HEADER    TRANSCRIPTION REGULATION                27-SEP-95   1BOR              
TITLE     TRANSCRIPTION FACTOR PML, A PROTO-ONCOPROTEIN, NMR, 1 REPRESENTATIVE  
TITLE    2 STRUCTURE AT PH 7.5, 30 C, IN THE PRESENCE OF ZINC                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR PML;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RING FINGER DOMAIN, RESIDUES 49 - 104;                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    PROTO-ONCOGENE, NUCLEAR BODIES (PODS), LEUKEMIA, TRANSCRIPTION        
KEYWDS   2 REGULATION                                                           
EXPDTA    SOLUTION NMR                                                          
AUTHOR    K.L.B.BORDEN,P.S.FREEMONT                                             
REVDAT   4   16-FEB-22 1BOR    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1BOR    1       VERSN                                    
REVDAT   2   01-APR-03 1BOR    1       JRNL                                     
REVDAT   1   01-APR-97 1BOR    0                                                
JRNL        AUTH   K.L.BORDEN,M.N.BODDY,J.LALLY,N.J.O'REILLY,S.MARTIN,K.HOWE,   
JRNL        AUTH 2 E.SOLOMON,P.S.FREEMONT                                       
JRNL        TITL   THE SOLUTION STRUCTURE OF THE RING FINGER DOMAIN FROM THE    
JRNL        TITL 2 ACUTE PROMYELOCYTIC LEUKAEMIA PROTO-ONCOPROTEIN PML.         
JRNL        REF    EMBO J.                       V.  14  1532 1995              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   7729428                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.S.FREEMONT                                                 
REMARK   1  TITL   THE RING FINGER. A NOVEL PROTEIN SEQUENCE MOTIF RELATED TO   
REMARK   1  TITL 2 THE ZINC FINGER                                              
REMARK   1  REF    ANN.N.Y.ACAD.SCI.             V. 684   174 1993              
REMARK   1  REFN                   ISSN 0077-8923                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171968.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 7.5                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : REPRESENTATIVE STRUCTURE           
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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    GLU A   3      -94.90     59.69                                   
REMARK 500    GLN A   5       15.96   -157.18                                   
REMARK 500    LEU A   7       23.29   -160.86                                   
REMARK 500    ARG A   8      -75.51   -127.31                                   
REMARK 500    ALA A  14      -63.93   -126.32                                   
REMARK 500    GLU A  15       86.24   -150.02                                   
REMARK 500    ALA A  16       99.55     21.27                                   
REMARK 500    LYS A  20      154.15    -47.49                                   
REMARK 500    LEU A  21      160.40    -38.65                                   
REMARK 500    CYS A  24       63.16   -113.94                                   
REMARK 500    LEU A  25       57.24     27.22                                   
REMARK 500    LEU A  28     -109.66    -81.31                                   
REMARK 500    SER A  30       89.52    -51.79                                   
REMARK 500    GLU A  34       65.00   -169.18                                   
REMARK 500    ALA A  35       25.50     47.55                                   
REMARK 500    GLN A  39       65.66    132.22                                   
REMARK 500    ILE A  42       38.28     30.91                                   
REMARK 500    CYS A  43      -78.52    -38.28                                   
REMARK 500    GLN A  44       71.89     24.10                                   
REMARK 500    ALA A  45      -64.39   -171.14                                   
REMARK 500    ALA A  51      -99.99   -100.22                                   
REMARK 500    ALA A  55     -178.38     74.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A   8         0.18    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A  57  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   9   SG                                                     
REMARK 620 2 CYS A  12   SG  106.6                                              
REMARK 620 3 CYS A  29   SG  110.5 112.1                                        
REMARK 620 4 CYS A  32   SG  108.5 109.8 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A  58  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  24   SG                                                     
REMARK 620 2 CYS A  24   O    64.8                                              
REMARK 620 3 HIS A  26   ND1 106.9  88.8                                        
REMARK 620 4 CYS A  40   SG  112.5  64.8 113.9                                  
REMARK 620 5 CYS A  43   SG  111.3 170.4 100.8 110.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZN1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: FIRST ZINC BINDING SITE.                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZN2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: SECOND ZINC BINDING SITE.                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 57                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 58                   
