HEADER    ZINC-BINDING PROTEIN                    31-JAN-96   1FRE              
TITLE     XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1     
TITLE    2 STRUCTURE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR FACTOR XNF7;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: BBOX;                                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE   3 ORGANISM_COMMON: AFRICAN CLAWED FROG;                                
SOURCE   4 ORGANISM_TAXID: 8355                                                 
KEYWDS    ZINC-BINDING PROTEIN, XNF7, BBOX, DEVELOPMENT, MID-BLASTULA-          
KEYWDS   2 TRANSITION                                                           
EXPDTA    SOLUTION NMR                                                          
AUTHOR    K.L.B.BORDEN,P.S.FREEMONT                                             
REVDAT   4   23-FEB-22 1FRE    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1FRE    1       VERSN                                    
REVDAT   2   01-APR-03 1FRE    1       JRNL                                     
REVDAT   1   12-FEB-97 1FRE    0                                                
JRNL        AUTH   K.L.BORDEN,J.M.LALLY,S.R.MARTIN,N.J.O'REILLY,L.D.ETKIN,      
JRNL        AUTH 2 P.S.FREEMONT                                                 
JRNL        TITL   NOVEL TOPOLOGY OF A ZINC-BINDING DOMAIN FROM A PROTEIN       
JRNL        TITL 2 INVOLVED IN REGULATING EARLY XENOPUS DEVELOPMENT.            
JRNL        REF    EMBO J.                       V.  14  5947 1995              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   8846787                                                      
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   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.A.REDDY,M.KLOC,L.ETKIN                                     
REMARK   1  TITL   THE CLONING AND CHARACTERIZATION OF A MATERNALLY EXPRESSED   
REMARK   1  TITL 2 NOVEL ZINC FINGER NUCLEAR PHOSPHOPROTEIN (XNF7) IN XENOPUS   
REMARK   1  TITL 3 LAEVIS                                                       
REMARK   1  REF    DEV.BIOL.                     V. 148   107 1991              
REMARK   1  REFN                   ISSN 0012-1606                               
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 1FRE 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_1000173382.                                   
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  : NULL                               
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     ARG A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A    15     O    LEU A    40              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   5      -80.53    -66.69                                   
REMARK 500    CYS A   6       68.44     14.25                                   
REMARK 500    GLU A   8       97.00     39.46                                   
REMARK 500    HIS A   9      -63.45    179.00                                   
REMARK 500    GLU A  11       45.86    -84.50                                   
REMARK 500    ARG A  12      -14.00    161.53                                   
REMARK 500    LEU A  15     -144.76   -166.76                                   
REMARK 500    CYS A  17      -87.42   -128.65                                   
REMARK 500    LYS A  18      161.58     60.87                                   
REMARK 500    ASP A  20       47.32    179.13                                   
REMARK 500    SER A  24      115.58     58.78                                   
REMARK 500    CYS A  25     -158.67   -137.73                                   
REMARK 500    CYS A  28       34.97   -172.38                                   
REMARK 500    ARG A  29       -0.08     78.64                                   
REMARK 500    ASP A  30      -40.54   -157.46                                   
REMARK 500    SER A  31       57.32     79.13                                   
REMARK 500    ALA A  35      -77.15     77.01                                   
REMARK 500    SER A  36       20.75   -152.79                                   
