HEADER    DNA BINDING PROTEIN                     03-AUG-21   7PC1              
TITLE     DNA BINDING DOMAIN OF PARTITION PROTEIN STBA OF PLASMID R388          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STBA;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PLASMID CONJUGATION, PLASMID PARTITION, HELIX-TURN-HELIX, DNA BINDING 
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GUYNET,G.MONCALIAN                                                  
REVDAT   1   10-AUG-22 7PC1    0                                                
JRNL        AUTH   V.QUEBRE,I.DEL CAMPO,A.CUEVAS,P.SIGUIER,J.RECH,P.T.N.LE,     
JRNL        AUTH 2 B.TON-HOANG,F.CORNET,J.Y.BOUET,G.MONCALIAN,F.DE LA CRUZ,     
JRNL        AUTH 3 C.GUYNET                                                     
JRNL        TITL   CHARACTERIZATION OF THE DNA BINDING DOMAIN OF STBA, A KEY    
JRNL        TITL 2 PROTEIN OF A NEW TYPE OF DNA SEGREGATION SYSTEM.             
JRNL        REF    J.MOL.BIOL.                   V. 434 67752 2022              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   35868361                                                     
JRNL        DOI    10.1016/J.JMB.2022.167752                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18_3855                                     
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6276                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 312                             
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 25.9400 -  3.0200    0.99     2951   164  0.0000 0.0000        
REMARK   3     2  3.0100 -  2.3900    1.00     3020   144  0.0000 0.0000        
REMARK   3     3  2.3900 -  2.0900    1.00     3016   180  0.0000 0.0000        
REMARK   3     4  2.0900 -  1.9000    0.97      622   136  0.0000 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.112            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.053           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.91                          
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            603                                  
REMARK   3   ANGLE     :  0.923            810                                  
REMARK   3   CHIRALITY :  0.051             89                                  
REMARK   3   PLANARITY :  0.005            108                                  
REMARK   3   DIHEDRAL  :  3.902             84                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 7PC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292116034.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6294                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX 1.18_3855                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRISODIUM CITRATE DIHYDRATE        
REMARK 280  PH5.6, 10% (V/V) ISO-PROPANOL AND 10% (V/V) PEG 4000, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       11.46433            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       22.92867            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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  51       35.28   -140.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7PC1 A    2    73  UNP    Q6I6C4   Q6I6C4_ECOLX     2     73             
SEQRES   1 A   72  ASN GLU THR ASP ALA LEU LYS ASP ARG ILE GLU ASN ILE          
SEQRES   2 A   72  ARG PRO ARG MSE THR LEU ALA ALA LYS LEU ARG GLU LEU          
SEQRES   3 A   72  MSE PRO GLU ILE ASP ARG GLN VAL ARG ALA GLY VAL GLN          
SEQRES   4 A   72  HIS ASP ASP ILE VAL GLU THR LEU ASN ALA ASN GLY PHE          
SEQRES   5 A   72  ASP VAL ASN LEU ASN THR PHE ARG SER TYR LEU TYR ARG          
SEQRES   6 A   72  TYR ARG LYS LYS ALA ARG ALA                                  
MODRES 7PC1 MSE A   18  MET  MODIFIED RESIDUE                                   
MODRES 7PC1 MSE A   28  MET  MODIFIED RESIDUE                                   
HET    MSE  A  18       8                                                       
HET    MSE  A  28       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *12(H2 O)                                                     
HELIX    1 AA1 THR A    4  ALA A   37  1                                  34    
HELIX    2 AA2 GLN A   40  ALA A   50  1                                  11    
HELIX    3 AA3 ASN A   56  ALA A   73  1                                  18    
LINK         C   ARG A  17                 N   MSE A  18     1555   1555  1.33  
LINK         C   MSE A  18                 N   THR A  19     1555   1555  1.34  
LINK         C   LEU A  27                 N   MSE A  28     1555   1555  1.32  
LINK         C   MSE A  28                 N   PRO A  29     1555   1555  1.35  
CRYST1   45.623   45.623   34.393  90.00  90.00 120.00 P 31          3          
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      0.021919  0.012655  0.000000        0.00000                         
SCALE2      0.000000  0.025310  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029076        0.00000                         
ATOM      1  N   ASN A   2      14.022 -12.545  25.914  1.00 44.58           N  
ATOM      2  CA  ASN A   2      12.972 -12.469  26.931  1.00 40.68           C  
ATOM      3  C   ASN A   2      12.783 -11.039  27.472  1.00 42.77           C  
ATOM      4  O   ASN A   2      11.667 -10.669  27.838  1.00 44.27           O  
ATOM      5  CB  ASN A   2      13.264 -13.449  28.075  1.00 40.76           C  
ATOM      6  CG  ASN A   2      12.316 -14.640  28.083  1.00 49.24           C  
ATOM      7  OD1 ASN A   2      11.224 -14.567  28.658  1.00 52.95           O  
ATOM      8  ND2 ASN A   2      12.720 -15.740  27.444  1.00 48.25           N  
ATOM      9  N   GLU A   3      13.856 -10.237  27.509  1.00 44.44           N  
ATOM     10  CA  GLU A   3      13.739  -8.824  27.877  1.00 41.95           C  
ATOM     11  C   GLU A   3      12.998  -8.056  26.783  1.00 39.42           C  
ATOM     12  O   GLU A   3      13.373  -8.126  25.608  1.00 39.75           O  
ATOM     13  CB  GLU A   3      15.128  -8.208  28.105  1.00 40.59           C  
ATOM     14  CG  GLU A   3      15.090  -6.777  28.657  1.00 38.16           C  
ATOM     15  CD  GLU A   3      16.450  -6.046  28.606  1.00 41.10           C  
ATOM     16  OE1 GLU A   3      17.478  -6.651  28.199  1.00 38.36           O  
ATOM     17  OE2 GLU A   3      16.480  -4.844  28.978  1.00 39.65           O  
ATOM     18  N   THR A   4      11.953  -7.317  27.156  1.00 35.63           N  
ATOM     19  CA  THR A   4      11.157  -6.667  26.121  1.00 38.80           C  
ATOM     20  C   THR A   4      11.961  -5.576  25.418  1.00 39.54           C  
ATOM     21  O   THR A   4      12.835  -4.929  26.000  1.00 39.71           O  
ATOM     22  CB  THR A   4       9.849  -6.084  26.678  1.00 37.21           C  
ATOM     23  OG1 THR A   4      10.124  -4.999  27.571  1.00 39.21           O  
ATOM     24  CG2 THR A   4       9.022  -7.147  27.386  1.00 35.93           C  
