HEADER    METALLOTHIONEIN                         14-MAY-90   1MRB              
TITLE     THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD7 METALLOTHIONEIN-2A IN 
TITLE    2 AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD7 METALLOTHIONEIN-2A;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986                                                 
KEYWDS    METALLOTHIONEIN                                                       
EXPDTA    SOLUTION NMR                                                          
AUTHOR    W.BRAUN,A.ARSENIEV,P.SCHULTZE,E.WOERGOETTER,G.WAGNER,M.VASAK,         
AUTHOR   2 J.H.R.KAEGI,K.WUTHRICH                                               
REVDAT   7   23-FEB-22 1MRB    1       REMARK LINK                              
REVDAT   6   24-FEB-09 1MRB    1       VERSN                                    
REVDAT   5   01-APR-03 1MRB    1       JRNL                                     
REVDAT   4   15-JUL-92 1MRB    1       HET                                      
REVDAT   3   15-APR-92 1MRB    1       REMARK                                   
REVDAT   2   15-JUL-91 1MRB    1       HEADER COMPND EXPDTA                     
REVDAT   1   15-APR-91 1MRB    0                                                
JRNL        AUTH   A.ARSENIEV,P.SCHULTZE,E.WORGOTTER,W.BRAUN,G.WAGNER,M.VASAK,  
JRNL        AUTH 2 J.H.KAGI,K.WUTHRICH                                          
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER                  
JRNL        TITL 2 [CD7]METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY    
JRNL        TITL 3 NUCLEAR MAGNETIC RESONANCE.                                  
JRNL        REF    J.MOL.BIOL.                   V. 201   637 1988              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   3418714                                                      
JRNL        DOI    10.1016/0022-2836(88)90644-4                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.WAGNER,D.NEUHAUS,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,        
REMARK   1  AUTH 2 K.WUTHRICH                                                   
REMARK   1  TITL   NUCLEAR MAGNETIC RESONANCE IDENTIFICATION OF "HALF-TURN" AND 
REMARK   1  TITL 2 310-HELIX SECONDARY STRUCTURE IN RABBIT LIVER                
REMARK   1  TITL 3 METALLOTHIONEIN-2                                            
REMARK   1  REF    J.MOL.BIOL.                   V. 187   131 1986              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.BRAUN,G.WAGNER,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,          
REMARK   1  AUTH 2 K.WUTHRICH                                                   
REMARK   1  TITL   POLYPEPTIDE FOLD IN THE TWO METAL CLUSTERS OF                
REMARK   1  TITL 2 METALLOTHIONEIN-2 BY NUCLEAR MAGNETIC RESONANCE IN SOLUTION  
REMARK   1  REF    J.MOL.BIOL.                   V. 187   125 1986              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.WAGNER,D.NEUHAUS,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,        
REMARK   1  AUTH 2 K.WUTHRICH                                                   
REMARK   1  TITL   SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS IN RABBIT-LIVER         
REMARK   1  TITL 2 METALLOTHIONEIN-2                                            
REMARK   1  REF    EUR.J.BIOCHEM.                V. 157   275 1986              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   D.NEUHAUS,G.WAGNER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH            
REMARK   1  TITL   SYSTEMATIC APPLICATION OF HIGH-RESOLUTION,PHASE-SENSITIVE    
REMARK   1  TITL 2 TWO-DIMENSIONAL 1H-NMR TECHNIQUES FOR THE IDENTIFICATION OF  
REMARK   1  TITL 3 THE AMINO-ACID-PROTON SPIN SYSTEMS IN PROTEINS               