REMARK 500    HIS A  37      -92.48    -49.77                                   
REMARK 500    ASN A  38      154.38    174.18                                   
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  12         0.28    SIDE CHAIN                              
REMARK 500    ARG A  29         0.28    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  43  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   6   SG                                                     
REMARK 620 2 HIS A   9   CD2  90.3                                              
REMARK 620 3 HIS A   9   NE2  95.6  40.9                                        
REMARK 620 4 CYS A  28   SG   97.6 151.0 110.3                                  
REMARK 620 5 HIS A  34   CD2  85.3 108.1 148.8 100.4                            
REMARK 620 6 HIS A  34   NE2 121.7  92.0 121.8 107.1  39.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZN1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE 1.                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 43                   
DBREF  1FRE A    1    42  UNP    Q92021   NF7B_XENLA     219    260             
SEQRES   1 A   42  ARG PRO LEU GLU LYS CYS SER GLU HIS ASP GLU ARG LEU          
SEQRES   2 A   42  LYS LEU TYR CYS LYS ASP ASP GLY THR LEU SER CYS VAL          
SEQRES   3 A   42  ILE CYS ARG ASP SER LEU LYS HIS ALA SER HIS ASN PHE          
SEQRES   4 A   42  LEU PRO ILE                                                  
HET     ZN  A  43       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
HELIX    1  H1 ILE A   27  SER A   31  1HELICAL TURN                       5    
SHEET    1  S1 1 LEU A  13  LYS A  18  0                                        
SHEET    1  S2 1 ASN A  38  PRO A  41  0                                        
LINK         SG  CYS A   6                ZN    ZN A  43     1555   1555  2.32  
LINK         CD2 HIS A   9                ZN    ZN A  43     1555   1555  1.90  
LINK         NE2 HIS A   9                ZN    ZN A  43     1555   1555  2.04  
LINK         SG  CYS A  28                ZN    ZN A  43     1555   1555  2.30  
LINK         CD2 HIS A  34                ZN    ZN A  43     1555   1555  2.18  
LINK         NE2 HIS A  34                ZN    ZN A  43     1555   1555  1.53  
SITE     1 ZN1  5 CYS A   6  HIS A   9  CYS A  28  HIS A  34                    
SITE     2 ZN1  5  ZN A  43                                                     
SITE     1 AC1  5 CYS A   6  HIS A   9  LEU A  13  CYS A  28                    
SITE     2 AC1  5 HIS A  34                                                     
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   4       0.674   7.196  -3.064  1.00  0.00           N  
ATOM      2  CA  GLU A   4       0.867   6.022  -2.185  1.00  0.00           C  
ATOM      3  C   GLU A   4       2.122   6.227  -1.332  1.00  0.00           C  
ATOM      4  O   GLU A   4       3.218   6.339  -1.844  1.00  0.00           O  
ATOM      5  CB  GLU A   4       1.029   4.774  -3.059  1.00  0.00           C  
ATOM      6  CG  GLU A   4       2.045   5.058  -4.167  1.00  0.00           C  
ATOM      7  CD  GLU A   4       1.587   4.385  -5.463  1.00  0.00           C  
ATOM      8  OE1 GLU A   4       1.357   3.187  -5.436  1.00  0.00           O  
ATOM      9  OE2 GLU A   4       1.475   5.080  -6.460  1.00  0.00           O  
ATOM     10  N   LYS A   5       1.977   6.267  -0.032  1.00  0.00           N  
ATOM     11  CA  LYS A   5       3.169   6.448   0.835  1.00  0.00           C  
ATOM     12  C   LYS A   5       4.036   5.204   0.700  1.00  0.00           C  
ATOM     13  O   LYS A   5       4.995   5.205  -0.044  1.00  0.00           O  
ATOM     14  CB  LYS A   5       2.740   6.623   2.295  1.00  0.00           C  
ATOM     15  CG  LYS A   5       3.319   7.928   2.846  1.00  0.00           C  
ATOM     16  CD  LYS A   5       3.689   7.741   4.318  1.00  0.00           C  
ATOM     17  CE  LYS A   5       5.077   8.330   4.576  1.00  0.00           C  
ATOM     18  NZ  LYS A   5       5.026   9.216   5.774  1.00  0.00           N  
