1.090  18.619  1.00 33.78           C  
ANISOU 1768  C   MET C  19     3778   5449   3607    587    116     40       C  
ATOM   1769  O   MET C  19       9.637  -0.826  19.597  1.00 28.18           O  
ANISOU 1769  O   MET C  19     3084   4678   2944    628    111     43       O  
ATOM   1770  CB  MET C  19      10.235  -1.321  16.509  1.00 25.94           C  
ANISOU 1770  CB  MET C  19     2796   4451   2611    596    135     30       C  
ATOM   1771  CG  MET C  19      10.629  -0.676  15.192  1.00 43.77           C  
ANISOU 1771  CG  MET C  19     5020   6742   4870    616    140     45       C  
ATOM   1772  SD  MET C  19      10.430  -1.798  13.813  1.00 42.87           S  
ANISOU 1772  SD  MET C  19     4934   6658   4697    552    156     18       S  
ATOM   1773  CE  MET C  19      11.516  -3.129  14.330  1.00 56.87           C  
ANISOU 1773  CE  MET C  19     6793   8328   6486    546    171    -20       C  
ATOM   1774  N   LYS C  20       7.885  -1.900  18.668  1.00 30.28           N  
ANISOU 1774  N   LYS C  20     3347   5045   3114    525    118     23       N  
ATOM   1775  CA  LYS C  20       7.493  -2.540  19.919  1.00 31.03           C  
ANISOU 1775  CA  LYS C  20     3477   5106   3206    502    115      6       C  
ATOM   1776  C   LYS C  20       8.603  -3.420  20.477  1.00 28.97           C  
ANISOU 1776  C   LYS C  20     3286   4749   2971    512    122    -20       C  
ATOM   1777  O   LYS C  20       9.189  -4.227  19.749  1.00 30.43           O  
ANISOU 1777  O   LYS C  20     3510   4910   3143    495    136    -42       O  
ATOM   1778  CB  LYS C  20       6.220  -3.366  19.712  1.00 40.82           C  
ANISOU 1778  CB  LYS C  20     4722   6406   4380    426    118    -11       C  
ATOM   1779  CG  LYS C  20       5.491  -3.690  21.009  1.00 37.07           C  
ANISOU 1779  CG  LYS C  20     4264   5922   3900    404    112    -18       C  
ATOM   1780  CD  LYS C  20       4.211  -4.458  20.729  1.00 46.89           C  
ANISOU 1780  CD  LYS C  20     5509   7233   5076    325    116    -34       C  
ATOM   1781  CE  LYS C  20       4.012  -5.561  21.743  1.00 52.88           C  
ANISOU 1781  CE  LYS C  20     6329   7942   5820    285    120    -66       C  
ATOM   1782  NZ  LYS C  20       2.626  -6.082  21.654  1.00 52.26           N  
ANISOU 1782  NZ  LYS C  20     6241   7938   5678    211    121    -76       N  
ATOM   1783  N   GLY C  21       8.902  -3.249  21.766  1.00 30.43           N  
ANISOU 1783  N   GLY C  21     3486   4882   3195    542    113    -17       N  
ATOM   1784  CA  GLY C  21       9.974  -3.967  22.421  1.00 34.90           C  
ANISOU 1784  CA  GLY C  21     4113   5359   3790    560    118    -37       C  
ATOM   1785  C   GLY C  21      11.280  -3.185  22.498  1.00 30.13           C  
ANISOU 1785  C   GLY C  21     3497   4708   3244    629    114    -20       C  
ATOM   1786  O   GLY C  21      12.190  -3.558  23.236  1.00 37.33           O  
ANISOU 1786  O   GLY C  21     4448   5549   4187    655    114    -30       O  
ATOM   1787  N   TYR C  22      11.379  -2.100  21.740  1.00 26.05           N  
ANISOU 1787  N   TYR C  22     2926   4233   2740    659    111      5       N  
ATOM   1788  CA  TYR C  22      12.634  -1.352  21.654  1.00 24.14           C  
ANISOU 1788  CA  TYR C  22     2672   3951   2548    720    109     20       C  
ATOM   1789  C   TYR C  22      12.509   0.091  22.112  1.00 24.97           C  
ANISOU 1789  C   TYR C  22     2724   4076   2685    762     98     54       C  
ATOM   1790  O   TYR C  22      11.435   0.695  21.996  1.00 27.98           O  
ANISOU 1790  O   TYR C  22     3065   4520   3046    750     94     71       O  
ATOM   1791  CB  TYR C  22      13.155  -1.370  20.211  1.00 24.55           C  
ANISOU 1791  CB  TYR C  22     2715   4022   2590    722    121     19       C  
ATOM   1792  CG  TYR C  22      13.538  -2.736  19.725  1.00 28.81           C  
ANISOU 1792  CG  TYR C  22     3312   4529   3105    689    137    -13       C  
ATOM   1793  CD1 TYR C  22      12.613  -3.559  19.094  1.00 32.41           C  
ANISOU 1793  CD1 TYR C  22     3783   5026   3504    627    146    -31       C  
ATOM   1794  CD2 TYR C  22      14.837  -3.209  19.890  1.00 30.61           C  
ANISOU 1794  CD2 TYR C  22     3581   4686   3364    720    144    -24       C  
ATOM   1795  CE1 TYR C  22      12.981  -4.824  18.632  1.00 39.85           C  
ANISOU 1795  CE1 TYR C  22     4785   5936   4422    595    164    -61       C  
ATOM   1796  CE2 TYR C  22      15.207  -4.462  19.431  1.00 34.23           C  
ANISOU 1796  CE2 TYR C  22     4095   5112   3799    693    162    -52       C  
ATOM   1797  CZ  TYR C  22      14.276  -5.269  18.814  1.00 40.55           C  
ANISOU 1797  CZ  TYR C  22     4915   5949   4542    630    173    -71       C  
ATOM   1798  OH  TYR C  22      14.660  -6.518  18.368  1.00 43.84           O  
ANISOU 1798  OH  TYR C  22     5394   6329   4934    603    195   -100       O  
ATOM   1799  N   PRO C  23      13.621   0.672  22.598  1.00 22.19           N  
ANISOU 1799  N   PRO C  23     2373   3673   2383    813     94     64       N  
ATOM   1800  CA  PRO C  23      13.614   2.109  22.858  1.00 22.49           C  
ANISOU 1800  CA  PRO C  23     2364   3729   2451    854     87     96       C  
ATOM   1801  C   PRO C  23      13.468   2.857  21.547  1.00 24.14           C  
ANISOU 1801  C   PRO C  23     2530   3994   2648    864     93    114       C  
ATOM   1802  O   PRO C  23      13.748   2.238  20.531  1.00 22.62           O  
ANISOU 1802  O   PRO C  23     2349   3809   2436    847    102     99       O  
ATOM   1803  CB  PRO C  23      14.993   2.361  23.502  1.00 23.80           C  
ANISOU 1803  CB  PRO C  23     2549   3826   2667    899     84     97       C  
ATOM   1804  CG  PRO C  23      15.856   1.274  22.980  1.00 25.96           C  
ANISOU 1804  CG  PRO C  23     2863   4063   2937    891     92     72       C  
ATOM   1805  CD  PRO C  23      14.940   0.069  22.875  1.00 24.10           C  
ANISOU 1805  CD  PRO C  23     2658   3843   2654    835     97     48       C  
ATOM   1806  N   HIS C  24      12.994   4.105  21.564  1.00 21.80           N  
ANISOU 1806  N   HIS C  24     2187   3736   2359    889     91    144       N  
ATOM   1807  CA  HIS C  24      13.030   4.961  20.386  1.00 26.25           C  
ANISOU 1807  CA  HIS C  24     2709   4345   2919    909     98    165       C  
ATOM   1808  C   HIS C  24      14.458   4.993  19.869  1.00 27.26           C  
ANISOU 1808  C   HIS C  24     2852   4428   3078    938    103    158       C  
ATOM   1809  O   HIS C  24      15.389   5.254  20.640  1.00 22.41           O  
ANISOU 1809  O   HIS C  24     2253   3758   2505    968    100    158       O  
ATOM   1810  CB  HIS C  24      12.550   6.360  20.722  1.00 28.94           C  
ANISOU 1810  CB  HIS C  24     3008   4715   3273    943     97    200       C  
ATOM   1811  CG  HIS C  24      11.122   6.413  21.162  1.00 27.51           C  
ANISOU 1811  CG  HIS C  24     2807   4585   3062    919     94    210       C  
ATOM   1812  ND1 HIS C  24      10.684   5.841  22.348  1.00 23.24           N  
ANISOU 1812  ND1 HIS C  24     2290   4019   2518    897     86    197       N  
ATOM   1813  CD2 HIS C  24      10.024   6.947  20.586  1.00 31.34           C  
ANISOU 1813  CD2 HIS C  24     3248   5146   3514    913     97    233       C  
ATOM   1814  CE1 HIS C  24       9.389   6.048  22.479  1.00 29.04           C  
ANISOU 1814  CE1 HIS C  24     2997   4813   3223    879     86    211       C  
ATOM   1815  NE2 HIS C  24       8.959   6.717  21.418  1.00 29.36           N  
ANISOU 1815  NE2 HIS C  24     2995   4918   3244    889     92    234       N  
ATOM   1816  N   TRP C  25      14.624   4.762  18.572  1.00 19.06           N  
ANISOU 1816  N   TRP C  25     1806   3416   2019    927    111    153       N  
ATOM   1817  CA  TRP C  25      15.924   4.310  18.056  1.00 21.31           C  
ANISOU 1817  CA  TRP C  25     2117   3655   2324    941    118    137       C  
ATOM   1818  C   TRP C  25      16.427   5.224  16.943  1.00 25.72           C  
ANISOU 1818  C   TRP C  25     2643   4237   2892    970    126    154       C  
ATOM   1819  O   TRP C  25      15.683   5.498  16.014  1.00 25.53           O  
ANISOU 1819  O   TRP C  25     2590   4273   2837    956    129    165       O  
ATOM   1820  CB  TRP C  25      15.795   2.870  17.534  1.00 19.29           C  
ANISOU 1820  CB  TRP C  25     1900   3396   2033    895    125    106       C  
ATOM   1821  CG  TRP C  25      17.128   2.138  17.400  1.00 20.15           C  
ANISOU 1821  CG  TRP C  25     2050   3442   2164    908    132     85       C  
ATOM   1822  CD1 TRP C  25      18.093   2.343  16.456  1.00 24.78           C  
ANISOU 1822  CD1 TRP C  25     2632   4019   2765    932    142     86       C  
ATOM   1823  CD2 TRP C  25      17.612   1.094  18.252  1.00 19.84           C  
ANISOU 1823  CD2 TRP C  25     2062   3343   2134    901    133     63       C  
ATOM   1824  NE1 TRP C  25      19.157   1.487  16.671  1.00 25.00           N  
ANISOU 1824  NE1 TRP C  25     2703   3986   2811    941    148     66       N  
ATOM   1825  CE2 TRP C  25      18.890   0.727  17.768  1.00 24.50           C  
ANISOU 1825  CE2 TRP C  25     2674   3891   2745    924    143     53       C  
ATOM   1826  CE3 TRP C  25      17.106   0.466  19.388  1.00 26.65           C  
ANISOU 1826  CE3 TRP C  25     2952   4183   2989    881    126     52       C  
ATOM   1827  CZ2 TRP C  25      19.642  -0.274  18.375  1.00 26.26           C  
ANISOU 1827  CZ2 TRP C  25     2947   4052   2979    928    147     33       C  
ATOM   1828  CZ3 TRP C  25      17.851  -0.530  19.980  1.00 24.92           C  
ANISOU 1828  CZ3 TRP C  25     2786   3902   2782    883    129     31       C  
ATOM   1829  CH2 TRP C  25      19.105  -0.892  19.476  1.00 25.77           C  
ANISOU 1829  CH2 TRP C  25     2914   3970   2908    908    140     23       C  
ATOM   1830  N   PRO C  26      17.684   5.693  17.034  1.00 27.79           N  
ANISOU 1830  N   PRO C  26     2908   4453   3196   1010    128    158       N  
ATOM   1831  CA  PRO C  26      18.235   6.584  16.004  1.00 25.13           C  
ANISOU 1831  CA  PRO C  26     2544   4135   2871   1038    136    173       C  
ATOM   1832  C   PRO C  26      18.119   5.944  14.632  1.00 26.41           C  
ANISOU 1832  C   PRO C  26     2708   4328   2999   1011    146    161       C  
ATOM   1833  O   PRO C  26      18.595   4.823  14.472  1.00 20.47           O  
ANISOU 1833  O   PRO C  26     1992   3545   2240    992    150    135       O  
ATOM   1834  CB  PRO C  26      19.715   6.733  16.411  1.00 22.09           C  
ANISOU 1834  CB  PRO C  26     2174   3687   2530   1073    137    169       C  
ATOM   1835  CG  PRO C  26      19.992   5.546  17.275  1.00 24.94           C  
ANISOU 1835  CG  PRO C  26     2579   4001   2896   1057    131    144       C  
ATOM   1836  CD  PRO C  26      18.708   5.298  18.023  1.00 22.76           C  
ANISOU 1836  CD  PRO C  26     2305   3748   2595   1027    123    145       C  
ATOM   1837  N   ALA C  27      17.514   6.629  13.668  1.00 25.11           N  
ANISOU 1837  N   ALA C  27     2507   4223   2812   1011    150    179       N  
ATOM   1838  CA  ALA C  27      17.242   6.008  12.374  1.00 21.11           C  
ANISOU 1838  CA  ALA C  27     2001   3754   2267    979    158    168       C  
ATOM   1839  C   ALA C  27      17.146   7.017  11.249  1.00 26.43           C  
ANISOU 1839  C   ALA C  27     2634   4476   2934    998    165    191       C  
ATOM   1840  O   ALA C  27      17.253   8.216  11.460  1.00 21.54           O  
ANISOU 1840  O   ALA C  27     1986   3861   2337   1036    164    217       O  
ATOM   1841  CB  ALA C  27      15.950   5.187  12.434  1.00 20.37           C  
ANISOU 1841  CB  ALA C  27     1913   3703   2125    926    154    158       C  
ATOM   1842  N   ARG C  28      16.946   6.505  10.042  1.00 22.79           N  
ANISOU 1842  N   ARG C  28     2173   4049   2438    969    172    182       N  
ATOM   1843  CA  ARG C  28      16.882   7.358   8.855  1.00 27.61           C  
ANISOU 1843  CA  ARG C  28     2747   4705   3037    984    179    202       C  
ATOM   1844  C   ARG C  28      15.769   6.905   7.915  1.00 27.85           C  
ANISOU 1844  C   ARG C  28     2763   4808   3010    938    179    201       C  
ATOM   1845  O   ARG C  28      15.505   5.706   7.806  1.00 27.53           O  
ANISOU 1845  O   ARG C  28     2753   4767   2941    891    180    175       O  
ATOM   1846  CB  ARG C  28      18.228   7.332   8.127  1.00 28.56           C  
ANISOU 1846  CB  ARG C  28     2884   4785   3183   1005    190    191       C  
ATOM   1847  CG  ARG C  28      18.241   8.034   6.758  1.00 27.79           C  
ANISOU 1847  CG  ARG C  28     2756   4731   3071   1014    199    207       C  
ATOM   1848  CD  ARG C  28      19.603   7.802   6.066  1.00 28.75           C  
ANISOU 1848  CD  ARG C  28     2900   4808   3216   1029    211    191       C  
ATOM   1849  NE  ARG C  28      19.771   6.415   5.629  1.00 27.82           N  
ANISOU 1849  NE  ARG C  28     2821   4673   3075    988    218    160       N  
ATOM   1850  CZ  ARG C  28      20.897   5.711   5.730  1.00 31.80           C  
ANISOU 1850  CZ  ARG C  28     3363   5117   3605    996    226    137       C  
ATOM   1851  NH1 ARG C  28      21.994   6.238   6.279  1.00 29.75           N  
ANISOU 1851  NH1 ARG C  28     3104   4808   3393   1040    226    142       N  
ATOM   1852  NH2 ARG C  28      20.925   4.463   5.290  1.00 32.90           N  
ANISOU 1852  NH2 ARG C  28     3540   5244   3717    957    235    111       N  
ATOM   1853  N   ILE C  29      15.123   7.866   7.250  1.00 25.69           N  
ANISOU 1853  N   ILE C  29     2445   4598   2719    951    180    230       N  
ATOM   1854  CA  ILE C  29      14.197   7.584   6.155  1.00 26.79           C  
ANISOU 1854  CA  ILE C  29     2564   4813   2804    912    181    234       C  
ATOM   1855  C   ILE C  29      14.976   7.232   4.875  1.00 30.98           C  
ANISOU 1855  C   ILE C  29     3109   5335   3327    902    193    219       C  
ATOM   1856  O   ILE C  29      15.704   8.076   4.338  1.00 29.79           O  
ANISOU 1856  O   ILE C  29     2944   5173   3202    942    200    233       O  
ATOM   1857  CB  ILE C  29      13.290   8.799   5.885  1.00 30.70           C  
ANISOU 1857  CB  ILE C  29     3003   5379   3283    936    178    274       C  
ATOM   1858  CG1 ILE C  29      12.635   9.247   7.194  1.00 23.28           C  
ANISOU 1858  CG1 ILE C  29     2051   4440   2356    953    170    291       C  
ATOM   1859  CG2 ILE C  29      12.246   8.468   4.841  1.00 30.22           C  
ANISOU 1859  CG2 ILE C  29     2917   5404   3161    893    177    279       C  
ATOM   1860  CD1 ILE C  29      11.620   8.258   7.762  1.00 33.09           C  
ANISOU 1860  CD1 ILE C  29     3302   5709   3562    901    160    275       C  
ATOM   1861  N   ASP C  30      14.857   5.994   4.400  1.00 28.25           N  
ANISOU 1861  N   ASP C  30     2794   4991   2948    849    197    190       N  
ATOM   1862  CA  ASP C  30      15.564   5.604   3.175  1.00 27.60           C  
ANISOU 1862  CA  ASP C  30     2730   4901   2857    837    210    175       C  
ATOM   1863  C   ASP C  30      14.741   5.998   1.943  1.00 29.87           C  
ANISOU 1863  C   ASP C  30     2979   5274   3098    817    211    193       C  
ATOM   1864  O   ASP C  30      13.580   6.387   2.054  1.00 31.68           O  
ANISOU 1864  O   ASP C  30     3170   5570   3296    806    201    215       O  
ATOM   1865  CB  ASP C  30      15.862   4.106   3.154  1.00 31.92           C  
ANISOU 1865  CB  ASP C  30     3334   5408   3388    790    218    136       C  
ATOM   1866  CG  ASP C  30      17.247   3.768   3.710  1.00 31.09           C  
ANISOU 1866  CG  ASP C  30     3269   5211   3333    822    226    118       C  
ATOM   1867  OD1 ASP C  30      18.084   4.686   3.856  1.00 29.77           O  
ANISOU 1867  OD1 ASP C  30     3086   5016   3211    876    226    133       O  
ATOM   1868  OD2 ASP C  30      17.496   2.576   3.971  1.00 36.97           O  
ANISOU 1868  OD2 ASP C  30     4064   5915   4070    793    234     88       O  
ATOM   1869  N   GLU C  31      15.356   5.912   0.767  1.00 33.19           N  
ANISOU 1869  N   GLU C  31     3407   5693   3512    814    223    186       N  
ATOM   1870  CA  GLU C  31      14.651   6.262  -0.455  1.00 38.54           C  
ANISOU 1870  CA  GLU C  31     4049   6449   4144    794    223    203       C  
ATOM   1871  C   GLU C  31      13.689   5.157  -0.786  1.00 40.35           C  
ANISOU 1871  C   GLU C  31     4291   6727   4313    721    221    184       C  
ATOM   1872  O   GLU C  31      13.919   4.002  -0.433  1.00 43.13           O  
ANISOU 1872  O   GLU C  31     4692   7035   4659    685    227    152       O  
ATOM   1873  CB  GLU C  31      15.607   6.451  -1.625  1.00 55.28           C  
ANISOU 1873  CB  GLU C  31     6178   8552   6275    809    237    199       C  
ATOM   1874  CG  GLU C  31      16.234   5.149  -2.022  1.00 63.25           C  
ANISOU 1874  CG  GLU C  31     7242   9517   7274    768    251    160       C  
ATOM   1875  CD  GLU C  31      17.131   5.250  -3.220  1.00 72.51           C  
ANISOU 1875  CD  GLU C  31     8424  10673   8452    778    266    154       C  
ATOM   1876  OE1 GLU C  31      16.663   5.713  -4.291  1.00 72.89           O  
ANISOU 1876  OE1 GLU C  31     8442  10785   8469    768    267    171       O  
ATOM   1877  OE2 GLU C  31      18.294   4.823  -3.085  1.00 74.76           O  
ANISOU 1877  OE2 GLU C  31     8748  10884   8773    794    278    133       O  
ATOM   1878  N   LEU C  32      12.615   5.506  -1.475  1.00 44.12           N  
ANISOU 1878  N   LEU C  32     4726   7295   4743    698    215    206       N  
ATOM   1879  CA  LEU C  32      11.735   4.496  -2.017  1.00 53.04           C  
ANISOU 1879  CA  LEU C  32     5865   8480   5809    623    215    188       C  
ATOM   1880  C   LEU C  32      11.960   4.408  -3.517  1.00 53.11           C  
ANISOU 1880  C   LEU C  32     5874   8519   5787    601    225    185       C  
ATOM   1881  O   LEU C  32      11.482   5.260  -4.264  1.00 58.43           O  
ANISOU 1881  O   LEU C  32     6499   9261   6441    615    220    216       O  
ATOM   1882  CB  LEU C  32      10.282   4.819  -1.703  1.00 59.56           C  
ANISOU 1882  CB  LEU C  32     6642   9394   6594    604    199    213       C  
ATOM   1883  CG  LEU C  32       9.335   3.643  -1.886  1.00 65.82           C  
ANISOU 1883  CG  LEU C  32     7450  10235   7322    520    197    191       C  
ATOM   1884  CD1 LEU C  32       9.807   2.473  -1.042  1.00 60.96           C  
ANISOU 1884  CD1 LEU C  32     6900   9540   6721    492    204    151       C  
ATOM   1885  CD2 LEU C  32       7.918   4.060  -1.521  1.00 71.60           C  
ANISOU 1885  CD2 LEU C  32     8127  11060   8018    507    181    219       C  
ATOM   1886  N   PRO C  33      12.710   3.387  -3.962  1.00 55.59           N  
ANISOU 1886  N   PRO C  33     6243   8780   6098    568    241    150       N  
ATOM   1887  CA  PRO C  33      13.005   3.241  -5.392  1.00 61.24           C  
ANISOU 1887  CA  PRO C  33     6965   9517   6786    545    253    144       C  
ATOM   1888  C   PRO C  33      11.731   3.098  -6.217  1.00 73.11           C  
ANISOU 1888  C   PRO C  33     8436  11126   8216    486    246    154       C  
ATOM   1889  O   PRO C  33      10.902   2.236  -5.926  1.00 74.22           O  
ANISOU 1889  O   PRO C  33     8590  11297   8314    426    243    138       O  
ATOM   1890  CB  PRO C  33      13.837   1.951  -5.462  1.00 54.33           C  
ANISOU 1890  CB  PRO C  33     6163   8566   5914    512    273    100       C  
ATOM   1891  CG  PRO C  33      14.268   1.674  -4.070  1.00 56.51           C  
ANISOU 1891  CG  PRO C  33     6468   8770   6235    538    271     89       C  
ATOM   1892  CD  PRO C  33      13.242   2.267  -3.169  1.00 53.72           C  
ANISOU 1892  CD  PRO C  33     6068   8465   5877    548    250    114       C  
ATOM   1893  N   GLU C  34      11.554   3.954  -7.215  1.00 78.54           N  
ANISOU 1893  N   GLU C  34     9080  11873   8889    504    244    181       N  
ATOM   1894  CA  GLU C  34      10.518   3.697  -8.197  1.00 75.92           C  
ANISOU 1894  CA  GLU C  34     8723  11639   8485    443    240    188       C  
ATOM   1895  C   GLU C  34      11.036   2.563  -9.066  1.00 61.61           C  
ANISOU 1895  C   GLU C  34     6969   9795   6646    384    259    149       C  
ATOM   1896  O   GLU C  34      12.230   2.479  -9.341  1.00 59.83           O  
ANISOU 1896  O   GLU C  34     6779   9493   6459    412    275    134       O  
ATOM   1897  CB  GLU C  34      10.186   4.945  -9.013  1.00 85.73           C  
ANISOU 1897  CB  GLU C  34     9903  12953   9718    481    232    230       C  
ATOM   1898  CG  GLU C  34       8.923   5.653  -8.540  1.00 94.45           C  
ANISOU 1898  CG  GLU C  34    10943  14145  10799    492    213    268       C  
ATOM   1899  CD  GLU C  34       9.186   6.625  -7.404  1.00 99.98           C  
ANISOU 1899  CD  GLU C  34    11625  14804  11560    570    207    291       C  
ATOM   1900  OE1 GLU C  34      10.370   6.939  -7.147  1.00102.26           O  
ANISOU 1900  OE1 GLU C  34    11941  15005  11908    620    217    283       O  
ATOM   1901  OE2 GLU C  34       8.209   7.069  -6.763  1.00 99.79           O  
ANISOU 1901  OE2 GLU C  34    11559  14835  11523    580    194    317       O  
ATOM   1902  N   GLY C  35      10.145   1.668  -9.465  1.00 60.39           N  
ANISOU 1902  N   GLY C  35     6824   9699   6424    303    259    134       N  
ATOM   1903  CA  GLY C  35      10.569   0.443 -10.109  1.00 54.88           C  
ANISOU 1903  CA  GLY C  35     6192   8964   5697    240    280     93       C  
ATOM   1904  C   GLY C  35      10.692  -0.655  -9.075  1.00 48.11           C  
ANISOU 1904  C   GLY C  35     5392   8040   4846    211    288     59       C  
ATOM   1905  O   GLY C  35      11.175  -1.745  -9.366  1.00 47.94           O  
ANISOU 1905  O   GLY C  35     5437   7967   4810    168    310     22       O  
ATOM   1906  N   ALA C  36      10.271  -0.356  -7.849  1.00 40.17           N  
ANISOU 1906  N   ALA C  36     4364   7033   3864    238    272     71       N  
ATOM   1907  CA  ALA C  36      10.148  -1.380  -6.826  1.00 35.55           C  
ANISOU 1907  CA  ALA C  36     3830   6401   3278    205    277     41       C  
ATOM   1908  C   ALA C  36       8.674  -1.639  -6.529  1.00 40.78           C  
ANISOU 1908  C   ALA C  36     4462   7154   3880    145    262     47       C  
ATOM   1909  O   ALA C  36       7.809  -0.813  -6.838  1.00 46.70           O  
ANISOU 1909  O   ALA C  36     5143   7997   4606    150    243     81       O  
ATOM   1910  CB  ALA C  36      10.894  -0.979  -5.530  1.00 31.27           C  
ANISOU 1910  CB  ALA C  36     3294   5775   2810    278    273     46       C  
ATOM   1911  N   VAL C  37       8.398  -2.801  -5.950  1.00 33.06           N  
ANISOU 1911  N   VAL C  37     3536   6149   2877     87    270     14       N  
ATOM   1912  CA  VAL C  37       7.086  -3.101  -5.386  1.00 32.34           C  
ANISOU 1912  CA  VAL C  37     3422   6129   2738     34    256     16       C  
ATOM   1913  C   VAL C  37       6.725  -1.968  -4.425  1.00 36.05           C  
ANISOU 1913  C   VAL C  37     3829   6621   3249    102    232     54       C  
ATOM   1914  O   VAL C  37       7.553  -1.563  -3.615  1.00 34.19           O  
ANISOU 1914  O   VAL C  37     3605   6306   3081    171    232     57       O  
ATOM   1915  CB  VAL C  37       7.092  -4.458  -4.641  1.00 28.92           C  
ANISOU 1915  CB  VAL C  37     3064   5635   2288    -21    271    -26       C  
ATOM   1916  CG1 VAL C  37       5.774  -4.683  -3.876  1.00 35.37           C  
ANISOU 1916  CG1 VAL C  37     3855   6519   3064    -68    255    -23       C  
ATOM   1917  CG2 VAL C  37       7.355  -5.602  -5.612  1.00 36.08           C  
ANISOU 1917  CG2 VAL C  37     4038   6524   3148    -94    298    -63       C  
ATOM   1918  N   LYS C  38       5.502  -1.450  -4.507  1.00 40.62           N  
ANISOU 1918  N   LYS C  38     4341   7306   3786     85    214     82       N  
ATOM   1919  CA  LYS C  38       5.122  -0.348  -3.628  1.00 45.56           C  
ANISOU 1919  CA  LYS C  38     4909   7955   4449    151    194    120       C  
ATOM   1920  C   LYS C  38       4.777  -0.875  -2.236  1.00 51.13           C  
ANISOU 1920  C   LYS C  38     5638   8625   5166    139    190    105       C  
ATOM   1921  O   LYS C  38       4.220  -1.961  -2.094  1.00 55.41           O  
ANISOU 1921  O   LYS C  38     6213   9180   5659     62    195     76       O  
ATOM   1922  CB  LYS C  38       3.947   0.436  -4.211  1.00 52.26           C  
ANISOU 1922  CB  LYS C  38     5675   8931   5250    143    177    160       C  
ATOM   1923  CG  LYS C  38       4.305   1.406  -5.345  1.00 57.11           C  
ANISOU 1923  CG  LYS C  38     6250   9578   5871    187    177    190       C  
ATOM   1924  CD  LYS C  38       5.780   1.786  -5.365  1.00 68.60           C  
ANISOU 1924  CD  LYS C  38     7740  10927   7398    254    190    183       C  
ATOM   1925  CE  LYS C  38       6.004   3.234  -4.926  1.00 74.15           C  
ANISOU 1925  CE  LYS C  38     8394  11625   8156    349    181    225       C  
ATOM   1926  NZ  LYS C  38       7.447   3.634  -4.980  1.00 75.90           N  
ANISOU 1926  NZ  LYS C  38     8647  11749   8444    411    193    219       N  
ATOM   1927  N   PRO C  39       5.137  -0.116  -1.196  1.00 57.36           N  
ANISOU 1927  N   PRO C  39     6411   9366   6017    213    182    123       N  
ATOM   1928  CA  PRO C  39       4.725  -0.459   0.167  1.00 58.93           C  
ANISOU 1928  CA  PRO C  39     6624   9540   6227    207    176    114       C  
ATOM   1929  C   PRO C  39       3.296  -0.023   0.425  1.00 55.71           C  
ANISOU 1929  C   PRO C  39     6151   9239   5778    188    158    142       C  
ATOM   1930  O   PRO C  39       2.737   0.719  -0.391  1.00 49.91           O  
ANISOU 1930  O   PRO C  39     5356   8593   5016    196    150    175       O  
ATOM   1931  CB  PRO C  39       5.698   0.337   1.031  1.00 62.19           C  
ANISOU 1931  CB  PRO C  39     7040   9867   6721    297    174    127       C  
ATOM   1932  CG  PRO C  39       5.981   1.546   0.211  1.00 58.99           C  
ANISOU 1932  CG  PRO C  39     6585   9495   6335    353    171    162       C  
ATOM   1933  CD  PRO C  39       5.982   1.088  -1.226  1.00 55.35           C  
ANISOU 1933  CD  PRO C  39     6131   9074   5824    303    180    151       C  
ATOM   1934  N   PRO C  40       2.702  -0.473   1.544  1.00 65.66           N  
ANISOU 1934  N   PRO C  40     7421  10493   7032    165    153    132       N  
ATOM   1935  CA  PRO C  40       1.411   0.086   1.944  1.00 60.84           C  
ANISOU 1935  CA  PRO C  40     6745   9979   6393    162    136    164       C  
ATOM   1936  C   PRO C  40       1.510   1.597   2.114  1.00 46.62           C  
ANISOU 1936  C   PRO C  40     4883   8191   4637    254    127    212       C  
ATOM   1937  O   PRO C  40       2.597   2.122   2.369  1.00 43.05           O  
ANISOU 1937  O   PRO C  40     4451   7656   4250    321    132    215       O  
ATOM   1938  CB  PRO C  40       1.121  -0.609   3.277  1.00 67.83           C  
ANISOU 1938  CB  PRO C  40     7666  10822   7286    138    135    141       C  
ATOM   1939  CG  PRO C  40       1.871  -1.887   3.194  1.00 68.54           C  
ANISOU 1939  CG  PRO C  40     7841  10831   7372     90    152     91       C  
ATOM   1940  CD  PRO C  40       3.125  -1.566   2.434  1.00 68.82           C  
ANISOU 1940  CD  PRO C  40     7896  10806   7447    137    162     91       C  
ATOM   1941  N   ALA C  41       0.386   2.283   1.964  1.00 45.36           N  
ANISOU 1941  N   ALA C  41     4652   8139   4444    258    115    250       N  
ATOM   1942  CA  ALA C  41       0.382   3.735   1.983  1.00 49.03           C  
ANISOU 1942  CA  ALA C  41     5060   8627   4943    343    110    298       C  
ATOM   1943  C   ALA C  41       0.880   4.265   3.315  1.00 45.32           C  
ANISOU 1943  C   ALA C  41     4605   8074   4542    409    110    304       C  
ATOM   1944  O   ALA C  41       0.660   3.640   4.354  1.00 37.62           O  
ANISOU 1944  O   ALA C  41     3658   7065   3571    384    108    283       O  
ATOM   1945  CB  ALA C  41      -1.001   4.261   1.699  1.00 55.10           C  
ANISOU 1945  CB  ALA C  41     5752   9527   5659    333     99    338       C  
ATOM   1946  N   ASN C  42       1.559   5.410   3.258  1.00 36.87           N  
ANISOU 1946  N   ASN C  42     3517   6970   3522    490    114    332       N  
ATOM   1947  CA  ASN C  42       1.997   6.142   4.439  1.00 41.18           C  
ANISOU 1947  CA  ASN C  42     4069   7447   4131    558    115    346       C  
ATOM   1948  C   ASN C  42       2.907   5.324   5.325  1.00 38.92           C  
ANISOU 1948  C   ASN C  42     3853   7049   3885    548    118    304       C  
ATOM   1949  O   ASN C  42       2.903   5.477   6.540  1.00 48.03           O  
ANISOU 1949  O   ASN C  42     5017   8159   5072    572    116    305       O  
ATOM   1950  CB  ASN C  42       0.791   6.618   5.240  1.00 50.63           C  
ANISOU 1950  CB  ASN C  42     5218   8709   5310    568    106    376       C  
ATOM   1951  CG  ASN C  42      -0.173   7.412   4.400  1.00 61.53           C  
ANISOU 1951  CG  ASN C  42     6526  10207   6648    581    103    421       C  
ATOM   1952  OD1 ASN C  42      -1.332   7.031   4.240  1.00 65.46           O  
ANISOU 1952  OD1 ASN C  42     6987  10797   7086    531     95    427       O  
ATOM   1953  ND2 ASN C  42       0.310   8.513   3.830  1.00 59.63           N  
ANISOU 1953  ND2 ASN C  42     6261   9963   6432    647    110    452       N  
ATOM   1954  N   LYS C  43       3.669   4.435   4.706  1.00 34.89           N  
ANISOU 1954  N   LYS C  43     3392   6495   3371    511    126    268       N  
ATOM   1955  CA  LYS C  43       4.719   3.712   5.392  1.00 33.79           C  
ANISOU 1955  CA  LYS C  43     3321   6245   3273    511    132    231       C  
ATOM   1956  C   LYS C  43       6.026   4.024   4.671  1.00 35.08           C  
ANISOU 1956  C   LYS C  43     3505   6350   3475    550    143    227       C  
ATOM   1957  O   LYS C  43       6.053   4.135   3.438  1.00 34.72           O  
ANISOU 1957  O   LYS C  43     3443   6348   3402    539    147    233       O  
ATOM   1958  CB  LYS C  43       4.431   2.208   5.416  1.00 37.96           C  
ANISOU 1958  CB  LYS C  43     3898   6768   3759    427    136    188       C  
ATOM   1959  CG  LYS C  43       3.255   1.796   6.310  1.00 45.90           C  
ANISOU 1959  CG  LYS C  43     4893   7816   4732    386    127    186       C  
ATOM   1960  CD  LYS C  43       3.729   0.968   7.500  1.00 47.52           C  
ANISOU 1960  CD  LYS C  43     5160   7929   4966    376    130    153       C  