DBREF  1BOR A    1    56  UNP    P29590   PML_HUMAN       49    104             
SEQRES   1 A   56  GLU GLU GLU PHE GLN PHE LEU ARG CYS GLN GLN CYS GLN          
SEQRES   2 A   56  ALA GLU ALA LYS CYS PRO LYS LEU LEU PRO CYS LEU HIS          
SEQRES   3 A   56  THR LEU CYS SER GLY CYS LEU GLU ALA SER GLY MET GLN          
SEQRES   4 A   56  CYS PRO ILE CYS GLN ALA PRO TRP PRO LEU GLY ALA ASP          
SEQRES   5 A   56  THR PRO ALA LEU                                              
HET     ZN  A  57       1                                                       
HET     ZN  A  58       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
HELIX    1   1 GLU A   34  MET A   38  1RIGHT-HANDED                       5    
HELIX    2   1 ALA A   45  PRO A   48  5RIGHT-HANDED 3/10                  4    
SHEET    1  B1 4 GLN A   5  ARG A   8  0                                        
SHEET    2  B1 4 PRO A  19  LEU A  21 -1                                        
SHEET    3  B1 4 HIS A  26  LEU A  28 -1                                        
SHEET    4  B1 4 THR A  53  LEU A  56  1                                        
LINK         SG  CYS A   9                ZN    ZN A  57     1555   1555  2.30  
LINK         SG  CYS A  12                ZN    ZN A  57     1555   1555  2.29  
LINK         SG  CYS A  24                ZN    ZN A  58     1555   1555  2.26  
LINK         O   CYS A  24                ZN    ZN A  58     1555   1555  2.67  
LINK         ND1 HIS A  26                ZN    ZN A  58     1555   1555  1.93  
LINK         SG  CYS A  29                ZN    ZN A  57     1555   1555  2.28  
LINK         SG  CYS A  32                ZN    ZN A  57     1555   1555  2.30  
LINK         SG  CYS A  40                ZN    ZN A  58     1555   1555  2.27  
LINK         SG  CYS A  43                ZN    ZN A  58     1555   1555  2.29  
SITE     1 ZN1  5 CYS A   9  CYS A  12  CYS A  29  CYS A  32                    
SITE     2 ZN1  5  ZN A  57                                                     
SITE     1 ZN2  5 HIS A  26  CYS A  24  CYS A  40  CYS A  43                    
SITE     2 ZN2  5  ZN A  58                                                     
SITE     1 AC1  4 CYS A   9  CYS A  12  CYS A  29  CYS A  32                    
SITE     1 AC2  5 LYS A  20  CYS A  24  HIS A  26  CYS A  40                    
SITE     2 AC2  5 CYS A  43                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   GLU A   1       5.264  -0.548  13.190  1.00  0.00           N  
ATOM      2  CA  GLU A   1       4.408  -0.192  14.358  1.00  0.00           C  
ATOM      3  C   GLU A   1       3.393   0.874  13.941  1.00  0.00           C  
ATOM      4  O   GLU A   1       2.249   0.849  14.349  1.00  0.00           O  
ATOM      5  CB  GLU A   1       5.287   0.354  15.486  1.00  0.00           C  
ATOM      6  CG  GLU A   1       4.560   0.194  16.823  1.00  0.00           C  
ATOM      7  CD  GLU A   1       5.136  -1.005  17.578  1.00  0.00           C  
ATOM      8  OE1 GLU A   1       5.921  -1.729  16.989  1.00  0.00           O  
ATOM      9  OE2 GLU A   1       4.782  -1.178  18.733  1.00  0.00           O  
ATOM     10  N   GLU A   2       3.803   1.810  13.130  1.00  0.00           N  
ATOM     11  CA  GLU A   2       2.861   2.875  12.687  1.00  0.00           C  
ATOM     12  C   GLU A   2       2.816   2.913  11.159  1.00  0.00           C  
ATOM     13  O   GLU A   2       3.768   2.560  10.491  1.00  0.00           O  
ATOM     14  CB  GLU A   2       3.335   4.229  13.217  1.00  0.00           C  
ATOM     15  CG  GLU A   2       3.341   4.203  14.746  1.00  0.00           C  
ATOM     16  CD  GLU A   2       2.063   4.857  15.272  1.00  0.00           C  
ATOM     17  OE1 GLU A   2       1.157   5.062  14.481  1.00  0.00           O  
ATOM     18  OE2 GLU A   2       2.011   5.142  16.458  1.00  0.00           O  
ATOM     19  N   GLU A   3       1.717   3.337  10.600  1.00  0.00           N  
ATOM     20  CA  GLU A   3       1.613   3.396   9.116  1.00  0.00           C  
ATOM     21  C   GLU A   3       1.815   1.994   8.536  1.00  0.00           C  
ATOM     22  O   GLU A   3       0.887   1.215   8.447  1.00  0.00           O  
ATOM     23  CB  GLU A   3       2.684   4.341   8.569  1.00  0.00           C  
ATOM     24  CG  GLU A   3       2.347   5.779   8.967  1.00  0.00           C  
ATOM     25  CD  GLU A   3       2.845   6.043  10.389  1.00  0.00           C  
ATOM     26  OE1 GLU A   3       3.811   5.412  10.784  1.00  0.00           O  
ATOM     27  OE2 GLU A   3       2.250   6.871  11.060  1.00  0.00           O  
ATOM     28  N   PHE A   4       3.018   1.665   8.142  1.00  0.00           N  
ATOM     29  CA  PHE A   4       3.270   0.311   7.570  1.00  0.00           C  
ATOM     30  C   PHE A   4       2.530  -0.737   8.401  1.00  0.00           C  
ATOM     31  O   PHE A   4       2.820  -0.938   9.563  1.00  0.00           O  
ATOM     32  CB  PHE A   4       4.772   0.012   7.599  1.00  0.00           C  
ATOM     33  CG  PHE A   4       4.998  -1.458   7.327  1.00  0.00           C  
ATOM     34  CD1 PHE A   4       4.292  -2.096   6.300  1.00  0.00           C  
ATOM     35  CD2 PHE A   4       5.908  -2.182   8.107  1.00  0.00           C  
ATOM     36  CE1 PHE A   4       4.497  -3.459   6.052  1.00  0.00           C  
ATOM     37  CE2 PHE A   4       6.112  -3.545   7.858  1.00  0.00           C  