REMARK   1  REF    EUR.J.BIOCHEM.                V. 151   257 1985              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.H.FREY,G.WAGNER,M.VASAK,O.W.SORENSEN,D.NEUHAUS,            
REMARK   1  AUTH 2 E.WOERGOETTER,J.H.R.KAEGI,R.R.ERNST,K.WUTHRICH               
REMARK   1  TITL   POLYPEPTIDE-METAL CLUSTER CONNECTIVIES IN METALLO THIONEIN 2 
REMARK   1  TITL 2 BY NOVEL 1H-113CD HETERONUCLEAR TWO-DIMENSIONAL NMR          
REMARK   1  TITL 3 EXPERIMENTS                                                  
REMARK   1  REF    J.AM.CHEM.SOC.                V. 107  6847 1985              
REMARK   1  REFN                   ISSN 0002-7863                               
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 1MRB 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_1000175125.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
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 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    SER A  32      -95.37    -70.50                                   
REMARK 500    CYS A  33      -19.31    152.84                                   
REMARK 500    LYS A  43       23.68   -156.76                                   
REMARK 500    CYS A  44       31.84   -147.91                                   
REMARK 500    GLN A  46       42.27   -150.09                                   
REMARK 500    CYS A  48      117.03    -38.79                                   
REMARK 500    ASP A  55       -8.01     83.55                                   
REMARK 500    SER A  58       13.89   -140.02                                   
REMARK 500    CYS A  60       21.70   -142.54                                   
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                              CD A 105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  33   SG                                                     
REMARK 620 2 CYS A  34   SG  104.3                                              
REMARK 620 3 CYS A  44   SG  112.8 107.3                                        
REMARK 620 4 CYS A  48   SG  123.8 104.3 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 107  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  34   SG                                                     
REMARK 620 2 CYS A  36   SG  109.3                                              
REMARK 620 3 CYS A  37   N    74.1  92.7                                        
REMARK 620 4 CYS A  37   SG  104.6 133.6  67.1                                  
REMARK 620 5 CYS A  50   SG   96.3 110.4 156.8  96.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 106  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  37   SG                                                     
REMARK 620 2 CYS A  41   SG  120.2                                              
REMARK 620 3 CYS A  44   SG  115.1  92.2                                        
REMARK 620 4 CYS A  60   SG   90.5 135.2 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  50   SG                                                     
REMARK 620 2 CYS A  57   SG  108.6                                              
REMARK 620 3 CYS A  59   SG  111.4 106.6                                        
REMARK 620 4 CYS A  60   SG   95.0 107.2 126.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CD1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD7                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 106                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 107                  
DBREF  1MRB A   31    61  UNP    P18055   MT2A_RABIT      32     62             
SEQRES   1 A   31  LYS SER CYS CYS SER CYS CYS PRO PRO GLY CYS ALA LYS          