ATOM     19  N   CYS A   6       3.680   4.146   1.408  1.00  0.00           N  
ATOM     20  CA  CYS A   6       4.445   2.848   1.349  1.00  0.00           C  
ATOM     21  C   CYS A   6       5.799   3.077   0.680  1.00  0.00           C  
ATOM     22  O   CYS A   6       6.037   2.651  -0.429  1.00  0.00           O  
ATOM     23  CB  CYS A   6       3.634   1.812   0.551  1.00  0.00           C  
ATOM     24  SG  CYS A   6       3.565   0.225   1.440  1.00  0.00           S  
ATOM     25  N   SER A   7       6.669   3.794   1.334  1.00  0.00           N  
ATOM     26  CA  SER A   7       7.995   4.100   0.731  1.00  0.00           C  
ATOM     27  C   SER A   7       9.036   3.090   1.205  1.00  0.00           C  
ATOM     28  O   SER A   7       8.873   2.456   2.225  1.00  0.00           O  
ATOM     29  CB  SER A   7       8.422   5.501   1.164  1.00  0.00           C  
ATOM     30  OG  SER A   7       7.743   6.466   0.371  1.00  0.00           O  
ATOM     31  N   GLU A   8      10.111   2.954   0.469  1.00  0.00           N  
ATOM     32  CA  GLU A   8      11.190   2.000   0.863  1.00  0.00           C  
ATOM     33  C   GLU A   8      10.577   0.721   1.421  1.00  0.00           C  
ATOM     34  O   GLU A   8      10.213   0.643   2.576  1.00  0.00           O  
ATOM     35  CB  GLU A   8      12.076   2.656   1.920  1.00  0.00           C  
ATOM     36  CG  GLU A   8      11.207   3.247   3.037  1.00  0.00           C  
ATOM     37  CD  GLU A   8      12.107   3.802   4.142  1.00  0.00           C  
ATOM     38  OE1 GLU A   8      12.777   3.011   4.785  1.00  0.00           O  
ATOM     39  OE2 GLU A   8      12.111   5.008   4.327  1.00  0.00           O  
ATOM     40  N   HIS A   9      10.450  -0.285   0.609  1.00  0.00           N  
ATOM     41  CA  HIS A   9       9.838  -1.539   1.098  1.00  0.00           C  
ATOM     42  C   HIS A   9       9.771  -2.578  -0.046  1.00  0.00           C  
ATOM     43  O   HIS A   9      10.409  -3.609   0.034  1.00  0.00           O  
ATOM     44  CB  HIS A   9       8.443  -1.222   1.659  1.00  0.00           C  
ATOM     45  CG  HIS A   9       7.595  -0.562   0.624  1.00  0.00           C  
ATOM     46  ND1 HIS A   9       8.110   0.184  -0.416  1.00  0.00           N  
ATOM     47  CD2 HIS A   9       6.258  -0.625   0.411  1.00  0.00           C  
ATOM     48  CE1 HIS A   9       7.099   0.507  -1.210  1.00  0.00           C  
ATOM     49  NE2 HIS A   9       5.930   0.038  -0.760  1.00  0.00           N  
ATOM     50  N   ASP A  10       9.035  -2.339  -1.117  1.00  0.00           N  
ATOM     51  CA  ASP A  10       8.998  -3.332  -2.210  1.00  0.00           C  
ATOM     52  C   ASP A  10       9.511  -2.671  -3.488  1.00  0.00           C  
ATOM     53  O   ASP A  10       9.314  -1.491  -3.704  1.00  0.00           O  
ATOM     54  CB  ASP A  10       7.569  -3.814  -2.406  1.00  0.00           C  
ATOM     55  CG  ASP A  10       7.386  -5.158  -1.698  1.00  0.00           C  
ATOM     56  OD1 ASP A  10       8.360  -5.663  -1.165  1.00  0.00           O  
ATOM     57  OD2 ASP A  10       6.274  -5.661  -1.702  1.00  0.00           O  
ATOM     58  N   GLU A  11      10.177  -3.408  -4.330  1.00  0.00           N  
ATOM     59  CA  GLU A  11      10.706  -2.802  -5.583  1.00  0.00           C  
ATOM     60  C   GLU A  11       9.615  -2.802  -6.654  1.00  0.00           C  
ATOM     61  O   GLU A  11       9.856  -3.156  -7.790  1.00  0.00           O  
ATOM     62  CB  GLU A  11      11.906  -3.615  -6.076  1.00  0.00           C  
ATOM     63  CG  GLU A  11      12.548  -2.904  -7.270  1.00  0.00           C  
ATOM     64  CD  GLU A  11      14.051  -2.756  -7.029  1.00  0.00           C  
ATOM     65  OE1 GLU A  11      14.733  -3.768  -7.024  1.00  0.00           O  
ATOM     66  OE2 GLU A  11      14.495  -1.633  -6.853  1.00  0.00           O  
ATOM     67  N   ARG A  12       8.419  -2.400  -6.302  1.00  0.00           N  
ATOM     68  CA  ARG A  12       7.309  -2.371  -7.302  1.00  0.00           C  
ATOM     69  C   ARG A  12       5.947  -2.319  -6.591  1.00  0.00           C  