ATOM     38  CZ  PHE A   4       5.406  -4.183   6.831  1.00  0.00           C  
ATOM     39  N   GLN A   5       1.574  -1.406   7.819  1.00  0.00           N  
ATOM     40  CA  GLN A   5       0.824  -2.434   8.589  1.00  0.00           C  
ATOM     41  C   GLN A   5       0.186  -3.451   7.640  1.00  0.00           C  
ATOM     42  O   GLN A   5      -0.686  -4.202   8.030  1.00  0.00           O  
ATOM     43  CB  GLN A   5      -0.272  -1.754   9.412  1.00  0.00           C  
ATOM     44  CG  GLN A   5      -0.773  -2.719  10.488  1.00  0.00           C  
ATOM     45  CD  GLN A   5      -2.140  -2.255  10.995  1.00  0.00           C  
ATOM     46  OE1 GLN A   5      -2.873  -1.594  10.286  1.00  0.00           O  
ATOM     47  NE2 GLN A   5      -2.517  -2.576  12.203  1.00  0.00           N  
ATOM     48  N   PHE A   6       0.608  -3.504   6.403  1.00  0.00           N  
ATOM     49  CA  PHE A   6       0.001  -4.501   5.479  1.00  0.00           C  
ATOM     50  C   PHE A   6       0.994  -4.924   4.403  1.00  0.00           C  
ATOM     51  O   PHE A   6       2.056  -4.352   4.251  1.00  0.00           O  
ATOM     52  CB  PHE A   6      -1.246  -3.932   4.809  1.00  0.00           C  
ATOM     53  CG  PHE A   6      -2.307  -5.007   4.800  1.00  0.00           C  
ATOM     54  CD1 PHE A   6      -2.597  -5.692   5.986  1.00  0.00           C  
ATOM     55  CD2 PHE A   6      -2.995  -5.325   3.623  1.00  0.00           C  
ATOM     56  CE1 PHE A   6      -3.572  -6.694   5.999  1.00  0.00           C  
ATOM     57  CE2 PHE A   6      -3.973  -6.331   3.637  1.00  0.00           C  
ATOM     58  CZ  PHE A   6      -4.260  -7.014   4.825  1.00  0.00           C  
ATOM     59  N   LEU A   7       0.645  -5.934   3.654  1.00  0.00           N  
ATOM     60  CA  LEU A   7       1.547  -6.423   2.578  1.00  0.00           C  
ATOM     61  C   LEU A   7       0.724  -7.250   1.588  1.00  0.00           C  
ATOM     62  O   LEU A   7       1.245  -8.095   0.886  1.00  0.00           O  
ATOM     63  CB  LEU A   7       2.625  -7.311   3.197  1.00  0.00           C  
ATOM     64  CG  LEU A   7       1.968  -8.275   4.186  1.00  0.00           C  
ATOM     65  CD1 LEU A   7       2.688  -9.623   4.147  1.00  0.00           C  
ATOM     66  CD2 LEU A   7       2.052  -7.690   5.597  1.00  0.00           C  
ATOM     67  N   ARG A   8      -0.561  -7.022   1.535  1.00  0.00           N  
ATOM     68  CA  ARG A   8      -1.418  -7.803   0.603  1.00  0.00           C  
ATOM     69  C   ARG A   8      -2.243  -6.851  -0.261  1.00  0.00           C  
ATOM     70  O   ARG A   8      -1.955  -6.646  -1.423  1.00  0.00           O  
ATOM     71  CB  ARG A   8      -2.350  -8.711   1.410  1.00  0.00           C  
ATOM     72  CG  ARG A   8      -1.530  -9.498   2.435  1.00  0.00           C  
ATOM     73  CD  ARG A   8      -2.305 -10.745   2.865  1.00  0.00           C  
ATOM     74  NE  ARG A   8      -2.260 -10.870   4.349  1.00  0.00           N  
ATOM     75  CZ  ARG A   8      -1.648 -11.882   4.900  1.00  0.00           C  
ATOM     76  NH1 ARG A   8      -0.574 -12.375   4.348  1.00  0.00           N  
ATOM     77  NH2 ARG A   8      -2.111 -12.401   6.005  1.00  0.00           N  
ATOM     78  N   CYS A   9      -3.266  -6.263   0.295  1.00  0.00           N  
ATOM     79  CA  CYS A   9      -4.101  -5.324  -0.501  1.00  0.00           C  
ATOM     80  C   CYS A   9      -5.203  -4.737   0.386  1.00  0.00           C  
ATOM     81  O   CYS A   9      -5.498  -5.238   1.454  1.00  0.00           O  
ATOM     82  CB  CYS A   9      -4.702  -6.075  -1.714  1.00  0.00           C  
ATOM     83  SG  CYS A   9      -6.431  -5.579  -2.001  1.00  0.00           S  
ATOM     84  N   GLN A  10      -5.826  -3.686  -0.073  1.00  0.00           N  
ATOM     85  CA  GLN A  10      -6.924  -3.068   0.705  1.00  0.00           C  
ATOM     86  C   GLN A  10      -8.070  -4.077   0.850  1.00  0.00           C  
ATOM     87  O   GLN A  10      -8.398  -4.513   1.936  1.00  0.00           O  
ATOM     88  CB  GLN A  10      -7.441  -1.840  -0.036  1.00  0.00           C  
ATOM     89  CG  GLN A  10      -8.561  -1.188   0.777  1.00  0.00           C  
ATOM     90  CD  GLN A  10      -9.685  -0.751  -0.163  1.00  0.00           C  
ATOM     91  OE1 GLN A  10     -10.141  -1.523  -0.984  1.00  0.00           O  
ATOM     92  NE2 GLN A  10     -10.155   0.463  -0.079  1.00  0.00           N  
ATOM     93  N   GLN A  11      -8.685  -4.443  -0.249  1.00  0.00           N  
ATOM     94  CA  GLN A  11      -9.819  -5.417  -0.194  1.00  0.00           C  
ATOM     95  C   GLN A  11      -9.385  -6.768  -0.782  1.00  0.00           C  
ATOM     96  O   GLN A  11      -9.464  -7.789  -0.127  1.00  0.00           O  
ATOM     97  CB  GLN A  11     -11.000  -4.869  -0.998  1.00  0.00           C  
ATOM     98  CG  GLN A  11     -12.192  -4.640  -0.068  1.00  0.00           C  
ATOM     99  CD  GLN A  11     -12.908  -5.969   0.183  1.00  0.00           C  
ATOM    100  OE1 GLN A  11     -13.919  -6.253  -0.428  1.00  0.00           O  
ATOM    101  NE2 GLN A  11     -12.424  -6.801   1.065  1.00  0.00           N  
ATOM    102  N   CYS A  12      -8.918  -6.785  -2.005  1.00  0.00           N  
ATOM    103  CA  CYS A  12      -8.472  -8.086  -2.609  1.00  0.00           C  