SEQRES   2 A   31  CYS ALA GLN GLY CYS ILE CYS LYS GLY ALA SER ASP LYS          
SEQRES   3 A   31  CYS SER CYS CYS ALA                                          
HET     CD  A 101       1                                                       
HET     CD  A 105       1                                                       
HET     CD  A 106       1                                                       
HET     CD  A 107       1                                                       
HETNAM      CD CADMIUM ION                                                      
FORMUL   2   CD    4(CD 2+)                                                     
LINK         SG  CYS A  33                CD    CD A 105     1555   1555  2.52  
LINK         SG  CYS A  34                CD    CD A 105     1555   1555  2.63  
LINK         SG  CYS A  34                CD    CD A 107     1555   1555  2.47  
LINK         SG  CYS A  36                CD    CD A 107     1555   1555  2.44  
LINK         SG  CYS A  37                CD    CD A 106     1555   1555  2.72  
LINK         N   CYS A  37                CD    CD A 107     1555   1555  3.10  
LINK         SG  CYS A  37                CD    CD A 107     1555   1555  2.44  
LINK         SG  CYS A  41                CD    CD A 106     1555   1555  2.48  
LINK         SG  CYS A  44                CD    CD A 105     1555   1555  2.53  
LINK         SG  CYS A  44                CD    CD A 106     1555   1555  2.64  
LINK         SG  CYS A  48                CD    CD A 105     1555   1555  2.50  
LINK         SG  CYS A  50                CD    CD A 101     1555   1555  2.53  
LINK         SG  CYS A  50                CD    CD A 107     1555   1555  2.70  
LINK         SG  CYS A  57                CD    CD A 101     1555   1555  2.50  
LINK         SG  CYS A  59                CD    CD A 101     1555   1555  2.47  
LINK         SG  CYS A  60                CD    CD A 101     1555   1555  2.64  
LINK         SG  CYS A  60                CD    CD A 106     1555   1555  2.49  
SITE     1 CD1  4 CYS A  50  CYS A  57  CYS A  59  CYS A  60                    
SITE     1 CD5  4 CYS A  33  CYS A  34  CYS A  44  CYS A  48                    
SITE     1 CD6  4 CYS A  37  CYS A  41  CYS A  44  CYS A  60                    
SITE     1 CD7  4 CYS A  34  CYS A  36  CYS A  37  CYS A  50                    
SITE     1 AC1  5 ILE A  49  CYS A  50  CYS A  57  CYS A  59                    
SITE     2 AC1  5 CYS A  60                                                     
SITE     1 AC2  4 CYS A  33  CYS A  34  CYS A  44  CYS A  48                    
SITE     1 AC3  5 CYS A  37  CYS A  41  LYS A  43  CYS A  44                    
SITE     2 AC3  5 CYS A  60                                                     
SITE     1 AC4  4 CYS A  34  CYS A  36  CYS A  37  CYS A  50                    
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   LYS A  31       0.000   0.000   0.000  1.00  3.37           N  
ATOM      2  CA  LYS A  31       1.453   0.000   0.000  1.00  2.46           C  
ATOM      3  C   LYS A  31       1.959   1.228   0.760  1.00  1.98           C  
ATOM      4  O   LYS A  31       1.463   2.335   0.557  1.00  2.52           O  
ATOM      5  CB  LYS A  31       1.989  -0.102  -1.429  1.00  2.72           C  
ATOM      6  CG  LYS A  31       3.337  -0.825  -1.459  1.00  3.19           C  
ATOM      7  CD  LYS A  31       4.062  -0.580  -2.784  1.00  4.20           C  
ATOM      8  CE  LYS A  31       3.105  -0.733  -3.969  1.00  4.95           C  
ATOM      9  NZ  LYS A  31       2.795   0.589  -4.559  1.00  6.14           N  
ATOM     10  H   LYS A  31      -0.338   0.478   0.828  1.00  3.48           H  
ATOM     11  HA  LYS A  31       1.780  -0.894   0.531  1.00  2.54           H  