ATOM     25  N   ASP A   5      11.677  -5.396  24.131  1.00 40.86           N  
ATOM     26  CA  ASP A   5      12.315  -4.317  23.398  1.00 41.59           C  
ATOM     27  C   ASP A   5      11.904  -2.967  23.943  1.00 36.21           C  
ATOM     28  O   ASP A   5      12.641  -2.001  23.753  1.00 36.88           O  
ATOM     29  CB  ASP A   5      11.984  -4.425  21.906  1.00 47.57           C  
ATOM     30  CG  ASP A   5      12.640  -5.637  21.251  1.00 55.30           C  
ATOM     31  OD1 ASP A   5      11.939  -6.357  20.499  1.00 58.02           O  
ATOM     32  OD2 ASP A   5      13.855  -5.870  21.493  1.00 55.64           O  
ATOM     33  N   ALA A   6      10.749  -2.898  24.617  1.00 35.42           N  
ATOM     34  CA  ALA A   6      10.306  -1.677  25.280  1.00 34.67           C  
ATOM     35  C   ALA A   6      11.229  -1.306  26.443  1.00 37.06           C  
ATOM     36  O   ALA A   6      11.661  -0.150  26.566  1.00 36.34           O  
ATOM     37  CB  ALA A   6       8.867  -1.852  25.766  1.00 31.37           C  
ATOM     38  N   LEU A   7      11.543  -2.271  27.312  1.00 34.61           N  
ATOM     39  CA  LEU A   7      12.499  -1.999  28.379  1.00 33.25           C  
ATOM     40  C   LEU A   7      13.881  -1.703  27.810  1.00 33.19           C  
ATOM     41  O   LEU A   7      14.552  -0.762  28.251  1.00 31.98           O  
ATOM     42  CB  LEU A   7      12.555  -3.179  29.343  1.00 33.67           C  
ATOM     43  CG  LEU A   7      13.503  -2.978  30.518  1.00 32.70           C  
ATOM     44  CD1 LEU A   7      13.114  -1.719  31.281  1.00 29.98           C  
ATOM     45  CD2 LEU A   7      13.494  -4.197  31.417  1.00 31.07           C  
ATOM     46  N   LYS A   8      14.319  -2.498  26.827  1.00 34.98           N  
ATOM     47  CA  LYS A   8      15.602  -2.264  26.167  1.00 34.48           C  
ATOM     48  C   LYS A   8      15.673  -0.856  25.580  1.00 35.35           C  
ATOM     49  O   LYS A   8      16.655  -0.131  25.786  1.00 33.90           O  
ATOM     50  CB  LYS A   8      15.810  -3.319  25.081  1.00 35.96           C  
ATOM     51  CG  LYS A   8      17.239  -3.770  24.875  1.00 40.80           C  
ATOM     52  CD  LYS A   8      17.322  -5.060  24.033  1.00 41.22           C  
ATOM     53  CE  LYS A   8      16.588  -6.204  24.723  1.00 44.17           C  
ATOM     54  NZ  LYS A   8      17.139  -7.544  24.376  1.00 47.50           N  
ATOM     55  N   ASP A   9      14.631  -0.451  24.844  1.00 36.67           N  
ATOM     56  CA  ASP A   9      14.614   0.881  24.245  1.00 37.73           C  
ATOM     57  C   ASP A   9      14.620   1.963  25.316  1.00 34.59           C  
ATOM     58  O   ASP A   9      15.316   2.975  25.179  1.00 34.39           O  
ATOM     59  CB  ASP A   9      13.392   1.040  23.330  1.00 39.60           C  
ATOM     60  CG  ASP A   9      13.416   2.353  22.521  1.00 49.49           C  
ATOM     61  OD1 ASP A   9      14.309   2.514  21.642  1.00 53.41           O  
ATOM     62  OD2 ASP A   9      12.529   3.216  22.751  1.00 49.31           O  
ATOM     63  N   ARG A  10      13.846   1.770  26.388  1.00 32.60           N  
ATOM     64  CA  ARG A  10      13.855   2.740  27.476  1.00 31.48           C  
ATOM     65  C   ARG A  10      15.268   2.938  28.004  1.00 31.42           C  
ATOM     66  O   ARG A  10      15.759   4.070  28.083  1.00 30.33           O  
ATOM     67  CB  ARG A  10      12.917   2.288  28.591  1.00 30.54           C  
ATOM     68  CG  ARG A  10      12.732   3.324  29.655  1.00 32.28           C  
ATOM     69  CD  ARG A  10      11.534   3.020  30.511  1.00 34.97           C  
ATOM     70  NE  ARG A  10      11.628   3.755  31.765  1.00 43.90           N  
ATOM     71  CZ  ARG A  10      11.136   3.329  32.925  1.00 45.09           C  
ATOM     72  NH1 ARG A  10      10.496   2.158  32.984  1.00 43.99           N  
ATOM     73  NH2 ARG A  10      11.283   4.076  34.023  1.00 42.00           N  
ATOM     74  N   ILE A  11      15.952   1.831  28.324  1.00 30.23           N  
ATOM     75  CA  ILE A  11      17.311   1.891  28.848  1.00 27.97           C  
ATOM     76  C   ILE A  11      18.249   2.556  27.845  1.00 30.53           C  
ATOM     77  O   ILE A  11      19.095   3.379  28.218  1.00 30.80           O  
ATOM     78  CB  ILE A  11      17.791   0.478  29.220  1.00 27.31           C  
ATOM     79  CG1 ILE A  11      17.080  -0.020  30.478  1.00 28.64           C  
ATOM     80  CG2 ILE A  11      19.287   0.480  29.430  1.00 28.96           C  
ATOM     81  CD1 ILE A  11      17.316  -1.515  30.781  1.00 26.58           C  
ATOM     82  N   GLU A  12      18.115   2.217  26.558  1.00 32.46           N  
ATOM     83  CA  GLU A  12      18.970   2.803  25.525  1.00 34.89           C  
ATOM     84  C   GLU A  12      18.767   4.310  25.370  1.00 32.49           C  
ATOM     85  O   GLU A  12      19.669   5.006  24.887  1.00 30.81           O  
ATOM     86  CB  GLU A  12      18.729   2.109  24.174  1.00 36.14           C  
ATOM     87  CG  GLU A  12      19.327   0.698  24.083  1.00 43.04           C  
ATOM     88  CD  GLU A  12      18.802  -0.140  22.896  1.00 47.29           C  
ATOM     89  OE1 GLU A  12      18.026   0.385  22.056  1.00 47.72           O  
ATOM     90  OE2 GLU A  12      19.179  -1.338  22.819  1.00 48.78           O  
ATOM     91  N   ASN A  13      17.621   4.845  25.768  1.00 30.98           N  
ATOM     92  CA  ASN A  13      17.391   6.257  25.531  1.00 34.28           C  
ATOM     93  C   ASN A  13      17.533   7.109  26.781  1.00 33.11           C  
ATOM     94  O   ASN A  13      17.317   8.325  26.714  1.00 33.44           O  
ATOM     95  CB  ASN A  13      16.032   6.451  24.867  1.00 33.76           C  
ATOM     96  CG  ASN A  13      16.106   6.166  23.388  1.00 37.73           C  
ATOM     97  OD1 ASN A  13      16.717   6.927  22.636  1.00 38.39           O  
ATOM     98  ND2 ASN A  13      15.546   5.037  22.966  1.00 39.07           N  
ATOM     99  N   ILE A  14      17.949   6.520  27.901  1.00 32.21           N  
ATOM    100  CA  ILE A  14      18.109   7.310  29.116  1.00 32.67           C  
ATOM    101  C   ILE A  14      19.147   8.401  28.900  1.00 33.53           C  
ATOM    102  O   ILE A  14      18.886   9.584  29.158  1.00 33.15           O  
ATOM    103  CB  ILE A  14      18.462   6.411  30.315  1.00 31.48           C  
ATOM    104  CG1 ILE A  14      17.236   5.619  30.742  1.00 31.53           C  
ATOM    105  CG2 ILE A  14      18.930   7.254  31.503  1.00 31.99           C  
ATOM    106  CD1 ILE A  14      17.537   4.546  31.734  1.00 32.73           C  
ATOM    107  N   ARG A  15      20.332   8.029  28.396  1.00 31.66           N  
ATOM    108  CA  ARG A  15      21.408   9.006  28.242  1.00 33.09           C  
ATOM    109  C   ARG A  15      21.120   9.975  27.095  1.00 34.27           C  
ATOM    110  O   ARG A  15      21.369  11.182  27.240  1.00 33.97           O  
ATOM    111  CB  ARG A  15      22.762   8.313  28.046  1.00 36.21           C  