ATOM   1961  CE  LYS C  43       2.578   0.556   8.403  1.00 51.09           C  
ANISOU 1961  CE  LYS C  43     5605   8422   5387    334    122    149       C  
ATOM   1962  NZ  LYS C  43       2.848  -0.763   9.028  1.00 56.23           N  
ANISOU 1962  NZ  LYS C  43     6329   9005   6032    285    129    104       N  
ATOM   1963  N   TYR C  44       7.090   4.192   5.448  1.00 35.21           N  
ANISOU 1963  N   TYR C  44     3556   6271   3553    597    146    218       N  
ATOM   1964  CA  TYR C  44       8.399   4.590   4.938  1.00 36.53           C  
ANISOU 1964  CA  TYR C  44     3740   6378   3763    642    156    216       C  
ATOM   1965  C   TYR C  44       9.447   3.525   5.219  1.00 35.80           C  
ANISOU 1965  C   TYR C  44     3717   6193   3694    625    165    175       C  
ATOM   1966  O   TYR C  44       9.377   2.827   6.234  1.00 33.81           O  
ANISOU 1966  O   TYR C  44     3498   5900   3448    607    162    155       O  
ATOM   1967  CB  TYR C  44       8.834   5.925   5.557  1.00 35.45           C  
ANISOU 1967  CB  TYR C  44     3576   6212   3681    720    154    248       C  
ATOM   1968  CG  TYR C  44       7.946   7.055   5.137  1.00 34.09           C  
ANISOU 1968  CG  TYR C  44     3340   6126   3488    746    150    291       C  
ATOM   1969  CD1 TYR C  44       6.741   7.310   5.784  1.00 38.33           C  
ANISOU 1969  CD1 TYR C  44     3841   6720   4001    740    141    312       C  
ATOM   1970  CD2 TYR C  44       8.289   7.841   4.055  1.00 37.26           C  
ANISOU 1970  CD2 TYR C  44     3716   6552   3891    777    156    312       C  
ATOM   1971  CE1 TYR C  44       5.913   8.345   5.367  1.00 38.52           C  
ANISOU 1971  CE1 TYR C  44     3806   6826   4005    768    139    355       C  
ATOM   1972  CE2 TYR C  44       7.487   8.861   3.640  1.00 37.66           C  
ANISOU 1972  CE2 TYR C  44     3709   6680   3921    804    154    353       C  
ATOM   1973  CZ  TYR C  44       6.302   9.112   4.291  1.00 41.40           C  
ANISOU 1973  CZ  TYR C  44     4147   7211   4371    800    146    376       C  
ATOM   1974  OH  TYR C  44       5.522  10.135   3.844  1.00 43.03           O  
ANISOU 1974  OH  TYR C  44     4297   7497   4556    832    147    420       O  
ATOM   1975  N   PRO C  45      10.418   3.379   4.304  1.00 30.09           N  
ANISOU 1975  N   PRO C  45     3015   5437   2981    632    177    163       N  
ATOM   1976  CA  PRO C  45      11.507   2.448   4.587  1.00 26.48           C  
ANISOU 1976  CA  PRO C  45     2621   4889   2549    627    188    128       C  
ATOM   1977  C   PRO C  45      12.429   3.092   5.603  1.00 30.81           C  
ANISOU 1977  C   PRO C  45     3175   5365   3165    692    184    137       C  
ATOM   1978  O   PRO C  45      12.883   4.220   5.393  1.00 30.12           O  
ANISOU 1978  O   PRO C  45     3056   5278   3110    746    184    162       O  
ATOM   1979  CB  PRO C  45      12.194   2.262   3.232  1.00 29.74           C  
ANISOU 1979  CB  PRO C  45     3047   5299   2952    619    202    119       C  
ATOM   1980  CG  PRO C  45      11.886   3.506   2.479  1.00 32.34           C  
ANISOU 1980  CG  PRO C  45     3316   5693   3278    652    196    155       C  
ATOM   1981  CD  PRO C  45      10.570   4.047   2.999  1.00 30.55           C  
ANISOU 1981  CD  PRO C  45     3041   5539   3027    647    181    182       C  
ATOM   1982  N   ILE C  46      12.684   2.377   6.689  1.00 24.91           N  
ANISOU 1982  N   ILE C  46     2469   4558   2436    686    183    115       N  
ATOM   1983  CA  ILE C  46      13.490   2.890   7.787  1.00 25.95           C  
ANISOU 1983  CA  ILE C  46     2609   4624   2627    741    179    122       C  
ATOM   1984  C   ILE C  46      14.839   2.162   7.841  1.00 29.60           C  
ANISOU 1984  C   ILE C  46     3124   5001   3120    753    191     95       C  
ATOM   1985  O   ILE C  46      14.893   0.937   7.720  1.00 29.70           O  
ANISOU 1985  O   ILE C  46     3185   4991   3109    711    200     65       O  
ATOM   1986  CB  ILE C  46      12.776   2.705   9.132  1.00 23.97           C  
ANISOU 1986  CB  ILE C  46     2362   4368   2377    731    168    122       C  
ATOM   1987  CG1 ILE C  46      11.346   3.256   9.075  1.00 29.40           C  
ANISOU 1987  CG1 ILE C  46     3000   5145   3028    713    158    146       C  
ATOM   1988  CG2 ILE C  46      13.602   3.350  10.269  1.00 23.00           C  
ANISOU 1988  CG2 ILE C  46     2243   4179   2315    789    162    131       C  
ATOM   1989  CD1 ILE C  46      11.271   4.709   8.685  1.00 29.87           C  
ANISOU 1989  CD1 ILE C  46     3002   5243   3102    763    155    185       C  
ATOM   1990  N   PHE C  47      15.915   2.917   8.032  1.00 26.20           N  
ANISOU 1990  N   PHE C  47     2687   4526   2742    810    191    107       N  
ATOM   1991  CA  PHE C  47      17.241   2.347   8.256  1.00 21.67           C  
ANISOU 1991  CA  PHE C  47     2157   3873   2203    831    201     86       C  
ATOM   1992  C   PHE C  47      17.607   2.613   9.708  1.00 24.85           C  
ANISOU 1992  C   PHE C  47     2568   4226   2650    865    190     91       C  
ATOM   1993  O   PHE C  47      17.621   3.766  10.101  1.00 24.00           O  
ANISOU 1993  O   PHE C  47     2423   4128   2569    903    182    116       O  
ATOM   1994  CB  PHE C  47      18.258   2.993   7.296  1.00 25.28           C  
ANISOU 1994  CB  PHE C  47     2600   4320   2685    867    210     95       C  
ATOM   1995  CG  PHE C  47      19.685   2.566   7.523  1.00 27.80           C  
ANISOU 1995  CG  PHE C  47     2956   4563   3044    896    220     79       C  
ATOM   1996  CD1 PHE C  47      20.181   1.420   6.918  1.00 30.08           C  
ANISOU 1996  CD1 PHE C  47     3290   4822   3316    872    237     52       C  
ATOM   1997  CD2 PHE C  47      20.529   3.325   8.317  1.00 24.62           C  
ANISOU 1997  CD2 PHE C  47     2542   4120   2693    948    214     92       C  
ATOM   1998  CE1 PHE C  47      21.499   1.026   7.111  1.00 30.91           C  
ANISOU 1998  CE1 PHE C  47     3428   4861   3457    902    247     40       C  
ATOM   1999  CE2 PHE C  47      21.848   2.932   8.532  1.00 30.92           C  
ANISOU 1999  CE2 PHE C  47     3370   4853   3525    975    222     79       C  
ATOM   2000  CZ  PHE C  47      22.334   1.780   7.921  1.00 34.02           C  
ANISOU 2000  CZ  PHE C  47     3805   5218   3902    955    238     54       C  
ATOM   2001  N   PHE C  48      17.920   1.575  10.489  1.00 23.54           N  
ANISOU 2001  N   PHE C  48     2449   4007   2488    851    193     67       N  
ATOM   2002  CA  PHE C  48      18.256   1.799  11.908  1.00 26.28           C  
ANISOU 2002  CA  PHE C  48     2804   4308   2875    882    181     72       C  
ATOM   2003  C   PHE C  48      19.757   1.935  12.058  1.00 25.38           C  
ANISOU 2003  C   PHE C  48     2703   4131   2808    928    186     70       C  
ATOM   2004  O   PHE C  48      20.501   1.029  11.687  1.00 24.66           O  
ANISOU 2004  O   PHE C  48     2651   4003   2716    923    200     49       O  
ATOM   2005  CB  PHE C  48      17.747   0.660  12.808  1.00 21.59           C  
ANISOU 2005  CB  PHE C  48     2252   3690   2261    845    180     49       C  
ATOM   2006  CG  PHE C  48      16.240   0.618  12.949  1.00 22.07           C  
ANISOU 2006  CG  PHE C  48     2296   3812   2279    801    172     53       C  
ATOM   2007  CD1 PHE C  48      15.607   1.307  13.967  1.00 23.21           C  
ANISOU 2007  CD1 PHE C  48     2414   3971   2436    814    157     72       C  
ATOM   2008  CD2 PHE C  48      15.463  -0.096  12.040  1.00 23.39           C  
ANISOU 2008  CD2 PHE C  48     2471   4025   2392    746    180     40       C  
ATOM   2009  CE1 PHE C  48      14.223   1.277  14.098  1.00 28.71           C  
ANISOU 2009  CE1 PHE C  48     3090   4726   3092    776    150     77       C  
ATOM   2010  CE2 PHE C  48      14.073  -0.129  12.162  1.00 28.34           C  
ANISOU 2010  CE2 PHE C  48     3077   4714   2977    705    172     44       C  
ATOM   2011  CZ  PHE C  48      13.457   0.567  13.191  1.00 30.32           C  
ANISOU 2011  CZ  PHE C  48     3298   4978   3242    721    157     64       C  
ATOM   2012  N   PHE C  49      20.203   3.046  12.633  1.00 27.08           N  
ANISOU 2012  N   PHE C  49     2890   4336   3064    973    177     91       N  
ATOM   2013  CA  PHE C  49      21.634   3.211  12.865  1.00 27.29           C  
ANISOU 2013  CA  PHE C  49     2926   4307   3134   1015    181     90       C  
ATOM   2014  C   PHE C  49      22.112   2.217  13.913  1.00 26.09           C  
ANISOU 2014  C   PHE C  49     2819   4098   2996   1015    179     72       C  
ATOM   2015  O   PHE C  49      21.323   1.749  14.730  1.00 24.16           O  
ANISOU 2015  O   PHE C  49     2590   3852   2736    990    171     65       O  
ATOM   2016  CB  PHE C  49      21.938   4.635  13.297  1.00 22.73           C  
ANISOU 2016  CB  PHE C  49     2310   3735   2594   1057    172    117       C  
ATOM   2017  CG  PHE C  49      21.740   5.632  12.213  1.00 20.92           C  
ANISOU 2017  CG  PHE C  49     2041   3553   2357   1067    177    136       C  
ATOM   2018  CD1 PHE C  49      22.617   5.664  11.125  1.00 31.61           C  
ANISOU 2018  CD1 PHE C  49     3393   4901   3717   1079    190    132       C  
ATOM   2019  CD2 PHE C  49      20.699   6.534  12.257  1.00 24.96           C  
ANISOU 2019  CD2 PHE C  49     2516   4114   2854   1065    171    159       C  
ATOM   2020  CE1 PHE C  49      22.451   6.572  10.111  1.00 29.76           C  
ANISOU 2020  CE1 PHE C  49     3124   4709   3474   1089    196    149       C  
ATOM   2021  CE2 PHE C  49      20.529   7.469  11.240  1.00 24.85           C  
ANISOU 2021  CE2 PHE C  49     2467   4144   2832   1078    178    178       C  
ATOM   2022  CZ  PHE C  49      21.408   7.485  10.168  1.00 27.85           C  
ANISOU 2022  CZ  PHE C  49     2847   4517   3217   1089    189    173       C  
ATOM   2023  N   GLY C  50      23.397   1.873  13.869  1.00 23.80           N  
ANISOU 2023  N   GLY C  50     2550   3760   2733   1042    187     63       N  
ATOM   2024  CA  GLY C  50      23.947   0.928  14.824  1.00 26.10           C  
ANISOU 2024  CA  GLY C  50     2884   3995   3037   1048    187     48       C  
ATOM   2025  C   GLY C  50      23.779  -0.524  14.424  1.00 31.34           C  
ANISOU 2025  C   GLY C  50     3600   4642   3667   1013    203     22       C  
ATOM   2026  O   GLY C  50      24.743  -1.286  14.400  1.00 28.92           O  
ANISOU 2026  O   GLY C  50     3327   4289   3371   1030    215      9       O  
ATOM   2027  N   THR C  51      22.547  -0.921  14.124  1.00 22.13           N  
ANISOU 2027  N   THR C  51     2440   3513   2457    965    204     13       N  
ATOM   2028  CA  THR C  51      22.280  -2.319  13.785  1.00 27.06           C  
ANISOU 2028  CA  THR C  51     3117   4121   3042    925    221    -13       C  
ATOM   2029  C   THR C  51      22.203  -2.527  12.285  1.00 27.11           C  
ANISOU 2029  C   THR C  51     3125   4158   3018    901    238    -21       C  
ATOM   2030  O   THR C  51      22.386  -3.642  11.795  1.00 28.46           O  
ANISOU 2030  O   THR C  51     3344   4305   3164    877    259    -43       O  
ATOM   2031  CB  THR C  51      20.966  -2.805  14.399  1.00 27.76           C  
ANISOU 2031  CB  THR C  51     3221   4231   3095    877    214    -23       C  
ATOM   2032  OG1 THR C  51      19.893  -2.026  13.866  1.00 28.18           O  
ANISOU 2032  OG1 THR C  51     3228   4355   3125    853    205     -8       O  
ATOM   2033  CG2 THR C  51      21.004  -2.653  15.934  1.00 28.71           C  
ANISOU 2033  CG2 THR C  51     3345   4319   3244    898    197    -16       C  
ATOM   2034  N   HIS C  52      21.901  -1.441  11.585  1.00 23.83           N  
ANISOU 2034  N   HIS C  52     2656   3793   2603    907    231     -2       N  
ATOM   2035  CA  HIS C  52      21.691  -1.430  10.132  1.00 26.67           C  
ANISOU 2035  CA  HIS C  52     3007   4194   2934    884    244     -4       C  
ATOM   2036  C   HIS C  52      20.527  -2.312   9.713  1.00 26.48           C  
ANISOU 2036  C   HIS C  52     3007   4204   2851    818    251    -22       C  
ATOM   2037  O   HIS C  52      20.406  -2.677   8.547  1.00 26.40           O  
ANISOU 2037  O   HIS C  52     3006   4217   2808    789    266    -32       O  
ATOM   2038  CB  HIS C  52      22.975  -1.825   9.399  1.00 33.35           C  
ANISOU 2038  CB  HIS C  52     3877   4999   3796    908    264    -14       C  
ATOM   2039  CG  HIS C  52      24.062  -0.801   9.518  1.00 32.84           C  
ANISOU 2039  CG  HIS C  52     3778   4917   3783    967    258      5       C  
ATOM   2040  ND1 HIS C  52      25.124  -0.737   8.653  1.00 32.01           N  
ANISOU 2040  ND1 HIS C  52     3674   4795   3695    992    273      4       N  
ATOM   2041  CD2 HIS C  52      24.229   0.210  10.407  1.00 30.58           C  
ANISOU 2041  CD2 HIS C  52     3456   4630   3534   1002    239     26       C  
ATOM   2042  CE1 HIS C  52      25.915   0.269   9.002  1.00 31.28           C  
ANISOU 2042  CE1 HIS C  52     3547   4693   3646   1040    263     23       C  
ATOM   2043  NE2 HIS C  52      25.391   0.857  10.060  1.00 32.10           N  
ANISOU 2043  NE2 HIS C  52     3629   4805   3762   1046    243     36       N  
ATOM   2044  N   GLU C  53      19.640  -2.612  10.663  1.00 27.09           N  
ANISOU 2044  N   GLU C  53     3092   4288   2912    792    240    -26       N  
ATOM   2045  CA  GLU C  53      18.388  -3.291  10.352  1.00 28.19           C  
ANISOU 2045  CA  GLU C  53     3246   4472   2994    726    244    -40       C  
ATOM   2046  C   GLU C  53      17.452  -2.366   9.586  1.00 29.36           C  
ANISOU 2046  C   GLU C  53     3335   4703   3117    710    234    -19       C  
ATOM   2047  O   GLU C  53      17.654  -1.156   9.553  1.00 30.43           O  
ANISOU 2047  O   GLU C  53     3421   4858   3284    753    222      7       O  
ATOM   2048  CB  GLU C  53      17.715  -3.776  11.638  1.00 33.26           C  
ANISOU 2048  CB  GLU C  53     3910   5100   3628    706    234    -48       C  
ATOM   2049  CG  GLU C  53      18.514  -4.831  12.393  1.00 43.50           C  
ANISOU 2049  CG  GLU C  53     5271   6316   4940    716    246    -69       C  
ATOM   2050  CD  GLU C  53      18.408  -6.222  11.772  1.00 64.87           C  
ANISOU 2050  CD  GLU C  53     8042   9006   7601    666    272   -100       C  
ATOM   2051  OE1 GLU C  53      17.704  -6.382  10.750  1.00 72.51           O  
ANISOU 2051  OE1 GLU C  53     9003  10025   8522    618    280   -106       O  
ATOM   2052  OE2 GLU C  53      19.029  -7.162  12.316  1.00 72.23           O  
ANISOU 2052  OE2 GLU C  53     9031   9872   8539    673    286   -118       O  
ATOM   2053  N   THR C  54      16.427  -2.939   8.960  1.00 27.30           N  
ANISOU 2053  N   THR C  54     3082   4493   2800    649    239    -31       N  
ATOM   2054  CA  THR C  54      15.456  -2.149   8.234  1.00 31.07           C  
ANISOU 2054  CA  THR C  54     3503   5056   3248    630    229    -10       C  
ATOM   2055  C   THR C  54      14.027  -2.583   8.562  1.00 34.83           C  
ANISOU 2055  C   THR C  54     3974   5585   3673    571    222    -16       C  
ATOM   2056  O   THR C  54      13.787  -3.707   9.030  1.00 40.01           O  
ANISOU 2056  O   THR C  54     4682   6214   4305    530    230    -42       O  
ATOM   2057  CB  THR C  54      15.667  -2.267   6.719  1.00 35.73           C  
ANISOU 2057  CB  THR C  54     4092   5674   3812    611    244    -15       C  
ATOM   2058  OG1 THR C  54      15.671  -3.655   6.367  1.00 37.15           O  
ANISOU 2058  OG1 THR C  54     4334   5828   3952    558    264    -48       O  
ATOM   2059  CG2 THR C  54      16.984  -1.626   6.306  1.00 37.78           C  
ANISOU 2059  CG2 THR C  54     4342   5893   4120    671    250     -5       C  
ATOM   2060  N   ALA C  55      13.089  -1.677   8.314  1.00 26.84           N  
ANISOU 2060  N   ALA C  55     2903   4652   2645    568    207     10       N  
ATOM   2061  CA  ALA C  55      11.667  -1.944   8.527  1.00 29.48           C  
ANISOU 2061  CA  ALA C  55     3221   5051   2928    514    199     10       C  
ATOM   2062  C   ALA C  55      10.862  -0.864   7.838  1.00 30.87           C  
ANISOU 2062  C   ALA C  55     3325   5317   3085    520    188     43       C  
ATOM   2063  O   ALA C  55      11.403   0.162   7.417  1.00 32.15           O  
ANISOU 2063  O   ALA C  55     3453   5484   3280    572    186     67       O  
ATOM   2064  CB  ALA C  55      11.336  -1.992   9.994  1.00 36.40           C  
ANISOU 2064  CB  ALA C  55     4105   5901   3824    522    188     10       C  
ATOM   2065  N   PHE C  56       9.566  -1.106   7.696  1.00 32.08           N  
ANISOU 2065  N   PHE C  56     3458   5547   3184    465    182     44       N  
ATOM   2066  CA  PHE C  56       8.679  -0.084   7.185  1.00 28.43           C  
ANISOU 2066  CA  PHE C  56     2925   5176   2701    473    171     79       C  
ATOM   2067  C   PHE C  56       7.811   0.414   8.324  1.00 34.88           C  
ANISOU 2067  C   PHE C  56     3709   6019   3524    485    156     98       C  
ATOM   2068  O   PHE C  56       7.156  -0.373   9.001  1.00 38.12           O  
ANISOU 2068  O   PHE C  56     4142   6432   3908    440    154     80       O  
ATOM   2069  CB  PHE C  56       7.818  -0.619   6.037  1.00 29.23           C  
ANISOU 2069  CB  PHE C  56     3016   5359   2732    404    175     72       C  
ATOM   2070  CG  PHE C  56       8.538  -0.667   4.722  1.00 24.86           C  
ANISOU 2070  CG  PHE C  56     2471   4801   2172    404    188     66       C  
ATOM   2071  CD1 PHE C  56       9.433  -1.685   4.444  1.00 35.48           C  
ANISOU 2071  CD1 PHE C  56     3884   6076   3521    383    206     32       C  
ATOM   2072  CD2 PHE C  56       8.329   0.310   3.774  1.00 32.04           C  
ANISOU 2072  CD2 PHE C  56     3324   5775   3074    426    183     97       C  
ATOM   2073  CE1 PHE C  56      10.113  -1.729   3.226  1.00 40.30           C  
ANISOU 2073  CE1 PHE C  56     4504   6681   4127    384    219     26       C  
ATOM   2074  CE2 PHE C  56       8.999   0.264   2.529  1.00 27.38           C  
ANISOU 2074  CE2 PHE C  56     2745   5182   2478    425    195     91       C  
ATOM   2075  CZ  PHE C  56       9.886  -0.753   2.269  1.00 36.32           C  
ANISOU 2075  CZ  PHE C  56     3942   6243   3613    403    213     56       C  
ATOM   2076  N   LEU C  57       7.829   1.722   8.538  1.00 26.84           N  
ANISOU 2076  N   LEU C  57     2641   5017   2540    546    147    135       N  
ATOM   2077  CA  LEU C  57       7.074   2.326   9.611  1.00 30.60           C  
ANISOU 2077  CA  LEU C  57     3086   5515   3026    566    135    156       C  
ATOM   2078  C   LEU C  57       6.308   3.534   9.105  1.00 34.30           C  
ANISOU 2078  C   LEU C  57     3484   6069   3481    594    129    199       C  
ATOM   2079  O   LEU C  57       6.720   4.187   8.140  1.00 32.66           O  
ANISOU 2079  O   LEU C  57     3252   5878   3278    622    134    216       O  
ATOM   2080  CB  LEU C  57       7.998   2.737  10.759  1.00 30.20           C  
ANISOU 2080  CB  LEU C  57     3058   5376   3041    623    134    158       C  
ATOM   2081  CG  LEU C  57       8.700   1.605  11.498  1.00 31.96           C  
ANISOU 2081  CG  LEU C  57     3349   5513   3281    604    138    120       C  
ATOM   2082  CD1 LEU C  57       9.589   2.178  12.604  1.00 28.87           C  
ANISOU 2082  CD1 LEU C  57     2970   5046   2954    665    134    127       C  
ATOM   2083  CD2 LEU C  57       7.679   0.647  12.096  1.00 38.83           C  
ANISOU 2083  CD2 LEU C  57     4239   6406   4109    542    135    100       C  
ATOM   2084  N   GLY C  58       5.192   3.826   9.762  1.00 31.74           N  
ANISOU 2084  N   GLY C  58     3125   5798   3138    587    121    218       N  
ATOM   2085  CA  GLY C  58       4.433   5.028   9.477  1.00 32.27           C  
ANISOU 2085  CA  GLY C  58     3124   5942   3194    623    116    263       C  
ATOM   2086  C   GLY C  58       4.757   6.152  10.447  1.00 31.89           C  
ANISOU 2086  C   GLY C  58     3062   5852   3201    695    116    289       C  
ATOM   2087  O   GLY C  58       5.415   5.938  11.470  1.00 29.71           O  
ANISOU 2087  O   GLY C  58     2827   5495   2967    710    116    272       O  
ATOM   2088  N   PRO C  59       4.283   7.364  10.138  1.00 34.44           N  
ANISOU 2088  N   PRO C  59     3330   6232   3523    740    117    332       N  
ATOM   2089  CA  PRO C  59       4.652   8.573  10.877  1.00 33.37           C  
ANISOU 2089  CA  PRO C  59     3183   6058   3438    812    121    361       C  
ATOM   2090  C   PRO C  59       4.267   8.528  12.359  1.00 35.31           C  
ANISOU 2090  C   PRO C  59     3441   6273   3702    816    116    359       C  
ATOM   2091  O   PRO C  59       4.829   9.312  13.128  1.00 33.53           O  
ANISOU 2091  O   PRO C  59     3223   5991   3525    868    121    372       O  
ATOM   2092  CB  PRO C  59       3.887   9.673  10.144  1.00 32.72           C  
ANISOU 2092  CB  PRO C  59     3038   6063   3331    844    125    407       C  
ATOM   2093  CG  PRO C  59       3.760   9.151   8.736  1.00 36.79           C  
ANISOU 2093  CG  PRO C  59     3541   6635   3801    803    124    398       C  
ATOM   2094  CD  PRO C  59       3.511   7.677   8.920  1.00 39.75           C  
ANISOU 2094  CD  PRO C  59     3952   7005   4145    727    117    356       C  
ATOM   2095  N   LYS C  60       3.359   7.630  12.745  1.00 26.62           N  
ANISOU 2095  N   LYS C  60     2343   5208   2563    760    109    343       N  
ATOM   2096  CA  LYS C  60       2.966   7.505  14.149  1.00 33.62           C  
ANISOU 2096  CA  LYS C  60     3243   6065   3465    759    105    339       C  
ATOM   2097  C   LYS C  60       4.156   7.072  14.981  1.00 32.65           C  
ANISOU 2097  C   LYS C  60     3181   5831   3393    769    105    309       C  
ATOM   2098  O   LYS C  60       4.241   7.395  16.170  1.00 34.78           O  
ANISOU 2098  O   LYS C  60     3463   6055   3696    794    103    314       O  
ATOM   2099  CB  LYS C  60       1.819   6.506  14.332  1.00 37.83           C  
ANISOU 2099  CB  LYS C  60     3773   6657   3945    689     97    323       C  
ATOM   2100  CG  LYS C  60       2.138   5.063  13.932  1.00 46.84           C  
ANISOU 2100  CG  LYS C  60     4962   7775   5061    621     96    276       C  
ATOM   2101  CD  LYS C  60       0.960   4.119  14.198  1.00 54.65           C  
ANISOU 2101  CD  LYS C  60     5949   8820   5994    549     90    260       C  
ATOM   2102  CE  LYS C  60       0.728   3.945  15.694  1.00 63.04           C  
ANISOU 2102  CE  LYS C  60     7034   9838   7079    551     87    252       C  
ATOM   2103  NZ  LYS C  60      -0.424   3.041  16.031  1.00 67.63           N  
ANISOU 2103  NZ  LYS C  60     7616  10472   7608    481     82    235       N  
ATOM   2104  N   ASP C  61       5.087   6.355  14.346  1.00 30.49           N  
ANISOU 2104  N   ASP C  61     2944   5515   3124    750    107    280       N  
ATOM   2105  CA  ASP C  61       6.207   5.767  15.065  1.00 31.11           C  
ANISOU 2105  CA  ASP C  61     3082   5493   3244    754    107    249       C  
ATOM   2106  C   ASP C  61       7.530   6.467  14.780  1.00 29.91           C  
ANISOU 2106  C   ASP C  61     2939   5284   3142    809    113    256       C  
ATOM   2107  O   ASP C  61       8.585   5.964  15.157  1.00 26.87           O  
ANISOU 2107  O   ASP C  61     2599   4820   2789    813    114    231       O  
ATOM   2108  CB  ASP C  61       6.311   4.282  14.729  1.00 36.89           C  
ANISOU 2108  CB  ASP C  61     3859   6211   3946    690    108    208       C  
ATOM   2109  CG  ASP C  61       5.142   3.486  15.286  1.00 48.85           C  
ANISOU 2109  CG  ASP C  61     5378   7766   5418    633    102    195       C  
ATOM   2110  OD1 ASP C  61       4.769   3.740  16.458  1.00 46.76           O  
ANISOU 2110  OD1 ASP C  61     5111   7485   5170    646     97    202       O  
ATOM   2111  OD2 ASP C  61       4.596   2.625  14.560  1.00 57.08           O  
ANISOU 2111  OD2 ASP C  61     6424   8854   6408    573    104    177       O  
ATOM   2112  N   LEU C  62       7.467   7.629  14.135  1.00 26.29           N  
ANISOU 2112  N   LEU C  62     2437   4864   2688    850    118    290       N  
ATOM   2113  CA  LEU C  62       8.676   8.356  13.732  1.00 26.93           C  
ANISOU 2113  CA  LEU C  62     2523   4898   2810    899    126    297       C  
ATOM   2114  C   LEU C  62       8.747   9.723  14.403  1.00 29.53           C  
ANISOU 2114  C   LEU C  62     2830   5214   3175    959    130    331       C  
ATOM   2115  O   LEU C  62       7.734  10.437  14.524  1.00 30.13           O  
ANISOU 2115  O   LEU C  62     2867   5349   3233    972    131    362       O  
ATOM   2116  CB  LEU C  62       8.732   8.520  12.208  1.00 29.37           C  
ANISOU 2116  CB  LEU C  62     2809   5257   3094    895    132    305       C  
ATOM   2117  CG  LEU C  62       8.594   7.226  11.406  1.00 24.40           C  
ANISOU 2117  CG  LEU C  62     2200   4649   2423    833    130    273       C  
ATOM   2118  CD1 LEU C  62       8.375   7.553   9.909  1.00 26.00           C  
ANISOU 2118  CD1 LEU C  62     2369   4918   2592    828    136    288       C  
ATOM   2119  CD2 LEU C  62       9.846   6.357  11.615  1.00 25.54           C  
ANISOU 2119  CD2 LEU C  62     2402   4704   2596    825    133    237       C  
ATOM   2120  N   PHE C  63       9.953  10.080  14.818  1.00 26.01           N  
ANISOU 2120  N   PHE C  63     2411   4694   2779    994    133    325       N  
ATOM   2121  CA  PHE C  63      10.205  11.285  15.600  1.00 26.46           C  
ANISOU 2121  CA  PHE C  63     2459   4721   2873   1046    139    351       C  
ATOM   2122  C   PHE C  63      11.389  12.065  15.039  1.00 33.55           C  
ANISOU 2122  C   PHE C  63     3360   5583   3804   1087    149    359       C  
ATOM   2123  O   PHE C  63      12.510  11.544  15.009  1.00 31.38           O  
ANISOU 2123  O   PHE C  63     3117   5251   3554   1083    147    333       O  
ATOM   2124  CB  PHE C  63      10.471  10.915  17.070  1.00 28.35           C  
ANISOU 2124  CB  PHE C  63     2734   4897   3142   1042    132    335       C  
ATOM   2125  CG  PHE C  63       9.301  10.241  17.751  1.00 30.28           C  
ANISOU 2125  CG  PHE C  63     2976   5172   3356   1004    123    329       C  
ATOM   2126  CD1 PHE C  63       9.048   8.884  17.552  1.00 30.80           C  
ANISOU 2126  CD1 PHE C  63     3065   5246   3392    949    115    297       C  
ATOM   2127  CD2 PHE C  63       8.464  10.955  18.600  1.00 26.04           C  
ANISOU 2127  CD2 PHE C  63     2420   4655   2820   1022    125    354       C  
ATOM   2128  CE1 PHE C  63       7.984   8.254  18.179  1.00 28.36           C  
ANISOU 2128  CE1 PHE C  63     2756   4966   3054    911    109    290       C  
ATOM   2129  CE2 PHE C  63       7.398  10.332  19.230  1.00 33.82           C  
ANISOU 2129  CE2 PHE C  63     3403   5669   3777    986    118    348       C  
ATOM   2130  CZ  PHE C  63       7.148   8.989  19.017  1.00 29.65           C  
ANISOU 2130  CZ  PHE C  63     2895   5151   3219    930    109    316       C  
ATOM   2131  N   PRO C  64      11.157  13.316  14.593  1.00 27.58           N  
ANISOU 2131  N   PRO C  64     2579   4852   3048   1119    160    392       N  
ATOM   2132  CA  PRO C  64      12.267  14.120  14.051  1.00 33.57           C  
ANISOU 2132  CA  PRO C  64     3365   5554   3835   1132    168    393       C  
ATOM   2133  C   PRO C  64      13.453  14.189  15.002  1.00 31.29           C  
ANISOU 2133  C   PRO C  64     3118   5176   3596   1140    166    376       C  
ATOM   2134  O   PRO C  64      13.282  14.552  16.166  1.00 33.28           O  
ANISOU 2134  O   PRO C  64     3387   5393   3864   1142    165    381       O  
ATOM   2135  CB  PRO C  64      11.633  15.498  13.865  1.00 37.39           C  
ANISOU 2135  CB  PRO C  64     3850   6047   4310   1138    179    427       C  
ATOM   2136  CG  PRO C  64      10.214  15.180  13.568  1.00 30.95           C  
ANISOU 2136  CG  PRO C  64     2994   5319   3447   1126    175    442       C  
ATOM   2137  CD  PRO C  64       9.874  14.025  14.479  1.00 29.18           C  
ANISOU 2137  CD  PRO C  64     2759   5109   3219   1114    163    423       C  
ATOM   2138  N   TYR C  65      14.643  13.838  14.505  1.00 25.65           N  
ANISOU 2138  N   TYR C  65     2418   4427   2901   1146    167    357       N  
ATOM   2139  CA  TYR C  65      15.799  13.605  15.358  1.00 29.69           C  
ANISOU 2139  CA  TYR C  65     2962   4864   3454   1151    163    337       C  
ATOM   2140  C   TYR C  65      16.197  14.808  16.206  1.00 31.85           C  
ANISOU 2140  C   TYR C  65     3265   5077   3759   1154    167    349       C  
ATOM   2141  O   TYR C  65      16.380  14.693  17.418  1.00 34.16           O  
ANISOU 2141  O   TYR C  65     3577   5330   4074   1153    161    342       O  
ATOM   2142  CB  TYR C  65      16.997  13.167  14.500  1.00 29.45           C  
ANISOU 2142  CB  TYR C  65     2940   4812   3436   1157    166    318       C  
ATOM   2143  CG  TYR C  65      18.308  13.142  15.246  1.00 36.20           C  
ANISOU 2143  CG  TYR C  65     3829   5590   4335   1162    162    302       C  
ATOM   2144  CD1 TYR C  65      18.537  12.216  16.252  1.00 32.20           C  
ANISOU 2144  CD1 TYR C  65     3336   5058   3841   1165    153    284       C  
ATOM   2145  CD2 TYR C  65      19.317  14.049  14.952  1.00 39.37           C  
ANISOU 2145  CD2 TYR C  65     4249   5947   4762   1164    169    305       C  
ATOM   2146  CE1 TYR C  65      19.724  12.187  16.938  1.00 29.22           C  
ANISOU 2146  CE1 TYR C  65     2988   4614   3501   1169    149    271       C  
ATOM   2147  CE2 TYR C  65      20.515  14.031  15.647  1.00 42.39           C  
ANISOU 2147  CE2 TYR C  65     4658   6266   5182   1166    165    291       C  
ATOM   2148  CZ  TYR C  65      20.713  13.091  16.634  1.00 40.84           C  
ANISOU 2148  CZ  TYR C  65     4473   6047   4997   1168    154    274       C  
ATOM   2149  OH  TYR C  65      21.904  13.046  17.328  1.00 36.85           O  
ANISOU 2149  OH  TYR C  65     3992   5483   4526   1169    150    262       O  
ATOM   2150  N   LYS C  66      16.328  15.959  15.565  1.00 33.35           N  
ANISOU 2150  N   LYS C  66     3459   5262   3949   1157    179    366       N  
ATOM   2151  CA  LYS C  66      16.800  17.158  16.248  1.00 42.11           C  
ANISOU 2151  CA  LYS C  66     4595   6318   5087   1160    186    376       C  
ATOM   2152  C   LYS C  66      15.798  17.568  17.328  1.00 40.26           C  
ANISOU 2152  C   LYS C  66     4362   6088   4846   1159    187    392       C  
ATOM   2153  O   LYS C  66      16.175  17.854  18.466  1.00 37.92           O  
ANISOU 2153  O   LYS C  66     4089   5743   4575   1159    186    388       O  