ATOM     12  N   SER A  32       2.939   0.990   1.619  1.00  1.47           N  
ATOM     13  CA  SER A  32       3.517   2.063   2.411  1.00  1.16           C  
ATOM     14  C   SER A  32       4.337   2.992   1.513  1.00  1.16           C  
ATOM     15  O   SER A  32       3.790   3.905   0.895  1.00  2.27           O  
ATOM     16  CB  SER A  32       4.390   1.507   3.537  1.00  1.28           C  
ATOM     17  OG  SER A  32       4.638   2.479   4.549  1.00  1.72           O  
ATOM     18  H   SER A  32       3.336   0.086   1.778  1.00  1.79           H  
ATOM     19  HA  SER A  32       2.668   2.595   2.839  1.00  1.33           H  
ATOM     20  N   CYS A  33       5.634   2.728   1.469  1.00  0.84           N  
ATOM     21  CA  CYS A  33       6.534   3.529   0.658  1.00  0.99           C  
ATOM     22  C   CYS A  33       7.928   3.472   1.287  1.00  0.78           C  
ATOM     23  O   CYS A  33       8.924   3.760   0.625  1.00  0.98           O  
ATOM     24  CB  CYS A  33       6.034   4.967   0.509  1.00  1.44           C  
ATOM     25  SG  CYS A  33       5.518   5.766   2.073  1.00  1.51           S  
ATOM     26  H   CYS A  33       6.070   1.983   1.975  1.00  1.58           H  
ATOM     27  HA  CYS A  33       6.540   3.083  -0.337  1.00  1.28           H  
ATOM     28  N   CYS A  34       7.954   3.098   2.558  1.00  0.84           N  
ATOM     29  CA  CYS A  34       9.208   2.999   3.284  1.00  0.90           C  
ATOM     30  C   CYS A  34       8.992   2.091   4.496  1.00  0.99           C  
ATOM     31  O   CYS A  34       7.898   1.566   4.695  1.00  1.05           O  
ATOM     32  CB  CYS A  34       9.737   4.377   3.689  1.00  1.04           C  
ATOM     33  SG  CYS A  34       8.588   5.369   4.710  1.00  1.35           S  
ATOM     34  H   CYS A  34       7.139   2.865   3.089  1.00  1.12           H  
ATOM     35  HA  CYS A  34       9.934   2.562   2.597  1.00  0.98           H  
ATOM     36  N   SER A  35      10.053   1.935   5.274  1.00  1.32           N  
ATOM     37  CA  SER A  35       9.993   1.099   6.462  1.00  1.50           C  
ATOM     38  C   SER A  35      10.348   1.924   7.701  1.00  1.55           C  
ATOM     39  O   SER A  35      10.509   1.376   8.790  1.00  1.97           O  
ATOM     40  CB  SER A  35      10.931  -0.103   6.338  1.00  1.70           C  
ATOM     41  OG  SER A  35      10.245  -1.337   6.528  1.00  3.09           O  
ATOM     42  H   SER A  35      10.939   2.366   5.106  1.00  1.59           H  
ATOM     43  HA  SER A  35       8.962   0.750   6.517  1.00  1.49           H  
ATOM     44  N   CYS A  36      10.460   3.228   7.492  1.00  1.21           N  
ATOM     45  CA  CYS A  36      10.793   4.133   8.578  1.00  1.25           C  
ATOM     46  C   CYS A  36       9.546   4.950   8.923  1.00  1.21           C  
ATOM     47  O   CYS A  36       9.519   5.652   9.932  1.00  1.51           O  
ATOM     48  CB  CYS A  36      11.981   5.029   8.223  1.00  1.22           C  
ATOM     49  SG  CYS A  36      12.207   5.332   6.433  1.00  1.63           S  
ATOM     50  H   CYS A  36      10.328   3.665   6.602  1.00  1.05           H  
ATOM     51  HA  CYS A  36      11.095   3.513   9.422  1.00  1.36           H  
ATOM     52  N   CYS A  37       8.544   4.830   8.064  1.00  1.17           N  
ATOM     53  CA  CYS A  37       7.296   5.548   8.266  1.00  1.15           C  
ATOM     54  C   CYS A  37       6.141   4.616   7.896  1.00  1.14           C  
ATOM     55  O   CYS A  37       6.114   4.058   6.800  1.00  1.18           O  
ATOM     56  CB  CYS A  37       7.258   6.850   7.464  1.00  1.18           C  
ATOM     57  SG  CYS A  37       8.740   7.908   7.646  1.00  1.28           S  