ATOM    104  C   CYS A  12      -7.080  -8.449  -2.069  1.00  0.00           C  
ATOM    105  O   CYS A  12      -6.084  -8.283  -2.744  1.00  0.00           O  
ATOM    106  CB  CYS A  12      -8.398  -8.033  -4.160  1.00  0.00           C  
ATOM    107  SG  CYS A  12      -8.633  -6.357  -4.839  1.00  0.00           S  
ATOM    108  N   GLN A  13      -6.998  -8.937  -0.854  1.00  0.00           N  
ATOM    109  CA  GLN A  13      -5.663  -9.299  -0.283  1.00  0.00           C  
ATOM    110  C   GLN A  13      -5.254 -10.701  -0.741  1.00  0.00           C  
ATOM    111  O   GLN A  13      -5.728 -11.699  -0.235  1.00  0.00           O  
ATOM    112  CB  GLN A  13      -5.712  -9.250   1.249  1.00  0.00           C  
ATOM    113  CG  GLN A  13      -6.865 -10.116   1.761  1.00  0.00           C  
ATOM    114  CD  GLN A  13      -7.675  -9.328   2.793  1.00  0.00           C  
ATOM    115  OE1 GLN A  13      -7.817  -8.127   2.682  1.00  0.00           O  
ATOM    116  NE2 GLN A  13      -8.215  -9.958   3.800  1.00  0.00           N  
ATOM    117  N   ALA A  14      -4.362 -10.774  -1.693  1.00  0.00           N  
ATOM    118  CA  ALA A  14      -3.894 -12.098  -2.193  1.00  0.00           C  
ATOM    119  C   ALA A  14      -2.366 -12.141  -2.116  1.00  0.00           C  
ATOM    120  O   ALA A  14      -1.791 -12.920  -1.382  1.00  0.00           O  
ATOM    121  CB  ALA A  14      -4.334 -12.283  -3.646  1.00  0.00           C  
ATOM    122  N   GLU A  15      -1.704 -11.297  -2.864  1.00  0.00           N  
ATOM    123  CA  GLU A  15      -0.215 -11.272  -2.830  1.00  0.00           C  
ATOM    124  C   GLU A  15       0.270  -9.852  -3.132  1.00  0.00           C  
ATOM    125  O   GLU A  15       0.566  -9.521  -4.262  1.00  0.00           O  
ATOM    126  CB  GLU A  15       0.341 -12.235  -3.882  1.00  0.00           C  
ATOM    127  CG  GLU A  15       1.731 -12.710  -3.453  1.00  0.00           C  
ATOM    128  CD  GLU A  15       2.366 -13.522  -4.584  1.00  0.00           C  
ATOM    129  OE1 GLU A  15       1.836 -14.574  -4.902  1.00  0.00           O  
ATOM    130  OE2 GLU A  15       3.372 -13.078  -5.112  1.00  0.00           O  
ATOM    131  N   ALA A  16       0.353  -9.029  -2.111  1.00  0.00           N  
ATOM    132  CA  ALA A  16       0.818  -7.606  -2.263  1.00  0.00           C  
ATOM    133  C   ALA A  16       0.660  -7.121  -3.713  1.00  0.00           C  
ATOM    134  O   ALA A  16       1.481  -7.409  -4.561  1.00  0.00           O  
ATOM    135  CB  ALA A  16       2.293  -7.518  -1.867  1.00  0.00           C  
ATOM    136  N   LYS A  17      -0.381  -6.388  -4.008  1.00  0.00           N  
ATOM    137  CA  LYS A  17      -0.571  -5.896  -5.407  1.00  0.00           C  
ATOM    138  C   LYS A  17      -0.071  -4.455  -5.523  1.00  0.00           C  
ATOM    139  O   LYS A  17      -0.030  -3.890  -6.597  1.00  0.00           O  
ATOM    140  CB  LYS A  17      -2.056  -5.953  -5.773  1.00  0.00           C  
ATOM    141  CG  LYS A  17      -2.220  -6.649  -7.125  1.00  0.00           C  
ATOM    142  CD  LYS A  17      -3.388  -7.635  -7.055  1.00  0.00           C  
ATOM    143  CE  LYS A  17      -3.287  -8.630  -8.213  1.00  0.00           C  
ATOM    144  NZ  LYS A  17      -4.410  -8.402  -9.166  1.00  0.00           N  
ATOM    145  N   CYS A  18       0.305  -3.855  -4.430  1.00  0.00           N  
ATOM    146  CA  CYS A  18       0.797  -2.451  -4.487  1.00  0.00           C  
ATOM    147  C   CYS A  18       2.275  -2.406  -4.068  1.00  0.00           C  
ATOM    148  O   CYS A  18       2.591  -2.614  -2.915  1.00  0.00           O  
ATOM    149  CB  CYS A  18      -0.039  -1.597  -3.528  1.00  0.00           C  
ATOM    150  SG  CYS A  18       0.824  -0.051  -3.138  1.00  0.00           S  
ATOM    151  N   PRO A  19       3.135  -2.118  -5.010  1.00  0.00           N  
ATOM    152  CA  PRO A  19       4.578  -2.015  -4.754  1.00  0.00           C  
ATOM    153  C   PRO A  19       4.901  -0.622  -4.201  1.00  0.00           C  
ATOM    154  O   PRO A  19       6.032  -0.314  -3.885  1.00  0.00           O  
ATOM    155  CB  PRO A  19       5.200  -2.195  -6.142  1.00  0.00           C  
ATOM    156  CG  PRO A  19       4.102  -1.810  -7.162  1.00  0.00           C  
ATOM    157  CD  PRO A  19       2.758  -1.880  -6.414  1.00  0.00           C  
ATOM    158  N   LYS A  20       3.911   0.227  -4.101  1.00  0.00           N  
ATOM    159  CA  LYS A  20       4.153   1.605  -3.592  1.00  0.00           C  
ATOM    160  C   LYS A  20       4.996   1.565  -2.315  1.00  0.00           C  
ATOM    161  O   LYS A  20       5.011   0.590  -1.589  1.00  0.00           O  
ATOM    162  CB  LYS A  20       2.820   2.297  -3.300  1.00  0.00           C  
ATOM    163  CG  LYS A  20       3.096   3.757  -2.951  1.00  0.00           C  
ATOM    164  CD  LYS A  20       1.797   4.463  -2.555  1.00  0.00           C  
ATOM    165  CE  LYS A  20       2.086   5.465  -1.437  1.00  0.00           C  
ATOM    166  NZ  LYS A  20       0.989   6.469  -1.371  1.00  0.00           N  
ATOM    167  N   LEU A  21       5.707   2.628  -2.054  1.00  0.00           N  
ATOM    168  CA  LEU A  21       6.577   2.695  -0.841  1.00  0.00           C  
ATOM    169  C   LEU A  21       5.896   2.027   0.358  1.00  0.00           C  
ATOM    170  O   LEU A  21       4.699   1.814   0.366  1.00  0.00           O  