ATOM     70  O   ARG A  12       4.936  -2.057  -7.211  1.00  0.00           O  
ATOM     71  CB  ARG A  12       7.378  -3.630  -8.181  1.00  0.00           C  
ATOM     72  CG  ARG A  12       6.046  -3.842  -8.907  1.00  0.00           C  
ATOM     73  CD  ARG A  12       5.796  -2.678  -9.868  1.00  0.00           C  
ATOM     74  NE  ARG A  12       5.499  -3.212 -11.226  1.00  0.00           N  
ATOM     75  CZ  ARG A  12       4.890  -2.462 -12.103  1.00  0.00           C  
ATOM     76  NH1 ARG A  12       5.453  -1.363 -12.525  1.00  0.00           N  
ATOM     77  NH2 ARG A  12       3.717  -2.810 -12.557  1.00  0.00           N  
ATOM     78  N   LEU A  13       5.893  -2.584  -5.310  1.00  0.00           N  
ATOM     79  CA  LEU A  13       4.575  -2.562  -4.618  1.00  0.00           C  
ATOM     80  C   LEU A  13       4.344  -1.214  -3.930  1.00  0.00           C  
ATOM     81  O   LEU A  13       5.141  -0.763  -3.131  1.00  0.00           O  
ATOM     82  CB  LEU A  13       4.525  -3.672  -3.562  1.00  0.00           C  
ATOM     83  CG  LEU A  13       4.494  -5.055  -4.224  1.00  0.00           C  
ATOM     84  CD1 LEU A  13       3.567  -5.022  -5.432  1.00  0.00           C  
ATOM     85  CD2 LEU A  13       5.899  -5.458  -4.680  1.00  0.00           C  
ATOM     86  N   LYS A  14       3.226  -0.592  -4.214  1.00  0.00           N  
ATOM     87  CA  LYS A  14       2.867   0.716  -3.575  1.00  0.00           C  
ATOM     88  C   LYS A  14       1.314   0.810  -3.589  1.00  0.00           C  
ATOM     89  O   LYS A  14       0.709   0.512  -4.600  1.00  0.00           O  
ATOM     90  CB  LYS A  14       3.471   1.870  -4.395  1.00  0.00           C  
ATOM     91  CG  LYS A  14       5.010   1.769  -4.413  1.00  0.00           C  
ATOM     92  CD  LYS A  14       5.593   2.309  -3.108  1.00  0.00           C  
ATOM     93  CE  LYS A  14       5.002   3.678  -2.797  1.00  0.00           C  
ATOM     94  NZ  LYS A  14       3.815   3.508  -1.916  1.00  0.00           N  
ATOM     95  N   LEU A  15       0.634   1.174  -2.505  1.00  0.00           N  
ATOM     96  CA  LEU A  15      -0.870   1.196  -2.592  1.00  0.00           C  
ATOM     97  C   LEU A  15      -1.532   1.930  -1.412  1.00  0.00           C  
ATOM     98  O   LEU A  15      -1.019   2.879  -0.941  1.00  0.00           O  
ATOM     99  CB  LEU A  15      -1.377  -0.241  -2.622  1.00  0.00           C  
ATOM    100  CG  LEU A  15      -2.668  -0.372  -3.417  1.00  0.00           C  
ATOM    101  CD1 LEU A  15      -3.644  -1.183  -2.554  1.00  0.00           C  
ATOM    102  CD2 LEU A  15      -3.263   1.017  -3.779  1.00  0.00           C  
ATOM    103  N   TYR A  16      -2.695   1.476  -0.951  1.00  0.00           N  
ATOM    104  CA  TYR A  16      -3.413   2.158   0.184  1.00  0.00           C  
ATOM    105  C   TYR A  16      -4.576   1.306   0.739  1.00  0.00           C  
ATOM    106  O   TYR A  16      -5.166   0.500   0.047  1.00  0.00           O  
ATOM    107  CB  TYR A  16      -3.944   3.494  -0.326  1.00  0.00           C  
ATOM    108  CG  TYR A  16      -5.385   3.750   0.021  1.00  0.00           C  
ATOM    109  CD1 TYR A  16      -6.398   3.163  -0.744  1.00  0.00           C  
ATOM    110  CD2 TYR A  16      -5.715   4.593   1.089  1.00  0.00           C  
ATOM    111  CE1 TYR A  16      -7.739   3.416  -0.440  1.00  0.00           C  
ATOM    112  CE2 TYR A  16      -7.057   4.849   1.388  1.00  0.00           C  
ATOM    113  CZ  TYR A  16      -8.066   4.261   0.626  1.00  0.00           C  
ATOM    114  OH  TYR A  16      -9.389   4.514   0.922  1.00  0.00           O  
ATOM    115  N   CYS A  17      -4.909   1.519   1.994  1.00  0.00           N  
ATOM    116  CA  CYS A  17      -6.036   0.777   2.645  1.00  0.00           C  
ATOM    117  C   CYS A  17      -6.973   1.798   3.300  1.00  0.00           C  
ATOM    118  O   CYS A  17      -7.928   2.254   2.707  1.00  0.00           O  
ATOM    119  CB  CYS A  17      -5.502  -0.155   3.734  1.00  0.00           C  
ATOM    120  SG  CYS A  17      -6.896  -0.833   4.670  1.00  0.00           S  