ATOM   2154  CB  LYS C  66      17.019  18.278  15.229  1.00 43.50           C  
ANISOU 2154  CB  LYS C  66     4773   6498   5258   1166    201    393       C  
ATOM   2155  CG  LYS C  66      17.265  19.662  15.805  1.00 53.61           C  
ANISOU 2155  CG  LYS C  66     6077   7738   6556   1172    214    408       C  
ATOM   2156  CD  LYS C  66      18.425  19.704  16.785  1.00 60.97           C  
ANISOU 2156  CD  LYS C  66     7035   8604   7527   1168    210    391       C  
ATOM   2157  CE  LYS C  66      18.793  21.150  17.114  1.00 58.32           C  
ANISOU 2157  CE  LYS C  66     6721   8233   7205   1173    226    405       C  
ATOM   2158  NZ  LYS C  66      17.579  21.976  17.380  1.00 59.60           N  
ANISOU 2158  NZ  LYS C  66     6880   8419   7344   1181    238    433       N  
ATOM   2159  N   GLU C  67      14.520  17.553  16.961  1.00 35.61           N  
ANISOU 2159  N   GLU C  67     3748   5560   4221   1159    190    410       N  
ATOM   2160  CA  GLU C  67      13.418  17.919  17.860  1.00 40.24           C  
ANISOU 2160  CA  GLU C  67     4331   6161   4796   1159    192    428       C  
ATOM   2161  C   GLU C  67      13.322  17.002  19.077  1.00 41.90           C  
ANISOU 2161  C   GLU C  67     4547   6355   5018   1153    179    411       C  
ATOM   2162  O   GLU C  67      12.993  17.449  20.173  1.00 36.48           O  
ANISOU 2162  O   GLU C  67     3874   5645   4343   1154    182    419       O  
ATOM   2163  CB  GLU C  67      12.089  17.908  17.087  1.00 41.24           C  
ANISOU 2163  CB  GLU C  67     4423   6368   4878   1159    195    449       C  
ATOM   2164  CG  GLU C  67      10.866  18.361  17.892  1.00 49.56           C  
ANISOU 2164  CG  GLU C  67     5470   7444   5915   1161    200    471       C  
ATOM   2165  CD  GLU C  67       9.565  18.379  17.072  1.00 52.80           C  
ANISOU 2165  CD  GLU C  67     5844   7939   6279   1159    203    495       C  
ATOM   2166  OE1 GLU C  67       9.574  17.941  15.899  1.00 48.68           O  
ANISOU 2166  OE1 GLU C  67     5300   7463   5735   1154    199    492       O  
ATOM   2167  OE2 GLU C  67       8.525  18.822  17.610  1.00 51.57           O  
ANISOU 2167  OE2 GLU C  67     5681   7807   6107   1163    209    516       O  
ATOM   2168  N   TYR C  68      13.628  15.722  18.900  1.00 39.25           N  
ANISOU 2168  N   TYR C  68     4201   6032   4680   1148    166    387       N  
ATOM   2169  CA  TYR C  68      13.414  14.750  19.971  1.00 34.88           C  
ANISOU 2169  CA  TYR C  68     3649   5472   4131   1144    154    372       C  
ATOM   2170  C   TYR C  68      14.705  14.174  20.550  1.00 37.39           C  
ANISOU 2170  C   TYR C  68     3996   5727   4485   1147    145    346       C  
ATOM   2171  O   TYR C  68      14.666  13.275  21.395  1.00 35.70           O  
ANISOU 2171  O   TYR C  68     3787   5504   4275   1146    134    331       O  
ATOM   2172  CB  TYR C  68      12.501  13.618  19.468  1.00 29.51           C  
ANISOU 2172  CB  TYR C  68     2932   4867   3412   1137    146    366       C  
ATOM   2173  CG  TYR C  68      11.055  14.053  19.422  1.00 32.93           C  
ANISOU 2173  CG  TYR C  68     3339   5363   3812   1131    151    391       C  
ATOM   2174  CD1 TYR C  68      10.276  14.041  20.574  1.00 35.42           C  
ANISOU 2174  CD1 TYR C  68     3654   5679   4125   1128    148    398       C  
ATOM   2175  CD2 TYR C  68      10.479  14.509  18.243  1.00 37.06           C  
ANISOU 2175  CD2 TYR C  68     3836   5942   4304   1129    158    410       C  
ATOM   2176  CE1 TYR C  68       8.966  14.459  20.553  1.00 34.83           C  
ANISOU 2176  CE1 TYR C  68     3554   5661   4019   1123    153    422       C  
ATOM   2177  CE2 TYR C  68       9.159  14.923  18.212  1.00 40.10           C  
ANISOU 2177  CE2 TYR C  68     4196   6385   4656   1124    162    436       C  
ATOM   2178  CZ  TYR C  68       8.411  14.893  19.371  1.00 38.65           C  
ANISOU 2178  CZ  TYR C  68     4013   6202   4472   1122    160    441       C  
ATOM   2179  OH  TYR C  68       7.105  15.311  19.340  1.00 39.82           O  
ANISOU 2179  OH  TYR C  68     4135   6407   4586   1118    166    468       O  
ATOM   2180  N   LYS C  69      15.843  14.715  20.120  1.00 37.60           N  
ANISOU 2180  N   LYS C  69     4040   5712   4535   1150    150    342       N  
ATOM   2181  CA  LYS C  69      17.150  14.212  20.543  1.00 41.09           C  
ANISOU 2181  CA  LYS C  69     4505   6097   5009   1152    143    320       C  
ATOM   2182  C   LYS C  69      17.322  14.177  22.055  1.00 41.45           C  
ANISOU 2182  C   LYS C  69     4574   6098   5078   1151    135    315       C  
ATOM   2183  O   LYS C  69      17.869  13.226  22.614  1.00 42.54           O  
ANISOU 2183  O   LYS C  69     4724   6211   5229   1154    124    295       O  
ATOM   2184  CB  LYS C  69      18.263  15.064  19.930  1.00 46.06           C  
ANISOU 2184  CB  LYS C  69     5148   6692   5659   1154    151    321       C  
ATOM   2185  CG  LYS C  69      19.664  14.690  20.391  1.00 42.41           C  
ANISOU 2185  CG  LYS C  69     4709   6174   5231   1155    144    301       C  
ATOM   2186  CD  LYS C  69      20.715  15.513  19.652  1.00 45.05           C  
ANISOU 2186  CD  LYS C  69     5050   6485   5582   1155    152    302       C  
ATOM   2187  CE  LYS C  69      22.106  15.321  20.256  1.00 48.52           C  
ANISOU 2187  CE  LYS C  69     5510   6870   6056   1154    146    286       C  
ATOM   2188  NZ  LYS C  69      23.075  16.313  19.712  1.00 55.96           N  
ANISOU 2188  NZ  LYS C  69     6458   7791   7014   1152    155    289       N  
ATOM   2189  N   ASP C  70      16.855  15.205  22.738  1.00 38.49           N  
ANISOU 2189  N   ASP C  70     4206   5710   4707   1149    142    333       N  
ATOM   2190  CA  ASP C  70      17.189  15.272  24.143  1.00 39.22           C  
ANISOU 2190  CA  ASP C  70     4322   5755   4824   1147    136    328       C  
ATOM   2191  C   ASP C  70      16.256  14.402  24.961  1.00 37.87           C  
ANISOU 2191  C   ASP C  70     4144   5604   4639   1147    126    324       C  
ATOM   2192  O   ASP C  70      16.624  13.947  26.040  1.00 46.51           O  
ANISOU 2192  O   ASP C  70     5257   6662   5752   1148    116    313       O  
ATOM   2193  CB  ASP C  70      17.224  16.723  24.603  1.00 57.01           C  
ANISOU 2193  CB  ASP C  70     6589   7981   7090   1147    149    347       C  
ATOM   2194  CG  ASP C  70      18.277  17.531  23.842  1.00 71.37           C  
ANISOU 2194  CG  ASP C  70     8416   9779   8924   1148    158    347       C  
ATOM   2195  OD1 ASP C  70      19.484  17.247  24.026  1.00 73.11           O  
ANISOU 2195  OD1 ASP C  70     8649   9961   9168   1145    151    331       O  
ATOM   2196  OD2 ASP C  70      17.910  18.431  23.056  1.00 74.19           O  
ANISOU 2196  OD2 ASP C  70     8765  10157   9266   1151    173    365       O  
ATOM   2197  N   LYS C  71      15.093  14.081  24.406  1.00 32.87           N  
ANISOU 2197  N   LYS C  71     3484   5033   3973   1147    128    333       N  
ATOM   2198  CA  LYS C  71      14.218  13.097  25.031  1.00 32.37           C  
ANISOU 2198  CA  LYS C  71     3408   4999   3891   1146    119    326       C  
ATOM   2199  C   LYS C  71      14.750  11.670  24.816  1.00 39.14           C  
ANISOU 2199  C   LYS C  71     4281   5846   4745   1130    106    295       C  
ATOM   2200  O   LYS C  71      14.796  10.865  25.747  1.00 38.57           O  
ANISOU 2200  O   LYS C  71     4237   5739   4678   1110     94    276       O  
ATOM   2201  CB  LYS C  71      12.802  13.229  24.475  1.00 38.97           C  
ANISOU 2201  CB  LYS C  71     4210   5908   4688   1141    125    344       C  
ATOM   2202  CG  LYS C  71      11.741  12.378  25.153  1.00 53.30           C  
ANISOU 2202  CG  LYS C  71     6024   7749   6480   1117    116    336       C  
ATOM   2203  CD  LYS C  71      10.395  13.120  25.142  1.00 59.48           C  
ANISOU 2203  CD  LYS C  71     6771   8591   7237   1126    126    367       C  
ATOM   2204  CE  LYS C  71       9.205  12.208  25.429  1.00 65.77           C  
ANISOU 2204  CE  LYS C  71     7564   9427   7999   1086    117    357       C  
ATOM   2205  NZ  LYS C  71       9.542  11.093  26.361  1.00 69.65           N  
ANISOU 2205  NZ  LYS C  71     8097   9866   8500   1054    102    324       N  
ATOM   2206  N   PHE C  72      15.158  11.365  23.588  1.00 30.25           N  
ANISOU 2206  N   PHE C  72     3146   4738   3609   1128    108    287       N  
ATOM   2207  CA  PHE C  72      15.444   9.977  23.211  1.00 29.65           C  
ANISOU 2207  CA  PHE C  72     3094   4653   3521   1097    100    256       C  
ATOM   2208  C   PHE C  72      16.921   9.639  22.995  1.00 32.49           C  
ANISOU 2208  C   PHE C  72     3474   4962   3907   1109     99    240       C  
ATOM   2209  O   PHE C  72      17.268   8.467  22.827  1.00 35.01           O  
ANISOU 2209  O   PHE C  72     3819   5263   4219   1088     94    214       O  
ATOM   2210  CB  PHE C  72      14.676   9.631  21.925  1.00 25.01           C  
ANISOU 2210  CB  PHE C  72     2483   4128   2892   1076    105    256       C  
ATOM   2211  CG  PHE C  72      13.178   9.683  22.075  1.00 30.79           C  
ANISOU 2211  CG  PHE C  72     3193   4915   3589   1055    105    269       C  
ATOM   2212  CD1 PHE C  72      12.558   9.182  23.209  1.00 35.20           C  
ANISOU 2212  CD1 PHE C  72     3770   5461   4143   1034     97    260       C  
ATOM   2213  CD2 PHE C  72      12.400  10.245  21.088  1.00 31.25           C  
ANISOU 2213  CD2 PHE C  72     3212   5041   3619   1059    113    290       C  
ATOM   2214  CE1 PHE C  72      11.178   9.244  23.344  1.00 31.69           C  
ANISOU 2214  CE1 PHE C  72     3302   5071   3666   1016     97    273       C  
ATOM   2215  CE2 PHE C  72      11.021  10.310  21.208  1.00 32.17           C  
ANISOU 2215  CE2 PHE C  72     3304   5216   3702   1042    113    304       C  
ATOM   2216  CZ  PHE C  72      10.410   9.806  22.339  1.00 38.62           C  
ANISOU 2216  CZ  PHE C  72     4139   6021   4515   1020    105    295       C  
ATOM   2217  N   GLY C  73      17.791  10.645  22.984  1.00 34.47           N  
ANISOU 2217  N   GLY C  73     3716   5194   4189   1144    104    254       N  
ATOM   2218  CA  GLY C  73      19.182  10.417  22.623  1.00 34.65           C  
ANISOU 2218  CA  GLY C  73     3751   5180   4235   1157    105    242       C  
ATOM   2219  C   GLY C  73      20.046  10.030  23.807  1.00 31.13           C  
ANISOU 2219  C   GLY C  73     3335   4676   3819   1161     94    229       C  
ATOM   2220  O   GLY C  73      21.226  10.351  23.846  1.00 43.17           O  
ANISOU 2220  O   GLY C  73     4865   6166   5371   1177     94    228       O  
ATOM   2221  N   LYS C  74      19.450   9.356  24.779  1.00 35.40           N  
ANISOU 2221  N   LYS C  74     3896   5202   4351   1140     84    219       N  
ATOM   2222  CA  LYS C  74      20.172   8.939  25.976  1.00 41.54           C  
ANISOU 2222  CA  LYS C  74     4704   5926   5153   1143     73    208       C  
ATOM   2223  C   LYS C  74      20.838   7.588  25.766  1.00 40.82           C  
ANISOU 2223  C   LYS C  74     4642   5809   5060   1132     69    182       C  
ATOM   2224  O   LYS C  74      20.337   6.774  24.998  1.00 37.48           O  
ANISOU 2224  O   LYS C  74     4225   5408   4608   1109     73    169       O  
ATOM   2225  CB  LYS C  74      19.224   8.866  27.172  1.00 38.95           C  
ANISOU 2225  CB  LYS C  74     4387   5593   4818   1126     66    210       C  
ATOM   2226  CG  LYS C  74      18.471  10.155  27.461  1.00 51.70           C  
ANISOU 2226  CG  LYS C  74     5977   7232   6433   1138     73    237       C  
ATOM   2227  CD  LYS C  74      18.423  10.421  28.963  1.00 60.86           C  
ANISOU 2227  CD  LYS C  74     7155   8357   7611   1139     66    241       C  
ATOM   2228  CE  LYS C  74      17.144  11.133  29.371  1.00 66.62           C  
ANISOU 2228  CE  LYS C  74     7869   9116   8326   1136     72    261       C  
ATOM   2229  NZ  LYS C  74      16.018  10.174  29.558  1.00 72.43           N  
ANISOU 2229  NZ  LYS C  74     8614   9874   9033   1104     67    249       N  
ATOM   2230  N   SER C  75      21.947   7.341  26.464  1.00 37.81           N  
ANISOU 2230  N   SER C  75     4280   5381   4706   1146     62    175       N  
ATOM   2231  CA  SER C  75      22.646   6.064  26.347  1.00 37.29           C  
ANISOU 2231  CA  SER C  75     4245   5286   4639   1142     60    153       C  
ATOM   2232  C   SER C  75      21.722   4.916  26.731  1.00 34.23           C  
ANISOU 2232  C   SER C  75     3888   4896   4223   1109     57    135       C  
ATOM   2233  O   SER C  75      20.895   5.062  27.623  1.00 36.27           O  
ANISOU 2233  O   SER C  75     4150   5155   4475   1095     50    139       O  
ATOM   2234  CB  SER C  75      23.899   6.041  27.231  1.00 40.19           C  
ANISOU 2234  CB  SER C  75     4625   5606   5038   1165     51    153       C  
ATOM   2235  OG  SER C  75      24.398   4.720  27.342  1.00 53.62           O  
ANISOU 2235  OG  SER C  75     6360   7277   6735   1161     50    133       O  
ATOM   2236  N   ASN C  76      21.846   3.790  26.037  1.00 30.64           N  
ANISOU 2236  N   ASN C  76     3456   4437   3749   1095     64    116       N  
ATOM   2237  CA  ASN C  76      21.014   2.605  26.286  1.00 34.62           C  
ANISOU 2237  CA  ASN C  76     3996   4938   4222   1059     64     96       C  
ATOM   2238  C   ASN C  76      21.864   1.365  26.048  1.00 37.16           C  
ANISOU 2238  C   ASN C  76     4356   5221   4541   1061     71     75       C  
ATOM   2239  O   ASN C  76      22.680   1.345  25.123  1.00 35.69           O  
ANISOU 2239  O   ASN C  76     4164   5035   4362   1079     80     74       O  
ATOM   2240  CB  ASN C  76      19.783   2.604  25.368  1.00 31.09           C  
ANISOU 2240  CB  ASN C  76     3531   4545   3736   1027     72     95       C  
ATOM   2241  CG  ASN C  76      18.753   1.550  25.745  1.00 31.77           C  
ANISOU 2241  CG  ASN C  76     3649   4635   3787    985     72     76       C  
ATOM   2242  OD1 ASN C  76      19.002   0.354  25.629  1.00 35.77           O  
ANISOU 2242  OD1 ASN C  76     4196   5115   4279    969     78     54       O  
ATOM   2243  ND2 ASN C  76      17.572   1.997  26.154  1.00 28.92           N  
ANISOU 2243  ND2 ASN C  76     3269   4308   3411    965     67     86       N  
ATOM   2244  N   LYS C  77      21.685   0.329  26.862  1.00 26.18           N  
ANISOU 2244  N   LYS C  77     3009   3798   3140   1045     68     59       N  
ATOM   2245  CA  LYS C  77      22.531  -0.863  26.719  1.00 26.24           C  
ANISOU 2245  CA  LYS C  77     3060   3765   3146   1052     78     41       C  
ATOM   2246  C   LYS C  77      22.097  -1.825  25.610  1.00 26.29           C  
ANISOU 2246  C   LYS C  77     3090   3785   3113   1021     96     21       C  
ATOM   2247  O   LYS C  77      22.811  -2.791  25.314  1.00 29.31           O  
ANISOU 2247  O   LYS C  77     3510   4136   3492   1029    109      7       O  
ATOM   2248  CB  LYS C  77      22.589  -1.615  28.045  1.00 39.45           C  
ANISOU 2248  CB  LYS C  77     4775   5393   4823   1050     70     32       C  
ATOM   2249  CG  LYS C  77      23.640  -1.065  28.994  1.00 58.35           C  
ANISOU 2249  CG  LYS C  77     7157   7755   7256   1089     56     46       C  
ATOM   2250  CD  LYS C  77      24.963  -0.820  28.275  1.00 63.26           C  
ANISOU 2250  CD  LYS C  77     7762   8372   7902   1127     62     54       C  
ATOM   2251  CE  LYS C  77      25.817   0.190  29.022  1.00 65.59           C  
ANISOU 2251  CE  LYS C  77     8028   8659   8236   1159     47     74       C  
ATOM   2252  NZ  LYS C  77      26.803   0.837  28.120  1.00 66.66           N  
ANISOU 2252  NZ  LYS C  77     8130   8807   8390   1188     53     84       N  
ATOM   2253  N   ARG C  78      20.945  -1.581  24.990  1.00 28.31           N  
ANISOU 2253  N   ARG C  78     3326   4090   3339    987     99     21       N  
ATOM   2254  CA  ARG C  78      20.495  -2.463  23.897  1.00 29.07           C  
ANISOU 2254  CA  ARG C  78     3444   4205   3394    952    116      2       C  
ATOM   2255  C   ARG C  78      21.574  -2.555  22.829  1.00 29.33           C  
ANISOU 2255  C   ARG C  78     3477   4229   3438    977    129      1       C  
ATOM   2256  O   ARG C  78      22.244  -1.569  22.527  1.00 31.31           O  
ANISOU 2256  O   ARG C  78     3688   4489   3718   1012    125     19       O  
ATOM   2257  CB  ARG C  78      19.184  -1.983  23.269  1.00 36.16           C  
ANISOU 2257  CB  ARG C  78     4309   5169   4260    916    115      7       C  
ATOM   2258  CG  ARG C  78      17.970  -2.167  24.160  1.00 46.07           C  
ANISOU 2258  CG  ARG C  78     5572   6438   5494    881    107      3       C  
ATOM   2259  CD  ARG C  78      17.802  -3.615  24.584  1.00 41.82           C  
ANISOU 2259  CD  ARG C  78     5097   5862   4929    849    116    -25       C  
ATOM   2260  NE  ARG C  78      17.242  -4.460  23.529  1.00 43.97           N  
ANISOU 2260  NE  ARG C  78     5391   6161   5154    804    133    -44       N  
ATOM   2261  CZ  ARG C  78      15.937  -4.577  23.290  1.00 43.29           C  
ANISOU 2261  CZ  ARG C  78     5295   6126   5027    754    133    -49       C  
ATOM   2262  NH1 ARG C  78      15.053  -3.879  24.007  1.00 32.45           N  
ANISOU 2262  NH1 ARG C  78     3890   4784   3656    748    118    -35       N  
ATOM   2263  NH2 ARG C  78      15.512  -5.379  22.328  1.00 44.97           N  
ANISOU 2263  NH2 ARG C  78     5531   6361   5196    710    149    -68       N  
ATOM   2264  N   LYS C  79      21.764  -3.756  22.294  1.00 28.43           N  
ANISOU 2264  N   LYS C  79     3410   4094   3300    960    148    -21       N  
ATOM   2265  CA  LYS C  79      22.852  -3.991  21.359  1.00 30.59           C  
ANISOU 2265  CA  LYS C  79     3689   4350   3583    985    164    -23       C  
ATOM   2266  C   LYS C  79      22.702  -3.120  20.119  1.00 33.67           C  
ANISOU 2266  C   LYS C  79     4032   4792   3969    984    166    -12       C  
ATOM   2267  O   LYS C  79      21.671  -3.142  19.449  1.00 32.87           O  
ANISOU 2267  O   LYS C  79     3923   4735   3832    944    170    -17       O  
ATOM   2268  CB  LYS C  79      22.930  -5.465  20.953  1.00 38.64           C  
ANISOU 2268  CB  LYS C  79     4772   5339   4570    962    187    -49       C  
ATOM   2269  CG  LYS C  79      23.042  -6.440  22.114  1.00 52.62           C  
ANISOU 2269  CG  LYS C  79     6597   7057   6339    962    189    -62       C  
ATOM   2270  CD  LYS C  79      24.377  -6.338  22.837  1.00 62.87           C  
ANISOU 2270  CD  LYS C  79     7898   8310   7682   1019    183    -50       C  
ATOM   2271  CE  LYS C  79      24.941  -7.721  23.166  1.00 66.47           C  
ANISOU 2271  CE  LYS C  79     8422   8708   8127   1027    202    -67       C  
ATOM   2272  NZ  LYS C  79      24.378  -8.818  22.319  1.00 63.48           N  
ANISOU 2272  NZ  LYS C  79     8094   8327   7700    983    229    -91       N  
ATOM   2273  N   GLY C  80      23.749  -2.358  19.825  1.00 26.45           N  
ANISOU 2273  N   GLY C  80     3088   3872   3090   1027    164      3       N  
ATOM   2274  CA  GLY C  80      23.749  -1.494  18.666  1.00 30.42           C  
ANISOU 2274  CA  GLY C  80     3547   4417   3592   1032    168     15       C  
ATOM   2275  C   GLY C  80      23.298  -0.083  18.949  1.00 23.86           C  
ANISOU 2275  C   GLY C  80     2663   3623   2778   1043    151     39       C  
ATOM   2276  O   GLY C  80      23.539   0.797  18.130  1.00 24.52           O  
ANISOU 2276  O   GLY C  80     2709   3735   2871   1058    153     53       O  
ATOM   2277  N   PHE C  81      22.643   0.152  20.093  1.00 22.73           N  
ANISOU 2277  N   PHE C  81     2517   3480   2638   1035    136     45       N  
ATOM   2278  CA  PHE C  81      22.067   1.478  20.335  1.00 21.29           C  
ANISOU 2278  CA  PHE C  81     2287   3334   2466   1043    124     68       C  
ATOM   2279  C   PHE C  81      23.093   2.615  20.406  1.00 25.18           C  
ANISOU 2279  C   PHE C  81     2748   3817   3001   1088    119     88       C  
ATOM   2280  O   PHE C  81      22.955   3.651  19.732  1.00 21.91           O  
ANISOU 2280  O   PHE C  81     2295   3440   2590   1098    121    105       O  
ATOM   2281  CB  PHE C  81      21.239   1.486  21.625  1.00 23.22           C  
ANISOU 2281  CB  PHE C  81     2539   3574   2709   1029    110     70       C  
ATOM   2282  CG  PHE C  81      20.380   2.704  21.750  1.00 21.33           C  
ANISOU 2282  CG  PHE C  81     2255   3379   2469   1029    102     93       C  
ATOM   2283  CD1 PHE C  81      19.095   2.717  21.220  1.00 22.85           C  
ANISOU 2283  CD1 PHE C  81     2433   3626   2624    996    105     95       C  
ATOM   2284  CD2 PHE C  81      20.867   3.855  22.355  1.00 22.96           C  
ANISOU 2284  CD2 PHE C  81     2436   3576   2712   1064     95    114       C  
ATOM   2285  CE1 PHE C  81      18.296   3.852  21.317  1.00 23.28           C  
ANISOU 2285  CE1 PHE C  81     2446   3723   2678   1001    100    118       C  
ATOM   2286  CE2 PHE C  81      20.077   4.991  22.470  1.00 28.46           C  
ANISOU 2286  CE2 PHE C  81     3097   4310   3407   1068     91    136       C  
ATOM   2287  CZ  PHE C  81      18.788   4.991  21.944  1.00 32.21           C  
ANISOU 2287  CZ  PHE C  81     3555   4839   3845   1039     94    139       C  
ATOM   2288  N   ASN C  82      24.120   2.434  21.224  1.00 28.12           N  
ANISOU 2288  N   ASN C  82     3137   4143   3404   1115    114     86       N  
ATOM   2289  CA  ASN C  82      25.087   3.502  21.415  1.00 28.85           C  
ANISOU 2289  CA  ASN C  82     3200   4227   3535   1153    109    104       C  
ATOM   2290  C   ASN C  82      25.916   3.708  20.161  1.00 28.84           C  
ANISOU 2290  C   ASN C  82     3183   4235   3539   1170    122    105       C  
ATOM   2291  O   ASN C  82      26.380   4.820  19.887  1.00 28.98           O  
ANISOU 2291  O   ASN C  82     3168   4267   3578   1193    122    122       O  
ATOM   2292  CB  ASN C  82      25.969   3.207  22.627  1.00 27.43           C  
ANISOU 2292  CB  ASN C  82     3040   3999   3383   1174     99    103       C  
ATOM   2293  CG  ASN C  82      25.193   3.268  23.926  1.00 29.59           C  
ANISOU 2293  CG  ASN C  82     3324   4265   3656   1160     85    106       C  
ATOM   2294  OD1 ASN C  82      24.185   3.980  24.033  1.00 25.62           O  
ANISOU 2294  OD1 ASN C  82     2799   3792   3141   1145     82    116       O  
ATOM   2295  ND2 ASN C  82      25.668   2.540  24.934  1.00 32.78           N  
ANISOU 2295  ND2 ASN C  82     3758   4626   4069   1166     78     97       N  
ATOM   2296  N   GLU C  83      26.066   2.650  19.369  1.00 24.04           N  
ANISOU 2296  N   GLU C  83     2602   3621   2911   1158    136     87       N  
ATOM   2297  CA  GLU C  83      26.719   2.797  18.070  1.00 27.19           C  
ANISOU 2297  CA  GLU C  83     2988   4032   3311   1170    150     87       C  
ATOM   2298  C   GLU C  83      25.815   3.593  17.136  1.00 29.95           C  
ANISOU 2298  C   GLU C  83     3305   4435   3640   1153    153     97       C  
ATOM   2299  O   GLU C  83      26.274   4.383  16.324  1.00 24.53           O  
ANISOU 2299  O   GLU C  83     2590   3767   2964   1171    159    108       O  
ATOM   2300  CB  GLU C  83      27.036   1.442  17.451  1.00 24.12           C  
ANISOU 2300  CB  GLU C  83     2640   3622   2903   1159    166     65       C  
ATOM   2301  CG  GLU C  83      28.187   0.666  18.148  1.00 24.43           C  
ANISOU 2301  CG  GLU C  83     2710   3608   2965   1186    168     58       C  
ATOM   2302  CD  GLU C  83      27.776  -0.021  19.458  1.00 36.41           C  
ANISOU 2302  CD  GLU C  83     4259   5096   4477   1176    158     51       C  
ATOM   2303  OE1 GLU C  83      26.586   0.031  19.844  1.00 37.97           O  
ANISOU 2303  OE1 GLU C  83     4459   5313   4655   1144    150     49       O  
ATOM   2304  OE2 GLU C  83      28.653  -0.633  20.104  1.00 41.31           O  
ANISOU 2304  OE2 GLU C  83     4905   5675   5115   1200    158     47       O  
ATOM   2305  N   GLY C  84      24.519   3.369  17.250  1.00 23.41           N  
ANISOU 2305  N   GLY C  84     2480   3635   2780   1119    149     95       N  
ATOM   2306  CA  GLY C  84      23.551   4.140  16.470  1.00 22.70           C  
ANISOU 2306  CA  GLY C  84     2356   3602   2668   1105    151    108       C  
ATOM   2307  C   GLY C  84      23.589   5.622  16.807  1.00 27.04           C  
ANISOU 2307  C   GLY C  84     2866   4166   3243   1132    144    134       C  
ATOM   2308  O   GLY C  84      23.481   6.479  15.925  1.00 23.83           O  
ANISOU 2308  O   GLY C  84     2428   3794   2832   1141    150    148       O  
ATOM   2309  N   LEU C  85      23.722   5.935  18.092  1.00 23.83           N  
ANISOU 2309  N   LEU C  85     2462   3732   2859   1146    132    141       N  
ATOM   2310  CA  LEU C  85      23.845   7.322  18.500  1.00 26.93           C  
ANISOU 2310  CA  LEU C  85     2824   4132   3276   1171    128    164       C  
ATOM   2311  C   LEU C  85      25.071   7.955  17.842  1.00 24.68           C  
ANISOU 2311  C   LEU C  85     2523   3837   3016   1201    136    170       C  
ATOM   2312  O   LEU C  85      25.032   9.104  17.404  1.00 31.07           O  
ANISOU 2312  O   LEU C  85     3306   4668   3831   1211    141    188       O  
ATOM   2313  CB  LEU C  85      23.945   7.419  20.015  1.00 26.31           C  
ANISOU 2313  CB  LEU C  85     2757   4019   3218   1178    115    167       C  
ATOM   2314  CG  LEU C  85      22.679   7.081  20.825  1.00 24.16           C  
ANISOU 2314  CG  LEU C  85     2496   3759   2926   1151    107    166       C  
ATOM   2315  CD1 LEU C  85      22.971   7.352  22.320  1.00 29.03           C  
ANISOU 2315  CD1 LEU C  85     3123   4337   3569   1163     95    171       C  
ATOM   2316  CD2 LEU C  85      21.451   7.847  20.359  1.00 26.46           C  
ANISOU 2316  CD2 LEU C  85     2757   4104   3193   1141    111    183       C  
ATOM   2317  N   TRP C  86      26.152   7.190  17.776  1.00 28.22           N  
ANISOU 2317  N   TRP C  86     2992   4251   3479   1211    139    155       N  
ATOM   2318  CA  TRP C  86      27.387   7.657  17.160  1.00 30.34           C  
ANISOU 2318  CA  TRP C  86     3248   4510   3771   1237    147    159       C  
ATOM   2319  C   TRP C  86      27.156   7.950  15.683  1.00 32.06           C  
ANISOU 2319  C   TRP C  86     3447   4765   3970   1233    160    161       C  
ATOM   2320  O   TRP C  86      27.454   9.047  15.188  1.00 33.03           O  
ANISOU 2320  O   TRP C  86     3558   4890   4103   1223    163    173       O  
ATOM   2321  CB  TRP C  86      28.511   6.619  17.341  1.00 28.08           C  
ANISOU 2321  CB  TRP C  86     2988   4183   3499   1249    148    142       C  
ATOM   2322  CG  TRP C  86      29.858   7.104  16.814  1.00 29.54           C  
ANISOU 2322  CG  TRP C  86     3168   4346   3709   1252    153    144       C  
ATOM   2323  CD1 TRP C  86      30.854   7.700  17.538  1.00 34.59           C  
ANISOU 2323  CD1 TRP C  86     3811   4950   4379   1242    142    148       C  
ATOM   2324  CD2 TRP C  86      30.321   7.057  15.457  1.00 27.05           C  
ANISOU 2324  CD2 TRP C  86     2845   4045   3388   1258    168    139       C  
ATOM   2325  NE1 TRP C  86      31.915   8.024  16.714  1.00 34.48           N  
ANISOU 2325  NE1 TRP C  86     3792   4930   4380   1242    150    147       N  
ATOM   2326  CE2 TRP C  86      31.612   7.642  15.429  1.00 32.89           C  
ANISOU 2326  CE2 TRP C  86     3584   4755   4157   1251    166    142       C  
ATOM   2327  CE3 TRP C  86      29.780   6.590  14.256  1.00 28.67           C  
ANISOU 2327  CE3 TRP C  86     3044   4285   3564   1264    184    133       C  
ATOM   2328  CZ2 TRP C  86      32.354   7.760  14.261  1.00 38.25           C  
ANISOU 2328  CZ2 TRP C  86     4256   5438   4839   1255    179    139       C  
ATOM   2329  CZ3 TRP C  86      30.534   6.702  13.084  1.00 31.35           C  
ANISOU 2329  CZ3 TRP C  86     3376   4629   3907   1271    198    131       C  
ATOM   2330  CH2 TRP C  86      31.794   7.289  13.101  1.00 33.74           C  
ANISOU 2330  CH2 TRP C  86     3680   4899   4241   1265    195    134       C  
ATOM   2331  N   GLU C  87      26.603   6.972  14.977  1.00 20.57           N  
ANISOU 2331  N   GLU C  87     2009   3323   2483   1208    166    146       N  
ATOM   2332  CA  GLU C  87      26.381   7.093  13.528  1.00 22.83           C  
ANISOU 2332  CA  GLU C  87     2282   3645   2748   1199    179    146       C  
ATOM   2333  C   GLU C  87      25.459   8.223  13.101  1.00 31.94           C  
ANISOU 2333  C   GLU C  87     3401   4848   3887   1197    180    168       C  
ATOM   2334  O   GLU C  87      25.722   8.898  12.101  1.00 29.23           O  
ANISOU 2334  O   GLU C  87     3036   4526   3543   1209    189    177       O  
ATOM   2335  CB  GLU C  87      25.815   5.787  12.966  1.00 25.52           C  
ANISOU 2335  CB  GLU C  87     2651   3992   3052   1164    186    126       C  
ATOM   2336  CG  GLU C  87      26.861   4.720  12.761  1.00 29.62           C  
ANISOU 2336  CG  GLU C  87     3204   4470   3580   1170    196    105       C  
ATOM   2337  CD  GLU C  87      26.319   3.490  12.070  1.00 35.10           C  
ANISOU 2337  CD  GLU C  87     3931   5171   4236   1133    207     85       C  
ATOM   2338  OE1 GLU C  87      25.101   3.236  12.164  1.00 26.86           O  
ANISOU 2338  OE1 GLU C  87     2891   4156   3160   1099    202     82       O  
ATOM   2339  OE2 GLU C  87      27.118   2.778  11.425  1.00 33.94           O  
ANISOU 2339  OE2 GLU C  87     3808   5001   4089   1138    222     71       O  
ATOM   2340  N   ILE C  88      24.371   8.437  13.835  1.00 27.96           N  
ANISOU 2340  N   ILE C  88     2891   4362   3370   1184    170    177       N  
ATOM   2341  CA  ILE C  88      23.407   9.432  13.383  1.00 28.97           C  
ANISOU 2341  CA  ILE C  88     2986   4541   3480   1184    172    199       C  
ATOM   2342  C   ILE C  88      24.029  10.823  13.464  1.00 34.65           C  
ANISOU 2342  C   ILE C  88     3697   5241   4228   1198    174    217       C  
ATOM   2343  O   ILE C  88      23.680  11.714  12.697  1.00 36.77           O  
ANISOU 2343  O   ILE C  88     3951   5534   4485   1191    180    233       O  
ATOM   2344  CB  ILE C  88      22.077   9.349  14.183  1.00 27.32           C  
ANISOU 2344  CB  ILE C  88     2775   4355   3249   1163    162    206       C  
ATOM   2345  CG1 ILE C  88      21.000  10.198  13.506  1.00 23.54           C  
ANISOU 2345  CG1 ILE C  88     2262   3938   2744   1162    167    229       C  
ATOM   2346  CG2 ILE C  88      22.260   9.708  15.672  1.00 23.37           C  
ANISOU 2346  CG2 ILE C  88     2283   3819   2779   1178    152    212       C  