ATOM    171  CB  LEU A  21       6.901   4.163  -0.515  1.00  0.00           C  
ATOM    172  CG  LEU A  21       5.693   5.063  -0.801  1.00  0.00           C  
ATOM    173  CD1 LEU A  21       4.675   4.946   0.334  1.00  0.00           C  
ATOM    174  CD2 LEU A  21       6.160   6.514  -0.914  1.00  0.00           C  
ATOM    175  N   LEU A  22       6.662   1.656   1.362  1.00  0.00           N  
ATOM    176  CA  LEU A  22       6.055   0.960   2.535  1.00  0.00           C  
ATOM    177  C   LEU A  22       6.051   1.776   3.861  1.00  0.00           C  
ATOM    178  O   LEU A  22       5.692   1.219   4.879  1.00  0.00           O  
ATOM    179  CB  LEU A  22       6.821  -0.343   2.785  1.00  0.00           C  
ATOM    180  CG  LEU A  22       5.885  -1.538   2.595  1.00  0.00           C  
ATOM    181  CD1 LEU A  22       6.556  -2.807   3.126  1.00  0.00           C  
ATOM    182  CD2 LEU A  22       4.582  -1.297   3.362  1.00  0.00           C  
ATOM    183  N   PRO A  23       6.425   3.042   3.863  1.00  0.00           N  
ATOM    184  CA  PRO A  23       6.423   3.838   5.109  1.00  0.00           C  
ATOM    185  C   PRO A  23       4.993   4.250   5.469  1.00  0.00           C  
ATOM    186  O   PRO A  23       4.651   4.412   6.624  1.00  0.00           O  
ATOM    187  CB  PRO A  23       7.264   5.066   4.762  1.00  0.00           C  
ATOM    188  CG  PRO A  23       7.220   5.195   3.225  1.00  0.00           C  
ATOM    189  CD  PRO A  23       6.870   3.797   2.683  1.00  0.00           C  
ATOM    190  N   CYS A  24       4.159   4.423   4.483  1.00  0.00           N  
ATOM    191  CA  CYS A  24       2.752   4.828   4.751  1.00  0.00           C  
ATOM    192  C   CYS A  24       1.810   3.692   4.341  1.00  0.00           C  
ATOM    193  O   CYS A  24       0.993   3.836   3.462  1.00  0.00           O  
ATOM    194  CB  CYS A  24       2.447   6.116   3.979  1.00  0.00           C  
ATOM    195  SG  CYS A  24       2.318   5.778   2.209  1.00  0.00           S  
ATOM    196  N   LEU A  25       1.929   2.558   4.995  1.00  0.00           N  
ATOM    197  CA  LEU A  25       1.051   1.384   4.679  1.00  0.00           C  
ATOM    198  C   LEU A  25       0.592   1.441   3.224  1.00  0.00           C  
ATOM    199  O   LEU A  25      -0.586   1.456   2.938  1.00  0.00           O  
ATOM    200  CB  LEU A  25      -0.179   1.405   5.592  1.00  0.00           C  
ATOM    201  CG  LEU A  25      -0.807   0.005   5.678  1.00  0.00           C  
ATOM    202  CD1 LEU A  25      -1.693  -0.072   6.920  1.00  0.00           C  
ATOM    203  CD2 LEU A  25      -1.669  -0.250   4.441  1.00  0.00           C  
ATOM    204  N   HIS A  26       1.497   1.482   2.292  1.00  0.00           N  
ATOM    205  CA  HIS A  26       1.048   1.533   0.880  1.00  0.00           C  
ATOM    206  C   HIS A  26       1.594   0.345   0.109  1.00  0.00           C  
ATOM    207  O   HIS A  26       2.267   0.471  -0.892  1.00  0.00           O  
ATOM    208  CB  HIS A  26       1.417   2.858   0.206  1.00  0.00           C  
ATOM    209  CG  HIS A  26       0.109   3.526  -0.137  1.00  0.00           C  
ATOM    210  ND1 HIS A  26      -0.388   4.566   0.597  1.00  0.00           N  
ATOM    211  CD2 HIS A  26      -0.894   3.193  -0.999  1.00  0.00           C  
ATOM    212  CE1 HIS A  26      -1.642   4.793   0.203  1.00  0.00           C  
ATOM    213  NE2 HIS A  26      -1.995   3.991  -0.775  1.00  0.00           N  
ATOM    214  N   THR A  27       1.239  -0.813   0.566  1.00  0.00           N  
ATOM    215  CA  THR A  27       1.626  -2.066  -0.111  1.00  0.00           C  
ATOM    216  C   THR A  27       0.324  -2.824  -0.298  1.00  0.00           C  
ATOM    217  O   THR A  27       0.257  -4.034  -0.211  1.00  0.00           O  
ATOM    218  CB  THR A  27       2.588  -2.873   0.760  1.00  0.00           C  
ATOM    219  OG1 THR A  27       3.703  -2.063   1.095  1.00  0.00           O  
ATOM    220  CG2 THR A  27       3.067  -4.105  -0.008  1.00  0.00           C  
ATOM    221  N   LEU A  28      -0.725  -2.079  -0.521  1.00  0.00           N  
ATOM    222  CA  LEU A  28      -2.065  -2.682  -0.682  1.00  0.00           C  
ATOM    223  C   LEU A  28      -2.229  -3.202  -2.110  1.00  0.00           C  
ATOM    224  O   LEU A  28      -1.636  -4.198  -2.472  1.00  0.00           O  
ATOM    225  CB  LEU A  28      -3.130  -1.620  -0.353  1.00  0.00           C  
ATOM    226  CG  LEU A  28      -3.105  -1.319   1.154  1.00  0.00           C  
ATOM    227  CD1 LEU A  28      -3.016  -2.621   1.950  1.00  0.00           C  
ATOM    228  CD2 LEU A  28      -1.890  -0.451   1.472  1.00  0.00           C  
ATOM    229  N   CYS A  29      -3.041  -2.589  -2.921  1.00  0.00           N  
ATOM    230  CA  CYS A  29      -3.214  -3.141  -4.288  1.00  0.00           C  
ATOM    231  C   CYS A  29      -3.602  -2.033  -5.267  1.00  0.00           C  
ATOM    232  O   CYS A  29      -4.722  -1.563  -5.304  1.00  0.00           O  
ATOM    233  CB  CYS A  29      -4.255  -4.273  -4.193  1.00  0.00           C  
ATOM    234  SG  CYS A  29      -5.617  -4.127  -5.374  1.00  0.00           S  
ATOM    235  N   SER A  30      -2.654  -1.618  -6.057  1.00  0.00           N  
ATOM    236  CA  SER A  30      -2.903  -0.544  -7.052  1.00  0.00           C  
ATOM    237  C   SER A  30      -4.132  -0.895  -7.889  1.00  0.00           C  