ATOM    112  CG  ARG A  15      23.393   7.795  29.351  1.00 41.00           C  
ATOM    113  CD  ARG A  15      24.861   7.395  29.168  1.00 41.98           C  
ATOM    114  NE  ARG A  15      25.733   8.459  29.663  1.00 52.02           N  
ATOM    115  CZ  ARG A  15      26.754   8.285  30.501  1.00 53.58           C  
ATOM    116  NH1 ARG A  15      27.064   7.067  30.941  1.00 48.27           N  
ATOM    117  NH2 ARG A  15      27.472   9.337  30.902  1.00 54.47           N  
ATOM    118  N   PRO A  16      20.613   9.511  25.945  1.00 33.06           N  
ATOM    119  CA  PRO A  16      20.194  10.479  24.918  1.00 32.61           C  
ATOM    120  C   PRO A  16      19.213  11.520  25.431  1.00 31.53           C  
ATOM    121  O   PRO A  16      19.341  12.699  25.085  1.00 30.90           O  
ATOM    122  CB  PRO A  16      19.563   9.582  23.847  1.00 33.13           C  
ATOM    123  CG  PRO A  16      20.327   8.302  23.961  1.00 30.42           C  
ATOM    124  CD  PRO A  16      20.565   8.125  25.430  1.00 31.69           C  
ATOM    125  N   ARG A  17      18.240  11.115  26.252  1.00 31.58           N  
ATOM    126  CA  ARG A  17      17.235  12.055  26.741  1.00 32.99           C  
ATOM    127  C   ARG A  17      17.823  13.057  27.734  1.00 31.97           C  
ATOM    128  O   ARG A  17      17.413  14.225  27.752  1.00 30.85           O  
ATOM    129  CB  ARG A  17      16.068  11.283  27.361  1.00 31.59           C  
ATOM    130  CG  ARG A  17      15.227  10.562  26.321  1.00 35.92           C  
ATOM    131  CD  ARG A  17      14.198   9.669  26.952  1.00 38.56           C  
ATOM    132  NE  ARG A  17      13.188  10.460  27.638  1.00 45.14           N  
ATOM    133  CZ  ARG A  17      11.994  10.758  27.127  1.00 50.96           C  
ATOM    134  NH1 ARG A  17      11.652  10.316  25.914  1.00 48.26           N  
ATOM    135  NH2 ARG A  17      11.136  11.494  27.835  1.00 48.41           N  
HETATM  136  N   MSE A  18      18.785  12.635  28.549  1.00 32.40           N  
HETATM  137  CA  MSE A  18      19.485  13.555  29.431  1.00 30.05           C  
HETATM  138  C   MSE A  18      20.212  14.624  28.630  1.00 32.24           C  
HETATM  139  O   MSE A  18      20.275  15.785  29.039  1.00 32.72           O  
HETATM  140  CB  MSE A  18      20.482  12.807  30.319  1.00 29.89           C  
HETATM  141  CG  MSE A  18      19.842  11.902  31.350  1.00 34.00           C  
HETATM  142 SE   MSE A  18      21.102  10.735  32.284  0.39 32.98          SE  
HETATM  143  CE  MSE A  18      22.644  11.890  32.491  1.00 30.64           C  
ATOM    144  N   THR A  19      20.792  14.224  27.495  1.00 32.66           N  
ATOM    145  CA  THR A  19      21.465  15.199  26.638  1.00 32.86           C  
ATOM    146  C   THR A  19      20.470  16.185  26.028  1.00 30.62           C  
ATOM    147  O   THR A  19      20.742  17.391  25.968  1.00 30.07           O  
ATOM    148  CB  THR A  19      22.256  14.476  25.550  1.00 32.30           C  
ATOM    149  OG1 THR A  19      23.170  13.565  26.171  1.00 32.98           O  
ATOM    150  CG2 THR A  19      23.031  15.471  24.672  1.00 28.24           C  
ATOM    151  N   LEU A  20      19.310  15.689  25.582  1.00 30.31           N  
ATOM    152  CA  LEU A  20      18.273  16.570  25.054  1.00 30.96           C  
ATOM    153  C   LEU A  20      17.738  17.490  26.135  1.00 30.28           C  
ATOM    154  O   LEU A  20      17.524  18.684  25.894  1.00 31.48           O  
ATOM    155  CB  LEU A  20      17.130  15.757  24.448  1.00 28.56           C  
ATOM    156  CG  LEU A  20      17.452  14.973  23.183  1.00 29.95           C  
ATOM    157  CD1 LEU A  20      16.251  14.159  22.802  1.00 31.73           C  
ATOM    158  CD2 LEU A  20      17.859  15.872  22.047  1.00 31.98           C  
ATOM    159  N   ALA A  21      17.511  16.954  27.332  1.00 30.84           N  
ATOM    160  CA  ALA A  21      17.083  17.803  28.435  1.00 32.31           C  
ATOM    161  C   ALA A  21      18.054  18.957  28.629  1.00 34.48           C  
ATOM    162  O   ALA A  21      17.641  20.112  28.784  1.00 35.59           O  
ATOM    163  CB  ALA A  21      16.957  16.976  29.713  1.00 31.86           C  
ATOM    164  N   ALA A  22      19.354  18.665  28.588  1.00 33.43           N  
ATOM    165  CA  ALA A  22      20.354  19.711  28.743  1.00 30.43           C  
ATOM    166  C   ALA A  22      20.297  20.705  27.592  1.00 32.60           C  
ATOM    167  O   ALA A  22      20.471  21.914  27.800  1.00 33.80           O  
ATOM    168  CB  ALA A  22      21.739  19.078  28.851  1.00 31.34           C  
ATOM    169  N   LYS A  23      20.074  20.212  26.366  1.00 31.99           N  
ATOM    170  CA  LYS A  23      19.947  21.105  25.214  1.00 32.57           C  
ATOM    171  C   LYS A  23      18.744  22.023  25.370  1.00 35.18           C  
ATOM    172  O   LYS A  23      18.786  23.197  24.975  1.00 33.66           O  
ATOM    173  CB  LYS A  23      19.811  20.296  23.927  1.00 31.63           C  
ATOM    174  CG  LYS A  23      21.028  19.487  23.536  1.00 32.43           C  
ATOM    175  CD  LYS A  23      22.267  20.333  23.491  1.00 34.44           C  
ATOM    176  CE  LYS A  23      23.418  19.546  22.898  1.00 35.31           C  
ATOM    177  NZ  LYS A  23      24.620  20.399  22.773  1.00 41.05           N  
ATOM    178  N   LEU A  24      17.655  21.491  25.935  1.00 34.46           N  
ATOM    179  CA  LEU A  24      16.445  22.278  26.120  1.00 33.30           C  
ATOM    180  C   LEU A  24      16.667  23.385  27.145  1.00 32.61           C  
ATOM    181  O   LEU A  24      16.219  24.519  26.944  1.00 34.43           O  
ATOM    182  CB  LEU A  24      15.292  21.353  26.520  1.00 30.85           C  
ATOM    183  CG  LEU A  24      13.913  21.993  26.703  1.00 33.81           C  
ATOM    184  CD1 LEU A  24      13.533  22.837  25.481  1.00 31.84           C  
ATOM    185  CD2 LEU A  24      12.856  20.918  27.013  1.00 32.60           C  
ATOM    186  N   ARG A  25      17.381  23.089  28.236  1.00 31.44           N  
ATOM    187  CA  ARG A  25      17.726  24.136  29.195  1.00 32.58           C  
ATOM    188  C   ARG A  25      18.554  25.240  28.546  1.00 34.65           C  
ATOM    189  O   ARG A  25      18.377  26.426  28.858  1.00 35.31           O  
ATOM    190  CB  ARG A  25      18.480  23.536  30.373  1.00 33.71           C  
ATOM    191  CG  ARG A  25      17.652  22.568  31.139  1.00 38.58           C  
ATOM    192  CD  ARG A  25      18.438  21.857  32.206  1.00 42.17           C  
ATOM    193  NE  ARG A  25      17.588  20.814  32.772  1.00 49.13           N  
ATOM    194  CZ  ARG A  25      17.890  19.524  32.803  1.00 47.01           C  
ATOM    195  NH1 ARG A  25      19.056  19.109  32.317  1.00 46.02           N  
ATOM    196  NH2 ARG A  25      17.028  18.658  33.335  1.00 46.46           N  
ATOM    197  N   GLU A  26      19.459  24.875  27.634  1.00 33.06           N  
ATOM    198  CA  GLU A  26      20.282  25.882  26.978  1.00 31.89           C  