ATOM   2347  CD1 ILE C  88      19.583   9.811  13.965  1.00 24.70           C  
ANISOU 2347  CD1 ILE C  88     2406   4121   2859   1132    159    231       C  
ATOM   2348  N   GLU C  89      24.992  10.982  14.362  1.00 34.83           N  
ANISOU 2348  N   GLU C  89     3741   5207   4284   1197    167    212       N  
ATOM   2349  CA  GLU C  89      25.755  12.217  14.460  1.00 35.42           C  
ANISOU 2349  CA  GLU C  89     3824   5249   4386   1188    168    222       C  
ATOM   2350  C   GLU C  89      26.921  12.272  13.466  1.00 40.66           C  
ANISOU 2350  C   GLU C  89     4488   5898   5061   1192    177    214       C  
ATOM   2351  O   GLU C  89      27.124  13.285  12.801  1.00 50.24           O  
ANISOU 2351  O   GLU C  89     5697   7116   6278   1187    184    224       O  
ATOM   2352  CB  GLU C  89      26.283  12.388  15.887  1.00 32.00           C  
ANISOU 2352  CB  GLU C  89     3408   4768   3980   1184    157    220       C  
ATOM   2353  CG  GLU C  89      25.221  12.866  16.859  1.00 48.04           C  
ANISOU 2353  CG  GLU C  89     5440   6808   6006   1176    151    233       C  
ATOM   2354  CD  GLU C  89      24.844  14.319  16.628  1.00 58.16           C  
ANISOU 2354  CD  GLU C  89     6717   8098   7285   1167    159    253       C  
ATOM   2355  OE1 GLU C  89      25.704  15.070  16.116  1.00 61.98           O  
ANISOU 2355  OE1 GLU C  89     7203   8565   7783   1166    166    255       O  
ATOM   2356  OE2 GLU C  89      23.691  14.708  16.944  1.00 49.62           O  
ANISOU 2356  OE2 GLU C  89     5628   7041   6186   1164    160    267       O  
ATOM   2357  N   ASN C  90      27.670  11.174  13.366  1.00 33.65           N  
ANISOU 2357  N   ASN C  90     3610   4995   4181   1204    177    196       N  
ATOM   2358  CA  ASN C  90      28.974  11.169  12.710  1.00 34.78           C  
ANISOU 2358  CA  ASN C  90     3758   5115   4343   1208    184    188       C  
ATOM   2359  C   ASN C  90      28.990  10.552  11.310  1.00 44.46           C  
ANISOU 2359  C   ASN C  90     4975   6369   5548   1219    199    180       C  
ATOM   2360  O   ASN C  90      29.861  10.866  10.495  1.00 40.45           O  
ANISOU 2360  O   ASN C  90     4467   5853   5051   1220    207    178       O  
ATOM   2361  CB  ASN C  90      29.986  10.437  13.596  1.00 36.70           C  
ANISOU 2361  CB  ASN C  90     4020   5315   4611   1216    177    175       C  
ATOM   2362  CG  ASN C  90      30.204  11.135  14.924  1.00 39.37           C  
ANISOU 2362  CG  ASN C  90     4365   5623   4972   1204    164    182       C  
ATOM   2363  OD1 ASN C  90      30.952  12.104  15.009  1.00 50.87           O  
ANISOU 2363  OD1 ASN C  90     5819   7061   6448   1195    164    187       O  
ATOM   2364  ND2 ASN C  90      29.529  10.662  15.962  1.00 32.54           N  
ANISOU 2364  ND2 ASN C  90     3507   4755   4102   1205    154    181       N  
ATOM   2365  N   ASN C  91      28.041   9.668  11.029  1.00 34.80           N  
ANISOU 2365  N   ASN C  91     3745   5184   4295   1228    203    175       N  
ATOM   2366  CA  ASN C  91      27.988   9.052   9.705  1.00 29.19           C  
ANISOU 2366  CA  ASN C  91     3025   4507   3560   1238    219    166       C  
ATOM   2367  C   ASN C  91      26.562   8.738   9.242  1.00 25.83           C  
ANISOU 2367  C   ASN C  91     2595   4127   3091   1208    218    167       C  
ATOM   2368  O   ASN C  91      26.286   7.607   8.890  1.00 28.69           O  
ANISOU 2368  O   ASN C  91     2983   4489   3430   1181    222    148       O  
ATOM   2369  CB  ASN C  91      28.837   7.775   9.707  1.00 32.99           C  
ANISOU 2369  CB  ASN C  91     3537   4950   4047   1239    225    143       C  
ATOM   2370  CG  ASN C  91      29.213   7.310   8.311  1.00 39.98           C  
ANISOU 2370  CG  ASN C  91     4429   5843   4917   1232    242    132       C  
ATOM   2371  OD1 ASN C  91      29.145   8.077   7.355  1.00 42.25           O  
ANISOU 2371  OD1 ASN C  91     4693   6161   5198   1236    250    142       O  
ATOM   2372  ND2 ASN C  91      29.608   6.045   8.190  1.00 37.43           N  
ANISOU 2372  ND2 ASN C  91     4141   5492   4587   1223    250    111       N  
ATOM   2373  N   PRO C  92      25.662   9.759   9.212  1.00 31.31           N  
ANISOU 2373  N   PRO C  92     3261   4862   3775   1210    215    189       N  
ATOM   2374  CA  PRO C  92      24.225   9.592   8.933  1.00 31.38           C  
ANISOU 2374  CA  PRO C  92     3261   4920   3742   1181    211    195       C  
ATOM   2375  C   PRO C  92      23.940   9.036   7.542  1.00 33.05           C  
ANISOU 2375  C   PRO C  92     3473   5164   3919   1156    221    185       C  
ATOM   2376  O   PRO C  92      22.883   8.450   7.303  1.00 26.21           O  
ANISOU 2376  O   PRO C  92     2610   4333   3014   1121    218    181       O  
ATOM   2377  CB  PRO C  92      23.671  11.020   9.031  1.00 35.33           C  
ANISOU 2377  CB  PRO C  92     3726   5452   4244   1202    211    225       C  
ATOM   2378  CG  PRO C  92      24.718  11.818   9.682  1.00 36.20           C  
ANISOU 2378  CG  PRO C  92     3861   5497   4396   1200    206    227       C  
ATOM   2379  CD  PRO C  92      26.015  11.182   9.346  1.00 31.52           C  
ANISOU 2379  CD  PRO C  92     3282   4869   3823   1210    212    208       C  
ATOM   2380  N   GLY C  93      24.872   9.241   6.620  1.00 28.60           N  
ANISOU 2380  N   GLY C  93     2908   4591   3367   1171    234    182       N  
ATOM   2381  CA  GLY C  93      24.675   8.763   5.269  1.00 33.48           C  
ANISOU 2381  CA  GLY C  93     3529   5239   3954   1148    244    174       C  
ATOM   2382  C   GLY C  93      25.150   7.352   4.999  1.00 29.49           C  
ANISOU 2382  C   GLY C  93     3064   4703   3439   1124    252    144       C  
ATOM   2383  O   GLY C  93      25.195   6.930   3.844  1.00 29.04           O  
ANISOU 2383  O   GLY C  93     3014   4661   3359   1106    264    135       O  
ATOM   2384  N   VAL C  94      25.478   6.597   6.046  1.00 29.24           N  
ANISOU 2384  N   VAL C  94     3060   4626   3423   1124    247    130       N  
ATOM   2385  CA  VAL C  94      26.042   5.264   5.838  1.00 28.55           C  
ANISOU 2385  CA  VAL C  94     3016   4502   3330   1108    258    103       C  
ATOM   2386  C   VAL C  94      25.023   4.373   5.116  1.00 36.44           C  
ANISOU 2386  C   VAL C  94     4034   5536   4278   1057    263     90       C  
ATOM   2387  O   VAL C  94      23.870   4.273   5.530  1.00 34.03           O  
ANISOU 2387  O   VAL C  94     3722   5261   3945   1030    253     93       O  
ATOM   2388  CB  VAL C  94      26.507   4.612   7.180  1.00 23.47           C  
ANISOU 2388  CB  VAL C  94     2401   3807   2711   1119    251     93       C  
ATOM   2389  CG1 VAL C  94      25.387   4.630   8.226  1.00 31.95           C  
ANISOU 2389  CG1 VAL C  94     3472   4896   3772   1100    234     99       C  
ATOM   2390  CG2 VAL C  94      26.975   3.197   6.934  1.00 34.53           C  
ANISOU 2390  CG2 VAL C  94     3849   5170   4099   1103    266     67       C  
ATOM   2391  N   LYS C  95      25.446   3.773   4.006  1.00 28.10           N  
ANISOU 2391  N   LYS C  95     2997   4475   3205   1044    281     75       N  
ATOM   2392  CA  LYS C  95      24.582   2.934   3.161  1.00 31.46           C  
ANISOU 2392  CA  LYS C  95     3441   4933   3578    992    290     61       C  
ATOM   2393  C   LYS C  95      23.374   3.676   2.570  1.00 32.38           C  
ANISOU 2393  C   LYS C  95     3518   5124   3661    970    281     79       C  
ATOM   2394  O   LYS C  95      22.447   3.060   2.051  1.00 32.77           O  
ANISOU 2394  O   LYS C  95     3577   5212   3663    922    283     70       O  
ATOM   2395  CB  LYS C  95      24.096   1.700   3.940  1.00 33.83           C  
ANISOU 2395  CB  LYS C  95     3785   5211   3858    958    289     40       C  
ATOM   2396  CG  LYS C  95      25.166   0.608   4.114  1.00 35.36           C  
ANISOU 2396  CG  LYS C  95     4031   5338   4067    967    307     17       C  
ATOM   2397  CD  LYS C  95      24.639  -0.517   4.988  1.00 38.62           C  
ANISOU 2397  CD  LYS C  95     4488   5727   4460    937    306     -1       C  
ATOM   2398  CE  LYS C  95      25.733  -1.522   5.314  1.00 35.90           C  
ANISOU 2398  CE  LYS C  95     4195   5313   4134    955    324    -19       C  
ATOM   2399  NZ  LYS C  95      25.225  -2.558   6.255  1.00 38.77           N  
ANISOU 2399  NZ  LYS C  95     4602   5650   4479    929    323    -35       N  
ATOM   2400  N   PHE C  96      23.394   4.999   2.633  1.00 31.35           N  
ANISOU 2400  N   PHE C  96     3343   5016   3553   1005    272    106       N  
ATOM   2401  CA  PHE C  96      22.287   5.785   2.105  1.00 30.53           C  
ANISOU 2401  CA  PHE C  96     3199   4983   3419    993    264    128       C  
ATOM   2402  C   PHE C  96      22.421   5.929   0.598  1.00 40.34           C  
ANISOU 2402  C   PHE C  96     4432   6256   4639    983    277    128       C  
ATOM   2403  O   PHE C  96      23.415   6.467   0.121  1.00 42.53           O  
ANISOU 2403  O   PHE C  96     4704   6510   4944   1016    287    132       O  
ATOM   2404  CB  PHE C  96      22.256   7.162   2.753  1.00 32.58           C  
ANISOU 2404  CB  PHE C  96     3419   5250   3709   1037    254    157       C  
ATOM   2405  CG  PHE C  96      21.099   8.006   2.308  1.00 30.56           C  
ANISOU 2405  CG  PHE C  96     3121   5066   3422   1031    247    183       C  
ATOM   2406  CD1 PHE C  96      19.788   7.582   2.525  1.00 26.89           C  
ANISOU 2406  CD1 PHE C  96     2650   4649   2917    993    238    185       C  
ATOM   2407  CD2 PHE C  96      21.315   9.210   1.667  1.00 34.41           C  
ANISOU 2407  CD2 PHE C  96     3577   5577   3921   1064    252    207       C  
ATOM   2408  CE1 PHE C  96      18.724   8.359   2.110  1.00 31.98           C  
ANISOU 2408  CE1 PHE C  96     3254   5366   3533    991    233    212       C  
ATOM   2409  CE2 PHE C  96      20.235   9.996   1.256  1.00 35.10           C  
ANISOU 2409  CE2 PHE C  96     3626   5733   3979   1064    248    234       C  
ATOM   2410  CZ  PHE C  96      18.951   9.559   1.473  1.00 31.06           C  
ANISOU 2410  CZ  PHE C  96     3105   5270   3427   1028    238    237       C  
ATOM   2411  N   THR C  97      21.424   5.469  -0.155  1.00 36.52           N  
ANISOU 2411  N   THR C  97     3947   5826   4103    936    278    125       N  
ATOM   2412  CA  THR C  97      21.540   5.497  -1.612  1.00 40.56           C  
ANISOU 2412  CA  THR C  97     4454   6367   4589    921    291    123       C  
ATOM   2413  C   THR C  97      20.662   6.561  -2.259  1.00 51.83           C  
ANISOU 2413  C   THR C  97     5831   7869   5993    925    284    154       C  
ATOM   2414  O   THR C  97      20.715   6.763  -3.473  1.00 57.23           O  
ANISOU 2414  O   THR C  97     6506   8584   6657    917    292    157       O  
ATOM   2415  CB  THR C  97      21.197   4.135  -2.217  1.00 38.43           C  
ANISOU 2415  CB  THR C  97     4224   6103   4275    862    302     96       C  
ATOM   2416  OG1 THR C  97      19.946   3.691  -1.691  1.00 49.52           O  
ANISOU 2416  OG1 THR C  97     5627   7547   5642    820    290     95       O  
ATOM   2417  CG2 THR C  97      22.257   3.108  -1.879  1.00 46.01           C  
ANISOU 2417  CG2 THR C  97     5239   6986   5258    865    317     67       C  
ATOM   2418  N   GLY C  98      19.887   7.265  -1.443  1.00 49.75           N  
ANISOU 2418  N   GLY C  98     5537   7635   5733    940    268    176       N  
ATOM   2419  CA  GLY C  98      18.936   8.249  -1.933  1.00 49.02           C  
ANISOU 2419  CA  GLY C  98     5396   7616   5614    946    262    208       C  
ATOM   2420  C   GLY C  98      19.561   9.391  -2.716  1.00 53.66           C  
ANISOU 2420  C   GLY C  98     5960   8208   6222    989    270    228       C  
ATOM   2421  O   GLY C  98      19.051   9.787  -3.761  1.00 62.02           O  
ANISOU 2421  O   GLY C  98     6992   9324   7247    981    273    244       O  
ATOM   2422  N   TYR C  99      20.653   9.931  -2.194  1.00 48.80           N  
ANISOU 2422  N   TYR C  99     5351   7533   5658   1034    275    229       N  
ATOM   2423  CA  TYR C  99      21.425  10.970  -2.870  1.00 39.82           C  
ANISOU 2423  CA  TYR C  99     4198   6388   4544   1075    286    244       C  
ATOM   2424  C   TYR C  99      22.796  11.029  -2.213  1.00 47.60           C  
ANISOU 2424  C   TYR C  99     5205   7296   5583   1107    292    231       C  
ATOM   2425  O   TYR C  99      23.128  10.137  -1.428  1.00 46.27           O  
ANISOU 2425  O   TYR C  99     5067   7085   5430   1095    288    209       O  
ATOM   2426  CB  TYR C  99      20.726  12.337  -2.809  1.00 32.10           C  
ANISOU 2426  CB  TYR C  99     3178   5457   3562   1107    282    282       C  
ATOM   2427  CG  TYR C  99      20.326  12.794  -1.418  1.00 38.03           C  
ANISOU 2427  CG  TYR C  99     3920   6197   4334   1129    272    297       C  
ATOM   2428  CD1 TYR C  99      21.208  13.503  -0.605  1.00 38.70           C  
ANISOU 2428  CD1 TYR C  99     4010   6226   4467   1171    275    301       C  
ATOM   2429  CD2 TYR C  99      19.057  12.524  -0.922  1.00 38.53           C  
ANISOU 2429  CD2 TYR C  99     3969   6306   4366   1105    259    306       C  
ATOM   2430  CE1 TYR C  99      20.830  13.926   0.665  1.00 39.89           C  
ANISOU 2430  CE1 TYR C  99     4160   6361   4634   1183    265    313       C  
ATOM   2431  CE2 TYR C  99      18.673  12.942   0.342  1.00 35.22           C  
ANISOU 2431  CE2 TYR C  99     3542   5875   3964   1125    251    319       C  
ATOM   2432  CZ  TYR C  99      19.560  13.638   1.130  1.00 36.43           C  
ANISOU 2432  CZ  TYR C  99     3704   5972   4166   1166    255    323       C  
ATOM   2433  OH  TYR C  99      19.164  14.043   2.388  1.00 33.81           O  
ANISOU 2433  OH  TYR C  99     3379   5618   3851   1172    245    333       O  
ATOM   2434  OXT TYR C  99      23.590  11.944  -2.444  1.00 55.29           O  
ANISOU 2434  OXT TYR C  99     6170   8252   6587   1145    300    242       O  
TER    2435      TYR C  99                                                      
ATOM   2436  P    DT D  11      17.713  -1.866 110.278  1.00 53.30           P  
ANISOU 2436  P    DT D  11     8443   5417   6393   -149   -601     98       P  
ATOM   2437  OP1  DT D  11      18.381  -3.127 110.659  1.00 50.13           O  
ANISOU 2437  OP1  DT D  11     8076   5000   5972   -118   -638    106       O  
ATOM   2438  OP2  DT D  11      16.261  -1.712 110.438  1.00 42.76           O  
ANISOU 2438  OP2  DT D  11     7086   4095   5064   -167   -550     71       O  
ATOM   2439  O5'  DT D  11      18.084  -1.439 108.778  1.00 37.17           O  
ANISOU 2439  O5'  DT D  11     6371   3379   4374   -117   -604    108       O  
ATOM   2440  C5'  DT D  11      19.019  -2.181 108.041  1.00 40.67           C  
ANISOU 2440  C5'  DT D  11     6820   3815   4817    -66   -641    126       C  
ATOM   2441  C4'  DT D  11      19.342  -1.476 106.738  1.00 42.06           C  
ANISOU 2441  C4'  DT D  11     6965   4000   5016    -44   -641    138       C  
ATOM   2442  O4'  DT D  11      18.237  -1.596 105.817  1.00 39.54           O  
ANISOU 2442  O4'  DT D  11     6616   3691   4715    -28   -599    112       O  
ATOM   2443  C3'  DT D  11      19.622   0.023 106.866  1.00 41.86           C  
ANISOU 2443  C3'  DT D  11     6928   3978   4996    -90   -637    152       C  
ATOM   2444  O3'  DT D  11      20.966   0.269 106.517  1.00 40.30           O  
ANISOU 2444  O3'  DT D  11     6683   3834   4794    -73   -666    179       O  
ATOM   2445  C2'  DT D  11      18.640   0.683 105.881  1.00 45.87           C  
ANISOU 2445  C2'  DT D  11     7400   4500   5529    -88   -590    134       C  
ATOM   2446  C1'  DT D  11      18.252  -0.477 104.978  1.00 40.04           C  
ANISOU 2446  C1'  DT D  11     6651   3764   4798    -34   -586    120       C  
ATOM   2447  N1   DT D  11      16.899  -0.332 104.323  1.00 41.89           N  
ANISOU 2447  N1   DT D  11     6857   4010   5048    -34   -537     94       N  
ATOM   2448  C2   DT D  11      16.819  -0.358 102.950  1.00 39.59           C  
ANISOU 2448  C2   DT D  11     6541   3726   4775      4   -530     93       C  
ATOM   2449  O2   DT D  11      17.788  -0.486 102.225  1.00 38.96           O  
ANISOU 2449  O2   DT D  11     6449   3655   4700     40   -558    112       O  
ATOM   2450  N3   DT D  11      15.559  -0.229 102.444  1.00 44.19           N  
ANISOU 2450  N3   DT D  11     7101   4319   5369      0   -488     72       N  
ATOM   2451  C4   DT D  11      14.387  -0.082 103.148  1.00 51.51           C  
ANISOU 2451  C4   DT D  11     8028   5252   6293    -34   -453     53       C  
ATOM   2452  O4   DT D  11      13.297   0.026 102.583  1.00 46.17           O  
ANISOU 2452  O4   DT D  11     7331   4585   5626    -32   -418     38       O  
ATOM   2453  C5   DT D  11      14.530  -0.066 104.592  1.00 46.11           C  
ANISOU 2453  C5   DT D  11     7368   4561   5590    -70   -460     54       C  
ATOM   2454  C7   DT D  11      13.320   0.092 105.469  1.00 49.40           C  
ANISOU 2454  C7   DT D  11     7783   4985   6002   -104   -424     37       C  
ATOM   2455  C6   DT D  11      15.768  -0.195 105.104  1.00 40.46           C  
ANISOU 2455  C6   DT D  11     6677   3834   4862    -69   -501     73       C  
ATOM   2456  P    DA D  12      21.547   1.767 106.456  1.00 54.98           P  
ANISOU 2456  P    DA D  12     8508   5728   6656   -114   -661    195       P  
ATOM   2457  OP1  DA D  12      22.992   1.682 106.753  1.00 49.99           O  
ANISOU 2457  OP1  DA D  12     7845   5145   6004   -109   -702    223       O  
ATOM   2458  OP2  DA D  12      20.658   2.679 107.217  1.00 48.46           O  
ANISOU 2458  OP2  DA D  12     7726   4858   5830   -175   -631    183       O  
ATOM   2459  O5'  DA D  12      21.480   2.114 104.905  1.00 47.42           O  
ANISOU 2459  O5'  DA D  12     7492   4803   5723    -76   -640    193       O  
ATOM   2460  C5'  DA D  12      22.173   1.282 103.993  1.00 47.76           C  
ANISOU 2460  C5'  DA D  12     7492   4884   5769    -15   -660    201       C  
ATOM   2461  C4'  DA D  12      22.086   1.823 102.582  1.00 56.05           C  
ANISOU 2461  C4'  DA D  12     8489   5965   6842     11   -638    199       C  
ATOM   2462  O4'  DA D  12      20.721   1.735 102.103  1.00 50.62           O  
ANISOU 2462  O4'  DA D  12     7821   5241   6172     15   -602    174       O  
ATOM   2463  C3'  DA D  12      22.499   3.280 102.420  1.00 58.84           C  
ANISOU 2463  C3'  DA D  12     8811   6346   7199    -27   -627    211       C  
ATOM   2464  O3'  DA D  12      23.143   3.442 101.175  1.00 65.74           O  
ANISOU 2464  O3'  DA D  12     9623   7271   8086     12   -629    221       O  
ATOM   2465  C2'  DA D  12      21.170   4.026 102.466  1.00 50.65           C  
ANISOU 2465  C2'  DA D  12     7804   5264   6175    -60   -583    192       C  
ATOM   2466  C1'  DA D  12      20.223   3.028 101.818  1.00 49.84           C  
ANISOU 2466  C1'  DA D  12     7710   5140   6085    -17   -569    172       C  
ATOM   2467  N9   DA D  12      18.884   3.103 102.353  1.00 46.51           N  
ANISOU 2467  N9   DA D  12     7339   4665   5667    -45   -540    151       N  
ATOM   2468  C8   DA D  12      18.526   3.149 103.672  1.00 51.25           C  
ANISOU 2468  C8   DA D  12     7996   5223   6253    -90   -541    146       C  
ATOM   2469  N7   DA D  12      17.233   3.194 103.867  1.00 41.31           N  
ANISOU 2469  N7   DA D  12     6748   3948   5000   -104   -502    123       N  
ATOM   2470  C5   DA D  12      16.714   3.174 102.586  1.00 43.77           C  
ANISOU 2470  C5   DA D  12     7031   4268   5331    -69   -482    116       C  
ATOM   2471  C6   DA D  12      15.410   3.212 102.110  1.00 40.08           C  
ANISOU 2471  C6   DA D  12     6543   3810   4876    -64   -439     95       C  
ATOM   2472  N6   DA D  12      14.350   3.276 102.910  1.00 38.56           N  
ANISOU 2472  N6   DA D  12     6352   3621   4677    -92   -407     78       N  
ATOM   2473  N1   DA D  12      15.230   3.179 100.773  1.00 55.90           N  
ANISOU 2473  N1   DA D  12     8523   5821   6897    -26   -432     95       N  
ATOM   2474  C2   DA D  12      16.304   3.117  99.977  1.00 53.80           C  
ANISOU 2474  C2   DA D  12     8229   5577   6634      6   -459    112       C  
ATOM   2475  N3   DA D  12      17.589   3.078 100.313  1.00 36.11           N  
ANISOU 2475  N3   DA D  12     5977   3361   4384      7   -493    130       N  
ATOM   2476  C4   DA D  12      17.723   3.116 101.644  1.00 44.23           C  
ANISOU 2476  C4   DA D  12     7051   4360   5396    -33   -506    133       C  
ATOM   2477  P    DT D  13      23.759   4.860 100.752  1.00 65.91           P  
ANISOU 2477  P    DT D  13     9603   7330   8111    -17   -619    235       P  
ATOM   2478  OP1  DT D  13      25.044   4.541 100.085  1.00 74.62           O  
ANISOU 2478  OP1  DT D  13    10648   8494   9211     22   -649    255       O  
ATOM   2479  OP2  DT D  13      23.752   5.765 101.926  1.00 58.45           O  
ANISOU 2479  OP2  DT D  13     8694   6364   7149    -85   -615    239       O  
ATOM   2480  O5'  DT D  13      22.720   5.390  99.651  1.00 55.97           O  
ANISOU 2480  O5'  DT D  13     8330   6059   6877     -4   -576    219       O  
ATOM   2481  C5'  DT D  13      22.318   4.514  98.610  1.00 53.78           C  
ANISOU 2481  C5'  DT D  13     8033   5786   6616     53   -571    208       C  
ATOM   2482  C4'  DT D  13      21.324   5.172  97.667  1.00 59.82           C  
ANISOU 2482  C4'  DT D  13     8785   6543   7402     57   -529    195       C  
ATOM   2483  O4'  DT D  13      19.979   5.109  98.212  1.00 61.39           O  
ANISOU 2483  O4'  DT D  13     9034   6688   7603     35   -502    176       O  
ATOM   2484  C3'  DT D  13      21.584   6.641  97.330  1.00 57.27           C  
ANISOU 2484  C3'  DT D  13     8437   6240   7084     28   -508    206       C  
ATOM   2485  O3'  DT D  13      21.400   6.802  95.935  1.00 58.01           O  
ANISOU 2485  O3'  DT D  13     8485   6359   7196     66   -490    203       O  
ATOM   2486  C2'  DT D  13      20.508   7.377  98.142  1.00 54.45           C  
ANISOU 2486  C2'  DT D  13     8130   5833   6726    -20   -475    196       C  
ATOM   2487  C1'  DT D  13      19.367   6.370  98.090  1.00 52.78           C  
ANISOU 2487  C1'  DT D  13     7946   5588   6522      4   -466    175       C  
ATOM   2488  N1   DT D  13      18.351   6.496  99.186  1.00 45.75           N  
ANISOU 2488  N1   DT D  13     7115   4642   5624    -36   -447    163       N  
ATOM   2489  C2   DT D  13      17.017   6.408  98.867  1.00 44.61           C  
ANISOU 2489  C2   DT D  13     6986   4470   5492    -28   -414    145       C  
ATOM   2490  O2   DT D  13      16.612   6.258  97.732  1.00 44.05           O  
ANISOU 2490  O2   DT D  13     6882   4419   5436      8   -399    140       O  
ATOM   2491  N3   DT D  13      16.161   6.506  99.932  1.00 41.91           N  
ANISOU 2491  N3   DT D  13     6700   4080   5143    -66   -398    135       N  
ATOM   2492  C4   DT D  13      16.493   6.672 101.257  1.00 41.46           C  
ANISOU 2492  C4   DT D  13     6686   3997   5069   -110   -411    140       C  
ATOM   2493  O4   DT D  13      15.639   6.746 102.144  1.00 39.85           O  
ANISOU 2493  O4   DT D  13     6496   3786   4859   -139   -386    125       O  
ATOM   2494  C5   DT D  13      17.910   6.755 101.532  1.00 44.78           C  
ANISOU 2494  C5   DT D  13     7088   4449   5476   -118   -447    158       C  
ATOM   2495  C7   DT D  13      18.390   6.939 102.945  1.00 45.48           C  
ANISOU 2495  C7   DT D  13     7219   4517   5543   -168   -465    165       C  
ATOM   2496  C6   DT D  13      18.764   6.654 100.495  1.00 44.70           C  
ANISOU 2496  C6   DT D  13     7022   4490   5473    -80   -463    169       C  
ATOM   2497  P    DA D  14      21.782   8.165  95.178  1.00 63.17           P  
ANISOU 2497  P    DA D  14     9100   7044   7858     55   -468    215       P  
ATOM   2498  OP1  DA D  14      22.692   7.802  94.070  1.00 62.86           O  
ANISOU 2498  OP1  DA D  14     9003   7056   7826    100   -487    224       O  
ATOM   2499  OP2  DA D  14      22.180   9.193  96.167  1.00 56.55           O  
ANISOU 2499  OP2  DA D  14     8285   6196   7004     -4   -465    225       O  
ATOM   2500  O5'  DA D  14      20.392   8.586  94.526  1.00 66.96           O  
ANISOU 2500  O5'  DA D  14     9587   7500   8356     62   -423    200       O  
ATOM   2501  C5'  DA D  14      19.557   7.575  93.977  1.00 59.55           C  
ANISOU 2501  C5'  DA D  14     8648   6550   7427    101   -419    185       C  
ATOM   2502  C4'  DA D  14      18.187   8.128  93.643  1.00 55.28           C  
ANISOU 2502  C4'  DA D  14     8121   5986   6898     96   -375    173       C  
ATOM   2503  O4'  DA D  14      17.370   8.192  94.837  1.00 47.80           O  
ANISOU 2503  O4'  DA D  14     7229   4989   5942     57   -362    165       O  
ATOM   2504  C3'  DA D  14      18.182   9.525  93.048  1.00 51.29           C  
ANISOU 2504  C3'  DA D  14     7591   5495   6401     85   -343    184       C  
ATOM   2505  O3'  DA D  14      17.199   9.582  92.050  1.00 56.78           O  
ANISOU 2505  O3'  DA D  14     8268   6195   7111    114   -313    176       O  
ATOM   2506  C2'  DA D  14      17.842  10.425  94.243  1.00 49.39           C  
ANISOU 2506  C2'  DA D  14     7401   5216   6150     31   -323    187       C  
ATOM   2507  C1'  DA D  14      16.951   9.519  95.084  1.00 48.33           C  
ANISOU 2507  C1'  DA D  14     7312   5041   6011     23   -327    170       C  
ATOM   2508  N9   DA D  14      17.054   9.740  96.524  1.00 45.20           N  
ANISOU 2508  N9   DA D  14     6967   4609   5599    -26   -333    172       N  
ATOM   2509  C8   DA D  14      18.200   9.889  97.261  1.00 48.79           C  
ANISOU 2509  C8   DA D  14     7428   5072   6037    -54   -362    184       C  
ATOM   2510  N7   DA D  14      17.986  10.040  98.547  1.00 44.17           N  
ANISOU 2510  N7   DA D  14     6895   4448   5438    -99   -361    182       N  
ATOM   2511  C5   DA D  14      16.605   9.976  98.666  1.00 42.43           C  
ANISOU 2511  C5   DA D  14     6705   4190   5226    -99   -329    167       C  
ATOM   2512  C6   DA D  14      15.739  10.066  99.779  1.00 39.72           C  
ANISOU 2512  C6   DA D  14     6420   3796   4876   -136   -311    158       C  
ATOM   2513  N6   DA D  14      16.168  10.243 101.034  1.00 34.40           N  
ANISOU 2513  N6   DA D  14     5787   3100   4184   -182   -325    162       N  
ATOM   2514  N1   DA D  14      14.412   9.954  99.550  1.00 38.72           N  
ANISOU 2514  N1   DA D  14     6294   3658   4760   -123   -277    143       N  
ATOM   2515  C2   DA D  14      13.994   9.774  98.295  1.00 40.55           C  
ANISOU 2515  C2   DA D  14     6495   3905   5007    -79   -267    141       C  
ATOM   2516  N3   DA D  14      14.713   9.667  97.172  1.00 36.98           N  
ANISOU 2516  N3   DA D  14     5989   3500   4564    -43   -281    148       N  
ATOM   2517  C4   DA D  14      16.018   9.782  97.430  1.00 45.16           C  
ANISOU 2517  C4   DA D  14     7013   4555   5589    -55   -312    161       C  
ATOM   2518  P    DT D  15      16.999  10.909  91.175  1.00 51.46           P  
ANISOU 2518  P    DT D  15     7566   5539   6447    117   -275    186       P  
ATOM   2519  OP1  DT D  15      16.671  10.488  89.801  1.00 50.77           O  
ANISOU 2519  OP1  DT D  15     7434   5483   6373    164   -269    182       O  
ATOM   2520  OP2  DT D  15      18.101  11.855  91.472  1.00 46.52           O  
ANISOU 2520  OP2  DT D  15     6935   4926   5813     88   -281    202       O  
ATOM   2521  O5'  DT D  15      15.678  11.535  91.776  1.00 50.38           O  
ANISOU 2521  O5'  DT D  15     7472   5361   6311     91   -234    181       O  
ATOM   2522  C5'  DT D  15      14.564  10.726  91.902  1.00 42.58           C  
ANISOU 2522  C5'  DT D  15     6502   4352   5325    101   -228    165       C  
ATOM   2523  C4'  DT D  15      13.525  11.410  92.734  1.00 37.50           C  
ANISOU 2523  C4'  DT D  15     5903   3667   4678     69   -192    163       C  
ATOM   2524  O4'  DT D  15      13.971  11.541  94.084  1.00 34.33           O  
ANISOU 2524  O4'  DT D  15     5548   3233   4263     24   -205    165       O  
ATOM   2525  C3'  DT D  15      13.166  12.816  92.291  1.00 44.38           C  
ANISOU 2525  C3'  DT D  15     6767   4541   5556     65   -147    177       C  
ATOM   2526  O3'  DT D  15      11.809  12.845  92.165  1.00 52.55           O  
ANISOU 2526  O3'  DT D  15     7810   5562   6594     75   -114    170       O  
ATOM   2527  C2'  DT D  15      13.628  13.716  93.457  1.00 47.43           C  
ANISOU 2527  C2'  DT D  15     7197   4895   5929     14   -139    186       C  
ATOM   2528  C1'  DT D  15      13.459  12.743  94.595  1.00 36.64           C  
ANISOU 2528  C1'  DT D  15     5872   3498   4554     -7   -165    172       C  
ATOM   2529  N1   DT D  15      14.203  13.018  95.851  1.00 35.89           N  
ANISOU 2529  N1   DT D  15     5818   3378   4442    -56   -181    177       N  
ATOM   2530  C2   DT D  15      13.505  13.070  97.035  1.00 37.38           C  
ANISOU 2530  C2   DT D  15     6062   3518   4622    -91   -168    170       C  
ATOM   2531  O2   DT D  15      12.286  13.011  97.098  1.00 34.02           O  
ANISOU 2531  O2   DT D  15     5648   3076   4202    -85   -138    161       O  
ATOM   2532  N3   DT D  15      14.280  13.237  98.154  1.00 39.34           N  
ANISOU 2532  N3   DT D  15     6345   3748   4854   -136   -187    175       N  
ATOM   2533  C4   DT D  15      15.648  13.320  98.213  1.00 41.63           C  
ANISOU 2533  C4   DT D  15     6617   4066   5134   -148   -220    185       C  
ATOM   2534  O4   DT D  15      16.248  13.462  99.278  1.00 37.46           O  
ANISOU 2534  O4   DT D  15     6123   3523   4589   -192   -237    189       O  
ATOM   2535  C5   DT D  15      16.328  13.221  96.936  1.00 40.69           C  
ANISOU 2535  C5   DT D  15     6437   3999   5026   -107   -234    192       C  
ATOM   2536  C7   DT D  15      17.822  13.297  96.871  1.00 50.65           C  
ANISOU 2536  C7   DT D  15     7671   5298   6277   -116   -269    204       C  
ATOM   2537  C6   DT D  15      15.582  13.054  95.830  1.00 39.30           C  
ANISOU 2537  C6   DT D  15     6228   3837   4866    -63   -214    187       C  
TER    2538       DT D  15                                                      
ATOM   2539  P    DA E  11       9.553  13.940 108.905  1.00 67.20           P  
ANISOU 2539  P    DA E  11     9973   7271   8288   -378    -61     85       P  
ATOM   2540  OP1  DA E  11      10.954  13.670 109.261  1.00 48.92           O  
ANISOU 2540  OP1  DA E  11     7678   4954   5956   -401   -102     92       O  