ATOM    238  O   SER A  30      -4.029  -1.524  -8.923  1.00  0.00           O  
ATOM    239  CB  SER A  30      -1.683  -0.430  -7.966  1.00  0.00           C  
ATOM    240  OG  SER A  30      -1.691   0.839  -8.607  1.00  0.00           O  
ATOM    241  N   GLY A  31      -5.295  -0.494  -7.455  1.00  0.00           N  
ATOM    242  CA  GLY A  31      -6.521  -0.808  -8.238  1.00  0.00           C  
ATOM    243  C   GLY A  31      -7.760  -0.657  -7.353  1.00  0.00           C  
ATOM    244  O   GLY A  31      -8.840  -0.371  -7.831  1.00  0.00           O  
ATOM    245  N   CYS A  32      -7.624  -0.853  -6.069  1.00  0.00           N  
ATOM    246  CA  CYS A  32      -8.812  -0.724  -5.178  1.00  0.00           C  
ATOM    247  C   CYS A  32      -8.424  -0.017  -3.871  1.00  0.00           C  
ATOM    248  O   CYS A  32      -9.229   0.113  -2.970  1.00  0.00           O  
ATOM    249  CB  CYS A  32      -9.377  -2.130  -4.884  1.00  0.00           C  
ATOM    250  SG  CYS A  32      -8.557  -2.875  -3.441  1.00  0.00           S  
ATOM    251  N   LEU A  33      -7.200   0.420  -3.746  1.00  0.00           N  
ATOM    252  CA  LEU A  33      -6.784   1.088  -2.482  1.00  0.00           C  
ATOM    253  C   LEU A  33      -6.323   2.515  -2.757  1.00  0.00           C  
ATOM    254  O   LEU A  33      -5.689   2.804  -3.751  1.00  0.00           O  
ATOM    255  CB  LEU A  33      -5.636   0.281  -1.864  1.00  0.00           C  
ATOM    256  CG  LEU A  33      -5.305   0.754  -0.442  1.00  0.00           C  
ATOM    257  CD1 LEU A  33      -4.391   1.971  -0.511  1.00  0.00           C  
ATOM    258  CD2 LEU A  33      -6.579   1.101   0.338  1.00  0.00           C  
ATOM    259  N   GLU A  34      -6.644   3.402  -1.861  1.00  0.00           N  
ATOM    260  CA  GLU A  34      -6.239   4.822  -2.007  1.00  0.00           C  
ATOM    261  C   GLU A  34      -6.524   5.533  -0.690  1.00  0.00           C  
ATOM    262  O   GLU A  34      -7.369   6.402  -0.607  1.00  0.00           O  
ATOM    263  CB  GLU A  34      -7.030   5.468  -3.139  1.00  0.00           C  
ATOM    264  CG  GLU A  34      -8.512   5.124  -2.986  1.00  0.00           C  
ATOM    265  CD  GLU A  34      -9.358   6.355  -3.315  1.00  0.00           C  
ATOM    266  OE1 GLU A  34      -8.891   7.183  -4.079  1.00  0.00           O  
ATOM    267  OE2 GLU A  34     -10.458   6.449  -2.796  1.00  0.00           O  
ATOM    268  N   ALA A  35      -5.836   5.147   0.353  1.00  0.00           N  
ATOM    269  CA  ALA A  35      -6.078   5.774   1.674  1.00  0.00           C  
ATOM    270  C   ALA A  35      -7.581   5.809   1.918  1.00  0.00           C  
ATOM    271  O   ALA A  35      -8.092   6.639   2.644  1.00  0.00           O  
ATOM    272  CB  ALA A  35      -5.525   7.191   1.675  1.00  0.00           C  
ATOM    273  N   SER A  36      -8.291   4.911   1.298  1.00  0.00           N  
ATOM    274  CA  SER A  36      -9.768   4.877   1.467  1.00  0.00           C  
ATOM    275  C   SER A  36     -10.134   3.996   2.660  1.00  0.00           C  
ATOM    276  O   SER A  36     -11.206   4.119   3.220  1.00  0.00           O  
ATOM    277  CB  SER A  36     -10.411   4.312   0.200  1.00  0.00           C  
ATOM    278  OG  SER A  36     -10.832   5.385  -0.633  1.00  0.00           O  
ATOM    279  N   GLY A  37      -9.267   3.104   3.062  1.00  0.00           N  
ATOM    280  CA  GLY A  37      -9.618   2.237   4.224  1.00  0.00           C  
ATOM    281  C   GLY A  37      -8.451   1.322   4.614  1.00  0.00           C  
ATOM    282  O   GLY A  37      -8.655   0.190   5.004  1.00  0.00           O  
ATOM    283  N   MET A  38      -7.237   1.795   4.545  1.00  0.00           N  
ATOM    284  CA  MET A  38      -6.095   0.931   4.949  1.00  0.00           C  
ATOM    285  C   MET A  38      -5.270   1.663   6.011  1.00  0.00           C  
ATOM    286  O   MET A  38      -4.736   1.038   6.901  1.00  0.00           O  
ATOM    287  CB  MET A  38      -5.223   0.589   3.736  1.00  0.00           C  
ATOM    288  CG  MET A  38      -4.931   1.848   2.922  1.00  0.00           C  
ATOM    289  SD  MET A  38      -3.524   2.719   3.656  1.00  0.00           S  
ATOM    290  CE  MET A  38      -2.605   3.002   2.126  1.00  0.00           C  
ATOM    291  N   GLN A  39      -5.192   2.981   5.914  1.00  0.00           N  
ATOM    292  CA  GLN A  39      -4.431   3.828   6.903  1.00  0.00           C  
ATOM    293  C   GLN A  39      -3.544   4.810   6.145  1.00  0.00           C  
ATOM    294  O   GLN A  39      -2.332   4.748   6.214  1.00  0.00           O  
ATOM    295  CB  GLN A  39      -3.548   2.989   7.837  1.00  0.00           C  
ATOM    296  CG  GLN A  39      -4.401   2.412   8.974  1.00  0.00           C  
ATOM    297  CD  GLN A  39      -4.251   3.279  10.224  1.00  0.00           C  
ATOM    298  OE1 GLN A  39      -3.971   2.778  11.295  1.00  0.00           O  
ATOM    299  NE2 GLN A  39      -4.431   4.568  10.134  1.00  0.00           N  
ATOM    300  N   CYS A  40      -4.135   5.727   5.430  1.00  0.00           N  
ATOM    301  CA  CYS A  40      -3.317   6.717   4.684  1.00  0.00           C  
ATOM    302  C   CYS A  40      -4.198   7.908   4.276  1.00  0.00           C  
ATOM    303  O   CYS A  40      -5.401   7.779   4.178  1.00  0.00           O  
ATOM    304  CB  CYS A  40      -2.677   6.034   3.469  1.00  0.00           C  