ATOM    199  C   GLU A  26      19.457  26.780  26.083  1.00 32.10           C  
ATOM    200  O   GLU A  26      19.876  27.899  25.795  1.00 36.23           O  
ATOM    201  CB  GLU A  26      21.379  25.225  26.148  1.00 36.88           C  
ATOM    202  CG  GLU A  26      22.277  24.287  26.931  1.00 40.88           C  
ATOM    203  CD  GLU A  26      23.245  23.534  26.041  1.00 44.75           C  
ATOM    204  OE1 GLU A  26      23.223  23.752  24.799  1.00 42.85           O  
ATOM    205  OE2 GLU A  26      24.001  22.699  26.588  1.00 47.11           O  
ATOM    206  N   LEU A  27      18.313  26.296  25.596  1.00 32.43           N  
ATOM    207  CA  LEU A  27      17.439  27.077  24.733  1.00 31.55           C  
ATOM    208  C   LEU A  27      16.553  28.035  25.509  1.00 30.79           C  
ATOM    209  O   LEU A  27      15.933  28.921  24.908  1.00 30.67           O  
ATOM    210  CB  LEU A  27      16.541  26.156  23.908  1.00 31.49           C  
ATOM    211  CG  LEU A  27      17.073  25.461  22.661  1.00 35.01           C  
ATOM    212  CD1 LEU A  27      16.162  24.305  22.326  1.00 34.59           C  
ATOM    213  CD2 LEU A  27      17.160  26.432  21.484  1.00 34.82           C  
HETATM  214  N   MSE A  28      16.462  27.877  26.819  1.00 30.82           N  
HETATM  215  CA  MSE A  28      15.462  28.622  27.578  1.00 32.57           C  
HETATM  216  C   MSE A  28      15.614  30.159  27.546  1.00 30.36           C  
HETATM  217  O   MSE A  28      14.604  30.840  27.460  1.00 27.71           O  
HETATM  218  CB  MSE A  28      15.426  28.102  29.021  1.00 32.01           C  
HETATM  219  CG  MSE A  28      14.734  26.745  29.111  1.00 31.36           C  
HETATM  220 SE   MSE A  28      12.864  26.880  28.592  0.56 39.85          SE  
HETATM  221  CE  MSE A  28      12.555  25.161  27.789  1.00 32.61           C  
ATOM    222  N   PRO A  29      16.842  30.707  27.605  1.00 31.21           N  
ATOM    223  CA  PRO A  29      16.966  32.170  27.463  1.00 30.82           C  
ATOM    224  C   PRO A  29      16.308  32.713  26.194  1.00 30.02           C  
ATOM    225  O   PRO A  29      15.553  33.691  26.258  1.00 29.91           O  
ATOM    226  CB  PRO A  29      18.492  32.385  27.489  1.00 27.98           C  
ATOM    227  CG  PRO A  29      19.006  31.278  28.291  1.00 27.92           C  
ATOM    228  CD  PRO A  29      18.150  30.101  27.935  1.00 31.02           C  
ATOM    229  N   GLU A  30      16.542  32.093  25.040  1.00 28.76           N  
ATOM    230  CA  GLU A  30      15.925  32.613  23.828  1.00 30.01           C  
ATOM    231  C   GLU A  30      14.429  32.312  23.805  1.00 32.95           C  
ATOM    232  O   GLU A  30      13.631  33.143  23.344  1.00 33.49           O  
ATOM    233  CB  GLU A  30      16.630  32.046  22.589  1.00 32.74           C  
ATOM    234  CG  GLU A  30      15.999  32.435  21.251  1.00 33.84           C  
ATOM    235  CD  GLU A  30      16.202  33.906  20.890  1.00 40.47           C  
ATOM    236  OE1 GLU A  30      17.027  34.579  21.546  1.00 42.65           O  
ATOM    237  OE2 GLU A  30      15.538  34.391  19.941  1.00 42.71           O  
ATOM    238  N   ILE A  31      14.024  31.143  24.314  1.00 28.54           N  
ATOM    239  CA  ILE A  31      12.595  30.828  24.379  1.00 30.39           C  
ATOM    240  C   ILE A  31      11.863  31.860  25.238  1.00 31.03           C  
ATOM    241  O   ILE A  31      10.808  32.381  24.856  1.00 30.18           O  
ATOM    242  CB  ILE A  31      12.379  29.396  24.911  1.00 31.68           C  
ATOM    243  CG1 ILE A  31      12.706  28.356  23.824  1.00 31.03           C  
ATOM    244  CG2 ILE A  31      10.941  29.235  25.487  1.00 27.60           C  
ATOM    245  CD1 ILE A  31      12.907  26.922  24.355  1.00 27.21           C  
ATOM    246  N   ASP A  32      12.418  32.168  26.414  1.00 30.37           N  
ATOM    247  CA  ASP A  32      11.811  33.148  27.310  1.00 30.11           C  
ATOM    248  C   ASP A  32      11.666  34.506  26.631  1.00 32.26           C  
ATOM    249  O   ASP A  32      10.613  35.148  26.733  1.00 33.81           O  
ATOM    250  CB  ASP A  32      12.651  33.262  28.583  1.00 29.55           C  
ATOM    251  CG  ASP A  32      12.064  34.225  29.581  1.00 34.78           C  
ATOM    252  OD1 ASP A  32      10.842  34.161  29.841  1.00 34.10           O  
ATOM    253  OD2 ASP A  32      12.825  35.065  30.101  1.00 40.01           O  
ATOM    254  N   ARG A  33      12.701  34.947  25.911  1.00 29.72           N  
ATOM    255  CA  ARG A  33      12.630  36.211  25.186  1.00 30.42           C  
ATOM    256  C   ARG A  33      11.461  36.221  24.198  1.00 32.32           C  
ATOM    257  O   ARG A  33      10.620  37.129  24.217  1.00 31.28           O  
ATOM    258  CB  ARG A  33      13.961  36.454  24.475  1.00 34.19           C  
ATOM    259  CG  ARG A  33      14.174  37.865  23.930  1.00 41.28           C  
ATOM    260  CD  ARG A  33      15.386  37.953  22.963  1.00 42.21           C  
ATOM    261  NE  ARG A  33      15.165  37.226  21.707  1.00 45.87           N  
ATOM    262  CZ  ARG A  33      14.367  37.639  20.716  1.00 48.83           C  
ATOM    263  NH1 ARG A  33      13.696  38.790  20.812  1.00 49.10           N  
ATOM    264  NH2 ARG A  33      14.231  36.895  19.621  1.00 46.22           N  
ATOM    265  N   GLN A  34      11.370  35.195  23.348  1.00 31.01           N  
ATOM    266  CA  GLN A  34      10.342  35.179  22.309  1.00 30.27           C  
ATOM    267  C   GLN A  34       8.953  35.019  22.898  1.00 30.01           C  
ATOM    268  O   GLN A  34       7.979  35.574  22.384  1.00 30.02           O  
ATOM    269  CB  GLN A  34      10.620  34.051  21.326  1.00 32.14           C  
ATOM    270  CG  GLN A  34      11.881  34.274  20.522  1.00 35.12           C  
ATOM    271  CD  GLN A  34      11.876  33.533  19.206  1.00 34.93           C  
ATOM    272  OE1 GLN A  34      10.846  33.015  18.770  1.00 35.35           O  
ATOM    273  NE2 GLN A  34      13.039  33.483  18.558  1.00 37.67           N  
ATOM    274  N   VAL A  35       8.847  34.242  23.969  1.00 31.11           N  
ATOM    275  CA  VAL A  35       7.556  33.923  24.551  1.00 30.67           C  
ATOM    276  C   VAL A  35       6.976  35.138  25.263  1.00 31.77           C  
ATOM    277  O   VAL A  35       5.763  35.375  25.214  1.00 32.27           O  
ATOM    278  CB  VAL A  35       7.754  32.696  25.462  1.00 32.35           C  
ATOM    279  CG1 VAL A  35       7.239  32.907  26.878  1.00 32.41           C  
ATOM    280  CG2 VAL A  35       7.192  31.460  24.785  1.00 31.54           C  
ATOM    281  N   ARG A  36       7.823  35.952  25.891  1.00 29.11           N  
ATOM    282  CA  ARG A  36       7.333  37.190  26.475  1.00 31.65           C  
ATOM    283  C   ARG A  36       7.020  38.239  25.415  1.00 33.15           C  
ATOM    284  O   ARG A  36       6.281  39.189  25.697  1.00 33.44           O  