ATOM   2541  OP2  DA E  11       8.730  14.852 109.728  1.00 66.56           O  
ANISOU 2541  OP2  DA E  11     9896   7191   8202   -395    -20     82       O  
ATOM   2542  O5'  DA E  11       9.580  14.515 107.417  1.00 54.55           O  
ANISOU 2542  O5'  DA E  11     8354   5668   6704   -351    -45     96       O  
ATOM   2543  C5'  DA E  11       8.398  15.008 106.816  1.00 48.84           C  
ANISOU 2543  C5'  DA E  11     7613   4947   5997   -328     -3     95       C  
ATOM   2544  C4'  DA E  11       8.067  14.171 105.606  1.00 49.47           C  
ANISOU 2544  C4'  DA E  11     7674   5029   6094   -288    -15     93       C  
ATOM   2545  O4'  DA E  11       9.109  14.382 104.616  1.00 41.38           O  
ANISOU 2545  O4'  DA E  11     6647   4002   5073   -278    -33    106       O  
ATOM   2546  C3'  DA E  11       8.042  12.671 105.898  1.00 55.36           C  
ANISOU 2546  C3'  DA E  11     8420   5778   6836   -280    -52     80       C  
ATOM   2547  O3'  DA E  11       6.683  12.061 105.859  1.00 68.03           O  
ANISOU 2547  O3'  DA E  11    10013   7387   8448   -263    -35     67       O  
ATOM   2548  C2'  DA E  11       9.037  12.037 104.930  1.00 42.23           C  
ANISOU 2548  C2'  DA E  11     6755   4113   5177   -260    -89     85       C  
ATOM   2549  C1'  DA E  11       9.437  13.162 103.990  1.00 39.96           C  
ANISOU 2549  C1'  DA E  11     6461   3824   4898   -253    -70    102       C  
ATOM   2550  N9   DA E  11      10.861  13.156 103.742  1.00 36.74           N  
ANISOU 2550  N9   DA E  11     6063   3411   4484   -261   -105    113       N  
ATOM   2551  C8   DA E  11      11.854  13.105 104.689  1.00 37.41           C  
ANISOU 2551  C8   DA E  11     6171   3494   4551   -295   -133    116       C  
ATOM   2552  N7   DA E  11      13.059  13.085 104.188  1.00 42.89           N  
ANISOU 2552  N7   DA E  11     6871   4183   5241   -295   -165    129       N  
ATOM   2553  C5   DA E  11      12.840  13.125 102.821  1.00 40.15           C  
ANISOU 2553  C5   DA E  11     6504   3838   4912   -257   -157    134       C  
ATOM   2554  C6   DA E  11      13.716  13.130 101.746  1.00 42.86           C  
ANISOU 2554  C6   DA E  11     6842   4180   5262   -237   -179    148       C  
ATOM   2555  N6   DA E  11      15.041  13.101 101.900  1.00 35.99           N  
ANISOU 2555  N6   DA E  11     5989   3305   4380   -256   -218    162       N  
ATOM   2556  N1   DA E  11      13.184  13.174 100.499  1.00 50.16           N  
ANISOU 2556  N1   DA E  11     7745   5107   6205   -197   -162    150       N  
ATOM   2557  C2   DA E  11      11.847  13.204 100.367  1.00 48.34           C  
ANISOU 2557  C2   DA E  11     7500   4882   5985   -181   -125    139       C  
ATOM   2558  N3   DA E  11      10.912  13.203 101.320  1.00 34.48           N  
ANISOU 2558  N3   DA E  11     5748   3128   4224   -199   -102    127       N  
ATOM   2559  C4   DA E  11      11.486  13.165 102.534  1.00 34.09           C  
ANISOU 2559  C4   DA E  11     5719   3075   4158   -236   -120    124       C  
ATOM   2560  P    DT E  12       5.635  12.230 104.641  1.00 65.23           P  
ANISOU 2560  P    DT E  12     9639   7035   8111   -229     -6     69       P  
ATOM   2561  OP1  DT E  12       5.984  13.364 103.764  1.00 74.44           O  
ANISOU 2561  OP1  DT E  12    10799   8198   9285   -219     15     85       O  
ATOM   2562  OP2  DT E  12       4.280  12.159 105.210  1.00 63.08           O  
ANISOU 2562  OP2  DT E  12     9364   6764   7837   -232     22     59       O  
ATOM   2563  O5'  DT E  12       5.764  10.879 103.813  1.00 56.22           O  
ANISOU 2563  O5'  DT E  12     8491   5897   6974   -202    -39     60       O  
ATOM   2564  C5'  DT E  12       6.878  10.667 103.019  1.00 49.15           C  
ANISOU 2564  C5'  DT E  12     7595   5000   6082   -188    -68     68       C  
ATOM   2565  C4'  DT E  12       6.530  10.618 101.564  1.00 54.83           C  
ANISOU 2565  C4'  DT E  12     8297   5721   6815   -152    -60     72       C  
ATOM   2566  O4'  DT E  12       7.726  10.915 100.806  1.00 45.17           O  
ANISOU 2566  O4'  DT E  12     7072   4495   5596   -140    -80     86       O  
ATOM   2567  C3'  DT E  12       6.133   9.236 101.112  1.00 61.09           C  
ANISOU 2567  C3'  DT E  12     9085   6517   7608   -130    -81     56       C  
ATOM   2568  O3'  DT E  12       5.481   9.292  99.861  1.00 71.93           O  
ANISOU 2568  O3'  DT E  12    10444   7894   8992    -99    -64     59       O  
ATOM   2569  C2'  DT E  12       7.490   8.556 101.010  1.00 58.75           C  
ANISOU 2569  C2'  DT E  12     8798   6219   7307   -125   -127     58       C  
ATOM   2570  C1'  DT E  12       8.372   9.692 100.468  1.00 49.88           C  
ANISOU 2570  C1'  DT E  12     7671   5092   6190   -123   -123     79       C  
ATOM   2571  N1   DT E  12       9.773   9.701 101.024  1.00 44.08           N  
ANISOU 2571  N1   DT E  12     6952   4351   5444   -142   -158     87       N  
ATOM   2572  C2   DT E  12      10.831   9.893 100.167  1.00 44.33           C  
ANISOU 2572  C2   DT E  12     6981   4380   5480   -126   -180    102       C  
ATOM   2573  O2   DT E  12      10.695  10.067  98.972  1.00 48.53           O  
ANISOU 2573  O2   DT E  12     7498   4916   6025    -94   -172    108       O  
ATOM   2574  N3   DT E  12      12.064   9.885 100.761  1.00 49.92           N  
ANISOU 2574  N3   DT E  12     7707   5082   6176   -146   -213    111       N  
ATOM   2575  C4   DT E  12      12.345   9.709 102.097  1.00 42.59           C  
ANISOU 2575  C4   DT E  12     6800   4151   5231   -181   -226    106       C  
ATOM   2576  O4   DT E  12      13.496   9.729 102.536  1.00 38.91           O  
ANISOU 2576  O4   DT E  12     6352   3679   4753   -200   -258    117       O  
ATOM   2577  C5   DT E  12      11.193   9.502 102.945  1.00 45.93           C  
ANISOU 2577  C5   DT E  12     7223   4577   5651   -195   -200     90       C  
ATOM   2578  C7   DT E  12      11.375   9.290 104.421  1.00 51.25           C  
ANISOU 2578  C7   DT E  12     7917   5249   6306   -230   -211     85       C  
ATOM   2579  C6   DT E  12       9.977   9.503 102.374  1.00 40.64           C  
ANISOU 2579  C6   DT E  12     6535   3914   4994   -175   -168     82       C  
ATOM   2580  P    DA E  13       4.706   7.992  99.325  1.00 59.50           P  
ANISOU 2580  P    DA E  13     8867   6324   7416    -79    -73     41       P  
ATOM   2581  OP1  DA E  13       3.540   8.475  98.549  1.00 62.82           O  
ANISOU 2581  OP1  DA E  13     9277   6746   7844    -62    -36     44       O  
ATOM   2582  OP2  DA E  13       4.591   7.047 100.461  1.00 42.18           O  
ANISOU 2582  OP2  DA E  13     6687   4130   5209   -102    -90     24       O  
ATOM   2583  O5'  DA E  13       5.739   7.326  98.320  1.00 45.77           O  
ANISOU 2583  O5'  DA E  13     7124   4585   5680    -51   -110     43       O  
ATOM   2584  C5'  DA E  13       6.311   8.101  97.279  1.00 41.21           C  
ANISOU 2584  C5'  DA E  13     6536   4008   5114    -27   -107     60       C  
ATOM   2585  C4'  DA E  13       7.480   7.366  96.657  1.00 44.78           C  
ANISOU 2585  C4'  DA E  13     6987   4460   5566     -4   -149     62       C  
ATOM   2586  O4'  DA E  13       8.648   7.499  97.506  1.00 41.46           O  
ANISOU 2586  O4'  DA E  13     6580   4034   5140    -26   -175     69       O  
ATOM   2587  C3'  DA E  13       7.279   5.854  96.504  1.00 49.33           C  
ANISOU 2587  C3'  DA E  13     7570   5039   6136      9   -174     42       C  
ATOM   2588  O3'  DA E  13       8.045   5.411  95.444  1.00 60.45           O  
ANISOU 2588  O3'  DA E  13     8971   6449   7549     45   -200     46       O  
ATOM   2589  C2'  DA E  13       7.890   5.337  97.782  1.00 45.47           C  
ANISOU 2589  C2'  DA E  13     7099   4545   5634    -17   -198     36       C  
ATOM   2590  C1'  DA E  13       9.126   6.201  97.777  1.00 39.05           C  
ANISOU 2590  C1'  DA E  13     6286   3727   4824    -20   -212     57       C  
ATOM   2591  N9   DA E  13       9.867   6.186  99.020  1.00 43.28           N  
ANISOU 2591  N9   DA E  13     6840   4256   5347    -50   -232     60       N  
ATOM   2592  C8   DA E  13       9.381   5.982 100.280  1.00 42.44           C  
ANISOU 2592  C8   DA E  13     6747   4149   5230    -82   -223     50       C  
ATOM   2593  N7   DA E  13      10.306   5.995 101.208  1.00 45.74           N  
ANISOU 2593  N7   DA E  13     7183   4561   5636   -103   -247     56       N  
ATOM   2594  C5   DA E  13      11.475   6.213 100.497  1.00 42.11           C  
ANISOU 2594  C5   DA E  13     6722   4098   5181    -86   -274     72       C  
ATOM   2595  C6   DA E  13      12.811   6.329 100.890  1.00 41.40           C  
ANISOU 2595  C6   DA E  13     6649   4000   5083    -96   -309     87       C  
ATOM   2596  N6   DA E  13      13.214   6.245 102.165  1.00 48.28           N  
ANISOU 2596  N6   DA E  13     7542   4866   5937   -129   -323     88       N  
ATOM   2597  N1   DA E  13      13.731   6.533  99.920  1.00 49.34           N  
ANISOU 2597  N1   DA E  13     7647   5005   6096    -72   -330    104       N  
ATOM   2598  C2   DA E  13      13.326   6.612  98.646  1.00 50.58           C  
ANISOU 2598  C2   DA E  13     7782   5168   6269    -37   -316    104       C  
ATOM   2599  N3   DA E  13      12.095   6.525  98.156  1.00 41.12           N  
ANISOU 2599  N3   DA E  13     6569   3977   5079    -25   -283     90       N  
ATOM   2600  C4   DA E  13      11.213   6.319  99.146  1.00 42.31           C  
ANISOU 2600  C4   DA E  13     6727   4128   5221    -52   -264     75       C  
ATOM   2601  P    DT E  14       7.398   5.192  94.000  1.00 48.42           P  
ANISOU 2601  P    DT E  14     7413   4952   6032     81   -186     42       P  
ATOM   2602  OP1  DT E  14       6.777   6.477  93.600  1.00 51.05           O  
ANISOU 2602  OP1  DT E  14     7724   5298   6375     82   -147     56       O  
ATOM   2603  OP2  DT E  14       6.608   3.923  94.076  1.00 38.59           O  
ANISOU 2603  OP2  DT E  14     6190   3697   4776     80   -191     18       O  
ATOM   2604  O5'  DT E  14       8.679   4.913  93.084  1.00 58.18           O  
ANISOU 2604  O5'  DT E  14     8609   6225   7274    114   -216     51       O  
ATOM   2605  C5'  DT E  14       9.348   3.674  93.208  1.00 41.55           C  
ANISOU 2605  C5'  DT E  14     6515   4114   5158    125   -251     40       C  
ATOM   2606  C4'  DT E  14      10.832   3.853  93.435  1.00 42.39           C  
ANISOU 2606  C4'  DT E  14     6614   4226   5265    130   -282     57       C  
ATOM   2607  O4'  DT E  14      11.078   4.437  94.738  1.00 51.57           O  
ANISOU 2607  O4'  DT E  14     7817   5355   6423     92   -285     64       O  
ATOM   2608  C3'  DT E  14      11.582   2.551  93.479  1.00 42.82           C  
ANISOU 2608  C3'  DT E  14     6679   4280   5309    149   -318     50       C  
ATOM   2609  O3'  DT E  14      11.851   2.113  92.149  1.00 33.00           O  
ANISOU 2609  O3'  DT E  14     5390   3075   4071    189   -322     49       O  
ATOM   2610  C2'  DT E  14      12.851   2.936  94.239  1.00 49.13           C  
ANISOU 2610  C2'  DT E  14     7486   5076   6106    137   -345     68       C  
ATOM   2611  C1'  DT E  14      12.363   4.028  95.188  1.00 49.16           C  
ANISOU 2611  C1'  DT E  14     7518   5051   6111     94   -323     73       C  
ATOM   2612  N1   DT E  14      12.311   3.612  96.656  1.00 39.74           N  
ANISOU 2612  N1   DT E  14     6384   3812   4902     60   -337     66       N  
ATOM   2613  C2   DT E  14      13.490   3.566  97.380  1.00 44.30           C  
ANISOU 2613  C2   DT E  14     6973   4388   5471     50   -369     79       C  
ATOM   2614  O2   DT E  14      14.579   3.820  96.906  1.00 48.73           O  
ANISOU 2614  O2   DT E  14     7498   4983   6035     67   -387     95       O  
ATOM   2615  N3   DT E  14      13.354   3.213  98.689  1.00 49.73           N  
ANISOU 2615  N3   DT E  14     7694   5058   6144     18   -374     72       N  
ATOM   2616  C4   DT E  14      12.190   2.913  99.349  1.00 48.07           C  
ANISOU 2616  C4   DT E  14     7488   4850   5926     -5   -347     52       C  
ATOM   2617  O4   DT E  14      12.173   2.608 100.546  1.00 36.02           O  
ANISOU 2617  O4   DT E  14     5981   3319   4386    -32   -352     47       O  
ATOM   2618  C5   DT E  14      10.988   2.975  98.547  1.00 41.22           C  
ANISOU 2618  C5   DT E  14     6601   3991   5069      6   -313     40       C  
ATOM   2619  C7   DT E  14       9.660   2.657  99.176  1.00 50.82           C  
ANISOU 2619  C7   DT E  14     7820   5211   6278    -17   -284     21       C  
ATOM   2620  C6   DT E  14      11.101   3.324  97.253  1.00 39.67           C  
ANISOU 2620  C6   DT E  14     6386   3799   4887     37   -310     47       C  
ATOM   2621  P    DA E  15      12.193   0.575  91.862  1.00 36.51           P  
ANISOU 2621  P    DA E  15     5846   3521   4505    217   -346     36       P  
ATOM   2622  OP1  DA E  15      12.331   0.418  90.390  1.00 35.71           O  
ANISOU 2622  OP1  DA E  15     5695   3462   4412    254   -341     36       O  
ATOM   2623  OP2  DA E  15      11.273  -0.337  92.572  1.00 32.30           O  
ANISOU 2623  OP2  DA E  15     5364   2949   3957    198   -341     14       O  
ATOM   2624  O5'  DA E  15      13.650   0.415  92.443  1.00 41.41           O  
ANISOU 2624  O5'  DA E  15     6472   4141   5121    224   -382     52       O  
ATOM   2625  C5'  DA E  15      14.654   1.299  92.006  1.00 41.97           C  
ANISOU 2625  C5'  DA E  15     6499   4246   5203    235   -390     74       C  
ATOM   2626  C4'  DA E  15      15.942   1.018  92.722  1.00 44.77           C  
ANISOU 2626  C4'  DA E  15     6863   4600   5549    237   -425     89       C  
ATOM   2627  O4'  DA E  15      15.778   1.220  94.147  1.00 41.42           O  
ANISOU 2627  O4'  DA E  15     6487   4137   5114    196   -430     88       O  
ATOM   2628  C3'  DA E  15      16.444  -0.391  92.558  1.00 45.93           C  
ANISOU 2628  C3'  DA E  15     7020   4746   5684    272   -449     83       C  
ATOM   2629  O3'  DA E  15      17.832  -0.344  92.523  1.00 56.73           O  
ANISOU 2629  O3'  DA E  15     8362   6142   7051    292   -477    104       O  
ATOM   2630  C2'  DA E  15      15.928  -1.106  93.810  1.00 43.16           C  
ANISOU 2630  C2'  DA E  15     6734   4348   5318    247   -454     70       C  
ATOM   2631  C1'  DA E  15      15.985   0.009  94.845  1.00 42.81           C  
ANISOU 2631  C1'  DA E  15     6703   4288   5274    203   -453     81       C  
ATOM   2632  N9   DA E  15      14.942  -0.081  95.849  1.00 43.80           N  
ANISOU 2632  N9   DA E  15     6883   4367   5392    166   -439     66       N  
ATOM   2633  C8   DA E  15      13.590  -0.100  95.629  1.00 51.69           C  
ANISOU 2633  C8   DA E  15     7895   5350   6394    154   -408     46       C  
ATOM   2634  N7   DA E  15      12.874  -0.159  96.722  1.00 45.60           N  
ANISOU 2634  N7   DA E  15     7170   4542   5614    118   -399     35       N  
ATOM   2635  C5   DA E  15      13.825  -0.167  97.730  1.00 46.41           C  
ANISOU 2635  C5   DA E  15     7292   4635   5706    104   -426     48       C  
ATOM   2636  C6   DA E  15      13.709  -0.213  99.115  1.00 46.70           C  
ANISOU 2636  C6   DA E  15     7351   4665   5729     66   -426     45       C  
ATOM   2637  N6   DA E  15      12.534  -0.268  99.740  1.00 42.67           N  
ANISOU 2637  N6   DA E  15     6843   4157   5213     36   -396     26       N  
ATOM   2638  N1   DA E  15      14.851  -0.206  99.843  1.00 58.63           N  
ANISOU 2638  N1   DA E  15     8881   6166   7231     62   -460     62       N  
ATOM   2639  C2   DA E  15      16.027  -0.149  99.196  1.00 55.38           C  
ANISOU 2639  C2   DA E  15     8450   5768   6823     94   -489     83       C  
ATOM   2640  N3   DA E  15      16.260  -0.098  97.883  1.00 36.76           N  
ANISOU 2640  N3   DA E  15     6039   3449   4477    131   -484     86       N  
ATOM   2641  C4   DA E  15      15.105  -0.110  97.205  1.00 45.67           C  
ANISOU 2641  C4   DA E  15     7165   4572   5616    134   -453     68       C  
TER    2642       DA E  15                                                      
ATOM   2643  P    DT F   1      48.874  16.573  37.689  1.00 64.99           P  
ANISOU 2643  P    DT F   1     7409   8832   8450   1174   -106    317       P  
ATOM   2644  OP1  DT F   1      50.343  16.708  37.569  1.00 49.62           O  
ANISOU 2644  OP1  DT F   1     5417   6934   6502   1176   -112    325       O  
ATOM   2645  OP2  DT F   1      48.274  16.104  38.959  1.00 52.57           O  
ANISOU 2645  OP2  DT F   1     5859   7240   6875   1176   -125    322       O  
ATOM   2646  O5'  DT F   1      48.322  15.680  36.466  1.00 45.62           O  
ANISOU 2646  O5'  DT F   1     4984   6342   6007   1183    -93    299       O  
ATOM   2647  C5'  DT F   1      49.148  15.431  35.327  1.00 53.77           C  
ANISOU 2647  C5'  DT F   1     5997   7389   7045   1189    -83    293       C  
ATOM   2648  C4'  DT F   1      48.317  15.332  34.060  1.00 56.25           C  
ANISOU 2648  C4'  DT F   1     6335   7674   7363   1189    -62    278       C  
ATOM   2649  O4'  DT F   1      47.683  14.029  33.970  1.00 49.39           O  
ANISOU 2649  O4'  DT F   1     5497   6771   6497   1199    -67    269       O  
ATOM   2650  C3'  DT F   1      47.187  16.356  33.937  1.00 66.66           C  
ANISOU 2650  C3'  DT F   1     7673   8979   8677   1176    -47    276       C  
ATOM   2651  O3'  DT F   1      47.166  16.834  32.612  1.00 76.13           O  
ANISOU 2651  O3'  DT F   1     8868  10180   9876   1173    -25    268       O  
ATOM   2652  C2'  DT F   1      45.940  15.527  34.254  1.00 59.95           C  
ANISOU 2652  C2'  DT F   1     6862   8091   7827   1178    -52    269       C  
ATOM   2653  C1'  DT F   1      46.330  14.207  33.614  1.00 53.46           C  
ANISOU 2653  C1'  DT F   1     6042   7258   7010   1191    -56    260       C  
ATOM   2654  N1   DT F   1      45.567  13.031  34.099  1.00 45.19           N  
ANISOU 2654  N1   DT F   1     5027   6182   5964   1199    -66    255       N  
ATOM   2655  C2   DT F   1      45.133  12.088  33.193  1.00 48.34           C  
ANISOU 2655  C2   DT F   1     5443   6560   6362   1207    -57    244       C  
ATOM   2656  O2   DT F   1      45.317  12.179  31.994  1.00 45.50           O  
ANISOU 2656  O2   DT F   1     5077   6206   6004   1208    -42    237       O  
ATOM   2657  N3   DT F   1      44.461  11.033  33.741  1.00 44.10           N  
ANISOU 2657  N3   DT F   1     4934   5999   5823   1215    -65    241       N  
ATOM   2658  C4   DT F   1      44.206  10.819  35.072  1.00 37.50           C  
ANISOU 2658  C4   DT F   1     4109   5154   4984   1216    -83    247       C  
ATOM   2659  O4   DT F   1      43.602   9.830  35.471  1.00 39.34           O  
ANISOU 2659  O4   DT F   1     4368   5364   5215   1224    -88    243       O  
ATOM   2660  C5   DT F   1      44.698  11.836  35.969  1.00 43.51           C  
ANISOU 2660  C5   DT F   1     4850   5936   5746   1206    -92    259       C  
ATOM   2661  C7   DT F   1      44.471  11.709  37.445  1.00 50.07           C  
ANISOU 2661  C7   DT F   1     5690   6760   6574   1205   -112    268       C  
ATOM   2662  C6   DT F   1      45.347  12.880  35.444  1.00 40.84           C  
ANISOU 2662  C6   DT F   1     4483   5623   5409   1199    -83    263       C  
ATOM   2663  P    DA F   2      46.516  18.257  32.254  1.00 61.48           P  
ANISOU 2663  P    DA F   2     7018   8327   8014   1162     -2    271       P  
ATOM   2664  OP1  DA F   2      47.606  19.059  31.649  1.00 66.39           O  
ANISOU 2664  OP1  DA F   2     7607   8984   8635   1160     10    275       O  
ATOM   2665  OP2  DA F   2      45.716  18.754  33.404  1.00 41.70           O  
ANISOU 2665  OP2  DA F   2     4529   5812   5503   1157     -6    280       O  
ATOM   2666  O5'  DA F   2      45.493  17.887  31.097  1.00 42.20           O  
ANISOU 2666  O5'  DA F   2     4604   5858   5573   1161     12    258       O  
ATOM   2667  C5'  DA F   2      45.851  16.925  30.121  1.00 39.97           C  
ANISOU 2667  C5'  DA F   2     4320   5571   5297   1169     12    247       C  
ATOM   2668  C4'  DA F   2      44.611  16.287  29.538  1.00 44.89           C  
ANISOU 2668  C4'  DA F   2     4974   6166   5918   1169     17    237       C  
ATOM   2669  O4'  DA F   2      44.185  15.191  30.394  1.00 42.25           O  
ANISOU 2669  O4'  DA F   2     4658   5813   5584   1175      0    236       O  
ATOM   2670  C3'  DA F   2      43.395  17.222  29.453  1.00 52.78           C  
ANISOU 2670  C3'  DA F   2     5990   7155   6907   1158     31    239       C  
ATOM   2671  O3'  DA F   2      42.574  16.831  28.382  1.00 64.27           O  
ANISOU 2671  O3'  DA F   2     7461   8598   8358   1158     42    230       O  
ATOM   2672  C2'  DA F   2      42.694  16.910  30.748  1.00 46.59           C  
ANISOU 2672  C2'  DA F   2     5225   6356   6122   1157     17    244       C  
ATOM   2673  C1'  DA F   2      42.842  15.409  30.716  1.00 38.92           C  
ANISOU 2673  C1'  DA F   2     4261   5373   5156   1167      3    235       C  
ATOM   2674  N9   DA F   2      42.508  14.761  31.963  1.00 41.85           N  
ANISOU 2674  N9   DA F   2     4646   5730   5527   1170    -15    238       N  
ATOM   2675  C8   DA F   2      42.672  15.252  33.226  1.00 40.11           C  
ANISOU 2675  C8   DA F   2     4421   5513   5305   1167    -27    249       C  
ATOM   2676  N7   DA F   2      42.238  14.443  34.164  1.00 44.14           N  
ANISOU 2676  N7   DA F   2     4949   6006   5815   1170    -42    249       N  
ATOM   2677  C5   DA F   2      41.742  13.361  33.456  1.00 36.94           C  
ANISOU 2677  C5   DA F   2     4054   5078   4902   1177    -39    238       C  
ATOM   2678  C6   DA F   2      41.137  12.168  33.859  1.00 34.80           C  
ANISOU 2678  C6   DA F   2     3806   4786   4629   1185    -49    232       C  
ATOM   2679  N6   DA F   2      40.927  11.848  35.142  1.00 38.50           N  
ANISOU 2679  N6   DA F   2     4287   5244   5097   1187    -65    237       N  
ATOM   2680  N1   DA F   2      40.755  11.302  32.889  1.00 38.61           N  
ANISOU 2680  N1   DA F   2     4301   5261   5109   1193    -40    222       N  
ATOM   2681  C2   DA F   2      40.966  11.628  31.612  1.00 39.14           C  
ANISOU 2681  C2   DA F   2     4357   5340   5176   1192    -24    217       C  
ATOM   2682  N3   DA F   2      41.544  12.714  31.113  1.00 36.95           N  
ANISOU 2682  N3   DA F   2     4056   5080   4901   1184    -15    221       N  
ATOM   2683  C4   DA F   2      41.896  13.553  32.098  1.00 39.81           C  
ANISOU 2683  C4   DA F   2     4409   5451   5266   1177    -23    231       C  
ATOM   2684  P    DT F   3      42.698  17.533  26.947  1.00 54.77           P  
ANISOU 2684  P    DT F   3     6251   7407   7153   1156     63    227       P  
ATOM   2685  OP1  DT F   3      44.099  17.345  26.493  1.00 62.52           O  
ANISOU 2685  OP1  DT F   3     7207   8405   8142   1162     62    225       O  
ATOM   2686  OP2  DT F   3      42.078  18.890  27.012  1.00 37.79           O  
ANISOU 2686  OP2  DT F   3     4105   5259   4993   1148     79    235       O  
ATOM   2687  O5'  DT F   3      41.740  16.633  26.044  1.00 45.09           O  
ANISOU 2687  O5'  DT F   3     5043   6167   5921   1158     67    217       O  
ATOM   2688  C5'  DT F   3      40.365  16.607  26.319  1.00 37.99           C  
ANISOU 2688  C5'  DT F   3     4165   5256   5012   1153     67    218       C  
ATOM   2689  C4'  DT F   3      39.873  15.180  26.403  1.00 43.13           C  
ANISOU 2689  C4'  DT F   3     4831   5894   5661   1161     56    210       C  
ATOM   2690  O4'  DT F   3      40.292  14.598  27.657  1.00 51.34           O  
ANISOU 2690  O4'  DT F   3     5873   6926   6709   1165     38    212       O  
ATOM   2691  C3'  DT F   3      38.366  15.052  26.409  1.00 42.11           C  
ANISOU 2691  C3'  DT F   3     4721   5758   5519   1157     59    210       C  
ATOM   2692  O3'  DT F   3      37.882  15.018  25.075  1.00 34.72           O  
ANISOU 2692  O3'  DT F   3     3786   4831   4574   1157     73    205       O  
ATOM   2693  C2'  DT F   3      38.143  13.722  27.124  1.00 50.16           C  
ANISOU 2693  C2'  DT F   3     5755   6764   6540   1165     44    205       C  
ATOM   2694  C1'  DT F   3      39.330  13.644  28.081  1.00 49.39           C  
ANISOU 2694  C1'  DT F   3     5647   6663   6456   1169     30    208       C  
ATOM   2695  N1   DT F   3      38.980  13.875  29.540  1.00 43.52           N  
ANISOU 2695  N1   DT F   3     4912   5910   5713   1164     18    215       N  
ATOM   2696  C2   DT F   3      38.287  12.893  30.225  1.00 44.61           C  
ANISOU 2696  C2   DT F   3     5070   6033   5847   1169      7    212       C  
ATOM   2697  O2   DT F   3      37.917  11.855  29.714  1.00 50.06           O  
ANISOU 2697  O2   DT F   3     5771   6717   6531   1178      8    204       O  
ATOM   2698  N3   DT F   3      38.040  13.168  31.540  1.00 41.84           N  
ANISOU 2698  N3   DT F   3     4727   5674   5498   1165     -5    219       N  
ATOM   2699  C4   DT F   3      38.411  14.292  32.233  1.00 46.67           C  
ANISOU 2699  C4   DT F   3     5328   6291   6113   1157     -5    229       C  
ATOM   2700  O4   DT F   3      38.147  14.442  33.423  1.00 36.36           O  
ANISOU 2700  O4   DT F   3     4031   4977   4808   1154    -15    236       O  
ATOM   2701  C5   DT F   3      39.130  15.287  31.465  1.00 43.62           C  
ANISOU 2701  C5   DT F   3     4921   5922   5729   1153      8    233       C  
ATOM   2702  C7   DT F   3      39.568  16.562  32.130  1.00 49.40           C  
ANISOU 2702  C7   DT F   3     5643   6665   6464   1148     12    245       C  
ATOM   2703  C6   DT F   3      39.381  15.033  30.168  1.00 42.53           C  
ANISOU 2703  C6   DT F   3     4776   5792   5592   1157     18    225       C  
ATOM   2704  P    DA F   4      36.420  15.582  24.743  1.00 35.30           P  
ANISOU 2704  P    DA F   4     3870   4911   4632   1150     84    211       P  
ATOM   2705  OP1  DA F   4      36.256  15.615  23.261  1.00 31.50           O  
ANISOU 2705  OP1  DA F   4     3383   4445   4142   1152     98    207       O  
ATOM   2706  OP2  DA F   4      36.122  16.809  25.496  1.00 29.79           O  
ANISOU 2706  OP2  DA F   4     3174   4212   3934   1142     88    222       O  
ATOM   2707  O5'  DA F   4      35.443  14.445  25.283  1.00 40.21           O  
ANISOU 2707  O5'  DA F   4     4508   5525   5245   1155     73    206       O  
ATOM   2708  C5'  DA F   4      35.610  13.095  24.859  1.00 39.00           C  
ANISOU 2708  C5'  DA F   4     4359   5369   5090   1167     69    195       C  
ATOM   2709  C4'  DA F   4      34.599  12.198  25.552  1.00 37.14           C  
ANISOU 2709  C4'  DA F   4     4141   5127   4844   1171     61    193       C  
ATOM   2710  O4'  DA F   4      34.926  12.122  26.963  1.00 41.71           O  
ANISOU 2710  O4'  DA F   4     4725   5688   5433   1170     46    196       O  
ATOM   2711  C3'  DA F   4      33.149  12.678  25.461  1.00 38.44           C  
ANISOU 2711  C3'  DA F   4     4309   5304   4992   1164     67    199       C  
ATOM   2712  O3'  DA F   4      32.258  11.581  25.218  1.00 43.78           O  
ANISOU 2712  O3'  DA F   4     4995   5987   5651   1173     67    192       O  
ATOM   2713  C2'  DA F   4      32.882  13.332  26.814  1.00 33.76           C  
ANISOU 2713  C2'  DA F   4     3723   4700   4405   1155     59    207       C  
ATOM   2714  C1'  DA F   4      33.874  12.653  27.747  1.00 40.94           C  
ANISOU 2714  C1'  DA F   4     4637   5589   5330   1161     44    203       C  
ATOM   2715  N9   DA F   4      34.441  13.599  28.686  1.00 45.50           N  
ANISOU 2715  N9   DA F   4     5210   6159   5919   1153     39    211       N  
ATOM   2716  C8   DA F   4      35.098  14.760  28.385  1.00 48.50           C  
ANISOU 2716  C8   DA F   4     5576   6546   6306   1147     48    218       C  
ATOM   2717  N7   DA F   4      35.481  15.440  29.434  1.00 40.49           N  
ANISOU 2717  N7   DA F   4     4561   5525   5299   1143     43    226       N  
ATOM   2718  C5   DA F   4      35.028  14.675  30.492  1.00 43.62           C  
ANISOU 2718  C5   DA F   4     4972   5908   5696   1145     28    224       C  
ATOM   2719  C6   DA F   4      35.120  14.848  31.864  1.00 30.66           C  
ANISOU 2719  C6   DA F   4     3336   4254   4059   1143     17    231       C  
ATOM   2720  N6   DA F   4      35.716  15.896  32.419  1.00 38.25           N  
ANISOU 2720  N6   DA F   4     4290   5218   5026   1139     19    240       N  
ATOM   2721  N1   DA F   4      34.566  13.904  32.655  1.00 53.86           N  
ANISOU 2721  N1   DA F   4     6291   7179   6995   1147      4    227       N  
ATOM   2722  C2   DA F   4      33.964  12.852  32.078  1.00 57.29           C  
ANISOU 2722  C2   DA F   4     6734   7613   7420   1154      4    217       C  
ATOM   2723  N3   DA F   4      33.826  12.575  30.784  1.00 39.02           N  
ANISOU 2723  N3   DA F   4     4415   5312   5100   1157     15    211       N  
ATOM   2724  C4   DA F   4      34.380  13.539  30.043  1.00 46.75           C  
ANISOU 2724  C4   DA F   4     5377   6303   6082   1152     26    215       C  
ATOM   2725  P    DT F   5      30.679  11.837  25.062  1.00 43.99           P  
ANISOU 2725  P    DT F   5     5023   6035   5656   1169     72    198       P  
ATOM   2726  OP1  DT F   5      30.183  10.887  24.041  1.00 48.89           O  
ANISOU 2726  OP1  DT F   5     5643   6676   6258   1180     79    190       O  
ATOM   2727  OP2  DT F   5      30.397  13.272  24.873  1.00 45.71           O  
ANISOU 2727  OP2  DT F   5     5232   6262   5874   1156     82    211       O  
ATOM   2728  O5'  DT F   5      30.097  11.426  26.492  1.00 54.15           O  
ANISOU 2728  O5'  DT F   5     6325   7307   6943   1169     59    199       O  
ATOM   2729  C5'  DT F   5      30.644  10.315  27.175  1.00 48.12           C  
ANISOU 2729  C5'  DT F   5     5575   6523   6186   1180     47    189       C  
ATOM   2730  C4'  DT F   5      29.947  10.087  28.505  1.00 48.11           C  
ANISOU 2730  C4'  DT F   5     5589   6508   6183   1178     36    191       C  
ATOM   2731  O4'  DT F   5      30.539  10.913  29.541  1.00 44.60           O  
ANISOU 2731  O4'  DT F   5     5144   6045   5756   1168     28    199       O  
ATOM   2732  C3'  DT F   5      28.452  10.366  28.524  1.00 47.65           C  
ANISOU 2732  C3'  DT F   5     5530   6471   6105   1174     41    197       C  
ATOM   2733  O3'  DT F   5      27.812   9.293  29.217  1.00 46.56           O  
ANISOU 2733  O3'  DT F   5     5408   6327   5956   1184     33    190       O  
ATOM   2734  C2'  DT F   5      28.353  11.712  29.267  1.00 47.00           C  