ATOM    121  N   LYS A  18      -6.688   2.163   4.525  1.00  0.00           N  
ATOM    122  CA  LYS A  18      -7.534   3.161   5.241  1.00  0.00           C  
ATOM    123  C   LYS A  18      -8.966   2.639   5.377  1.00  0.00           C  
ATOM    124  O   LYS A  18      -9.380   1.732   4.682  1.00  0.00           O  
ATOM    125  CB  LYS A  18      -7.530   4.476   4.465  1.00  0.00           C  
ATOM    126  CG  LYS A  18      -6.091   4.993   4.356  1.00  0.00           C  
ATOM    127  CD  LYS A  18      -5.919   6.229   5.244  1.00  0.00           C  
ATOM    128  CE  LYS A  18      -7.012   7.250   4.919  1.00  0.00           C  
ATOM    129  NZ  LYS A  18      -6.504   8.625   5.190  1.00  0.00           N  
ATOM    130  N   ASP A  19      -9.722   3.206   6.280  1.00  0.00           N  
ATOM    131  CA  ASP A  19     -11.126   2.750   6.483  1.00  0.00           C  
ATOM    132  C   ASP A  19     -11.904   2.844   5.169  1.00  0.00           C  
ATOM    133  O   ASP A  19     -11.836   3.828   4.460  1.00  0.00           O  
ATOM    134  CB  ASP A  19     -11.798   3.632   7.538  1.00  0.00           C  
ATOM    135  CG  ASP A  19     -11.348   5.082   7.356  1.00  0.00           C  
ATOM    136  OD1 ASP A  19     -10.333   5.443   7.929  1.00  0.00           O  
ATOM    137  OD2 ASP A  19     -12.025   5.808   6.647  1.00  0.00           O  
ATOM    138  N   ASP A  20     -12.648   1.821   4.844  1.00  0.00           N  
ATOM    139  CA  ASP A  20     -13.443   1.834   3.582  1.00  0.00           C  
ATOM    140  C   ASP A  20     -14.194   0.514   3.447  1.00  0.00           C  
ATOM    141  O   ASP A  20     -14.182  -0.122   2.412  1.00  0.00           O  
ATOM    142  CB  ASP A  20     -12.528   1.985   2.373  1.00  0.00           C  
ATOM    143  CG  ASP A  20     -11.082   1.653   2.751  1.00  0.00           C  
ATOM    144  OD1 ASP A  20     -10.854   0.561   3.244  1.00  0.00           O  
ATOM    145  OD2 ASP A  20     -10.229   2.498   2.539  1.00  0.00           O  
ATOM    146  N   GLY A  21     -14.833   0.097   4.490  1.00  0.00           N  
ATOM    147  CA  GLY A  21     -15.580  -1.189   4.449  1.00  0.00           C  
ATOM    148  C   GLY A  21     -14.620  -2.326   4.797  1.00  0.00           C  
ATOM    149  O   GLY A  21     -14.888  -3.141   5.657  1.00  0.00           O  
ATOM    150  N   THR A  22     -13.494  -2.376   4.140  1.00  0.00           N  
ATOM    151  CA  THR A  22     -12.504  -3.450   4.435  1.00  0.00           C  
ATOM    152  C   THR A  22     -11.413  -2.894   5.354  1.00  0.00           C  
ATOM    153  O   THR A  22     -10.455  -2.298   4.904  1.00  0.00           O  
ATOM    154  CB  THR A  22     -11.873  -3.939   3.129  1.00  0.00           C  
ATOM    155  OG1 THR A  22     -12.884  -4.080   2.140  1.00  0.00           O  
ATOM    156  CG2 THR A  22     -11.193  -5.289   3.363  1.00  0.00           C  
ATOM    157  N   LEU A  23     -11.550  -3.080   6.639  1.00  0.00           N  
ATOM    158  CA  LEU A  23     -10.519  -2.557   7.580  1.00  0.00           C  
ATOM    159  C   LEU A  23      -9.182  -3.252   7.313  1.00  0.00           C  
ATOM    160  O   LEU A  23      -9.078  -4.461   7.371  1.00  0.00           O  
ATOM    161  CB  LEU A  23     -10.956  -2.833   9.021  1.00  0.00           C  
ATOM    162  CG  LEU A  23     -11.199  -4.332   9.203  1.00  0.00           C  
ATOM    163  CD1 LEU A  23     -10.213  -4.889  10.232  1.00  0.00           C  
ATOM    164  CD2 LEU A  23     -12.630  -4.559   9.695  1.00  0.00           C  
ATOM    165  N   SER A  24      -8.157  -2.496   7.021  1.00  0.00           N  
ATOM    166  CA  SER A  24      -6.827  -3.115   6.752  1.00  0.00           C  
ATOM    167  C   SER A  24      -6.946  -4.087   5.577  1.00  0.00           C  
ATOM    168  O   SER A  24      -7.633  -5.086   5.657  1.00  0.00           O  
ATOM    169  CB  SER A  24      -6.359  -3.876   7.992  1.00  0.00           C  
ATOM    170  OG  SER A  24      -6.079  -2.951   9.034  1.00  0.00           O  
ATOM    171  N   CYS A  25      -6.283  -3.811   4.486  1.00  0.00           N  