ATOM    285  CB  ARG A  36       8.343  37.731  27.487  1.00 32.14           C  
ATOM    286  CG  ARG A  36       8.260  37.023  28.836  1.00 35.02           C  
ATOM    287  CD  ARG A  36       9.109  37.720  29.881  1.00 40.22           C  
ATOM    288  NE  ARG A  36      10.512  37.316  29.796  1.00 44.12           N  
ATOM    289  CZ  ARG A  36      11.473  38.054  29.243  1.00 44.29           C  
ATOM    290  NH1 ARG A  36      11.188  39.243  28.721  1.00 49.02           N  
ATOM    291  NH2 ARG A  36      12.719  37.605  29.210  1.00 41.40           N  
ATOM    292  N   ALA A  37       7.559  38.095  24.210  1.00 31.20           N  
ATOM    293  CA  ALA A  37       7.224  38.986  23.114  1.00 28.80           C  
ATOM    294  C   ALA A  37       5.930  38.575  22.423  1.00 34.17           C  
ATOM    295  O   ALA A  37       5.520  39.225  21.455  1.00 36.69           O  
ATOM    296  CB  ALA A  37       8.378  39.024  22.109  1.00 26.67           C  
ATOM    297  N   GLY A  38       5.283  37.507  22.883  1.00 30.46           N  
ATOM    298  CA  GLY A  38       4.037  37.066  22.304  1.00 29.13           C  
ATOM    299  C   GLY A  38       4.081  35.741  21.567  1.00 29.93           C  
ATOM    300  O   GLY A  38       3.044  35.322  21.048  1.00 31.64           O  
ATOM    301  N   VAL A  39       5.219  35.057  21.485  1.00 30.22           N  
ATOM    302  CA  VAL A  39       5.205  33.731  20.881  1.00 29.79           C  
ATOM    303  C   VAL A  39       4.545  32.764  21.854  1.00 29.44           C  
ATOM    304  O   VAL A  39       4.848  32.771  23.055  1.00 29.73           O  
ATOM    305  CB  VAL A  39       6.623  33.277  20.502  1.00 31.53           C  
ATOM    306  CG1 VAL A  39       6.568  31.886  19.908  1.00 31.55           C  
ATOM    307  CG2 VAL A  39       7.245  34.236  19.496  1.00 31.36           C  
ATOM    308  N   GLN A  40       3.619  31.949  21.343  1.00 29.94           N  
ATOM    309  CA  GLN A  40       2.833  31.040  22.172  1.00 29.86           C  
ATOM    310  C   GLN A  40       3.671  29.850  22.638  1.00 27.68           C  
ATOM    311  O   GLN A  40       4.510  29.338  21.894  1.00 28.60           O  
ATOM    312  CB  GLN A  40       1.632  30.546  21.379  1.00 30.52           C  
ATOM    313  CG  GLN A  40       0.336  31.289  21.618  1.00 35.46           C  
ATOM    314  CD  GLN A  40      -0.851  30.383  21.331  1.00 45.22           C  
ATOM    315  OE1 GLN A  40      -1.401  29.742  22.241  1.00 45.99           O  
ATOM    316  NE2 GLN A  40      -1.223  30.281  20.052  1.00 42.58           N  
ATOM    317  N   HIS A  41       3.443  29.401  23.879  1.00 28.01           N  
ATOM    318  CA  HIS A  41       4.117  28.187  24.355  1.00 28.41           C  
ATOM    319  C   HIS A  41       3.825  27.007  23.437  1.00 26.70           C  
ATOM    320  O   HIS A  41       4.730  26.247  23.078  1.00 23.49           O  
ATOM    321  CB  HIS A  41       3.689  27.842  25.782  1.00 24.87           C  
ATOM    322  CG  HIS A  41       4.137  28.831  26.802  1.00 26.39           C  
ATOM    323  ND1 HIS A  41       3.889  28.672  28.146  1.00 25.61           N  
ATOM    324  CD2 HIS A  41       4.798  30.006  26.671  1.00 26.31           C  
ATOM    325  CE1 HIS A  41       4.390  29.705  28.803  1.00 26.90           C  
ATOM    326  NE2 HIS A  41       4.950  30.526  27.931  1.00 25.86           N  
ATOM    327  N   ASP A  42       2.554  26.845  23.056  1.00 24.45           N  
ATOM    328  CA  ASP A  42       2.141  25.748  22.192  1.00 26.43           C  
ATOM    329  C   ASP A  42       2.917  25.734  20.883  1.00 28.10           C  
ATOM    330  O   ASP A  42       3.176  24.658  20.325  1.00 26.02           O  
ATOM    331  CB  ASP A  42       0.642  25.848  21.902  1.00 30.85           C  
ATOM    332  CG  ASP A  42      -0.222  25.277  23.022  1.00 36.87           C  
ATOM    333  OD1 ASP A  42      -1.392  25.685  23.171  1.00 41.38           O  
ATOM    334  OD2 ASP A  42       0.262  24.398  23.758  1.00 40.19           O  
ATOM    335  N   ASP A  43       3.273  26.912  20.365  1.00 26.56           N  
ATOM    336  CA  ASP A  43       4.012  26.967  19.107  1.00 28.02           C  
ATOM    337  C   ASP A  43       5.417  26.408  19.276  1.00 27.27           C  
ATOM    338  O   ASP A  43       5.894  25.640  18.431  1.00 25.88           O  
ATOM    339  CB  ASP A  43       4.080  28.409  18.584  1.00 31.46           C  
ATOM    340  CG  ASP A  43       2.758  28.890  17.977  1.00 34.81           C  
ATOM    341  OD1 ASP A  43       1.753  28.144  17.983  1.00 36.21           O  
ATOM    342  OD2 ASP A  43       2.728  30.034  17.490  1.00 40.32           O  
ATOM    343  N   ILE A  44       6.095  26.780  20.360  1.00 25.78           N  
ATOM    344  CA  ILE A  44       7.438  26.259  20.593  1.00 28.05           C  
ATOM    345  C   ILE A  44       7.386  24.767  20.901  1.00 24.85           C  
ATOM    346  O   ILE A  44       8.239  23.996  20.444  1.00 24.52           O  
ATOM    347  CB  ILE A  44       8.132  27.063  21.710  1.00 28.52           C  
ATOM    348  CG1 ILE A  44       8.222  28.537  21.292  1.00 29.93           C  
ATOM    349  CG2 ILE A  44       9.530  26.506  21.997  1.00 25.18           C  
ATOM    350  CD1 ILE A  44       8.999  29.400  22.253  1.00 30.22           C  
ATOM    351  N   VAL A  45       6.372  24.334  21.652  1.00 23.35           N  
ATOM    352  CA  VAL A  45       6.242  22.919  21.964  1.00 23.65           C  
ATOM    353  C   VAL A  45       6.044  22.108  20.688  1.00 24.70           C  
ATOM    354  O   VAL A  45       6.626  21.031  20.532  1.00 23.85           O  
ATOM    355  CB  VAL A  45       5.111  22.695  22.985  1.00 23.10           C  
ATOM    356  CG1 VAL A  45       4.854  21.219  23.158  1.00 25.20           C  
ATOM    357  CG2 VAL A  45       5.510  23.287  24.318  1.00 23.16           C  
ATOM    358  N   GLU A  46       5.263  22.625  19.737  1.00 23.48           N  
ATOM    359  CA  GLU A  46       5.109  21.932  18.458  1.00 23.98           C  
ATOM    360  C   GLU A  46       6.452  21.770  17.742  1.00 26.29           C  
ATOM    361  O   GLU A  46       6.762  20.691  17.221  1.00 25.61           O  
ATOM    362  CB  GLU A  46       4.122  22.673  17.557  1.00 25.63           C  
ATOM    363  CG  GLU A  46       3.976  21.988  16.211  1.00 26.50           C  
ATOM    364  CD  GLU A  46       3.269  22.810  15.151  1.00 27.18           C  
ATOM    365  OE1 GLU A  46       2.764  23.914  15.447  1.00 30.56           O  
ATOM    366  OE2 GLU A  46       3.200  22.322  14.004  1.00 29.34           O  
ATOM    367  N   THR A  47       7.260  22.836  17.695  1.00 24.16           N  
ATOM    368  CA  THR A  47       8.564  22.747  17.040  1.00 26.16           C  
ATOM    369  C   THR A  47       9.462  21.728  17.737  1.00 25.67           C  
ATOM    370  O   THR A  47      10.130  20.919  17.079  1.00 26.13           O  
ATOM    371  CB  THR A  47       9.231  24.124  17.005  1.00 26.47           C  