ANISOU 2734  C2'  DT F   5     5444   6382   6034   1159     42    211       C  
ATOM   2735  C1'  DT F   5      29.531  11.619  30.232  1.00 45.00           C  
ANISOU 2735  C1'  DT F   5     5198   6099   5801   1159     29    209       C  
ATOM   2736  N1   DT F   5      30.132  12.942  30.676  1.00 37.37           N  
ANISOU 2736  N1   DT F   5     4224   5124   4849   1148     32    220       N  
ATOM   2737  C2   DT F   5      30.355  13.164  32.023  1.00 40.47           C  
ANISOU 2737  C2   DT F   5     4627   5498   5252   1145     21    224       C  
ATOM   2738  O2   DT F   5      30.038  12.382  32.893  1.00 42.20           O  
ANISOU 2738  O2   DT F   5     4860   5704   5469   1149      9    220       O  
ATOM   2739  N3   DT F   5      30.945  14.356  32.321  1.00 39.61           N  
ANISOU 2739  N3   DT F   5     4511   5386   5153   1138     26    234       N  
ATOM   2740  C4   DT F   5      31.351  15.325  31.442  1.00 34.69           C  
ANISOU 2740  C4   DT F   5     3874   4775   4531   1134     41    239       C  
ATOM   2741  O4   DT F   5      31.875  16.368  31.823  1.00 39.56           O  
ANISOU 2741  O4   DT F   5     4487   5388   5155   1130     47    248       O  
ATOM   2742  C5   DT F   5      31.119  15.036  30.045  1.00 39.79           C  
ANISOU 2742  C5   DT F   5     4511   5439   5168   1137     51    233       C  
ATOM   2743  C7   DT F   5      31.524  16.032  28.995  1.00 50.43           C  
ANISOU 2743  C7   DT F   5     5846   6799   6515   1134     67    238       C  
ATOM   2744  C6   DT F   5      30.538  13.862  29.728  1.00 37.87           C  
ANISOU 2744  C6   DT F   5     4273   5200   4914   1143     45    224       C  
ATOM   2745  P    DA F   6      26.210   9.184  29.332  1.00 46.62           P  
ANISOU 2745  P    DA F   6     5414   6359   5939   1184     36    193       P  
ATOM   2746  OP1  DA F   6      25.936   7.734  29.438  1.00 51.87           O  
ANISOU 2746  OP1  DA F   6     6095   7023   6589   1202     31    179       O  
ATOM   2747  OP2  DA F   6      25.526  10.013  28.308  1.00 41.74           O  
ANISOU 2747  OP2  DA F   6     4776   5776   5308   1176     50    203       O  
ATOM   2748  O5'  DA F   6      25.909   9.827  30.755  1.00 37.40           O  
ANISOU 2748  O5'  DA F   6     4256   5172   4782   1173     27    203       O  
ATOM   2749  C5'  DA F   6      26.505   9.253  31.897  1.00 41.84           C  
ANISOU 2749  C5'  DA F   6     4838   5702   5357   1178     13    197       C  
ATOM   2750  C4'  DA F   6      26.068   9.994  33.131  1.00 48.88           C  
ANISOU 2750  C4'  DA F   6     5736   6580   6255   1167      7    207       C  
ATOM   2751  O4'  DA F   6      26.775  11.256  33.216  1.00 48.93           O  
ANISOU 2751  O4'  DA F   6     5732   6579   6278   1155     12    218       O  
ATOM   2752  C3'  DA F   6      24.580  10.335  33.157  1.00 54.57           C  
ANISOU 2752  C3'  DA F   6     6452   7325   6957   1163     15    215       C  
ATOM   2753  O3'  DA F   6      24.087  10.127  34.445  1.00 61.44           O  
ANISOU 2753  O3'  DA F   6     7338   8178   7827   1163      6    216       O  
ATOM   2754  C2'  DA F   6      24.541  11.811  32.764  1.00 52.80           C  
ANISOU 2754  C2'  DA F   6     6213   7112   6738   1151     29    231       C  
ATOM   2755  C1'  DA F   6      25.849  12.319  33.349  1.00 45.89           C  
ANISOU 2755  C1'  DA F   6     5343   6207   5887   1146     23    232       C  
ATOM   2756  N9   DA F   6      26.389  13.450  32.630  1.00 43.02           N  
ANISOU 2756  N9   DA F   6     4966   5850   5531   1139     36    240       N  
ATOM   2757  C8   DA F   6      26.329  13.668  31.283  1.00 42.74           C  
ANISOU 2757  C8   DA F   6     4915   5838   5486   1140     48    240       C  
ATOM   2758  N7   DA F   6      26.927  14.762  30.898  1.00 40.54           N  
ANISOU 2758  N7   DA F   6     4629   5559   5217   1134     59    248       N  
ATOM   2759  C5   DA F   6      27.419  15.298  32.074  1.00 31.25           C  
ANISOU 2759  C5   DA F   6     3461   4358   4054   1131     54    253       C  
ATOM   2760  C6   DA F   6      28.151  16.462  32.341  1.00 37.74           C  
ANISOU 2760  C6   DA F   6     4282   5171   4887   1127     61    262       C  
ATOM   2761  N6   DA F   6      28.531  17.319  31.386  1.00 34.16           N  
ANISOU 2761  N6   DA F   6     3817   4728   4433   1126     76    267       N  
ATOM   2762  N1   DA F   6      28.481  16.714  33.632  1.00 51.54           N  
ANISOU 2762  N1   DA F   6     6041   6897   6646   1125     54    266       N  
ATOM   2763  C2   DA F   6      28.093  15.841  34.577  1.00 56.54           C  
ANISOU 2763  C2   DA F   6     6686   7518   7279   1127     38    261       C  
ATOM   2764  N3   DA F   6      27.401  14.706  34.441  1.00 45.58           N  
ANISOU 2764  N3   DA F   6     5302   6136   5881   1131     30    252       N  
ATOM   2765  C4   DA F   6      27.095  14.495  33.153  1.00 38.04           C  
ANISOU 2765  C4   DA F   6     4335   5204   4915   1133     39    248       C  
ATOM   2766  P    DT F   7      22.517  10.254  34.749  1.00 55.42           P  
ANISOU 2766  P    DT F   7     6575   7439   7045   1159     11    223       P  
ATOM   2767  OP1  DT F   7      22.182   9.011  35.479  1.00 58.49           O  
ANISOU 2767  OP1  DT F   7     6994   7806   7424   1141     -2    205       O  
ATOM   2768  OP2  DT F   7      21.773  10.657  33.535  1.00 42.64           O  
ANISOU 2768  OP2  DT F   7     4930   5862   5407   1160     26    231       O  
ATOM   2769  O5'  DT F   7      22.459  11.507  35.729  1.00 40.47           O  
ANISOU 2769  O5'  DT F   7     4684   5527   5164   1150     15    240       O  
ATOM   2770  C5'  DT F   7      23.390  11.604  36.796  1.00 41.62           C  
ANISOU 2770  C5'  DT F   7     4847   5636   5331   1148      3    239       C  
ATOM   2771  C4'  DT F   7      23.391  13.003  37.381  1.00 45.68           C  
ANISOU 2771  C4'  DT F   7     5362   6141   5856   1138     13    255       C  
ATOM   2772  O4'  DT F   7      24.151  13.900  36.522  1.00 40.59           O  
ANISOU 2772  O4'  DT F   7     4701   5501   5218   1133     24    260       O  
ATOM   2773  C3'  DT F   7      22.007  13.653  37.511  1.00 50.61           C  
ANISOU 2773  C3'  DT F   7     5982   6782   6464   1135     28    269       C  
ATOM   2774  O3'  DT F   7      22.019  14.510  38.620  1.00 65.19           O  
ANISOU 2774  O3'  DT F   7     7843   8606   8321   1131     31    280       O  
ATOM   2775  C2'  DT F   7      21.946  14.482  36.237  1.00 44.25           C  
ANISOU 2775  C2'  DT F   7     5157   6004   5654   1133     46    277       C  
ATOM   2776  C1'  DT F   7      23.354  15.031  36.276  1.00 32.81           C  
ANISOU 2776  C1'  DT F   7     3710   4532   4225   1129     44    276       C  
ATOM   2777  N1   DT F   7      23.800  15.738  35.031  1.00 36.15           N  
ANISOU 2777  N1   DT F   7     4117   4972   4648   1128     58    280       N  
ATOM   2778  C2   DT F   7      24.651  16.811  35.154  1.00 36.42           C  
ANISOU 2778  C2   DT F   7     4152   4992   4694   1125     66    288       C  
ATOM   2779  O2   DT F   7      25.078  17.197  36.220  1.00 35.63           O  
ANISOU 2779  O2   DT F   7     4064   4868   4605   1123     63    292       O  
ATOM   2780  N3   DT F   7      25.009  17.410  33.974  1.00 34.12           N  
ANISOU 2780  N3   DT F   7     3847   4716   4401   1124     80    290       N  
ATOM   2781  C4   DT F   7      24.592  17.066  32.715  1.00 37.90           C  
ANISOU 2781  C4   DT F   7     4311   5222   4866   1126     84    287       C  
ATOM   2782  O4   DT F   7      24.970  17.672  31.720  1.00 42.37           O  
ANISOU 2782  O4   DT F   7     4868   5800   5431   1126     96    290       O  
ATOM   2783  C5   DT F   7      23.671  15.940  32.649  1.00 43.60           C  
ANISOU 2783  C5   DT F   7     5032   5961   5574   1129     75    280       C  
ATOM   2784  C7   DT F   7      23.148  15.469  31.317  1.00 45.91           C  
ANISOU 2784  C7   DT F   7     5307   6287   5848   1133     80    277       C  
ATOM   2785  C6   DT F   7      23.323  15.338  33.801  1.00 37.48           C  
ANISOU 2785  C6   DT F   7     4270   5170   4800   1130     63    276       C  
ATOM   2786  P    DA F   8      21.154  14.210  39.938  1.00 63.47           P  
ANISOU 2786  P    DA F   8     7643   8373   8098   1132     25    283       P  
ATOM   2787  OP1  DA F   8      22.106  13.516  40.832  1.00 61.44           O  
ANISOU 2787  OP1  DA F   8     7406   8083   7856   1127      4    271       O  
ATOM   2788  OP2  DA F   8      19.830  13.614  39.628  1.00 40.92           O  
ANISOU 2788  OP2  DA F   8     4782   5544   5220   1128     28    280       O  
ATOM   2789  O5'  DA F   8      20.808  15.685  40.471  1.00 55.72           O  
ANISOU 2789  O5'  DA F   8     6667   7384   7121   1128     46    304       O  
ATOM   2790  C5'  DA F   8      21.614  16.272  41.463  1.00 46.61           C  
ANISOU 2790  C5'  DA F   8     5530   6198   5983   1126     44    309       C  
ATOM   2791  C4'  DA F   8      22.266  17.558  40.980  1.00 39.46           C  
ANISOU 2791  C4'  DA F   8     4617   5292   5084   1124     63    321       C  
ATOM   2792  O4'  DA F   8      22.814  17.397  39.662  1.00 42.89           O  
ANISOU 2792  O4'  DA F   8     5031   5747   5517   1124     62    313       O  
ATOM   2793  C3'  DA F   8      21.348  18.740  40.820  1.00 39.32           C  
ANISOU 2793  C3'  DA F   8     4601   5285   5056   1127     92    340       C  
ATOM   2794  O3'  DA F   8      21.087  19.302  42.065  1.00 35.93           O  
ANISOU 2794  O3'  DA F   8     4193   4829   4629   1128     99    352       O  
ATOM   2795  C2'  DA F   8      22.206  19.671  39.967  1.00 43.11           C  
ANISOU 2795  C2'  DA F   8     5071   5769   5540   1127    106    346       C  
ATOM   2796  C1'  DA F   8      22.993  18.690  39.106  1.00 41.30           C  
ANISOU 2796  C1'  DA F   8     4824   5551   5315   1124     86    327       C  
ATOM   2797  N9   DA F   8      22.547  18.669  37.730  1.00 39.99           N  
ANISOU 2797  N9   DA F   8     4641   5417   5137   1125     95    326       N  
ATOM   2798  C8   DA F   8      21.708  17.763  37.152  1.00 38.41           C  
ANISOU 2798  C8   DA F   8     4430   5242   4923   1126     88    319       C  
ATOM   2799  N7   DA F   8      21.476  17.991  35.882  1.00 35.40           N  
ANISOU 2799  N7   DA F   8     4032   4889   4531   1127     99    322       N  
ATOM   2800  C5   DA F   8      22.219  19.133  35.612  1.00 31.71           C  
ANISOU 2800  C5   DA F   8     3566   4412   4071   1127    114    330       C  
ATOM   2801  C6   DA F   8      22.414  19.870  34.437  1.00 34.19           C  
ANISOU 2801  C6   DA F   8     3869   4743   4380   1129    131    337       C  
ATOM   2802  N6   DA F   8      21.834  19.552  33.276  1.00 32.27           N  
ANISOU 2802  N6   DA F   8     3609   4532   4121   1130    133    336       N  
ATOM   2803  N1   DA F   8      23.217  20.960  34.503  1.00 37.08           N  
ANISOU 2803  N1   DA F   8     4241   5093   4754   1130    145    345       N  
ATOM   2804  C2   DA F   8      23.779  21.273  35.678  1.00 38.62           C  
ANISOU 2804  C2   DA F   8     4452   5260   4963   1130    143    347       C  
ATOM   2805  N3   DA F   8      23.688  20.639  36.852  1.00 35.11           N  
ANISOU 2805  N3   DA F   8     4018   4797   4525   1128    126    342       N  
ATOM   2806  C4   DA F   8      22.882  19.566  36.744  1.00 40.91           C  
ANISOU 2806  C4   DA F   8     4748   5546   5251   1126    113    333       C  
ATOM   2807  P    DT F   9      19.911  20.372  42.221  1.00 37.59           P  
ANISOU 2807  P    DT F   9     4411   5044   4827   1133    131    374       P  
ATOM   2808  OP1  DT F   9      19.767  20.613  43.681  1.00 39.03           O  
ANISOU 2808  OP1  DT F   9     4621   5193   5015   1132    133    382       O  
ATOM   2809  OP2  DT F   9      18.734  19.954  41.431  1.00 36.94           O  
ANISOU 2809  OP2  DT F   9     4310   4998   4727   1135    134    375       O  
ATOM   2810  O5'  DT F   9      20.504  21.692  41.560  1.00 41.22           O  
ANISOU 2810  O5'  DT F   9     4869   5504   5287   1137    156    387       O  
ATOM   2811  C5'  DT F   9      21.695  22.273  42.065  1.00 34.68           C  
ANISOU 2811  C5'  DT F   9     4054   4651   4474   1137    158    389       C  
ATOM   2812  C4'  DT F   9      22.006  23.540  41.305  1.00 41.57           C  
ANISOU 2812  C4'  DT F   9     4925   5528   5342   1143    188    403       C  
ATOM   2813  O4'  DT F   9      22.182  23.224  39.893  1.00 45.08           O  
ANISOU 2813  O4'  DT F   9     5344   6002   5781   1141    182    394       O  
ATOM   2814  C3'  DT F   9      20.906  24.595  41.390  1.00 49.38           C  
ANISOU 2814  C3'  DT F   9     5929   6517   6316   1152    224    426       C  
ATOM   2815  O3'  DT F   9      21.471  25.869  41.671  1.00 52.57           O  
ANISOU 2815  O3'  DT F   9     6353   6899   6722   1160    253    442       O  
ATOM   2816  C2'  DT F   9      20.228  24.544  40.018  1.00 42.90           C  
ANISOU 2816  C2'  DT F   9     5085   5734   5480   1154    229    427       C  
ATOM   2817  C1'  DT F   9      21.347  24.047  39.102  1.00 42.52           C  
ANISOU 2817  C1'  DT F   9     5018   5697   5441   1148    210    409       C  
ATOM   2818  N1   DT F   9      20.834  23.236  37.938  1.00 39.56           N  
ANISOU 2818  N1   DT F   9     4618   5358   5056   1145    197    399       N  
ATOM   2819  C2   DT F   9      21.079  23.656  36.649  1.00 39.90           C  
ANISOU 2819  C2   DT F   9     4647   5421   5092   1147    207    401       C  
ATOM   2820  O2   DT F   9      21.716  24.643  36.379  1.00 39.98           O  
ANISOU 2820  O2   DT F   9     4663   5422   5104   1152    226    409       O  
ATOM   2821  N3   DT F   9      20.558  22.857  35.675  1.00 34.90           N  
ANISOU 2821  N3   DT F   9     3992   4820   4448   1144    195    392       N  
ATOM   2822  C4   DT F   9      19.822  21.707  35.848  1.00 40.67           C  
ANISOU 2822  C4   DT F   9     4714   5566   5173   1141    176    383       C  
ATOM   2823  O4   DT F   9      19.400  21.056  34.898  1.00 36.78           O  
ANISOU 2823  O4   DT F   9     4202   5104   4669   1140    169    377       O  
ATOM   2824  C5   DT F   9      19.594  21.319  37.225  1.00 44.86           C  
ANISOU 2824  C5   DT F   9     5260   6073   5711   1139    167    381       C  
ATOM   2825  C7   DT F   9      18.810  20.086  37.544  1.00 52.17           C  
ANISOU 2825  C7   DT F   9     6180   7013   6631   1137    147    371       C  
ATOM   2826  C6   DT F   9      20.102  22.097  38.188  1.00 45.58           C  
ANISOU 2826  C6   DT F   9     5372   6132   5814   1141    177    389       C  
ATOM   2827  P    DA F  10      20.525  27.147  41.884  1.00 50.02           P  
ANISOU 2827  P    DA F  10     6055   6566   6385   1173    297    469       P  
ATOM   2828  OP1  DA F  10      21.202  28.056  42.835  1.00 59.20           O  
ANISOU 2828  OP1  DA F  10     7250   7689   7554   1175    319    480       O  
ATOM   2829  OP2  DA F  10      19.140  26.697  42.136  1.00 49.43           O  
ANISOU 2829  OP2  DA F  10     5978   6504   6299   1173    295    473       O  
ATOM   2830  O5'  DA F  10      20.558  27.833  40.459  1.00 52.94           O  
ANISOU 2830  O5'  DA F  10     6412   6962   6743   1180    317    475       O  
ATOM   2831  C5'  DA F  10      21.744  27.793  39.722  1.00 47.12           C  
ANISOU 2831  C5'  DA F  10     5660   6230   6014   1176    307    464       C  
ATOM   2832  C4'  DA F  10      21.639  28.675  38.506  1.00 47.79           C  
ANISOU 2832  C4'  DA F  10     5741   6333   6085   1185    333    475       C  
ATOM   2833  O4'  DA F  10      21.239  27.900  37.354  1.00 40.70           O  
ANISOU 2833  O4'  DA F  10     4813   5472   5180   1180    313    464       O  
ATOM   2834  C3'  DA F  10      20.638  29.802  38.615  1.00 47.22           C  
ANISOU 2834  C3'  DA F  10     5692   6255   5994   1200    374    502       C  
ATOM   2835  O3'  DA F  10      21.125  30.855  37.893  1.00 46.43           O  
ANISOU 2835  O3'  DA F  10     5600   6153   5887   1210    403    514       O  
ATOM   2836  C2'  DA F  10      19.384  29.221  37.969  1.00 42.82           C  
ANISOU 2836  C2'  DA F  10     5113   5735   5422   1200    364    503       C  
ATOM   2837  C1'  DA F  10      19.974  28.331  36.891  1.00 41.36           C  
ANISOU 2837  C1'  DA F  10     4897   5576   5242   1189    333    481       C  
ATOM   2838  N9   DA F  10      19.192  27.144  36.628  1.00 31.76           N  
ANISOU 2838  N9   DA F  10     3657   4388   4022   1181    305    470       N  
ATOM   2839  C8   DA F  10      18.645  26.294  37.550  1.00 31.96           C  
ANISOU 2839  C8   DA F  10     3682   4409   4051   1175    287    463       C  
ATOM   2840  N7   DA F  10      18.004  25.278  37.016  1.00 40.66           N  
ANISOU 2840  N7   DA F  10     4761   5543   5146   1170    266    452       N  
ATOM   2841  C5   DA F  10      18.158  25.474  35.649  1.00 34.01           C  
ANISOU 2841  C5   DA F  10     3901   4726   4293   1172    270    453       C  
ATOM   2842  C6   DA F  10      17.720  24.746  34.536  1.00 46.07           C  
ANISOU 2842  C6   DA F  10     5402   6292   5809   1169    257    446       C  
ATOM   2843  N6   DA F  10      16.999  23.626  34.638  1.00 41.84           N  
ANISOU 2843  N6   DA F  10     4851   5778   5267   1163    237    437       N  
ATOM   2844  N1   DA F  10      18.046  25.218  33.304  1.00 45.91           N  
ANISOU 2844  N1   DA F  10     5373   6289   5781   1172    266    450       N  
ATOM   2845  C2   DA F  10      18.765  26.345  33.217  1.00 44.02           C  
ANISOU 2845  C2   DA F  10     5150   6029   5547   1179    288    460       C  
ATOM   2846  N3   DA F  10      19.248  27.112  34.198  1.00 30.92           N  
ANISOU 2846  N3   DA F  10     3516   4334   3898   1183    304    467       N  
ATOM   2847  C4   DA F  10      18.902  26.615  35.399  1.00 36.13           C  
ANISOU 2847  C4   DA F  10     4185   4978   4565   1179    293    463       C  
TER    2848       DA F  10                                                      
ATOM   2849  P    DT G   1      14.775  22.754  23.915  1.00 67.96           P  
ANISOU 2849  P    DT G   1     7993   9402   8428   1182    245    466       P  
ATOM   2850  OP1  DT G   1      14.721  23.381  22.571  1.00 76.41           O  
ANISOU 2850  OP1  DT G   1     9054  10499   9480   1190    257    480       O  
ATOM   2851  OP2  DT G   1      15.421  21.451  24.180  1.00 75.28           O  
ANISOU 2851  OP2  DT G   1     8916  10316   9372   1169    221    436       O  
ATOM   2852  O5'  DT G   1      15.375  23.795  24.970  1.00 41.67           O  
ANISOU 2852  O5'  DT G   1     4695   6017   5121   1186    259    471       O  
ATOM   2853  C5'  DT G   1      15.492  25.153  24.626  1.00 38.91           C  
ANISOU 2853  C5'  DT G   1     4360   5659   4767   1199    285    492       C  
ATOM   2854  C4'  DT G   1      16.604  25.817  25.408  1.00 36.30           C  
ANISOU 2854  C4'  DT G   1     4057   5272   4462   1198    292    485       C  
ATOM   2855  O4'  DT G   1      16.450  25.554  26.822  1.00 33.37           O  
ANISOU 2855  O4'  DT G   1     3698   4876   4105   1193    287    480       O  
ATOM   2856  C3'  DT G   1      18.023  25.371  25.040  1.00 28.21           C  
ANISOU 2856  C3'  DT G   1     3033   4225   3461   1188    278    460       C  
ATOM   2857  O3'  DT G   1      18.804  26.530  24.859  1.00 41.24           O  
ANISOU 2857  O3'  DT G   1     4702   5851   5119   1195    298    468       O  
ATOM   2858  C2'  DT G   1      18.476  24.563  26.270  1.00 34.31           C  
ANISOU 2858  C2'  DT G   1     3813   4967   4257   1176    259    440       C  
ATOM   2859  C1'  DT G   1      17.711  25.276  27.375  1.00 31.19           C  
ANISOU 2859  C1'  DT G   1     3433   4559   3857   1183    275    459       C  
ATOM   2860  N1   DT G   1      17.479  24.495  28.651  1.00 36.84           N  
ANISOU 2860  N1   DT G   1     4154   5260   4585   1176    259    448       N  
ATOM   2861  C2   DT G   1      17.831  25.064  29.856  1.00 37.01           C  
ANISOU 2861  C2   DT G   1     4199   5242   4621   1177    267    451       C  
ATOM   2862  O2   DT G   1      18.400  26.136  29.950  1.00 31.53           O  
ANISOU 2862  O2   DT G   1     3523   4525   3932   1183    287    461       O  
ATOM   2863  N3   DT G   1      17.526  24.316  30.962  1.00 35.45           N  
ANISOU 2863  N3   DT G   1     4004   5033   4431   1170    252    443       N  
ATOM   2864  C4   DT G   1      16.902  23.092  30.996  1.00 42.29           C  
ANISOU 2864  C4   DT G   1     4853   5924   5291   1164    231    431       C  
ATOM   2865  O4   DT G   1      16.672  22.504  32.060  1.00 37.98           O  
ANISOU 2865  O4   DT G   1     4314   5364   4753   1160    219    425       O  
ATOM   2866  C5   DT G   1      16.531  22.554  29.700  1.00 36.67           C  
ANISOU 2866  C5   DT G   1     4117   5255   4562   1164    225    429       C  
ATOM   2867  C7   DT G   1      15.844  21.227  29.600  1.00 43.42           C  
ANISOU 2867  C7   DT G   1     4950   6141   5405   1158    205    418       C  
ATOM   2868  C6   DT G   1      16.816  23.282  28.605  1.00 40.38           C  
ANISOU 2868  C6   DT G   1     4582   5735   5024   1169    238    438       C  
ATOM   2869  P    DA G   2      20.239  26.474  24.153  1.00 37.65           P  
ANISOU 2869  P    DA G   2     4245   5379   4681   1189    293    450       P  
ATOM   2870  OP1  DA G   2      20.273  27.658  23.267  1.00 37.69           O  
ANISOU 2870  OP1  DA G   2     4257   5392   4672   1203    318    469       O  
ATOM   2871  OP2  DA G   2      20.537  25.127  23.632  1.00 36.78           O  
ANISOU 2871  OP2  DA G   2     4114   5283   4576   1177    266    427       O  
ATOM   2872  O5'  DA G   2      21.258  26.717  25.365  1.00 35.46           O  
ANISOU 2872  O5'  DA G   2     3987   5056   4430   1184    292    440       O  
ATOM   2873  C5'  DA G   2      21.232  27.937  26.047  1.00 40.80           C  
ANISOU 2873  C5'  DA G   2     4688   5710   5106   1194    318    459       C  
ATOM   2874  C4'  DA G   2      22.072  27.872  27.307  1.00 44.75           C  
ANISOU 2874  C4'  DA G   2     5202   6173   5629   1187    312    447       C  
ATOM   2875  O4'  DA G   2      21.446  26.998  28.269  1.00 42.42           O  
ANISOU 2875  O4'  DA G   2     4904   5876   5338   1180    293    441       O  
ATOM   2876  C3'  DA G   2      23.496  27.348  27.110  1.00 44.84           C  
ANISOU 2876  C3'  DA G   2     5204   6170   5661   1177    294    424       C  
ATOM   2877  O3'  DA G   2      24.407  28.305  27.611  1.00 41.99           O  
ANISOU 2877  O3'  DA G   2     4861   5782   5311   1181    312    429       O  
ATOM   2878  C2'  DA G   2      23.528  26.039  27.915  1.00 45.09           C  
ANISOU 2878  C2'  DA G   2     5229   6196   5708   1164    263    405       C  
ATOM   2879  C1'  DA G   2      22.438  26.281  28.943  1.00 43.78           C  
ANISOU 2879  C1'  DA G   2     5075   6025   5533   1169    272    419       C  
ATOM   2880  N9   DA G   2      21.832  25.060  29.447  1.00 37.08           N  
ANISOU 2880  N9   DA G   2     4218   5185   4687   1161    247    408       N  
ATOM   2881  C8   DA G   2      21.317  24.033  28.710  1.00 35.92           C  
ANISOU 2881  C8   DA G   2     4051   5068   4531   1156    231    398       C  
ATOM   2882  N7   DA G   2      20.818  23.066  29.431  1.00 35.62           N  
ANISOU 2882  N7   DA G   2     4009   5030   4493   1151    213    390       N  
ATOM   2883  C5   DA G   2      21.018  23.498  30.737  1.00 32.40           C  
ANISOU 2883  C5   DA G   2     3621   4591   4098   1151    217    394       C  
ATOM   2884  C6   DA G   2      20.705  22.925  31.976  1.00 35.99           C  
ANISOU 2884  C6   DA G   2     4084   5029   4560   1147    205    389       C  
ATOM   2885  N6   DA G   2      20.103  21.734  32.100  1.00 40.06           N  
ANISOU 2885  N6   DA G   2     4589   5560   5070   1143    185    378       N  
ATOM   2886  N1   DA G   2      21.037  23.621  33.093  1.00 44.12           N  
ANISOU 2886  N1   DA G   2     5135   6028   5601   1149    214    396       N  
ATOM   2887  C2   DA G   2      21.643  24.811  32.954  1.00 46.68           C  
ANISOU 2887  C2   DA G   2     5470   6338   5927   1156    236    408       C  
ATOM   2888  N3   DA G   2      21.983  25.453  31.833  1.00 33.30           N  
ANISOU 2888  N3   DA G   2     3770   4656   4226   1160    251    413       N  
ATOM   2889  C4   DA G   2      21.639  24.730  30.754  1.00 30.35           C  
ANISOU 2889  C4   DA G   2     3376   4313   3843   1157    239    405       C  
ATOM   2890  P    DT G   3      25.984  28.009  27.631  1.00 49.02           P  
ANISOU 2890  P    DT G   3     5744   6657   6223   1173    299    409       P  
ATOM   2891  OP1  DT G   3      26.663  29.294  27.357  1.00 51.02           O  
ANISOU 2891  OP1  DT G   3     6011   6901   6475   1184    329    421       O  
ATOM   2892  OP2  DT G   3      26.277  26.813  26.810  1.00 42.07           O  
ANISOU 2892  OP2  DT G   3     4841   5795   5350   1163    272    389       O  
ATOM   2893  O5'  DT G   3      26.234  27.664  29.170  1.00 42.85           O  
ANISOU 2893  O5'  DT G   3     4971   5851   5458   1168    287    404       O  
ATOM   2894  C5'  DT G   3      25.642  28.490  30.145  1.00 41.13           C  
ANISOU 2894  C5'  DT G   3     4777   5616   5234   1176    308    423       C  
ATOM   2895  C4'  DT G   3      26.004  28.034  31.541  1.00 50.25           C  
ANISOU 2895  C4'  DT G   3     5938   6749   6405   1170    293    415       C  
ATOM   2896  O4'  DT G   3      25.184  26.896  31.926  1.00 48.62           O  
ANISOU 2896  O4'  DT G   3     5724   6550   6199   1162    268    406       O  
ATOM   2897  C3'  DT G   3      27.453  27.590  31.726  1.00 52.03           C  
ANISOU 2897  C3'  DT G   3     6152   6966   6650   1163    275    398       C  
ATOM   2898  O3'  DT G   3      27.872  28.015  33.007  1.00 63.63           O  
ANISOU 2898  O3'  DT G   3     7638   8412   8129   1166    282    405       O  
ATOM   2899  C2'  DT G   3      27.346  26.065  31.638  1.00 43.95           C  
ANISOU 2899  C2'  DT G   3     5111   5954   5635   1151    238    378       C  
ATOM   2900  C1'  DT G   3      26.025  25.844  32.356  1.00 39.01           C  
ANISOU 2900  C1'  DT G   3     4496   5325   4999   1152    237    386       C  
ATOM   2901  N1   DT G   3      25.351  24.542  32.057  1.00 35.45           N  
ANISOU 2901  N1   DT G   3     4031   4891   4546   1145    212    372       N  
ATOM   2902  C2   DT G   3      24.855  23.800  33.104  1.00 35.67           C  
ANISOU 2902  C2   DT G   3     4066   4910   4578   1141    196    368       C  
ATOM   2903  O2   DT G   3      24.940  24.145  34.257  1.00 42.40           O  
ANISOU 2903  O2   DT G   3     4933   5741   5437   1142    199    374       O  
ATOM   2904  N3   DT G   3      24.244  22.632  32.749  1.00 34.23           N  
ANISOU 2904  N3   DT G   3     3870   4744   4390   1136    177    356       N  
ATOM   2905  C4   DT G   3      24.073  22.141  31.478  1.00 37.85           C  
ANISOU 2905  C4   DT G   3     4312   5230   4840   1135    173    350       C  
ATOM   2906  O4   DT G   3      23.503  21.079  31.263  1.00 33.79           O  
ANISOU 2906  O4   DT G   3     3789   4731   4319   1133    158    340       O  
ATOM   2907  C5   DT G   3      24.623  22.960  30.413  1.00 39.81           C  
ANISOU 2907  C5   DT G   3     4554   5486   5085   1139    189    355       C  
ATOM   2908  C7   DT G   3      24.502  22.512  28.985  1.00 41.97           C  
ANISOU 2908  C7   DT G   3     4811   5788   5348   1139    187    349       C  
ATOM   2909  C6   DT G   3      25.225  24.115  30.750  1.00 31.42           C  
ANISOU 2909  C6   DT G   3     3504   4407   4028   1143    208    365       C  
ATOM   2910  P    DA G   4      29.425  28.096  33.409  1.00 75.38           P  
ANISOU 2910  P    DA G   4     9118   9891   9632   1165    276    398       P  
ATOM   2911  OP1  DA G   4      29.648  29.491  33.857  1.00 74.93           O  
ANISOU 2911  OP1  DA G   4     9083   9818   9570   1178    315    418       O  
ATOM   2912  OP2  DA G   4      30.265  27.520  32.334  1.00 73.74           O  
ANISOU 2912  OP2  DA G   4     8884   9703   9431   1159    258    381       O  
ATOM   2913  O5'  DA G   4      29.500  27.138  34.691  1.00 56.30           O  
ANISOU 2913  O5'  DA G   4     6701   7463   7229   1158    246    389       O  
ATOM   2914  C5'  DA G   4      28.534  27.291  35.723  1.00 50.36           C  
ANISOU 2914  C5'  DA G   4     5970   6693   6471   1160    253    401       C  
ATOM   2915  C4'  DA G   4      28.582  26.139  36.710  1.00 53.82           C  
ANISOU 2915  C4'  DA G   4     6405   7123   6921   1152    219    388       C  
ATOM   2916  O4'  DA G   4      27.888  24.981  36.180  1.00 51.75           O  
ANISOU 2916  O4'  DA G   4     6131   6876   6657   1144    195    374       O  
ATOM   2917  C3'  DA G   4      29.971  25.657  37.101  1.00 58.03           C  
ANISOU 2917  C3'  DA G   4     6923   7657   7469   1148    196    378       C  
ATOM   2918  O3'  DA G   4      29.951  25.355  38.477  1.00 69.34           O  
ANISOU 2918  O3'  DA G   4     8370   9068   8906   1139    182    378       O  
ATOM   2919  C2'  DA G   4      30.162  24.406  36.235  1.00 52.64           C  
ANISOU 2919  C2'  DA G   4     6217   6991   6790   1140    167    356       C  
ATOM   2920  C1'  DA G   4      28.745  23.857  36.175  1.00 51.85           C  
ANISOU 2920  C1'  DA G   4     6127   6893   6682   1137    163    355       C  
ATOM   2921  N9   DA G   4      28.439  23.112  34.966  1.00 42.96           N  
ANISOU 2921  N9   DA G   4     4986   5787   5552   1133    154    342       N  
ATOM   2922  C8   DA G   4      28.714  23.483  33.680  1.00 44.62           C  
ANISOU 2922  C8   DA G   4     5183   6014   5757   1134    166    341       C  
ATOM   2923  N7   DA G   4      28.277  22.636  32.779  1.00 45.82           N  
ANISOU 2923  N7   DA G   4     5324   6182   5904   1131    155    330       N  
ATOM   2924  C5   DA G   4      27.644  21.661  33.525  1.00 37.33           C  
ANISOU 2924  C5   DA G   4     4254   5101   4829   1128    136    324       C  
ATOM   2925  C6   DA G   4      26.977  20.494  33.158  1.00 35.31           C  
ANISOU 2925  C6   DA G   4     3992   4857   4566   1125    121    313       C  
ATOM   2926  N6   DA G   4      26.829  20.106  31.886  1.00 32.08           N  
ANISOU 2926  N6   DA G   4     3569   4469   4149   1125    122    307       N  
ATOM   2927  N1   DA G   4      26.468  19.725  34.148  1.00 47.91           N  
ANISOU 2927  N1   DA G   4     5597   6442   6164   1124    106    309       N  