ATOM    172  CA  CYS A  25      -6.368  -4.731   3.322  1.00  0.00           C  
ATOM    173  C   CYS A  25      -4.973  -4.885   2.739  1.00  0.00           C  
ATOM    174  O   CYS A  25      -3.989  -4.612   3.398  1.00  0.00           O  
ATOM    175  CB  CYS A  25      -7.291  -4.128   2.259  1.00  0.00           C  
ATOM    176  SG  CYS A  25      -8.643  -3.226   3.059  1.00  0.00           S  
ATOM    177  N   VAL A  26      -4.874  -5.284   1.501  1.00  0.00           N  
ATOM    178  CA  VAL A  26      -3.533  -5.405   0.869  1.00  0.00           C  
ATOM    179  C   VAL A  26      -2.734  -4.177   1.253  1.00  0.00           C  
ATOM    180  O   VAL A  26      -3.183  -3.098   1.006  1.00  0.00           O  
ATOM    181  CB  VAL A  26      -3.700  -5.420  -0.646  1.00  0.00           C  
ATOM    182  CG1 VAL A  26      -4.323  -6.744  -1.083  1.00  0.00           C  
ATOM    183  CG2 VAL A  26      -4.608  -4.261  -1.063  1.00  0.00           C  
ATOM    184  N   ILE A  27      -1.579  -4.303   1.862  1.00  0.00           N  
ATOM    185  CA  ILE A  27      -0.832  -3.060   2.228  1.00  0.00           C  
ATOM    186  C   ILE A  27      -0.070  -2.547   1.001  1.00  0.00           C  
ATOM    187  O   ILE A  27       0.725  -1.632   1.075  1.00  0.00           O  
ATOM    188  CB  ILE A  27       0.165  -3.296   3.361  1.00  0.00           C  
ATOM    189  CG1 ILE A  27      -0.567  -3.525   4.688  1.00  0.00           C  
ATOM    190  CG2 ILE A  27       1.034  -2.045   3.483  1.00  0.00           C  
ATOM    191  CD1 ILE A  27      -1.722  -2.531   4.829  1.00  0.00           C  
ATOM    192  N   CYS A  28      -0.316  -3.109  -0.128  1.00  0.00           N  
ATOM    193  CA  CYS A  28       0.368  -2.635  -1.349  1.00  0.00           C  
ATOM    194  C   CYS A  28      -0.263  -3.351  -2.512  1.00  0.00           C  
ATOM    195  O   CYS A  28       0.378  -3.726  -3.473  1.00  0.00           O  
ATOM    196  CB  CYS A  28       1.850  -2.948  -1.269  1.00  0.00           C  
ATOM    197  SG  CYS A  28       2.758  -1.411  -1.517  1.00  0.00           S  
ATOM    198  N   ARG A  29      -1.531  -3.576  -2.387  1.00  0.00           N  
ATOM    199  CA  ARG A  29      -2.264  -4.315  -3.444  1.00  0.00           C  
ATOM    200  C   ARG A  29      -1.967  -5.803  -3.262  1.00  0.00           C  
ATOM    201  O   ARG A  29      -2.454  -6.642  -3.994  1.00  0.00           O  
ATOM    202  CB  ARG A  29      -1.791  -3.855  -4.826  1.00  0.00           C  
ATOM    203  CG  ARG A  29      -2.950  -3.944  -5.821  1.00  0.00           C  
ATOM    204  CD  ARG A  29      -2.400  -4.208  -7.224  1.00  0.00           C  
ATOM    205  NE  ARG A  29      -1.821  -2.951  -7.776  1.00  0.00           N  
ATOM    206  CZ  ARG A  29      -0.681  -2.980  -8.412  1.00  0.00           C  
ATOM    207  NH1 ARG A  29       0.402  -3.361  -7.792  1.00  0.00           N  
ATOM    208  NH2 ARG A  29      -0.625  -2.629  -9.668  1.00  0.00           N  
ATOM    209  N   ASP A  30      -1.171  -6.135  -2.273  1.00  0.00           N  
ATOM    210  CA  ASP A  30      -0.843  -7.556  -2.023  1.00  0.00           C  
ATOM    211  C   ASP A  30      -0.403  -7.725  -0.566  1.00  0.00           C  
ATOM    212  O   ASP A  30      -0.768  -8.678   0.092  1.00  0.00           O  
ATOM    213  CB  ASP A  30       0.283  -7.982  -2.965  1.00  0.00           C  
ATOM    214  CG  ASP A  30      -0.109  -9.278  -3.678  1.00  0.00           C  
ATOM    215  OD1 ASP A  30      -1.013  -9.230  -4.497  1.00  0.00           O  
ATOM    216  OD2 ASP A  30       0.501 -10.295  -3.394  1.00  0.00           O  
ATOM    217  N   SER A  31       0.367  -6.799  -0.057  1.00  0.00           N  
ATOM    218  CA  SER A  31       0.821  -6.890   1.363  1.00  0.00           C  
ATOM    219  C   SER A  31       1.988  -7.878   1.489  1.00  0.00           C  
ATOM    220  O   SER A  31       1.932  -8.830   2.240  1.00  0.00           O  
ATOM    221  CB  SER A  31      -0.349  -7.346   2.245  1.00  0.00           C  
ATOM    222  OG  SER A  31      -0.341  -8.763   2.364  1.00  0.00           O  