ATOM    372  OG1 THR A  47       8.356  25.057  16.372  1.00 27.16           O  
ATOM    373  CG2 THR A  47      10.526  24.067  16.224  1.00 27.83           C  
ATOM    374  N   LEU A  48       9.462  21.735  19.069  1.00 24.99           N  
ATOM    375  CA  LEU A  48      10.217  20.750  19.830  1.00 25.54           C  
ATOM    376  C   LEU A  48       9.731  19.334  19.541  1.00 27.37           C  
ATOM    377  O   LEU A  48      10.543  18.411  19.396  1.00 29.37           O  
ATOM    378  CB  LEU A  48      10.108  21.063  21.324  1.00 24.61           C  
ATOM    379  CG  LEU A  48      10.819  22.332  21.778  1.00 23.33           C  
ATOM    380  CD1 LEU A  48      10.449  22.679  23.205  1.00 23.36           C  
ATOM    381  CD2 LEU A  48      12.322  22.124  21.635  1.00 25.20           C  
ATOM    382  N   ASN A  49       8.409  19.141  19.448  1.00 26.16           N  
ATOM    383  CA  ASN A  49       7.853  17.795  19.277  1.00 28.20           C  
ATOM    384  C   ASN A  49       8.043  17.274  17.861  1.00 28.60           C  
ATOM    385  O   ASN A  49       7.929  16.062  17.634  1.00 31.16           O  
ATOM    386  CB  ASN A  49       6.352  17.758  19.622  1.00 27.69           C  
ATOM    387  CG  ASN A  49       6.060  17.949  21.119  1.00 28.69           C  
ATOM    388  OD1 ASN A  49       4.937  18.263  21.494  1.00 30.57           O  
ATOM    389  ND2 ASN A  49       7.056  17.752  21.961  1.00 30.48           N  
ATOM    390  N   ALA A  50       8.307  18.160  16.905  1.00 28.09           N  
ATOM    391  CA  ALA A  50       8.633  17.756  15.547  1.00 29.40           C  
ATOM    392  C   ALA A  50      10.123  17.482  15.358  1.00 30.47           C  
ATOM    393  O   ALA A  50      10.531  17.099  14.259  1.00 29.92           O  
ATOM    394  CB  ALA A  50       8.169  18.826  14.552  1.00 27.26           C  
ATOM    395  N   ASN A  51      10.941  17.637  16.399  1.00 28.57           N  
ATOM    396  CA  ASN A  51      12.380  17.552  16.210  1.00 30.38           C  
ATOM    397  C   ASN A  51      13.050  16.808  17.353  1.00 32.28           C  
ATOM    398  O   ASN A  51      14.176  17.135  17.747  1.00 34.20           O  
ATOM    399  CB  ASN A  51      12.995  18.937  16.051  1.00 30.85           C  
ATOM    400  CG  ASN A  51      12.619  19.593  14.730  1.00 33.77           C  
ATOM    401  OD1 ASN A  51      13.184  19.269  13.685  1.00 34.20           O  
ATOM    402  ND2 ASN A  51      11.666  20.528  14.775  1.00 32.32           N  
ATOM    403  N   GLY A  52      12.378  15.790  17.899  1.00 32.36           N  
ATOM    404  CA  GLY A  52      13.016  14.866  18.818  1.00 32.54           C  
ATOM    405  C   GLY A  52      12.824  15.125  20.301  1.00 34.49           C  
ATOM    406  O   GLY A  52      13.320  14.338  21.115  1.00 36.58           O  
ATOM    407  N   PHE A  53      12.152  16.201  20.693  1.00 30.91           N  
ATOM    408  CA  PHE A  53      11.906  16.473  22.105  1.00 32.85           C  
ATOM    409  C   PHE A  53      10.459  16.105  22.385  1.00 36.04           C  
ATOM    410  O   PHE A  53       9.552  16.753  21.855  1.00 37.95           O  
ATOM    411  CB  PHE A  53      12.131  17.940  22.456  1.00 30.13           C  
ATOM    412  CG  PHE A  53      13.524  18.428  22.235  1.00 29.79           C  
ATOM    413  CD1 PHE A  53      13.969  18.754  20.959  1.00 28.55           C  
ATOM    414  CD2 PHE A  53      14.370  18.635  23.314  1.00 30.17           C  
ATOM    415  CE1 PHE A  53      15.247  19.238  20.757  1.00 29.37           C  
ATOM    416  CE2 PHE A  53      15.654  19.118  23.127  1.00 31.25           C  
ATOM    417  CZ  PHE A  53      16.097  19.418  21.843  1.00 31.54           C  
ATOM    418  N   ASP A  54      10.229  15.094  23.226  1.00 36.31           N  
ATOM    419  CA  ASP A  54       8.861  14.653  23.486  1.00 37.87           C  
ATOM    420  C   ASP A  54       8.176  15.413  24.638  1.00 36.68           C  
ATOM    421  O   ASP A  54       7.130  14.975  25.119  1.00 43.03           O  
ATOM    422  CB  ASP A  54       8.833  13.142  23.736  1.00 40.49           C  
ATOM    423  CG  ASP A  54       9.377  12.761  25.089  1.00 47.72           C  
ATOM    424  OD1 ASP A  54       9.957  13.644  25.764  1.00 51.76           O  
ATOM    425  OD2 ASP A  54       9.216  11.580  25.483  1.00 51.72           O  
ATOM    426  N   VAL A  55       8.728  16.550  25.054  1.00 35.86           N  
ATOM    427  CA  VAL A  55       8.170  17.373  26.121  1.00 34.20           C  
ATOM    428  C   VAL A  55       6.695  17.708  25.868  1.00 33.38           C  
ATOM    429  O   VAL A  55       6.273  17.926  24.728  1.00 37.01           O  
ATOM    430  CB  VAL A  55       9.045  18.638  26.230  1.00 35.34           C  
ATOM    431  CG1 VAL A  55       8.924  19.487  24.950  1.00 33.84           C  
ATOM    432  CG2 VAL A  55       8.691  19.461  27.444  1.00 35.76           C  
ATOM    433  N   ASN A  56       5.899  17.752  26.939  1.00 31.77           N  
ATOM    434  CA  ASN A  56       4.547  18.293  26.847  1.00 33.77           C  
ATOM    435  C   ASN A  56       4.518  19.724  27.399  1.00 30.94           C  
ATOM    436  O   ASN A  56       5.515  20.257  27.887  1.00 31.33           O  
ATOM    437  CB  ASN A  56       3.518  17.405  27.565  1.00 31.95           C  
ATOM    438  CG  ASN A  56       3.870  17.137  29.021  1.00 32.34           C  
ATOM    439  OD1 ASN A  56       4.137  18.046  29.806  1.00 32.96           O  
ATOM    440  ND2 ASN A  56       3.856  15.876  29.386  1.00 40.23           N  
ATOM    441  N   LEU A  57       3.344  20.349  27.316  1.00 29.44           N  
ATOM    442  CA  LEU A  57       3.208  21.742  27.726  1.00 28.29           C  
ATOM    443  C   LEU A  57       3.536  21.931  29.200  1.00 28.82           C  
ATOM    444  O   LEU A  57       4.152  22.933  29.578  1.00 28.00           O  
ATOM    445  CB  LEU A  57       1.792  22.236  27.427  1.00 27.17           C  
ATOM    446  CG  LEU A  57       1.592  23.736  27.534  1.00 27.92           C  
ATOM    447  CD1 LEU A  57       2.603  24.504  26.699  1.00 25.49           C  
ATOM    448  CD2 LEU A  57       0.195  24.077  27.113  1.00 31.02           C  
ATOM    449  N   ASN A  58       3.120  20.987  30.050  1.00 30.47           N  
ATOM    450  CA  ASN A  58       3.429  21.080  31.476  1.00 31.48           C  
ATOM    451  C   ASN A  58       4.927  21.014  31.719  1.00 29.96           C  
ATOM    452  O   ASN A  58       5.473  21.798  32.502  1.00 30.02           O  
ATOM    453  CB  ASN A  58       2.732  19.960  32.246  1.00 33.56           C  
ATOM    454  CG  ASN A  58       1.438  20.400  32.854  1.00 41.19           C  
ATOM    455  OD1 ASN A  58       0.597  21.001  32.184  1.00 43.63           O  
ATOM    456  ND2 ASN A  58       1.264  20.116  34.140  1.00 49.99           N  
ATOM    457  N   THR A  59       5.609  20.079  31.058  1.00 28.30           N  
ATOM    458  CA  THR A  59       7.040  19.930  31.265  1.00 28.44           C  