ATOM   2928  C2   DA G   4      26.636  20.117  35.419  1.00 47.05           C  
ANISOU 2928  C2   DA G   4     5502   6311   6062   1124    105    316       C  
ATOM   2929  N3   DA G   4      27.235  21.213  35.885  1.00 39.93           N  
ANISOU 2929  N3   DA G   4     4608   5398   5167   1126    119    327       N  
ATOM   2930  C4   DA G   4      27.734  21.939  34.877  1.00 41.97           C  
ANISOU 2930  C4   DA G   4     4856   5667   5422   1128    134    331       C  
ATOM   2931  P    DT G   5      31.262  24.847  39.245  1.00 57.33           P  
ANISOU 2931  P    DT G   5     6845   7541   7396   1114    153    365       P  
ATOM   2932  OP1  DT G   5      31.347  25.648  40.488  1.00 62.83           O  
ANISOU 2932  OP1  DT G   5     7575   8210   8087   1084    163    371       O  
ATOM   2933  OP2  DT G   5      32.407  24.789  38.312  1.00 57.61           O  
ANISOU 2933  OP2  DT G   5     6852   7600   7437   1119    149    358       O  
ATOM   2934  O5'  DT G   5      30.864  23.357  39.635  1.00 61.92           O  
ANISOU 2934  O5'  DT G   5     7419   8124   7984   1121    119    353       O  
ATOM   2935  C5'  DT G   5      29.561  23.099  40.130  1.00 48.66           C  
ANISOU 2935  C5'  DT G   5     5757   6433   6299   1125    121    357       C  
ATOM   2936  C4'  DT G   5      29.381  21.621  40.404  1.00 50.88           C  
ANISOU 2936  C4'  DT G   5     6030   6716   6585   1129     88    343       C  
ATOM   2937  O4'  DT G   5      29.040  20.930  39.179  1.00 49.09           O  
ANISOU 2937  O4'  DT G   5     5789   6507   6355   1127     83    330       O  
ATOM   2938  C3'  DT G   5      30.612  20.920  40.970  1.00 47.48           C  
ANISOU 2938  C3'  DT G   5     5594   6282   6166   1117     59    332       C  
ATOM   2939  O3'  DT G   5      30.204  20.119  42.085  1.00 52.11           O  
ANISOU 2939  O3'  DT G   5     6197   6848   6752   1106     38    326       O  
ATOM   2940  C2'  DT G   5      31.147  20.093  39.781  1.00 43.24           C  
ANISOU 2940  C2'  DT G   5     5030   5767   5633   1127     47    319       C  
ATOM   2941  C1'  DT G   5      29.868  19.799  39.009  1.00 48.66           C  
ANISOU 2941  C1'  DT G   5     5721   6457   6309   1125     57    314       C  
ATOM   2942  N1   DT G   5      30.019  19.563  37.505  1.00 46.21           N  
ANISOU 2942  N1   DT G   5     5393   6167   5996   1124     61    304       N  
ATOM   2943  C2   DT G   5      29.333  18.505  36.924  1.00 45.05           C  
ANISOU 2943  C2   DT G   5     5245   6027   5844   1122     52    292       C  
ATOM   2944  O2   DT G   5      28.654  17.721  37.558  1.00 58.49           O  
ANISOU 2944  O2   DT G   5     6959   7722   7543   1122     40    288       O  
ATOM   2945  N3   DT G   5      29.481  18.389  35.571  1.00 43.43           N  
ANISOU 2945  N3   DT G   5     5026   5841   5636   1122     58    286       N  
ATOM   2946  C4   DT G   5      30.204  19.204  34.742  1.00 42.96           C  
ANISOU 2946  C4   DT G   5     4954   5791   5578   1123     72    289       C  
ATOM   2947  O4   DT G   5      30.262  19.009  33.526  1.00 43.33           O  
ANISOU 2947  O4   DT G   5     4989   5853   5621   1123     77    283       O  
ATOM   2948  C5   DT G   5      30.889  20.309  35.396  1.00 41.60           C  
ANISOU 2948  C5   DT G   5     4783   5611   5411   1125     82    301       C  
ATOM   2949  C7   DT G   5      31.715  21.265  34.580  1.00 53.24           C  
ANISOU 2949  C7   DT G   5     6244   7097   6886   1127    100    306       C  
ATOM   2950  C6   DT G   5      30.759  20.440  36.731  1.00 44.46           C  
ANISOU 2950  C6   DT G   5     5160   5957   5777   1125     77    309       C  
ATOM   2951  P    DA G   6      31.266  19.285  42.949  1.00 53.55           P  
ANISOU 2951  P    DA G   6     6380   7024   6943   1094      6    317       P  
ATOM   2952  OP1  DA G   6      30.796  19.272  44.351  1.00 59.32           O  
ANISOU 2952  OP1  DA G   6     7141   7728   7672   1072     -1    318       O  
ATOM   2953  OP2  DA G   6      32.634  19.747  42.616  1.00 57.16           O  
ANISOU 2953  OP2  DA G   6     6817   7497   7406   1090      5    318       O  
ATOM   2954  O5'  DA G   6      31.136  17.810  42.364  1.00 47.86           O  
ANISOU 2954  O5'  DA G   6     5645   6314   6225   1117    -13    304       O  
ATOM   2955  C5'  DA G   6      29.892  17.160  42.408  1.00 42.84           C  
ANISOU 2955  C5'  DA G   6     5023   5671   5583   1123    -14    299       C  
ATOM   2956  C4'  DA G   6      29.955  15.844  41.681  1.00 36.90           C  
ANISOU 2956  C4'  DA G   6     4263   4927   4831   1127    -29    283       C  
ATOM   2957  O4'  DA G   6      30.164  16.079  40.267  1.00 33.67           O  
ANISOU 2957  O4'  DA G   6     3835   4538   4421   1127    -15    278       O  
ATOM   2958  C3'  DA G   6      31.084  14.905  42.116  1.00 37.66           C  
ANISOU 2958  C3'  DA G   6     4356   5019   4936   1132    -54    275       C  
ATOM   2959  O3'  DA G   6      30.584  13.603  42.118  1.00 39.03           O  
ANISOU 2959  O3'  DA G   6     4541   5184   5104   1136    -66    262       O  
ATOM   2960  C2'  DA G   6      32.115  15.079  41.007  1.00 38.83           C  
ANISOU 2960  C2'  DA G   6     4479   5186   5090   1133    -49    272       C  
ATOM   2961  C1'  DA G   6      31.190  15.234  39.820  1.00 36.34           C  
ANISOU 2961  C1'  DA G   6     4161   4882   4766   1131    -30    268       C  
ATOM   2962  N9   DA G   6      31.790  15.873  38.674  1.00 36.99           N  
ANISOU 2962  N9   DA G   6     4223   4982   4851   1130    -16    268       N  
ATOM   2963  C8   DA G   6      32.592  16.983  38.669  1.00 47.29           C  
ANISOU 2963  C8   DA G   6     5514   6293   6159   1129     -6    279       C  
ATOM   2964  N7   DA G   6      32.966  17.359  37.471  1.00 40.34           N  
ANISOU 2964  N7   DA G   6     4619   5430   5280   1128      7    276       N  
ATOM   2965  C5   DA G   6      32.335  16.451  36.643  1.00 43.62           C  
ANISOU 2965  C5   DA G   6     5036   5848   5689   1129      6    265       C  
ATOM   2966  C6   DA G   6      32.320  16.316  35.263  1.00 44.07           C  
ANISOU 2966  C6   DA G   6     5083   5920   5743   1129     16    258       C  
ATOM   2967  N6   DA G   6      32.988  17.145  34.458  1.00 34.14           N  
ANISOU 2967  N6   DA G   6     3809   4675   4488   1128     29    261       N  
ATOM   2968  N1   DA G   6      31.593  15.293  34.734  1.00 53.91           N  
ANISOU 2968  N1   DA G   6     6334   7168   6981   1132     12    248       N  
ATOM   2969  C2   DA G   6      30.925  14.472  35.568  1.00 51.09           C  
ANISOU 2969  C2   DA G   6     5993   6799   6620   1134      0    245       C  
ATOM   2970  N3   DA G   6      30.857  14.508  36.903  1.00 28.13           N  
ANISOU 2970  N3   DA G   6     3097   3874   3715   1133    -11    250       N  
ATOM   2971  C4   DA G   6      31.595  15.534  37.376  1.00 32.72           C  
ANISOU 2971  C4   DA G   6     3673   4455   4306   1130     -7    260       C  
ATOM   2972  P    DT G   7      31.350  12.438  42.890  1.00 42.34           P  
ANISOU 2972  P    DT G   7     4969   5589   5527   1144    -91    256       P  
ATOM   2973  OP1  DT G   7      30.332  11.861  43.803  1.00 39.12           O  
ANISOU 2973  OP1  DT G   7     4590   5163   5113   1145    -99    253       O  
ATOM   2974  OP2  DT G   7      32.638  12.941  43.395  1.00 38.68           O  
ANISOU 2974  OP2  DT G   7     4492   5131   5073   1145   -101    265       O  
ATOM   2975  O5'  DT G   7      31.689  11.385  41.733  1.00 34.88           O  
ANISOU 2975  O5'  DT G   7     4017   4654   4582   1153    -92    242       O  
ATOM   2976  C5'  DT G   7      30.663  10.928  40.910  1.00 38.22           C  
ANISOU 2976  C5'  DT G   7     4446   5082   4995   1154    -80    233       C  
ATOM   2977  C4'  DT G   7      31.193  10.320  39.626  1.00 40.75           C  
ANISOU 2977  C4'  DT G   7     4753   5416   5315   1161    -75    224       C  
ATOM   2978  O4'  DT G   7      31.634  11.341  38.708  1.00 41.69           O  
ANISOU 2978  O4'  DT G   7     4849   5554   5439   1154    -61    229       O  
ATOM   2979  C3'  DT G   7      32.354   9.321  39.758  1.00 41.67           C  
ANISOU 2979  C3'  DT G   7     4871   5524   5438   1174    -89    219       C  
ATOM   2980  O3'  DT G   7      31.896   8.034  39.335  1.00 40.48           O  
ANISOU 2980  O3'  DT G   7     4737   5367   5276   1188    -88    207       O  
ATOM   2981  C2'  DT G   7      33.428   9.888  38.808  1.00 43.79           C  
ANISOU 2981  C2'  DT G   7     5112   5811   5716   1172    -81    222       C  
ATOM   2982  C1'  DT G   7      32.593  10.752  37.873  1.00 40.33           C  
ANISOU 2982  C1'  DT G   7     4665   5388   5272   1163    -62    223       C  
ATOM   2983  N1   DT G   7      33.345  11.840  37.167  1.00 38.83           N  
ANISOU 2983  N1   DT G   7     4451   5215   5090   1156    -51    229       N  
ATOM   2984  C2   DT G   7      33.302  11.900  35.788  1.00 38.18           C  
ANISOU 2984  C2   DT G   7     4356   5147   5003   1156    -36    224       C  
ATOM   2985  O2   DT G   7      32.708  11.091  35.099  1.00 34.72           O  
ANISOU 2985  O2   DT G   7     3925   4712   4555   1162    -32    215       O  
ATOM   2986  N3   DT G   7      33.996  12.942  35.233  1.00 39.70           N  
ANISOU 2986  N3   DT G   7     4529   5354   5203   1150    -26    230       N  
ATOM   2987  C4   DT G   7      34.702  13.919  35.899  1.00 45.59           C  
ANISOU 2987  C4   DT G   7     5265   6101   5956   1146    -28    240       C  
ATOM   2988  O4   DT G   7      35.297  14.822  35.296  1.00 36.07           O  
ANISOU 2988  O4   DT G   7     4042   4909   4753   1142    -17    244       O  
ATOM   2989  C5   DT G   7      34.694  13.806  37.353  1.00 46.38           C  
ANISOU 2989  C5   DT G   7     5377   6187   6058   1146    -44    246       C  
ATOM   2990  C7   DT G   7      35.430  14.804  38.200  1.00 52.94           C  
ANISOU 2990  C7   DT G   7     6198   7022   6895   1143    -47    258       C  
ATOM   2991  C6   DT G   7      34.016  12.788  37.903  1.00 39.10           C  
ANISOU 2991  C6   DT G   7     4476   5250   5132   1150    -55    240       C  
ATOM   2992  P    DA G   8      32.878   6.756  39.291  1.00 45.31           P  
ANISOU 2992  P    DA G   8     5358   5967   5889   1207    -96    200       P  
ATOM   2993  OP1  DA G   8      32.029   5.572  39.556  1.00 40.77           O  
ANISOU 2993  OP1  DA G   8     4815   5376   5299   1220    -98    190       O  
ATOM   2994  OP2  DA G   8      34.079   7.045  40.096  1.00 43.40           O  
ANISOU 2994  OP2  DA G   8     5106   5723   5662   1206   -110    210       O  
ATOM   2995  O5'  DA G   8      33.217   6.610  37.737  1.00 42.98           O  
ANISOU 2995  O5'  DA G   8     5047   5690   5593   1212    -80    194       O  
ATOM   2996  C5'  DA G   8      32.180   6.166  36.871  1.00 38.77           C  
ANISOU 2996  C5'  DA G   8     4522   5163   5043   1217    -67    185       C  
ATOM   2997  C4'  DA G   8      32.607   6.147  35.416  1.00 41.37           C  
ANISOU 2997  C4'  DA G   8     4835   5511   5373   1222    -52    181       C  
ATOM   2998  O4'  DA G   8      33.116   7.446  35.019  1.00 45.72           O  
ANISOU 2998  O4'  DA G   8     5358   6078   5937   1205    -48    189       O  
ATOM   2999  C3'  DA G   8      33.689   5.138  35.078  1.00 45.66           C  
ANISOU 2999  C3'  DA G   8     5384   6045   5920   1241    -52    176       C  
ATOM   3000  O3'  DA G   8      33.403   4.567  33.822  1.00 49.44           O  
ANISOU 3000  O3'  DA G   8     5865   6533   6386   1253    -36    166       O  
ATOM   3001  C2'  DA G   8      34.962   5.982  35.049  1.00 43.56           C  
ANISOU 3001  C2'  DA G   8     5090   5788   5673   1233    -56    186       C  
ATOM   3002  C1'  DA G   8      34.447   7.329  34.556  1.00 42.51           C  
ANISOU 3002  C1'  DA G   8     4937   5674   5541   1212    -47    190       C  
ATOM   3003  N9   DA G   8      35.198   8.445  35.097  1.00 40.29           N  
ANISOU 3003  N9   DA G   8     4637   5398   5275   1199    -54    201       N  
ATOM   3004  C8   DA G   8      35.465   8.682  36.413  1.00 48.74           C  
ANISOU 3004  C8   DA G   8     5710   6458   6351   1195    -69    209       C  
ATOM   3005  N7   DA G   8      36.163   9.765  36.630  1.00 39.03           N  
ANISOU 3005  N7   DA G   8     4460   5240   5132   1186    -71    218       N  
ATOM   3006  C5   DA G   8      36.369  10.275  35.368  1.00 40.37           C  
ANISOU 3006  C5   DA G   8     4612   5426   5302   1182    -55    216       C  
ATOM   3007  C6   DA G   8      37.041  11.405  34.929  1.00 34.59           C  
ANISOU 3007  C6   DA G   8     3856   4710   4577   1174    -48    222       C  
ATOM   3008  N6   DA G   8      37.651  12.253  35.763  1.00 35.55           N  
ANISOU 3008  N6   DA G   8     3966   4838   4705   1168    -55    233       N  
ATOM   3009  N1   DA G   8      37.065  11.644  33.598  1.00 54.71           N  
ANISOU 3009  N1   DA G   8     6393   7271   7123   1173    -32    218       N  
ATOM   3010  C2   DA G   8      36.450  10.779  32.780  1.00 52.32           C  
ANISOU 3010  C2   DA G   8     6103   6966   6812   1180    -25    208       C  
ATOM   3011  N3   DA G   8      35.779   9.669  33.086  1.00 34.11           N  
ANISOU 3011  N3   DA G   8     3817   4646   4496   1189    -30    202       N  
ATOM   3012  C4   DA G   8      35.777   9.475  34.407  1.00 35.38           C  
ANISOU 3012  C4   DA G   8     3989   4793   4660   1190    -45    206       C  
ATOM   3013  P    DT G   9      34.180   3.251  33.336  1.00 76.07           P  
ANISOU 3013  P    DT G   9     9255   9894   9755   1280    -29    159       P  
ATOM   3014  OP1  DT G   9      33.167   2.388  32.682  1.00 79.85           O  
ANISOU 3014  OP1  DT G   9     9756  10374  10211   1295    -16    146       O  
ATOM   3015  OP2  DT G   9      34.990   2.728  34.460  1.00 66.51           O  
ANISOU 3015  OP2  DT G   9     8056   8662   8553   1289    -43    164       O  
ATOM   3016  O5'  DT G   9      35.172   3.817  32.216  1.00 52.62           O  
ANISOU 3016  O5'  DT G   9     6255   6942   6797   1276    -19    162       O  
ATOM   3017  C5'  DT G   9      34.647   4.631  31.186  1.00 52.06           C  
ANISOU 3017  C5'  DT G   9     6166   6894   6722   1262     -8    161       C  
ATOM   3018  C4'  DT G   9      35.750   5.283  30.377  1.00 56.53           C  
ANISOU 3018  C4'  DT G   9     6704   7472   7302   1257     -2    166       C  
ATOM   3019  O4'  DT G   9      36.326   6.384  31.107  1.00 54.61           O  
ANISOU 3019  O4'  DT G   9     6441   7232   7076   1240    -14    176       O  
ATOM   3020  C3'  DT G   9      36.912   4.370  29.980  1.00 57.70           C  
ANISOU 3020  C3'  DT G   9     6856   7612   7456   1279      3    163       C  
ATOM   3021  O3'  DT G   9      36.999   4.384  28.558  1.00 67.68           O  
ANISOU 3021  O3'  DT G   9     8111   8891   8715   1282     20    158       O  
ATOM   3022  C2'  DT G   9      38.141   5.010  30.665  1.00 48.81           C  
ANISOU 3022  C2'  DT G   9     5708   6487   6350   1271    -10    174       C  
ATOM   3023  C1'  DT G   9      37.692   6.457  30.803  1.00 46.22           C  
ANISOU 3023  C1'  DT G   9     5360   6173   6026   1245    -13    180       C  
ATOM   3024  N1   DT G   9      38.344   7.238  31.892  1.00 38.12           N  
ANISOU 3024  N1   DT G   9     4320   5148   5014   1234    -29    191       N  
ATOM   3025  C2   DT G   9      38.969   8.428  31.585  1.00 38.30           C  
ANISOU 3025  C2   DT G   9     4316   5188   5047   1221    -26    197       C  
ATOM   3026  O2   DT G   9      39.054   8.865  30.453  1.00 39.89           O  
ANISOU 3026  O2   DT G   9     4506   5403   5248   1217    -12    194       O  
ATOM   3027  N3   DT G   9      39.503   9.090  32.656  1.00 36.67           N  
ANISOU 3027  N3   DT G   9     4100   4984   4849   1213    -39    206       N  
ATOM   3028  C4   DT G   9      39.461   8.704  33.977  1.00 36.22           C  
ANISOU 3028  C4   DT G   9     4055   4915   4793   1216    -56    211       C  
ATOM   3029  O4   DT G   9      39.965   9.376  34.873  1.00 39.76           O  
ANISOU 3029  O4   DT G   9     4491   5369   5248   1209    -67    221       O  
ATOM   3030  C5   DT G   9      38.788   7.457  34.235  1.00 41.92           C  
ANISOU 3030  C5   DT G   9     4805   5617   5505   1230    -58    204       C  
ATOM   3031  C7   DT G   9      38.698   6.936  35.639  1.00 45.98           C  
ANISOU 3031  C7   DT G   9     5337   6115   6019   1235    -76    208       C  
ATOM   3032  C6   DT G   9      38.255   6.795  33.193  1.00 38.70           C  
ANISOU 3032  C6   DT G   9     4409   5206   5088   1238    -44    194       C  
ATOM   3033  P    DA G  10      38.116   3.552  27.759  1.00 60.54           P  
ANISOU 3033  P    DA G  10     7207   7982   7813   1305     32    155       P  
ATOM   3034  OP1  DA G  10      37.460   3.053  26.525  1.00 65.41           O  
ANISOU 3034  OP1  DA G  10     7836   8606   8412   1315     52    144       O  
ATOM   3035  OP2  DA G  10      38.789   2.601  28.676  1.00 51.79           O  
ANISOU 3035  OP2  DA G  10     6117   6852   6709   1324     24    157       O  
ATOM   3036  O5'  DA G  10      39.133   4.695  27.322  1.00 53.26           O  
ANISOU 3036  O5'  DA G  10     6250   7077   6910   1289     31    162       O  
ATOM   3037  C5'  DA G  10      38.625   5.980  27.014  1.00 47.14           C  
ANISOU 3037  C5'  DA G  10     5457   6319   6136   1265     31    165       C  
ATOM   3038  C4'  DA G  10      39.733   6.923  26.584  1.00 51.67           C  
ANISOU 3038  C4'  DA G  10     6000   6906   6725   1256     33    171       C  
ATOM   3039  O4'  DA G  10      40.359   7.551  27.729  1.00 46.68           O  
ANISOU 3039  O4'  DA G  10     5356   6274   6106   1247     17    180       O  
ATOM   3040  C3'  DA G  10      40.858   6.292  25.818  1.00 55.00           C  
ANISOU 3040  C3'  DA G  10     6416   7329   7152   1274     42    168       C  
ATOM   3041  O3'  DA G  10      41.348   7.264  24.933  1.00 64.89           O  
ANISOU 3041  O3'  DA G  10     7644   8598   8411   1262     50    170       O  
ATOM   3042  C2'  DA G  10      41.872   5.945  26.923  1.00 45.04           C  
ANISOU 3042  C2'  DA G  10     5151   6059   5903   1283     28    176       C  
ATOM   3043  C1'  DA G  10      41.698   7.137  27.864  1.00 47.07           C  
ANISOU 3043  C1'  DA G  10     5395   6324   6167   1260     13    184       C  
ATOM   3044  N9   DA G  10      41.888   6.863  29.288  1.00 45.46           N  
ANISOU 3044  N9   DA G  10     5197   6110   5967   1264     -5    191       N  
ATOM   3045  C8   DA G  10      41.464   5.768  29.994  1.00 46.25           C  
ANISOU 3045  C8   DA G  10     5323   6190   6059   1278    -11    189       C  
ATOM   3046  N7   DA G  10      41.725   5.833  31.284  1.00 39.96           N  
ANISOU 3046  N7   DA G  10     4526   5388   5268   1276    -28    197       N  
ATOM   3047  C5   DA G  10      42.330   7.073  31.438  1.00 35.32           C  
ANISOU 3047  C5   DA G  10     3909   4820   4690   1260    -34    204       C  
ATOM   3048  C6   DA G  10      42.833   7.750  32.566  1.00 35.51           C  
ANISOU 3048  C6   DA G  10     3918   4853   4722   1251    -50    215       C  
ATOM   3049  N6   DA G  10      42.800   7.240  33.807  1.00 39.63           N  
ANISOU 3049  N6   DA G  10     4452   5363   5242   1257    -66    221       N  
ATOM   3050  N1   DA G  10      43.373   8.972  32.374  1.00 37.82           N  
ANISOU 3050  N1   DA G  10     4183   5167   5021   1237    -49    220       N  
ATOM   3051  C2   DA G  10      43.406   9.474  31.134  1.00 45.91           C  
ANISOU 3051  C2   DA G  10     5196   6201   6045   1231    -32    215       C  
ATOM   3052  N3   DA G  10      42.962   8.934  29.993  1.00 39.61           N  
ANISOU 3052  N3   DA G  10     4411   5398   5242   1238    -17    205       N  
ATOM   3053  C4   DA G  10      42.429   7.723  30.220  1.00 41.81           C  
ANISOU 3053  C4   DA G  10     4716   5657   5514   1252    -19    201       C  
TER    3054       DA G  10                                                      
HETATM 3055  C1  MLA A 101       8.470   8.858  82.683  1.00 36.94           C  
ANISOU 3055  C1  MLA A 101     5502   3879   4655    354   -100    129       C  
HETATM 3056  O1A MLA A 101       7.332   8.815  83.195  1.00 48.15           O  
ANISOU 3056  O1A MLA A 101     6943   5285   6068    338    -80    122       O  
HETATM 3057  O1B MLA A 101       8.716   9.856  81.960  1.00 34.55           O  
ANISOU 3057  O1B MLA A 101     5168   3600   4361    371    -83    146       O  
HETATM 3058  C2  MLA A 101       9.509   7.756  82.911  1.00 27.94           C  
ANISOU 3058  C2  MLA A 101     4374   2729   3511    354   -142    116       C  
HETATM 3059  C3  MLA A 101       8.918   6.515  83.567  1.00 40.97           C  
ANISOU 3059  C3  MLA A 101     6061   4356   5149    338   -155     94       C  
HETATM 3060  O3A MLA A 101       7.687   6.378  83.751  1.00 55.62           O  
ANISOU 3060  O3A MLA A 101     7929   6208   6998    326   -134     85       O  
HETATM 3061  O3B MLA A 101       9.658   5.571  83.942  1.00 44.56           O  
ANISOU 3061  O3B MLA A 101     6536   4796   5599    336   -186     84       O  
HETATM 3062  C   TRS A 102       4.208 -11.719  80.349  1.00 73.58           C  
ANISOU 3062  C   TRS A 102    10580   8403   8975    245   -173   -243       C  
HETATM 3063  C1  TRS A 102       5.557 -12.205  79.834  1.00 79.11           C  
ANISOU 3063  C1  TRS A 102    11286   9092   9682    292   -186   -233       C  
HETATM 3064  C2  TRS A 102       4.390 -10.802  81.553  1.00 73.61           C  
ANISOU 3064  C2  TRS A 102    10582   8382   9003    245   -186   -224       C  
HETATM 3065  C3  TRS A 102       3.332 -12.899  80.738  1.00 69.81           C  
ANISOU 3065  C3  TRS A 102    10167   7898   8460    203   -157   -276       C  
HETATM 3066  N   TRS A 102       3.535 -10.977  79.284  1.00 73.90           N  
ANISOU 3066  N   TRS A 102    10555   8505   9020    239   -159   -238       N  
HETATM 3067  O1  TRS A 102       6.264 -11.133  79.249  1.00 82.75           O  
ANISOU 3067  O1  TRS A 102    11681   9587  10173    326   -197   -205       O  
HETATM 3068  O2  TRS A 102       5.110 -11.479  82.561  1.00 72.18           O  
ANISOU 3068  O2  TRS A 102    10461   8146   8818    254   -202   -226       O  
HETATM 3069  O3  TRS A 102       2.074 -12.407  81.138  1.00 66.72           O  
ANISOU 3069  O3  TRS A 102     9764   7524   8064    162   -143   -284       O  
HETATM 3070  C1  MLA B 101      23.504  14.531  50.519  1.00 46.12           C  
ANISOU 3070  C1  MLA B 101     5650   5914   5960   1007    -59    278       C  
HETATM 3071  O1A MLA B 101      22.918  15.630  50.351  1.00 44.75           O  
ANISOU 3071  O1A MLA B 101     5474   5745   5783   1007    -34    291       O  
HETATM 3072  O1B MLA B 101      22.890  13.492  50.183  1.00 56.64           O  
ANISOU 3072  O1B MLA B 101     6982   7253   7284   1013    -67    266       O  
HETATM 3073  C2  MLA B 101      24.907  14.465  51.105  1.00 27.70           C  
ANISOU 3073  C2  MLA B 101     3319   3568   3636   1000    -79    277       C  
HETATM 3074  C3  MLA B 101      25.359  13.021  51.285  1.00 44.14           C  
ANISOU 3074  C3  MLA B 101     5406   5645   5719   1007   -107    262       C  
HETATM 3075  O3A MLA B 101      25.125  12.153  50.408  1.00 55.23           O  
ANISOU 3075  O3A MLA B 101     6800   7064   7119   1023   -109    252       O  
HETATM 3076  O3B MLA B 101      25.998  12.659  52.304  1.00 39.52           O  
ANISOU 3076  O3B MLA B 101     4839   5041   5138    996   -126    260       O  
HETATM 3077  C   TRS B 102       5.651  20.137  53.684  1.00 65.80           C  
ANISOU 3077  C   TRS B 102     8168   8548   8286   1052    253    459       C  
HETATM 3078  C1  TRS B 102       6.780  20.866  54.408  1.00 70.69           C  
ANISOU 3078  C1  TRS B 102     8829   9105   8926   1045    259    459       C  
HETATM 3079  C2  TRS B 102       5.352  18.788  54.311  1.00 58.10           C  
ANISOU 3079  C2  TRS B 102     7201   7567   7306   1015    222    429       C  
HETATM 3080  C3  TRS B 102       6.004  19.925  52.216  1.00 64.79           C  
ANISOU 3080  C3  TRS B 102     7998   8465   8153   1069    243    458       C  
HETATM 3081  N   TRS B 102       4.428  20.934  53.780  1.00 67.03           N  
ANISOU 3081  N   TRS B 102     8313   8728   8427   1076    291    489       N  
HETATM 3082  O1  TRS B 102       6.354  21.265  55.695  1.00 74.12           O  
ANISOU 3082  O1  TRS B 102     9301   9498   9361   1033    276    465       O  
HETATM 3083  O2  TRS B 102       4.302  18.206  53.574  1.00 53.77           O  
ANISOU 3083  O2  TRS B 102     6614   7081   6736   1019    220    430       O  
HETATM 3084  O3  TRS B 102       5.097  18.998  51.657  1.00 62.83           O  
ANISOU 3084  O3  TRS B 102     7716   8271   7885   1062    230    450       O  
HETATM 3085  C1  MLA C 101      14.400  -1.519  16.475  1.00 51.17           C  
ANISOU 3085  C1  MLA C 101     6072   7440   5931    719    153     12       C  
HETATM 3086  O1A MLA C 101      13.217  -1.738  16.813  1.00 63.77           O  
ANISOU 3086  O1A MLA C 101     7661   9076   7492    679    148     10       O  
HETATM 3087  O1B MLA C 101      14.855  -0.360  16.635  1.00 49.75           O  
ANISOU 3087  O1B MLA C 101     5853   7259   5791    769    145     37       O  
HETATM 3088  C2  MLA C 101      15.224  -2.650  15.887  1.00 26.36           C  
ANISOU 3088  C2  MLA C 101     2984   4252   2779    706    172    -16       C  
HETATM 3089  C3  MLA C 101      16.688  -2.276  15.769  1.00 42.93           C  
ANISOU 3089  C3  MLA C 101     5085   6299   4927    763    176     -9       C  
HETATM 3090  O3A MLA C 101      17.391  -2.687  14.805  1.00 35.82           O  
ANISOU 3090  O3A MLA C 101     4204   5385   4023    764    191    -20       O  
HETATM 3091  O3B MLA C 101      17.221  -1.557  16.651  1.00 61.21           O  
ANISOU 3091  O3B MLA C 101     7385   8586   7288    809    164      7       O  
HETATM 3092  C   TRS C 102       1.303  11.828  13.643  1.00 76.28           C  
ANISOU 3092  C   TRS C 102     8478  11632   8871    940    130    497       C  
HETATM 3093  C1  TRS C 102       1.217  12.136  12.167  1.00 72.96           C  
ANISOU 3093  C1  TRS C 102     8023  11279   8420    944    133    515       C  
HETATM 3094  C2  TRS C 102       2.750  11.708  14.073  1.00 81.23           C  
ANISOU 3094  C2  TRS C 102     9162  12146   9554    956    131    469       C  
HETATM 3095  C3  TRS C 102       0.503  10.570  13.978  1.00 74.27           C  
ANISOU 3095  C3  TRS C 102     8231  11411   8577    867    117    469       C  
HETATM 3096  N   TRS C 102       0.733  12.983  14.346  1.00 74.63           N  
ANISOU 3096  N   TRS C 102     8255  11426   8675    987    140    536       N  
HETATM 3097  O1  TRS C 102       0.305  13.198  12.092  1.00 78.64           O  
ANISOU 3097  O1  TRS C 102     8717  12041   9120    971    140    559       O  
HETATM 3098  O2  TRS C 102       2.826  12.235  15.374  1.00 85.58           O  
ANISOU 3098  O2  TRS C 102     9729  12645  10144    990    135    478       O  
HETATM 3099  O3  TRS C 102       0.556  10.297  15.364  1.00 66.10           O  
ANISOU 3099  O3  TRS C 102     7229  10315   7571    864    114    453       O  
HETATM 3100  O   HOH A 201      -3.876 -12.250  78.564  1.00 56.64           O  
ANISOU 3100  O   HOH A 201     8356   6482   6681    -17    -47   -348       O  
HETATM 3101  O   HOH A 202      -2.676  -7.167  74.268  1.00 68.05           O  
ANISOU 3101  O   HOH A 202     9456   8161   8241    152    -54   -213       O  
HETATM 3102  O   HOH A 203       1.721   7.314  68.057  1.00 34.06           O  
ANISOU 3102  O   HOH A 203     4616   4122   4205    578     22    140       O  
HETATM 3103  O   HOH A 204      -5.937 -13.754  77.611  1.00 69.06           O  
ANISOU 3103  O   HOH A 204     9945   8125   8170   -116     -9   -403       O  
HETATM 3104  O   HOH A 205       5.075  -8.890  71.876  1.00 44.89           O  
ANISOU 3104  O   HOH A 205     6573   5098   5387    369   -142   -179       O  
HETATM 3105  O   HOH A 206       2.371   6.035  62.260  1.00 47.82           O  
ANISOU 3105  O   HOH A 206     6197   6061   5910    635      5    133       O  
HETATM 3106  O   HOH A 207       5.158  16.812  92.029  1.00 43.83           O  
ANISOU 3106  O   HOH A 207     6764   4390   5501    104    158    208       O  
HETATM 3107  O   HOH A 208       3.368   9.562  70.286  1.00 53.98           O  
ANISOU 3107  O   HOH A 208     7204   6527   6778    589     33    176       O  
HETATM 3108  O   HOH A 209      13.799  -2.676  78.469  1.00 52.28           O  
ANISOU 3108  O   HOH A 209     7467   5868   6530    531   -307     16       O  
HETATM 3109  O   HOH A 210      -4.882  -1.769  77.778  1.00 39.99           O  
ANISOU 3109  O   HOH A 210     5818   4602   4776    179     -3   -109       O  
HETATM 3110  O   HOH A 211       5.814   5.635  67.236  1.00 46.36           O  
ANISOU 3110  O   HOH A 211     6207   5613   5795    604    -58    108       O  
HETATM 3111  O   HOH A 212       8.072  -4.880  85.722  1.00 46.97           O  
ANISOU 3111  O   HOH A 212     7123   4950   5771    301   -269    -83       O  
HETATM 3112  O   HOH A 213       1.058   5.958  92.486  1.00 34.52           O  
ANISOU 3112  O   HOH A 213     5598   3253   4264     83    -27     19       O  
HETATM 3113  O   HOH A 214      -3.123  -9.797  84.464  1.00 39.80           O  
ANISOU 3113  O   HOH A 214     6330   4145   4647     -2    -84   -297       O  
HETATM 3114  O   HOH A 215       1.891  17.223  81.451  1.00 44.03           O  
ANISOU 3114  O   HOH A 215     6345   4831   5555    441    243    277       O  
HETATM 3115  O   HOH A 216       9.205  12.522  86.073  1.00 35.10           O  
ANISOU 3115  O   HOH A 216     5384   3528   4425    262    -45    174       O  
HETATM 3116  O   HOH A 217      -7.634  12.303  73.465  1.00 45.03           O  
ANISOU 3116  O   HOH A 217     6012   5561   5538    564    275    268       O  
HETATM 3117  O   HOH A 218       2.858  14.136  90.253  1.00 29.02           O  
ANISOU 3117  O   HOH A 218     4792   2607   3627    173    132    174       O  
HETATM 3118  O   HOH A 219       1.728   3.774  90.261  1.00 25.62           O  
ANISOU 3118  O   HOH A 219     4408   2201   3126    129    -77     -9       O  
HETATM 3119  O   HOH A 220       1.880  -7.538  79.640  1.00 31.76           O  
ANISOU 3119  O   HOH A 220     5087   3248   3732    220   -141   -192       O  
HETATM 3120  O   HOH A 221       1.645 -12.230  83.790  1.00 45.27           O  
ANISOU 3120  O   HOH A 221     7125   4725   5352    124   -153   -288       O  
HETATM 3121  O   HOH A 222      -3.016  16.731  77.465  1.00 36.77           O  