ATOM    305  SG  CYS A  40      -1.020   5.524   3.931  1.00  0.00           S  
ATOM    306  N   PRO A  41      -3.568   9.046   4.096  1.00  0.00           N  
ATOM    307  CA  PRO A  41      -4.254  10.306   3.747  1.00  0.00           C  
ATOM    308  C   PRO A  41      -4.459  10.417   2.235  1.00  0.00           C  
ATOM    309  O   PRO A  41      -3.593  10.898   1.531  1.00  0.00           O  
ATOM    310  CB  PRO A  41      -3.268  11.378   4.215  1.00  0.00           C  
ATOM    311  CG  PRO A  41      -1.872  10.705   4.249  1.00  0.00           C  
ATOM    312  CD  PRO A  41      -2.108   9.182   4.228  1.00  0.00           C  
ATOM    313  N   ILE A  42      -5.596   9.989   1.740  1.00  0.00           N  
ATOM    314  CA  ILE A  42      -5.875  10.066   0.270  1.00  0.00           C  
ATOM    315  C   ILE A  42      -4.569   9.928  -0.517  1.00  0.00           C  
ATOM    316  O   ILE A  42      -4.356  10.591  -1.512  1.00  0.00           O  
ATOM    317  CB  ILE A  42      -6.539  11.408  -0.059  1.00  0.00           C  
ATOM    318  CG1 ILE A  42      -6.723  11.558  -1.581  1.00  0.00           C  
ATOM    319  CG2 ILE A  42      -5.657  12.547   0.457  1.00  0.00           C  
ATOM    320  CD1 ILE A  42      -6.994  10.192  -2.226  1.00  0.00           C  
ATOM    321  N   CYS A  43      -3.690   9.079  -0.057  1.00  0.00           N  
ATOM    322  CA  CYS A  43      -2.385   8.889  -0.746  1.00  0.00           C  
ATOM    323  C   CYS A  43      -2.586   8.948  -2.262  1.00  0.00           C  
ATOM    324  O   CYS A  43      -2.329   9.954  -2.891  1.00  0.00           O  
ATOM    325  CB  CYS A  43      -1.812   7.530  -0.348  1.00  0.00           C  
ATOM    326  SG  CYS A  43      -0.597   7.799   0.977  1.00  0.00           S  
ATOM    327  N   GLN A  44      -3.066   7.873  -2.826  1.00  0.00           N  
ATOM    328  CA  GLN A  44      -3.332   7.799  -4.301  1.00  0.00           C  
ATOM    329  C   GLN A  44      -2.473   8.798  -5.086  1.00  0.00           C  
ATOM    330  O   GLN A  44      -2.972   9.777  -5.605  1.00  0.00           O  
ATOM    331  CB  GLN A  44      -4.809   8.103  -4.556  1.00  0.00           C  
ATOM    332  CG  GLN A  44      -5.316   7.243  -5.716  1.00  0.00           C  
ATOM    333  CD  GLN A  44      -5.664   8.141  -6.904  1.00  0.00           C  
ATOM    334  OE1 GLN A  44      -4.788   8.670  -7.558  1.00  0.00           O  
ATOM    335  NE2 GLN A  44      -6.917   8.336  -7.214  1.00  0.00           N  
ATOM    336  N   ALA A  45      -1.193   8.558  -5.201  1.00  0.00           N  
ATOM    337  CA  ALA A  45      -0.338   9.501  -5.980  1.00  0.00           C  
ATOM    338  C   ALA A  45       1.071   8.915  -6.169  1.00  0.00           C  
ATOM    339  O   ALA A  45       1.464   8.638  -7.285  1.00  0.00           O  
ATOM    340  CB  ALA A  45      -0.266  10.852  -5.266  1.00  0.00           C  
ATOM    341  N   PRO A  46       1.798   8.732  -5.085  1.00  0.00           N  
ATOM    342  CA  PRO A  46       3.166   8.168  -5.141  1.00  0.00           C  
ATOM    343  C   PRO A  46       3.125   6.634  -5.248  1.00  0.00           C  
ATOM    344  O   PRO A  46       4.045   5.955  -4.843  1.00  0.00           O  
ATOM    345  CB  PRO A  46       3.774   8.579  -3.800  1.00  0.00           C  
ATOM    346  CG  PRO A  46       2.586   8.820  -2.838  1.00  0.00           C  
ATOM    347  CD  PRO A  46       1.346   9.070  -3.717  1.00  0.00           C  
ATOM    348  N   TRP A  47       2.061   6.089  -5.776  1.00  0.00           N  
ATOM    349  CA  TRP A  47       1.939   4.606  -5.895  1.00  0.00           C  
ATOM    350  C   TRP A  47       3.117   3.983  -6.663  1.00  0.00           C  
ATOM    351  O   TRP A  47       3.619   2.953  -6.260  1.00  0.00           O  
ATOM    352  CB  TRP A  47       0.632   4.273  -6.616  1.00  0.00           C  
ATOM    353  CG  TRP A  47      -0.159   3.309  -5.801  1.00  0.00           C  
ATOM    354  CD1 TRP A  47       0.019   1.969  -5.794  1.00  0.00           C  
ATOM    355  CD2 TRP A  47      -1.250   3.585  -4.882  1.00  0.00           C  
ATOM    356  NE1 TRP A  47      -0.893   1.405  -4.924  1.00  0.00           N  
ATOM    357  CE2 TRP A  47      -1.693   2.361  -4.333  1.00  0.00           C  
ATOM    358  CE3 TRP A  47      -1.894   4.766  -4.469  1.00  0.00           C  
ATOM    359  CZ2 TRP A  47      -2.730   2.312  -3.409  1.00  0.00           C  
ATOM    360  CZ3 TRP A  47      -2.941   4.713  -3.540  1.00  0.00           C  
ATOM    361  CH2 TRP A  47      -3.354   3.488  -3.011  1.00  0.00           C  
ATOM    362  N   PRO A  48       3.517   4.591  -7.753  1.00  0.00           N  
ATOM    363  CA  PRO A  48       4.619   4.057  -8.575  1.00  0.00           C  
ATOM    364  C   PRO A  48       5.975   4.286  -7.899  1.00  0.00           C  
ATOM    365  O   PRO A  48       6.920   3.561  -8.135  1.00  0.00           O  
ATOM    366  CB  PRO A  48       4.497   4.830  -9.891  1.00  0.00           C  
ATOM    367  CG  PRO A  48       3.711   6.122  -9.568  1.00  0.00           C  
ATOM    368  CD  PRO A  48       2.935   5.851  -8.265  1.00  0.00           C  
ATOM    369  N   LEU A  49       6.081   5.275  -7.055  1.00  0.00           N  
ATOM    370  CA  LEU A  49       7.382   5.521  -6.368  1.00  0.00           C  