ATOM    223  N   LEU A  32       3.057  -7.658   0.772  1.00  0.00           N  
ATOM    224  CA  LEU A  32       4.213  -8.592   0.880  1.00  0.00           C  
ATOM    225  C   LEU A  32       5.394  -7.870   1.529  1.00  0.00           C  
ATOM    226  O   LEU A  32       5.826  -6.832   1.072  1.00  0.00           O  
ATOM    227  CB  LEU A  32       4.611  -9.084  -0.514  1.00  0.00           C  
ATOM    228  CG  LEU A  32       3.931 -10.424  -0.797  1.00  0.00           C  
ATOM    229  CD1 LEU A  32       2.435 -10.313  -0.496  1.00  0.00           C  
ATOM    230  CD2 LEU A  32       4.127 -10.794  -2.269  1.00  0.00           C  
ATOM    231  N   LYS A  33       5.914  -8.411   2.598  1.00  0.00           N  
ATOM    232  CA  LYS A  33       7.060  -7.752   3.286  1.00  0.00           C  
ATOM    233  C   LYS A  33       6.593  -6.416   3.866  1.00  0.00           C  
ATOM    234  O   LYS A  33       7.385  -5.606   4.304  1.00  0.00           O  
ATOM    235  CB  LYS A  33       8.191  -7.507   2.284  1.00  0.00           C  
ATOM    236  CG  LYS A  33       9.540  -7.677   2.987  1.00  0.00           C  
ATOM    237  CD  LYS A  33      10.470  -8.520   2.111  1.00  0.00           C  
ATOM    238  CE  LYS A  33      11.882  -8.500   2.700  1.00  0.00           C  
ATOM    239  NZ  LYS A  33      12.133  -9.773   3.433  1.00  0.00           N  
ATOM    240  N   HIS A  34       5.308  -6.181   3.871  1.00  0.00           N  
ATOM    241  CA  HIS A  34       4.784  -4.899   4.420  1.00  0.00           C  
ATOM    242  C   HIS A  34       4.197  -5.140   5.806  1.00  0.00           C  
ATOM    243  O   HIS A  34       4.625  -4.556   6.781  1.00  0.00           O  
ATOM    244  CB  HIS A  34       3.669  -4.354   3.491  1.00  0.00           C  
ATOM    245  CG  HIS A  34       4.316  -3.820   2.234  1.00  0.00           C  
ATOM    246  ND1 HIS A  34       5.480  -4.358   1.702  1.00  0.00           N  
ATOM    247  CD2 HIS A  34       3.964  -2.794   1.395  1.00  0.00           C  
ATOM    248  CE1 HIS A  34       5.778  -3.654   0.590  1.00  0.00           C  
ATOM    249  NE2 HIS A  34       4.886  -2.692   0.361  1.00  0.00           N  
ATOM    250  N   ALA A  35       3.216  -5.994   5.897  1.00  0.00           N  
ATOM    251  CA  ALA A  35       2.590  -6.270   7.220  1.00  0.00           C  
ATOM    252  C   ALA A  35       1.654  -5.116   7.594  1.00  0.00           C  
ATOM    253  O   ALA A  35       0.449  -5.228   7.488  1.00  0.00           O  
ATOM    254  CB  ALA A  35       3.678  -6.406   8.285  1.00  0.00           C  
ATOM    255  N   SER A  36       2.193  -4.010   8.037  1.00  0.00           N  
ATOM    256  CA  SER A  36       1.320  -2.865   8.418  1.00  0.00           C  
ATOM    257  C   SER A  36       2.074  -1.540   8.252  1.00  0.00           C  
ATOM    258  O   SER A  36       1.707  -0.538   8.833  1.00  0.00           O  
ATOM    259  CB  SER A  36       0.887  -3.022   9.876  1.00  0.00           C  
ATOM    260  OG  SER A  36      -0.023  -4.110   9.981  1.00  0.00           O  
ATOM    261  N   HIS A  37       3.116  -1.515   7.463  1.00  0.00           N  
ATOM    262  CA  HIS A  37       3.862  -0.236   7.275  1.00  0.00           C  
ATOM    263  C   HIS A  37       2.856   0.869   6.940  1.00  0.00           C  
ATOM    264  O   HIS A  37       2.299   1.496   7.820  1.00  0.00           O  
ATOM    265  CB  HIS A  37       4.883  -0.393   6.138  1.00  0.00           C  
ATOM    266  CG  HIS A  37       5.275   0.959   5.591  1.00  0.00           C  
ATOM    267  ND1 HIS A  37       5.933   1.915   6.353  1.00  0.00           N  
ATOM    268  CD2 HIS A  37       5.106   1.524   4.353  1.00  0.00           C  
ATOM    269  CE1 HIS A  37       6.131   2.993   5.565  1.00  0.00           C  
ATOM    270  NE2 HIS A  37       5.646   2.804   4.339  1.00  0.00           N  
ATOM    271  N   ASN A  38       2.607   1.112   5.681  1.00  0.00           N  
ATOM    272  CA  ASN A  38       1.624   2.176   5.319  1.00  0.00           C  
ATOM    273  C   ASN A  38       1.605   2.378   3.803  1.00  0.00           C  