ANISOU 3121  O   HOH A 222     5208   4169   4594    570    321    317       O  
HETATM 3122  O   HOH A 223       0.887  17.536  78.973  1.00 37.30           O  
ANISOU 3122  O   HOH A 223     5386   4087   4697    516    271    302       O  
HETATM 3123  O   HOH A 224       7.556   3.599  85.322  1.00 26.00           O  
ANISOU 3123  O   HOH A 224     4268   2393   3217    291   -181     39       O  
HETATM 3124  O   HOH A 225      -0.778  -0.201  95.212  1.00 50.31           O  
ANISOU 3124  O   HOH A 225     7752   5183   6179    -26    -91   -108       O  
HETATM 3125  O   HOH A 226      -2.378  15.459  69.854  1.00 52.92           O  
ANISOU 3125  O   HOH A 226     6959   6534   6615    702    259    332       O  
HETATM 3126  O   HOH A 227      -4.071  -9.344  81.654  1.00 50.44           O  
ANISOU 3126  O   HOH A 227     7550   5635   5978      7    -59   -290       O  
HETATM 3127  O   HOH A 228       6.622  -4.436  87.978  1.00 37.09           O  
ANISOU 3127  O   HOH A 228     5943   3637   4512    231   -254    -95       O  
HETATM 3128  O   HOH A 229      -5.739   7.895  85.728  1.00 37.25           O  
ANISOU 3128  O   HOH A 229     5594   3979   4579    227    159     77       O  
HETATM 3129  O   HOH A 230      -4.448   8.587  95.407  1.00 51.39           O  
ANISOU 3129  O   HOH A 230     7816   5325   6385     12    156     39       O  
HETATM 3130  O   HOH A 231       3.938  17.061  88.657  1.00 44.93           O  
ANISOU 3130  O   HOH A 231     6763   4653   5656    219    195    230       O  
HETATM 3131  O   HOH A 232      13.069   8.877  74.635  1.00 48.93           O  
ANISOU 3131  O   HOH A 232     6732   5643   6215    549   -151    164       O  
HETATM 3132  O   HOH A 233      11.473  -4.094  78.927  1.00 36.97           O  
ANISOU 3132  O   HOH A 233     5599   3894   4553    480   -278    -30       O  
HETATM 3133  O   HOH A 234      -4.033  -0.682  66.596  1.00 38.68           O  
ANISOU 3133  O   HOH A 234     5242   4886   4567    334      8    -38       O  
HETATM 3134  O   HOH A 235      -1.028   8.828  97.348  1.00 58.61           O  
ANISOU 3134  O   HOH A 235     8743   6217   7311    -34     76     38       O  
HETATM 3135  O   HOH A 236      15.889  -7.686  68.672  1.00 46.01           O  
ANISOU 3135  O   HOH A 236     6555   5241   5683    724   -251    -33       O  
HETATM 3136  O   HOH A 237      13.934   0.189  83.226  1.00 49.98           O  
ANISOU 3136  O   HOH A 237     7252   5481   6257    430   -326     53       O  
HETATM 3137  O   HOH A 238      -0.401  20.719  87.010  1.00 55.75           O  
ANISOU 3137  O   HOH A 238     8087   6078   7020    344    418    322       O  
HETATM 3138  O   HOH A 239      -6.042  -2.964  90.132  1.00 45.58           O  
ANISOU 3138  O   HOH A 239     7025   4805   5490    -43    -10   -189       O  
HETATM 3139  O   HOH A 240      12.002  10.445  76.010  1.00 41.05           O  
ANISOU 3139  O   HOH A 240     5773   4606   5217    513   -111    179       O  
HETATM 3140  O   HOH A 241      14.892  -5.658  81.135  1.00 61.49           O  
ANISOU 3140  O   HOH A 241     8787   6921   7655    535   -352     -3       O  
HETATM 3141  O   HOH A 242       9.201  -8.577  78.099  1.00 42.13           O  
ANISOU 3141  O   HOH A 242     6391   4504   5112    435   -240   -124       O  
HETATM 3142  O   HOH A 243      11.616  -6.944  77.984  1.00 45.77           O  
ANISOU 3142  O   HOH A 243     6776   4989   5626    503   -276    -68       O  
HETATM 3143  O   HOH A 244      -6.219  -1.480  66.934  1.00 55.87           O  
ANISOU 3143  O   HOH A 244     7416   7125   6689    264     29    -61       O  
HETATM 3144  O   HOH A 245      -0.553  19.692  78.237  1.00 45.25           O  
ANISOU 3144  O   HOH A 245     6368   5127   5697    579    367    360       O  
HETATM 3145  O   HOH A 246       8.475   5.049  67.392  1.00 59.53           O  
ANISOU 3145  O   HOH A 246     7902   7229   7489    625   -103    102       O  
HETATM 3146  O   HOH B 201      20.562   8.138  66.027  1.00 39.60           O  
ANISOU 3146  O   HOH B 201     5256   4706   5085    766   -225    197       O  
HETATM 3147  O   HOH B 202       8.321  18.901  62.367  1.00 41.84           O  
ANISOU 3147  O   HOH B 202     5429   5152   5316    854    179    369       O  
HETATM 3148  O   HOH B 203      30.312   5.995  41.787  1.00 38.26           O  
ANISOU 3148  O   HOH B 203     4531   5032   4972   1206   -115    195       O  
HETATM 3149  O   HOH B 204      24.567  26.547  43.139  1.00 63.12           O  
ANISOU 3149  O   HOH B 204     7724   8176   8085   1115    238    426       O  
HETATM 3150  O   HOH B 205      24.388  23.738  44.004  1.00 57.58           O  
ANISOU 3150  O   HOH B 205     7000   7479   7397   1101    161    391       O  
HETATM 3151  O   HOH B 206       7.932  15.570  54.527  1.00 30.57           O  
ANISOU 3151  O   HOH B 206     3750   4021   3843    944    115    340       O  
HETATM 3152  O   HOH B 207      21.063  12.858  66.598  1.00 44.06           O  
ANISOU 3152  O   HOH B 207     5803   5273   5665    718   -165    249       O  
HETATM 3153  O   HOH B 208      17.642   9.729  43.932  1.00 24.60           O  
ANISOU 3153  O   HOH B 208     2838   3384   3124   1036    -28    220       O  
HETATM 3154  O   HOH B 209      27.037   5.419  43.802  1.00 26.12           O  
ANISOU 3154  O   HOH B 209     3069   3454   3402   1147   -119    178       O  
HETATM 3155  O   HOH B 210       7.435   3.729  45.904  1.00 50.31           O  
ANISOU 3155  O   HOH B 210     6179   6785   6151    785    -15    119       O  
HETATM 3156  O   HOH B 211       9.296   6.942  56.446  1.00 35.33           O  
ANISOU 3156  O   HOH B 211     4498   4517   4410    794    -47    161       O  
HETATM 3157  O   HOH B 212      20.286  14.859  48.726  1.00 25.93           O  
ANISOU 3157  O   HOH B 212     3066   3413   3372   1028    -10    288       O  
HETATM 3158  O   HOH B 213      25.575   0.350  64.163  1.00 46.89           O  
ANISOU 3158  O   HOH B 213     6201   5633   5982    945   -329    164       O  
HETATM 3159  O   HOH B 214      24.739   8.428  37.853  1.00 41.39           O  
ANISOU 3159  O   HOH B 214     4871   5551   5306   1156    -37    199       O  
HETATM 3160  O   HOH B 215      23.796   8.505  63.560  1.00 49.40           O  
ANISOU 3160  O   HOH B 215     6395   6026   6348    831   -246    218       O  
HETATM 3161  O   HOH B 216       1.288  16.740  55.901  1.00 36.59           O  
ANISOU 3161  O   HOH B 216     4461   4919   4523    959    222    413       O  
HETATM 3162  O   HOH B 217      12.887  20.145  65.374  1.00 39.31           O  
ANISOU 3162  O   HOH B 217     5234   4670   5032    761    137    352       O  
HETATM 3163  O   HOH B 218      18.278   2.290  38.711  1.00 50.06           O  
ANISOU 3163  O   HOH B 218     6124   6653   6243    996    -33     98       O  
HETATM 3164  O   HOH B 219      15.326  21.762  55.122  1.00 36.55           O  
ANISOU 3164  O   HOH B 219     4597   4600   4691    969    171    398       O  
HETATM 3165  O   HOH B 220      28.875  11.839  47.944  1.00 41.05           O  
ANISOU 3165  O   HOH B 220     4921   5328   5348   1082   -127    255       O  
HETATM 3166  O   HOH B 221      27.974   9.747  61.120  1.00 45.39           O  
ANISOU 3166  O   HOH B 221     5760   5621   5865    888   -264    252       O  
HETATM 3167  O   HOH B 222      26.306  -1.047  56.620  1.00 37.49           O  
ANISOU 3167  O   HOH B 222     4888   4565   4792   1064   -255    140       O  
HETATM 3168  O   HOH B 223      25.515   3.153  39.301  1.00 44.17           O  
ANISOU 3168  O   HOH B 223     5352   5803   5629   1150    -69    136       O  
HETATM 3169  O   HOH B 224      10.107   4.353  64.825  1.00 52.85           O  
ANISOU 3169  O   HOH B 224     6997   6436   6647    675   -121    100       O  
HETATM 3170  O   HOH B 225       3.345  12.297  49.592  1.00 33.61           O  
ANISOU 3170  O   HOH B 225     3949   4726   4094    923    107    322       O  
HETATM 3171  O   HOH B 226      20.070  -2.484  60.688  1.00 44.46           O  
ANISOU 3171  O   HOH B 226     5965   5326   5602    892   -235     68       O  
HETATM 3172  O   HOH B 227       0.276  19.041  54.937  1.00 35.58           O  
ANISOU 3172  O   HOH B 227     4286   4850   4383   1038    292    485       O  
HETATM 3173  O   HOH B 228       7.780   6.385  44.118  1.00 47.67           O  
ANISOU 3173  O   HOH B 228     5746   6524   5842    860      8    181       O  
HETATM 3174  O   HOH B 229      28.469  15.270  58.081  1.00 44.17           O  
ANISOU 3174  O   HOH B 229     5515   5543   5726    867   -162    292       O  
HETATM 3175  O   HOH B 230       5.608  15.959  47.235  1.00 56.01           O  
ANISOU 3175  O   HOH B 230     6733   7569   6979   1047    157    398       O  
HETATM 3176  O   HOH B 231      17.192   0.987  48.116  1.00 40.35           O  
ANISOU 3176  O   HOH B 231     5098   5187   5045    925   -102     79       O  
HETATM 3177  O   HOH B 232      12.816  18.113  46.038  1.00 39.04           O  
ANISOU 3177  O   HOH B 232     4637   5255   4943   1098    135    385       O  
HETATM 3178  O   HOH B 233      23.222  -7.957  49.523  1.00 45.85           O  
ANISOU 3178  O   HOH B 233     6109   5612   5700   1060   -109      9       O  
HETATM 3179  O   HOH B 234      29.975   5.003  45.272  1.00 40.65           O  
ANISOU 3179  O   HOH B 234     4907   5268   5272   1184   -154    195       O  
HETATM 3180  O   HOH B 235      20.711  22.081  50.817  1.00 48.63           O  
ANISOU 3180  O   HOH B 235     6017   6208   6254   1006    127    380       O  
HETATM 3181  O   HOH B 236      19.026  -1.173  68.274  1.00 66.26           O  
ANISOU 3181  O   HOH B 236     8873   7932   8371    776   -293     84       O  
HETATM 3182  O   HOH B 237      18.867   8.365  41.635  1.00 33.85           O  
ANISOU 3182  O   HOH B 237     3987   4585   4288   1055    -34    198       O  
HETATM 3183  O   HOH B 238      31.430  -0.423  47.953  1.00 46.23           O  
ANISOU 3183  O   HOH B 238     5761   5859   5946   1249   -192    172       O  
HETATM 3184  O   HOH B 239      19.162  -6.009  49.020  1.00 51.92           O  
ANISOU 3184  O   HOH B 239     6815   6474   6438    932    -99    -12       O  
HETATM 3185  O   HOH B 240      26.419  -2.010  61.276  1.00 54.95           O  
ANISOU 3185  O   HOH B 240     7211   6678   6990   1030   -307    148       O  
HETATM 3186  O   HOH B 241      -2.021  11.125  45.926  1.00 70.90           O  
ANISOU 3186  O   HOH B 241     8469   9819   8651    882    135    357       O  
HETATM 3187  O   HOH B 242      10.712  22.409  56.059  1.00 39.08           O  
ANISOU 3187  O   HOH B 242     4929   4946   4973   1002    250    443       O  
HETATM 3188  O   HOH B 243      16.567  12.255  42.420  1.00 39.72           O  
ANISOU 3188  O   HOH B 243     4688   5371   5032   1068     17    267       O  
HETATM 3189  O   HOH B 244      28.643  13.282  50.483  1.00 50.95           O  
ANISOU 3189  O   HOH B 244     6217   6541   6602   1029   -130    270       O  
HETATM 3190  O   HOH B 245      33.175   1.583  47.945  1.00 61.04           O  
ANISOU 3190  O   HOH B 245     7552   7786   7855   1260   -209    205       O  
HETATM 3191  O   HOH B 246      11.042  18.757  65.432  1.00 62.98           O  
ANISOU 3191  O   HOH B 246     8218   7692   8019    768    129    338       O  
HETATM 3192  O   HOH B 247       5.151  11.184  70.757  1.00 41.76           O  
ANISOU 3192  O   HOH B 247     5674   4930   5263    608     35    203       O  
HETATM 3193  O   HOH B 248      25.298  -8.258  48.614  1.00 58.51           O  
ANISOU 3193  O   HOH B 248     7692   7216   7324   1133   -105     29       O  
HETATM 3194  O   HOH B 249       0.590  19.651  52.688  1.00 44.29           O  
ANISOU 3194  O   HOH B 249     5324   6029   5476   1088    301    511       O  
HETATM 3195  O   HOH B 250      18.552   3.492  36.518  1.00 49.79           O  
ANISOU 3195  O   HOH B 250     6022   6685   6210   1021    -17    118       O  
HETATM 3196  O   HOH B 251      26.023   9.123  62.997  1.00 41.05           O  
ANISOU 3196  O   HOH B 251     5288   5008   5302    850   -263    237       O  
HETATM 3197  O   HOH C 201       8.612  15.530   7.181  1.00 51.46           O  
ANISOU 3197  O   HOH C 201     5459   8219   5875   1103    188    500       O  
HETATM 3198  O   HOH C 202      14.727   1.823   0.161  1.00 50.91           O  
ANISOU 3198  O   HOH C 202     5783   7916   5645    630    245     88       O  
HETATM 3199  O   HOH C 203      16.329  -5.643   8.885  1.00 41.78           O  
ANISOU 3199  O   HOH C 203     5044   6264   4567    558    276    -93       O  
HETATM 3200  O   HOH C 204      25.191  -3.244  24.956  1.00 38.28           O  
ANISOU 3200  O   HOH C 204     4662   5214   4669   1097    121     10       O  
HETATM 3201  O   HOH C 205       4.596   4.782   1.545  1.00 43.77           O  
ANISOU 3201  O   HOH C 205     4499   7674   4458    505    141    276       O  
HETATM 3202  O   HOH C 206       5.958  11.653  12.456  1.00 30.22           O  
ANISOU 3202  O   HOH C 206     2773   5546   3164    986    141    426       O  
HETATM 3203  O   HOH C 207       7.082  18.058  14.224  1.00 51.76           O  
ANISOU 3203  O   HOH C 207     5612   8029   6026   1147    203    541       O  
HETATM 3204  O   HOH C 208       6.574  17.201  17.473  1.00 36.51           O  
ANISOU 3204  O   HOH C 208     3704   6035   4134   1136    190    518       O  
HETATM 3205  O   HOH C 209      12.641   1.412  18.340  1.00 24.57           O  
ANISOU 3205  O   HOH C 209     2581   4156   2600    776    116     86       O  
HETATM 3206  O   HOH C 210      16.011  17.764  21.379  1.00 46.22           O  
ANISOU 3206  O   HOH C 210     5173   6725   5662   1154    176    382       O  
HETATM 3207  O   HOH C 211      20.358   0.516  29.129  1.00 39.99           O  
ANISOU 3207  O   HOH C 211     4774   5532   4889   1020     47     63       O  
HETATM 3208  O   HOH C 212      15.767   6.307  23.081  1.00 26.11           O  
ANISOU 3208  O   HOH C 212     2730   4158   3033   1012     86    178       O  
HETATM 3209  O   HOH C 213      24.146   0.145  23.210  1.00 26.88           O  
ANISOU 3209  O   HOH C 213     3074   3901   3238   1095    108     54       O  
HETATM 3210  O   HOH C 214      14.225  14.946  10.585  1.00 39.96           O  
ANISOU 3210  O   HOH C 214     4176   6361   4645   1146    189    392       O  
HETATM 3211  O   HOH C 215      27.888   0.278  12.108  1.00 45.67           O  
ANISOU 3211  O   HOH C 215     5386   6401   5565   1129    240     33       O  
HETATM 3212  O   HOH C 216      27.717  10.134   6.333  1.00 47.82           O  
ANISOU 3212  O   HOH C 216     5342   6949   5876   1233    249    180       O  
HETATM 3213  O   HOH C 217       6.088   0.868  20.401  1.00 42.34           O  
ANISOU 3213  O   HOH C 217     4747   6664   4676    597     90    104       O  
HETATM 3214  O   HOH C 218      25.968  -2.142  21.450  1.00 40.32           O  
ANISOU 3214  O   HOH C 218     4849   5547   4922   1112    150     19       O  
HETATM 3215  O   HOH C 219       4.167   2.208  11.858  1.00 40.64           O  
ANISOU 3215  O   HOH C 219     4309   6891   4242    510    112    175       O  
HETATM 3216  O   HOH C 220      20.975  -2.383   5.838  1.00 43.83           O  
ANISOU 3216  O   HOH C 220     5195   6469   4988    779    293    -31       O  
HETATM 3217  O   HOH C 221      29.333   4.021  10.272  1.00 34.15           O  
ANISOU 3217  O   HOH C 221     3792   5013   4168   1204    237     86       O  
HETATM 3218  O   HOH C 222      23.075  10.640  18.715  1.00 42.39           O  
ANISOU 3218  O   HOH C 222     4725   6128   5252   1187    131    220       O  
HETATM 3219  O   HOH C 223      19.256  -4.520  19.013  1.00 36.63           O  
ANISOU 3219  O   HOH C 223     4440   5268   4210    829    182    -49       O  
HETATM 3220  O   HOH C 224       6.083  -1.795  16.485  1.00 53.46           O  
ANISOU 3220  O   HOH C 224     6208   8158   5947    446    122     37       O  
HETATM 3221  O   HOH C 225       5.233   5.649  18.533  1.00 41.05           O  
ANISOU 3221  O   HOH C 225     4372   6685   4540    756     94    246       O  
HETATM 3222  O   HOH C 226      30.615   5.288   5.599  1.00 50.44           O  
ANISOU 3222  O   HOH C 226     5806   7144   6214   1217    288     90       O  
HETATM 3223  O   HOH C 227       2.813   7.977  18.607  1.00 61.63           O  
ANISOU 3223  O   HOH C 227     6849   9458   7111    812     99    339       O  
HETATM 3224  O   HOH C 228      25.110  11.379   0.284  1.00 61.58           O  
ANISOU 3224  O   HOH C 228     7008   8921   7469   1178    289    216       O  
HETATM 3225  O   HOH C 229      17.633   5.746  25.331  1.00 34.97           O  
ANISOU 3225  O   HOH C 229     3916   5149   4222   1040     70    158       O  
HETATM 3226  O   HOH C 230      15.585  16.485  12.766  1.00 48.77           O  
ANISOU 3226  O   HOH C 230     5367   7319   5844   1160    194    392       O  
HETATM 3227  O   HOH C 231       8.828  -4.727  16.856  1.00 41.97           O  
ANISOU 3227  O   HOH C 231     4954   6470   4524    427    158    -53       O  
HETATM 3228  O   HOH C 232      16.105   4.307  27.342  1.00 59.31           O  
ANISOU 3228  O   HOH C 232     7051   8208   7275    983     56    134       O  
HETATM 3229  O   HOH C 233      10.196  21.123  -0.874  1.00 47.35           O  
ANISOU 3229  O   HOH C 233     4951   7763   5276   1205    258    627       O  
HETATM 3230  O   HOH C 234      16.507  15.450   2.122  1.00 47.95           O  
ANISOU 3230  O   HOH C 234     5123   7525   5571   1160    236    397       O  
HETATM 3231  O   HOH C 235      13.733  16.422  23.012  1.00 45.92           O  
ANISOU 3231  O   HOH C 235     5111   6746   5590   1149    161    386       O  
HETATM 3232  O   HOH C 236       8.632  -3.671   9.115  1.00 45.37           O  
ANISOU 3232  O   HOH C 236     5250   7184   4806    347    193    -21       O  
HETATM 3233  O   HOH C 237      29.112  13.476   8.970  1.00 58.73           O  
ANISOU 3233  O   HOH C 237     6755   8212   7348   1200    219    212       O  
HETATM 3234  O   HOH C 238      11.562  10.514  -0.681  1.00 48.57           O  
ANISOU 3234  O   HOH C 238     5119   7965   5372    905    200    354       O  
HETATM 3235  O   HOH C 239      18.103  -5.162  16.709  1.00 47.61           O  
ANISOU 3235  O   HOH C 239     5833   6742   5517    747    207    -68       O  
HETATM 3236  O   HOH C 240      23.047  11.272  21.253  1.00 49.36           O  
ANISOU 3236  O   HOH C 240     5636   6949   6169   1176    114    228       O  
HETATM 3237  O   HOH C 241      13.250   5.785  24.501  1.00 39.06           O  
ANISOU 3237  O   HOH C 241     4370   5847   4623    954     76    178       O  
HETATM 3238  O   HOH C 242       1.150   5.656  10.970  1.00 51.20           O  
ANISOU 3238  O   HOH C 242     5417   8516   5519    596     98    318       O  
HETATM 3239  O   HOH C 243      26.475  -3.612  17.834  1.00 52.86           O  
ANISOU 3239  O   HOH C 243     6478   7154   6452   1084    211    -13       O  
HETATM 3240  O   HOH C 244      25.076  -4.413  16.253  1.00 56.41           O  
ANISOU 3240  O   HOH C 244     6953   7649   6830   1009    235    -37       O  
HETATM 3241  O   HOH C 245       1.447   3.280  11.025  1.00 49.12           O  
ANISOU 3241  O   HOH C 245     5246   8197   5219    481     99    239       O  
HETATM 3242  O   HOH C 246      30.438   0.239  11.093  1.00 38.65           O  
ANISOU 3242  O   HOH C 246     4496   5467   4723   1196    265     33       O  
HETATM 3243  O   HOH C 247      15.523  15.913  -0.191  1.00 60.38           O  
ANISOU 3243  O   HOH C 247     6648   9221   7074   1154    244    428       O  
HETATM 3244  O   HOH C 248      20.283  -0.774   3.916  1.00 42.28           O  
ANISOU 3244  O   HOH C 248     4912   6386   4765    773    286      1       O  
HETATM 3245  O   HOH C 249      -1.396   6.609  12.104  1.00 58.01           O  
ANISOU 3245  O   HOH C 249     6179   9529   6334    605     89    379       O  
HETATM 3246  O   HOH D 101      17.783  -4.302 112.893  1.00 43.09           O  
ANISOU 3246  O   HOH D 101     7237   4097   5038   -150   -636     88       O  
HETATM 3247  O   HOH D 102      18.674  10.212 102.113  1.00 46.77           O  
ANISOU 3247  O   HOH D 102     7347   4708   5716   -225   -397    188       O  
HETATM 3248  O   HOH D 103      17.455  14.072  92.981  1.00 46.93           O  
ANISOU 3248  O   HOH D 103     7064   4916   5850      1   -220    213       O  
HETATM 3249  O   HOH D 104      24.698   3.993  93.460  1.00 59.03           O  
ANISOU 3249  O   HOH D 104     8471   6632   7327    237   -585    236       O  
HETATM 3250  O   HOH E 101       7.027   1.693  93.150  1.00 52.22           O  
ANISOU 3250  O   HOH E 101     7909   5445   6488    116   -230     -8       O  
HETATM 3251  O   HOH E 102      16.163   5.059  95.339  1.00 49.10           O  
ANISOU 3251  O   HOH E 102     7450   5108   6097     99   -394    126       O  
HETATM 3252  O   HOH E 103       9.275   7.488  93.194  1.00 47.91           O  
ANISOU 3252  O   HOH E 103     7287   4928   5987     96   -182     88       O  
HETATM 3253  O   HOH E 104      17.386  13.060 103.512  1.00 51.67           O  
ANISOU 3253  O   HOH E 104     8026   5283   6324   -333   -293    183       O  
HETATM 3254  O   HOH E 105       8.887  11.688  97.300  1.00 61.17           O  
ANISOU 3254  O   HOH E 105     9066   6525   7651    -58    -86    120       O  
HETATM 3255  O   HOH E 106       4.356  10.499  96.562  1.00 45.51           O  
ANISOU 3255  O   HOH E 106     7063   4555   5675    -16     -7     86       O  
HETATM 3256  O   HOH E 107      15.819   4.690  92.984  1.00 52.06           O  
ANISOU 3256  O   HOH E 107     7751   5537   6493    168   -376    119       O  
HETATM 3257  O   HOH F 101      20.512  17.264  34.051  1.00 55.94           O  
ANISOU 3257  O   HOH F 101     6603   7546   7104   1131    103    318       O  
HETATM 3258  O   HOH F 102      29.195  14.357  26.446  1.00 59.61           O  
ANISOU 3258  O   HOH F 102     7002   8016   7632   1145     80    228       O  
HETATM 3259  O   HOH F 103      33.823  17.153  26.626  1.00 43.29           O  
ANISOU 3259  O   HOH F 103     4908   5916   5624   1135     89    234       O  
HETATM 3260  O   HOH F 104      18.580  15.674  38.692  1.00 59.83           O  
ANISOU 3260  O   HOH F 104     7150   7981   7600   1133     71    315       O  
HETATM 3261  O   HOH F 105      24.103  25.757  36.264  1.00 45.56           O  
ANISOU 3261  O   HOH F 105     5378   6102   5832   1154    238    407       O  
HETATM 3262  O   HOH F 106      16.911  21.709  40.589  1.00 40.31           O  
ANISOU 3262  O   HOH F 106     4729   5462   5123   1148    188    413       O  
HETATM 3263  O   HOH F 107      43.638  14.698  26.038  1.00 54.06           O  
ANISOU 3263  O   HOH F 107     6161   7306   7074   1180     48    209       O  
HETATM 3264  O   HOH F 108      20.562  17.751  31.603  1.00 52.45           O  
ANISOU 3264  O   HOH F 108     6132   7152   6644   1133    120    323       O  
HETATM 3265  O   HOH F 109      21.746   6.448  34.376  1.00 62.25           O  
ANISOU 3265  O   HOH F 109     7502   8288   7861   1117     -4    166       O  
HETATM 3266  O   HOH F 110      25.765  21.176  38.769  1.00 50.75           O  
ANISOU 3266  O   HOH F 110     6020   6729   6536   1127    114    343       O  
HETATM 3267  O   HOH F 111      39.757  19.737  25.403  1.00 42.49           O  
ANISOU 3267  O   HOH F 111     4733   5846   5567   1140    111    236       O  
HETATM 3268  O   HOH F 112      18.066  15.641  41.671  1.00 44.15           O  
ANISOU 3268  O   HOH F 112     5217   5932   5627   1120     60    318       O  
HETATM 3269  O   HOH F 113      15.946  21.973  36.964  1.00 49.48           O  
ANISOU 3269  O   HOH F 113     5830   6728   6243   1155    206    423       O  
HETATM 3270  O   HOH F 114      43.698  13.284  27.961  1.00 46.09           O  
ANISOU 3270  O   HOH F 114     5165   6278   6069   1191     18    213       O  
HETATM 3271  O   HOH F 115      26.326  11.151  25.157  1.00 49.02           O  
ANISOU 3271  O   HOH F 115     5659   6742   6223   1171     78    209       O  
HETATM 3272  O   HOH F 116      37.832  10.350  25.545  1.00 48.82           O  
ANISOU 3272  O   HOH F 116     5611   6584   6355   1201     48    180       O  
HETATM 3273  O   HOH F 117      15.300  18.283  42.331  1.00 43.49           O  
ANISOU 3273  O   HOH F 117     5130   5878   5518   1142    128    379       O  
HETATM 3274  O   HOH F 118      16.669  16.612  38.371  1.00 55.17           O  
ANISOU 3274  O   HOH F 118     6544   7435   6983   1137    100    342       O  
HETATM 3275  O   HOH G 101      33.803  18.484  41.309  1.00 50.31           O  
ANISOU 3275  O   HOH G 101     5906   6662   6548   1123    -15    306       O  
HETATM 3276  O   HOH G 102      16.638  20.843  25.930  1.00 45.92           O  
ANISOU 3276  O   HOH G 102     5226   6525   5698   1159    203    409       O  
HETATM 3277  O   HOH G 103      38.474   9.926  28.360  1.00 52.21           O  
ANISOU 3277  O   HOH G 103     6051   6986   6800   1204     15    189       O  
HETATM 3278  O   HOH G 104      42.622  10.510  28.162  1.00 47.52           O  
ANISOU 3278  O   HOH G 104     5393   6421   6242   1217      8    200       O  
HETATM 3279  O   HOH G 105      41.714   5.274  35.003  1.00 56.54           O  
ANISOU 3279  O   HOH G 105     6651   7462   7370   1280    -76    215       O  
HETATM 3280  O   HOH G 106      27.655  30.921  34.781  1.00 61.98           O  
ANISOU 3280  O   HOH G 106     7497   8148   7906   1195    369    455       O  
HETATM 3281  O   HOH G 107      29.905  13.257  46.012  1.00 39.95           O  
ANISOU 3281  O   HOH G 107     4727   5234   5218   1102   -101    268       O  
HETATM 3282  O   HOH G 108      22.020  23.334  25.278  1.00 47.45           O  
ANISOU 3282  O   HOH G 108     5471   6585   5973   1156    224    383       O  
HETATM 3283  O   HOH G 109      13.250  25.885  22.408  1.00 61.67           O  
ANISOU 3283  O   HOH G 109     7203   8655   7576   1225    308    543       O  
HETATM 3284  O   HOH G 110      34.101   9.041  30.773  1.00 39.40           O  
ANISOU 3284  O   HOH G 110     4495   5337   5138   1195     -1    187       O  
HETATM 3285  O   HOH G 111      37.352  16.961  37.017  1.00 57.80           O  
ANISOU 3285  O   HOH G 111     6765   7680   7518   1140    -21    272       O  
CONECT 3055 3056 3057 3058                                                      
CONECT 3056 3055                                                                
CONECT 3057 3055                                                                
CONECT 3058 3055 3059                                                           
CONECT 3059 3058 3060 3061                                                      
CONECT 3060 3059                                                                
CONECT 3061 3059                                                                
CONECT 3062 3063 3064 3065 3066                                                 
CONECT 3063 3062 3067                                                           
CONECT 3064 3062 3068                                                           
CONECT 3065 3062 3069                                                           
CONECT 3066 3062                                                                
CONECT 3067 3063                                                                
CONECT 3068 3064                                                                
CONECT 3069 3065                                                                
CONECT 3070 3071 3072 3073                                                      
CONECT 3071 3070                                                                
CONECT 3072 3070                                                                
CONECT 3073 3070 3074                                                           
CONECT 3074 3073 3075 3076                                                      
CONECT 3075 3074                                                                
CONECT 3076 3074                                                                
CONECT 3077 3078 3079 3080 3081                                                 
CONECT 3078 3077 3082                                                           
CONECT 3079 3077 3083                                                           
CONECT 3080 3077 3084                                                           
CONECT 3081 3077                                                                
CONECT 3082 3078                                                                
CONECT 3083 3079                                                                
CONECT 3084 3080                                                                
CONECT 3085 3086 3087 3088                                                      
CONECT 3086 3085                                                                
CONECT 3087 3085                                                                
CONECT 3088 3085 3089                                                           
CONECT 3089 3088 3090 3091                                                      
CONECT 3090 3089                                                                
CONECT 3091 3089                                                                
CONECT 3092 3093 3094 3095 3096                                                 
CONECT 3093 3092 3097                                                           
CONECT 3094 3092 3098                                                           
CONECT 3095 3092 3099                                                           
CONECT 3096 3092                                                                
CONECT 3097 3093                                                                
CONECT 3098 3094                                                                
CONECT 3099 3095                                                                
MASTER      371    0    6    9   15    0   10    6 3278    7   45   32          
END

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Related entries of code: 6iiq

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
2kdz	RCSB PDB PDBbind	16-mer
2kmk	RCSB PDB PDBbind	16-mer
2ko0	RCSB PDB PDBbind	16-mer
3co6	RCSB PDB PDBbind	16-mer
3co7	RCSB PDB PDBbind	16-mer
3coa	RCSB PDB PDBbind	16-mer
3f27	RCSB PDB PDBbind	16-mer
3fyl	RCSB PDB PDBbind	16-mer
3g8u	RCSB PDB PDBbind	16-mer
3g99	RCSB PDB PDBbind	16-mer
3g9m	RCSB PDB PDBbind	16-mer
3oqm	RCSB PDB PDBbind	16-mer
3oqn	RCSB PDB PDBbind	16-mer
6mg3	RCSB PDB PDBbind	16-mer
6mg1	RCSB PDB PDBbind	16-mer
6g1l	RCSB PDB PDBbind	16-mer

Entry Information

PDB ID	6iiq
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	HRP3 PWWP domain
Ligand Name	16-mer
EC.Number	E.C.-.-.-.-
Resolution	1.85(Å)
Affinity (Kd/Ki/IC50)	Kd=1.3uM
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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