ATOM    459  C   THR A  59       7.794  21.122  30.712  1.00 30.26           C  
ATOM    460  O   THR A  59       8.718  21.632  31.356  1.00 31.16           O  
ATOM    461  CB  THR A  59       7.519  18.640  30.613  1.00 32.20           C  
ATOM    462  OG1 THR A  59       6.751  17.546  31.128  1.00 35.84           O  
ATOM    463  CG2 THR A  59       9.002  18.404  30.898  1.00 31.94           C  
ATOM    464  N   PHE A  60       7.406  21.585  29.523  1.00 28.84           N  
ATOM    465  CA  PHE A  60       8.010  22.779  28.944  1.00 25.57           C  
ATOM    466  C   PHE A  60       7.913  23.961  29.905  1.00 26.95           C  
ATOM    467  O   PHE A  60       8.896  24.676  30.135  1.00 27.18           O  
ATOM    468  CB  PHE A  60       7.321  23.070  27.603  1.00 26.04           C  
ATOM    469  CG  PHE A  60       7.655  24.402  27.014  1.00 26.03           C  
ATOM    470  CD1 PHE A  60       8.750  24.543  26.176  1.00 25.62           C  
ATOM    471  CD2 PHE A  60       6.864  25.521  27.289  1.00 27.29           C  
ATOM    472  CE1 PHE A  60       9.061  25.770  25.628  1.00 26.81           C  
ATOM    473  CE2 PHE A  60       7.174  26.754  26.755  1.00 25.88           C  
ATOM    474  CZ  PHE A  60       8.272  26.875  25.914  1.00 28.38           C  
ATOM    475  N   ARG A  61       6.740  24.170  30.503  1.00 27.75           N  
ATOM    476  CA  ARG A  61       6.575  25.312  31.401  1.00 28.60           C  
ATOM    477  C   ARG A  61       7.442  25.162  32.645  1.00 27.89           C  
ATOM    478  O   ARG A  61       8.009  26.149  33.127  1.00 27.51           O  
ATOM    479  CB  ARG A  61       5.099  25.485  31.772  1.00 29.01           C  
ATOM    480  CG  ARG A  61       4.329  26.317  30.759  1.00 28.01           C  
ATOM    481  CD  ARG A  61       2.834  26.085  30.816  1.00 28.20           C  
ATOM    482  NE  ARG A  61       2.157  26.909  29.818  1.00 28.15           N  
ATOM    483  CZ  ARG A  61       0.860  26.848  29.539  1.00 28.06           C  
ATOM    484  NH1 ARG A  61       0.076  25.997  30.196  1.00 28.57           N  
ATOM    485  NH2 ARG A  61       0.352  27.645  28.601  1.00 26.07           N  
ATOM    486  N   SER A  62       7.575  23.931  33.156  1.00 27.76           N  
ATOM    487  CA  SER A  62       8.487  23.648  34.268  1.00 29.99           C  
ATOM    488  C   SER A  62       9.902  24.129  33.980  1.00 29.61           C  
ATOM    489  O   SER A  62      10.522  24.812  34.804  1.00 29.23           O  
ATOM    490  CB  SER A  62       8.521  22.149  34.561  1.00 28.76           C  
ATOM    491  OG  SER A  62       7.313  21.743  35.154  1.00 39.86           O  
ATOM    492  N   TYR A  63      10.451  23.724  32.832  1.00 29.64           N  
ATOM    493  CA  TYR A  63      11.783  24.173  32.452  1.00 31.50           C  
ATOM    494  C   TYR A  63      11.829  25.687  32.380  1.00 29.87           C  
ATOM    495  O   TYR A  63      12.792  26.309  32.840  1.00 31.99           O  
ATOM    496  CB  TYR A  63      12.182  23.582  31.101  1.00 31.39           C  
ATOM    497  CG  TYR A  63      12.663  22.157  31.099  1.00 32.17           C  
ATOM    498  CD1 TYR A  63      13.985  21.860  30.814  1.00 37.76           C  
ATOM    499  CD2 TYR A  63      11.792  21.101  31.314  1.00 35.07           C  
ATOM    500  CE1 TYR A  63      14.439  20.539  30.779  1.00 41.50           C  
ATOM    501  CE2 TYR A  63      12.234  19.770  31.280  1.00 36.51           C  
ATOM    502  CZ  TYR A  63      13.560  19.498  31.010  1.00 38.94           C  
ATOM    503  OH  TYR A  63      14.024  18.199  30.980  1.00 38.99           O  
ATOM    504  N   LEU A  64      10.790  26.293  31.802  1.00 27.59           N  
ATOM    505  CA  LEU A  64      10.759  27.739  31.657  1.00 29.92           C  
ATOM    506  C   LEU A  64      10.711  28.419  33.017  1.00 29.80           C  
ATOM    507  O   LEU A  64      11.431  29.396  33.264  1.00 28.61           O  
ATOM    508  CB  LEU A  64       9.559  28.142  30.803  1.00 30.64           C  
ATOM    509  CG  LEU A  64       9.406  29.627  30.489  1.00 28.73           C  
ATOM    510  CD1 LEU A  64      10.611  30.120  29.697  1.00 29.63           C  
ATOM    511  CD2 LEU A  64       8.105  29.889  29.736  1.00 26.19           C  
ATOM    512  N   TYR A  65       9.860  27.915  33.914  1.00 31.08           N  
ATOM    513  CA  TYR A  65       9.778  28.482  35.256  1.00 30.75           C  
ATOM    514  C   TYR A  65      11.107  28.343  35.995  1.00 31.92           C  
ATOM    515  O   TYR A  65      11.571  29.297  36.631  1.00 32.23           O  
ATOM    516  CB  TYR A  65       8.657  27.816  36.048  1.00 27.41           C  
ATOM    517  CG  TYR A  65       7.255  28.006  35.498  1.00 31.56           C  
ATOM    518  CD1 TYR A  65       6.945  29.032  34.598  1.00 33.01           C  
ATOM    519  CD2 TYR A  65       6.228  27.148  35.887  1.00 32.51           C  
ATOM    520  CE1 TYR A  65       5.639  29.185  34.105  1.00 33.46           C  
ATOM    521  CE2 TYR A  65       4.935  27.289  35.405  1.00 33.16           C  
ATOM    522  CZ  TYR A  65       4.640  28.300  34.522  1.00 34.40           C  
ATOM    523  OH  TYR A  65       3.338  28.393  34.068  1.00 34.04           O  
ATOM    524  N   ARG A  66      11.743  27.169  35.905  1.00 31.83           N  
ATOM    525  CA  ARG A  66      13.034  26.968  36.562  1.00 34.59           C  
ATOM    526  C   ARG A  66      14.097  27.904  36.006  1.00 36.34           C  
ATOM    527  O   ARG A  66      14.865  28.506  36.767  1.00 38.59           O  
ATOM    528  CB  ARG A  66      13.498  25.525  36.419  1.00 35.54           C  
ATOM    529  CG  ARG A  66      14.785  25.275  37.201  1.00 43.98           C  
ATOM    530  CD  ARG A  66      15.125  23.786  37.292  1.00 51.78           C  
ATOM    531  NE  ARG A  66      14.952  23.145  35.994  1.00 50.96           N  
ATOM    532  CZ  ARG A  66      15.900  23.079  35.063  1.00 53.35           C  
ATOM    533  NH1 ARG A  66      17.111  23.602  35.298  1.00 51.21           N  
ATOM    534  NH2 ARG A  66      15.630  22.487  33.900  1.00 47.09           N  
ATOM    535  N   TYR A  67      14.174  28.026  34.678  1.00 33.31           N  
ATOM    536  CA  TYR A  67      15.094  28.992  34.093  1.00 34.70           C  
ATOM    537  C   TYR A  67      14.864  30.380  34.686  1.00 37.11           C  
ATOM    538  O   TYR A  67      15.813  31.064  35.090  1.00 36.17           O  
ATOM    539  CB  TYR A  67      14.941  29.038  32.571  1.00 32.10           C  
ATOM    540  CG  TYR A  67      15.615  30.264  32.018  1.00 35.87           C  
ATOM    541  CD1 TYR A  67      17.009  30.375  32.029  1.00 34.02           C  
ATOM    542  CD2 TYR A  67      14.866  31.352  31.551  1.00 35.31           C  
ATOM    543  CE1 TYR A  67      17.638  31.515  31.547  1.00 34.00           C  
ATOM    544  CE2 TYR A  67      15.492  32.501  31.073  1.00 34.16           C  