ATOM    274  O   ASN A  38       2.577   2.128   3.123  1.00  0.00           O  
ATOM    275  CB  ASN A  38       2.024   3.488   5.997  1.00  0.00           C  
ATOM    276  CG  ASN A  38       0.778   4.175   6.560  1.00  0.00           C  
ATOM    277  OD1 ASN A  38      -0.318   3.960   6.081  1.00  0.00           O  
ATOM    278  ND2 ASN A  38       0.901   5.001   7.563  1.00  0.00           N  
ATOM    279  N   PHE A  39       0.509   2.854   3.271  1.00  0.00           N  
ATOM    280  CA  PHE A  39       0.442   3.094   1.802  1.00  0.00           C  
ATOM    281  C   PHE A  39      -0.771   3.992   1.445  1.00  0.00           C  
ATOM    282  O   PHE A  39      -1.790   3.970   2.107  1.00  0.00           O  
ATOM    283  CB  PHE A  39       0.418   1.761   1.017  1.00  0.00           C  
ATOM    284  CG  PHE A  39      -0.801   0.920   1.287  1.00  0.00           C  
ATOM    285  CD1 PHE A  39      -1.580   1.095   2.435  1.00  0.00           C  
ATOM    286  CD2 PHE A  39      -1.110  -0.058   0.388  1.00  0.00           C  
ATOM    287  CE1 PHE A  39      -2.680   0.273   2.650  1.00  0.00           C  
ATOM    288  CE2 PHE A  39      -2.207  -0.877   0.584  1.00  0.00           C  
ATOM    289  CZ  PHE A  39      -3.000  -0.716   1.716  1.00  0.00           C  
ATOM    290  N   LEU A  40      -0.664   4.753   0.370  1.00  0.00           N  
ATOM    291  CA  LEU A  40      -1.795   5.631  -0.090  1.00  0.00           C  
ATOM    292  C   LEU A  40      -2.184   5.234  -1.540  1.00  0.00           C  
ATOM    293  O   LEU A  40      -1.416   4.604  -2.236  1.00  0.00           O  
ATOM    294  CB  LEU A  40      -1.412   7.103   0.005  1.00  0.00           C  
ATOM    295  CG  LEU A  40      -2.063   7.724   1.262  1.00  0.00           C  
ATOM    296  CD1 LEU A  40      -3.468   8.233   0.943  1.00  0.00           C  
ATOM    297  CD2 LEU A  40      -2.145   6.698   2.404  1.00  0.00           C  
ATOM    298  N   PRO A  41      -3.403   5.541  -1.918  1.00  0.00           N  
ATOM    299  CA  PRO A  41      -3.963   5.154  -3.230  1.00  0.00           C  
ATOM    300  C   PRO A  41      -3.616   6.154  -4.327  1.00  0.00           C  
ATOM    301  O   PRO A  41      -3.701   7.347  -4.139  1.00  0.00           O  
ATOM    302  CB  PRO A  41      -5.471   5.158  -2.976  1.00  0.00           C  
ATOM    303  CG  PRO A  41      -5.709   6.081  -1.752  1.00  0.00           C  
ATOM    304  CD  PRO A  41      -4.339   6.297  -1.080  1.00  0.00           C  
ATOM    305  N   ILE A  42      -3.252   5.662  -5.482  1.00  0.00           N  
ATOM    306  CA  ILE A  42      -2.916   6.568  -6.615  1.00  0.00           C  
ATOM    307  C   ILE A  42      -4.125   7.444  -6.947  1.00  0.00           C  
ATOM    308  O   ILE A  42      -3.918   8.554  -7.407  1.00  0.00           O  
ATOM    309  CB  ILE A  42      -2.538   5.733  -7.841  1.00  0.00           C  
ATOM    310  CG1 ILE A  42      -3.714   4.833  -8.228  1.00  0.00           C  
ATOM    311  CG2 ILE A  42      -1.321   4.866  -7.513  1.00  0.00           C  
ATOM    312  CD1 ILE A  42      -3.472   4.248  -9.620  1.00  0.00           C  
ATOM    313  OXT ILE A  42      -5.237   6.989  -6.736  1.00  0.00           O  
TER     314      ILE A  42                                                      
HETATM  315 ZN    ZN A  43       4.525  -1.266  -0.050  1.00  0.00          ZN  
CONECT   24  315                                                                
CONECT   47  315                                                                
CONECT   49  315                                                                
CONECT  197  315                                                                
CONECT  247  315                                                                
CONECT  249  315                                                                
CONECT  315   24   47   49  197                                                 
CONECT  315  247  249                                                           
MASTER      174    0    1    1    2    0    4    6  314    1    8    4          
END