ATOM    371  C   LEU A  49       7.347   4.890  -4.972  1.00  0.00           C  
ATOM    372  O   LEU A  49       6.552   5.265  -4.133  1.00  0.00           O  
ATOM    373  CB  LEU A  49       7.624   7.027  -6.248  1.00  0.00           C  
ATOM    374  CG  LEU A  49       8.964   7.376  -6.899  1.00  0.00           C  
ATOM    375  CD1 LEU A  49       9.133   8.896  -6.940  1.00  0.00           C  
ATOM    376  CD2 LEU A  49      10.101   6.759  -6.083  1.00  0.00           C  
ATOM    377  N   GLY A  50       8.200   3.932  -4.716  1.00  0.00           N  
ATOM    378  CA  GLY A  50       8.206   3.279  -3.373  1.00  0.00           C  
ATOM    379  C   GLY A  50       9.605   3.379  -2.752  1.00  0.00           C  
ATOM    380  O   GLY A  50      10.582   3.588  -3.443  1.00  0.00           O  
ATOM    381  N   ALA A  51       9.718   3.229  -1.453  1.00  0.00           N  
ATOM    382  CA  ALA A  51      11.062   3.316  -0.815  1.00  0.00           C  
ATOM    383  C   ALA A  51      11.586   1.900  -0.546  1.00  0.00           C  
ATOM    384  O   ALA A  51      12.079   1.235  -1.436  1.00  0.00           O  
ATOM    385  CB  ALA A  51      10.955   4.093   0.499  1.00  0.00           C  
ATOM    386  N   ASP A  52      11.475   1.424   0.667  1.00  0.00           N  
ATOM    387  CA  ASP A  52      11.960   0.049   0.973  1.00  0.00           C  
ATOM    388  C   ASP A  52      10.756  -0.883   1.105  1.00  0.00           C  
ATOM    389  O   ASP A  52      10.254  -1.115   2.187  1.00  0.00           O  
ATOM    390  CB  ASP A  52      12.747   0.058   2.286  1.00  0.00           C  
ATOM    391  CG  ASP A  52      12.070   1.002   3.281  1.00  0.00           C  
ATOM    392  OD1 ASP A  52      10.851   1.047   3.290  1.00  0.00           O  
ATOM    393  OD2 ASP A  52      12.783   1.664   4.017  1.00  0.00           O  
ATOM    394  N   THR A  53      10.281  -1.414   0.012  1.00  0.00           N  
ATOM    395  CA  THR A  53       9.101  -2.322   0.081  1.00  0.00           C  
ATOM    396  C   THR A  53       9.400  -3.613  -0.690  1.00  0.00           C  
ATOM    397  O   THR A  53      10.474  -3.774  -1.233  1.00  0.00           O  
ATOM    398  CB  THR A  53       7.873  -1.632  -0.531  1.00  0.00           C  
ATOM    399  OG1 THR A  53       7.671  -2.114  -1.852  1.00  0.00           O  
ATOM    400  CG2 THR A  53       8.077  -0.117  -0.570  1.00  0.00           C  
ATOM    401  N   PRO A  54       8.433  -4.498  -0.706  1.00  0.00           N  
ATOM    402  CA  PRO A  54       8.551  -5.795  -1.393  1.00  0.00           C  
ATOM    403  C   PRO A  54       8.271  -5.631  -2.889  1.00  0.00           C  
ATOM    404  O   PRO A  54       9.002  -6.120  -3.726  1.00  0.00           O  
ATOM    405  CB  PRO A  54       7.467  -6.648  -0.728  1.00  0.00           C  
ATOM    406  CG  PRO A  54       6.435  -5.659  -0.131  1.00  0.00           C  
ATOM    407  CD  PRO A  54       7.133  -4.288  -0.038  1.00  0.00           C  
ATOM    408  N   ALA A  55       7.214  -4.945  -3.229  1.00  0.00           N  
ATOM    409  CA  ALA A  55       6.882  -4.749  -4.668  1.00  0.00           C  
ATOM    410  C   ALA A  55       6.327  -6.052  -5.246  1.00  0.00           C  
ATOM    411  O   ALA A  55       6.180  -7.038  -4.550  1.00  0.00           O  
ATOM    412  CB  ALA A  55       8.144  -4.345  -5.433  1.00  0.00           C  
ATOM    413  N   LEU A  56       6.014  -6.064  -6.512  1.00  0.00           N  
ATOM    414  CA  LEU A  56       5.465  -7.303  -7.133  1.00  0.00           C  
ATOM    415  C   LEU A  56       5.926  -7.390  -8.590  1.00  0.00           C  
ATOM    416  O   LEU A  56       6.454  -6.407  -9.084  1.00  0.00           O  
ATOM    417  CB  LEU A  56       3.937  -7.261  -7.084  1.00  0.00           C  
ATOM    418  CG  LEU A  56       3.461  -5.816  -7.252  1.00  0.00           C  
ATOM    419  CD1 LEU A  56       2.232  -5.784  -8.161  1.00  0.00           C  
ATOM    420  CD2 LEU A  56       3.096  -5.238  -5.882  1.00  0.00           C  
ATOM    421  OXT LEU A  56       5.743  -8.439  -9.187  1.00  0.00           O  
TER     422      LEU A  56                                                      
HETATM  423 ZN    ZN A  57      -7.295  -4.729  -3.951  1.00  0.00          ZN  
HETATM  424 ZN    ZN A  58       0.071   5.849   1.970  1.00  0.00          ZN  
CONECT   83  423                                                                
CONECT  107  423                                                                
CONECT  193  424                                                                
CONECT  195  424                                                                
CONECT  210  424                                                                
CONECT  234  423                                                                
CONECT  250  423                                                                
CONECT  305  424                                                                
CONECT  326  424                                                                
CONECT  423   83  107  234  250                                                 
CONECT  424  193  195  210  305                                                 
CONECT  424  326                                                                
MASTER      165    0    2    2    4    0    7    6  423    1   12    5          
END