ATOM    545  CZ  TYR A  67      16.876  32.571  31.077  1.00 34.17           C  
ATOM    546  OH  TYR A  67      17.497  33.697  30.602  1.00 38.69           O  
ATOM    547  N   ARG A  68      13.592  30.792  34.774  1.00 34.72           N  
ATOM    548  CA  ARG A  68      13.260  32.132  35.247  1.00 33.97           C  
ATOM    549  C   ARG A  68      13.656  32.343  36.707  1.00 36.73           C  
ATOM    550  O   ARG A  68      14.173  33.407  37.062  1.00 39.75           O  
ATOM    551  CB  ARG A  68      11.767  32.393  35.054  1.00 30.92           C  
ATOM    552  CG  ARG A  68      11.375  32.685  33.627  1.00 29.49           C  
ATOM    553  CD  ARG A  68       9.872  32.821  33.504  1.00 31.55           C  
ATOM    554  NE  ARG A  68       9.502  33.207  32.152  1.00 32.14           N  
ATOM    555  CZ  ARG A  68       8.286  33.067  31.641  1.00 31.32           C  
ATOM    556  NH1 ARG A  68       7.308  32.553  32.379  1.00 31.18           N  
ATOM    557  NH2 ARG A  68       8.057  33.434  30.386  1.00 31.73           N  
ATOM    558  N   LYS A  69      13.402  31.360  37.576  1.00 36.19           N  
ATOM    559  CA  LYS A  69      13.834  31.487  38.966  1.00 40.24           C  
ATOM    560  C   LYS A  69      15.345  31.647  39.049  1.00 41.79           C  
ATOM    561  O   LYS A  69      15.850  32.587  39.667  1.00 45.63           O  
ATOM    562  CB  LYS A  69      13.394  30.275  39.785  1.00 42.28           C  
ATOM    563  CG  LYS A  69      11.898  30.087  39.910  1.00 47.07           C  
ATOM    564  CD  LYS A  69      11.575  29.000  40.944  1.00 53.37           C  
ATOM    565  CE  LYS A  69      10.204  29.195  41.619  1.00 57.95           C  
ATOM    566  NZ  LYS A  69       9.743  30.615  41.659  1.00 57.96           N  
ATOM    567  N   LYS A  70      16.086  30.742  38.415  1.00 41.06           N  
ATOM    568  CA  LYS A  70      17.541  30.831  38.453  1.00 44.31           C  
ATOM    569  C   LYS A  70      18.035  32.145  37.838  1.00 45.04           C  
ATOM    570  O   LYS A  70      19.013  32.734  38.319  1.00 47.37           O  
ATOM    571  CB  LYS A  70      18.142  29.603  37.758  1.00 42.84           C  
ATOM    572  CG  LYS A  70      19.332  29.867  36.862  1.00 50.85           C  
ATOM    573  CD  LYS A  70      19.033  29.492  35.409  1.00 52.47           C  
ATOM    574  CE  LYS A  70      19.678  28.163  35.016  1.00 57.93           C  
ATOM    575  NZ  LYS A  70      20.957  27.889  35.746  1.00 61.65           N  
ATOM    576  N   ALA A  71      17.341  32.646  36.809  1.00 44.02           N  
ATOM    577  CA  ALA A  71      17.750  33.894  36.167  1.00 43.87           C  
ATOM    578  C   ALA A  71      17.547  35.089  37.091  1.00 49.63           C  
ATOM    579  O   ALA A  71      18.432  35.945  37.217  1.00 54.22           O  
ATOM    580  CB  ALA A  71      16.984  34.099  34.861  1.00 40.38           C  
ATOM    581  N   ARG A  72      16.385  35.176  37.743  1.00 47.69           N  
ATOM    582  CA  ARG A  72      16.147  36.286  38.660  1.00 49.54           C  
ATOM    583  C   ARG A  72      17.135  36.275  39.829  1.00 52.71           C  
ATOM    584  O   ARG A  72      17.363  37.326  40.435  1.00 56.46           O  
ATOM    585  CB  ARG A  72      14.679  36.254  39.140  1.00 52.47           C  
ATOM    586  CG  ARG A  72      14.323  37.128  40.358  1.00 55.68           C  
ATOM    587  CD  ARG A  72      13.712  36.270  41.472  1.00 58.07           C  
ATOM    588  NE  ARG A  72      14.547  35.093  41.757  1.00 60.34           N  
ATOM    589  CZ  ARG A  72      14.083  33.886  42.097  1.00 56.65           C  
ATOM    590  NH1 ARG A  72      12.775  33.674  42.206  1.00 59.46           N  
ATOM    591  NH2 ARG A  72      14.926  32.883  42.328  1.00 51.15           N  
ATOM    592  N   ALA A  73      17.771  35.135  40.118  1.00 51.56           N  
ATOM    593  CA  ALA A  73      18.711  35.017  41.241  1.00 49.11           C  
ATOM    594  C   ALA A  73      20.162  35.221  40.815  1.00 47.22           C  
ATOM    595  O   ALA A  73      20.449  35.995  39.905  1.00 49.90           O  
ATOM    596  CB  ALA A  73      18.551  33.661  41.917  1.00 44.38           C  
TER     597      ALA A  73                                                      
HETATM  598  O   HOH A 101      21.051  20.179  32.302  1.00 47.26           O  
HETATM  599  O   HOH A 102       6.941  15.793  29.254  1.00 43.78           O  
HETATM  600  O   HOH A 103       2.694  30.041  32.179  1.00 30.38           O  
HETATM  601  O   HOH A 104       5.687  32.923  29.375  1.00 31.12           O  
HETATM  602  O   HOH A 105       3.036  19.475  20.144  1.00 30.43           O  
HETATM  603  O   HOH A 106       9.813  14.338  16.777  1.00 43.90           O  
HETATM  604  O   HOH A 107       4.581  20.016  13.786  1.00 36.90           O  
HETATM  605  O   HOH A 108      15.301  24.884  32.699  1.00 43.32           O  
HETATM  606  O   HOH A 109      21.357   5.446  28.063  1.00 43.21           O  
HETATM  607  O   HOH A 110       5.167  18.527  16.349  1.00 28.96           O  
HETATM  608  O   HOH A 111      16.723 -10.988  26.800  1.00 48.31           O  
HETATM  609  O   HOH A 112      20.809  24.006  22.735  1.00 57.62           O  
CONECT  127  136                                                                
CONECT  136  127  137                                                           
CONECT  137  136  138  140                                                      
CONECT  138  137  139  144                                                      
CONECT  139  138                                                                
CONECT  140  137  141                                                           
CONECT  141  140  142                                                           
CONECT  142  141  143                                                           
CONECT  143  142                                                                
CONECT  144  138                                                                
CONECT  208  214                                                                
CONECT  214  208  215                                                           
CONECT  215  214  216  218                                                      
CONECT  216  215  217  222                                                      
CONECT  217  216                                                                
CONECT  218  215  219                                                           
CONECT  219  218  220                                                           
CONECT  220  219  221                                                           
CONECT  221  220                                                                
CONECT  222  216                                                                
MASTER      205    0    2    3    0    0    0    6  608    1   20    6          
END                                                                             