ATOM     58  H   CYS A  37       8.574   4.257   7.246  1.00  1.38           H  
ATOM     59  HA  CYS A  37       7.256   5.815   9.321  1.00  1.21           H  
ATOM     60  N   PRO A  38       5.189   4.472   8.857  1.00  1.20           N  
ATOM     61  CA  PRO A  38       4.033   3.617   8.643  1.00  1.25           C  
ATOM     62  C   PRO A  38       3.029   4.279   7.698  1.00  1.32           C  
ATOM     63  O   PRO A  38       3.242   5.404   7.249  1.00  1.35           O  
ATOM     64  CB  PRO A  38       3.467   3.368  10.031  1.00  1.41           C  
ATOM     65  CG  PRO A  38       4.041   4.460  10.919  1.00  1.50           C  
ATOM     66  CD  PRO A  38       5.187   5.117  10.167  1.00  1.35           C  
ATOM     67  HA  PRO A  38       4.338   2.688   8.162  1.00  1.25           H  
ATOM     68  N   PRO A  39       1.927   3.533   7.417  1.00  1.41           N  
ATOM     69  CA  PRO A  39       0.889   4.036   6.533  1.00  1.57           C  
ATOM     70  C   PRO A  39       0.036   5.094   7.235  1.00  1.69           C  
ATOM     71  O   PRO A  39      -1.188   4.976   7.288  1.00  1.73           O  
ATOM     72  CB  PRO A  39       0.093   2.808   6.123  1.00  1.67           C  
ATOM     73  CG  PRO A  39       0.421   1.736   7.150  1.00  1.58           C  
ATOM     74  CD  PRO A  39       1.641   2.197   7.930  1.00  1.44           C  
ATOM     75  HA  PRO A  39       1.337   4.529   5.670  1.00  1.61           H  
ATOM     76  N   GLY A  40       0.715   6.105   7.757  1.00  1.83           N  
ATOM     77  CA  GLY A  40       0.035   7.183   8.454  1.00  2.03           C  
ATOM     78  C   GLY A  40       1.007   8.314   8.797  1.00  1.66           C  
ATOM     79  O   GLY A  40       0.773   9.076   9.734  1.00  1.73           O  
ATOM     80  H   GLY A  40       1.710   6.194   7.710  1.00  1.87           H  
ATOM     81  N   CYS A  41       2.078   8.387   8.020  1.00  1.43           N  
ATOM     82  CA  CYS A  41       3.087   9.411   8.230  1.00  1.18           C  
ATOM     83  C   CYS A  41       2.610  10.700   7.557  1.00  1.08           C  
ATOM     84  O   CYS A  41       1.829  10.657   6.608  1.00  1.37           O  
ATOM     85  CB  CYS A  41       4.457   8.970   7.711  1.00  1.22           C  
ATOM     86  SG  CYS A  41       4.860   9.546   6.021  1.00  1.89           S  
ATOM     87  H   CYS A  41       2.261   7.763   7.260  1.00  1.55           H  
ATOM     88  HA  CYS A  41       3.176   9.547   9.308  1.00  1.28           H  
ATOM     89  N   ALA A  42       3.100  11.816   8.076  1.00  1.02           N  
ATOM     90  CA  ALA A  42       2.733  13.115   7.537  1.00  1.24           C  
ATOM     91  C   ALA A  42       3.959  13.756   6.884  1.00  1.26           C  
ATOM     92  O   ALA A  42       4.198  14.953   7.044  1.00  1.90           O  
ATOM     93  CB  ALA A  42       2.146  13.983   8.652  1.00  1.69           C  
ATOM     94  H   ALA A  42       3.735  11.843   8.848  1.00  1.11           H  
ATOM     95  HA  ALA A  42       1.969  12.956   6.777  1.00  1.25           H  
ATOM     96  N   LYS A  43       4.705  12.932   6.163  1.00  0.91           N  
ATOM     97  CA  LYS A  43       5.900  13.404   5.485  1.00  0.89           C  
ATOM     98  C   LYS A  43       6.221  12.469   4.317  1.00  0.87           C  
ATOM     99  O   LYS A  43       7.366  12.391   3.876  1.00  1.64           O  
ATOM    100  CB  LYS A  43       7.052  13.563   6.479  1.00  1.07           C  
ATOM    101  CG  LYS A  43       6.594  14.306   7.735  1.00  1.84           C  
ATOM    102  CD  LYS A  43       6.605  15.820   7.511  1.00  2.12           C  
ATOM    103  CE  LYS A  43       8.011  16.392   7.699  1.00  2.36           C  
ATOM    104  NZ  LYS A  43       8.243  16.743   9.118  1.00  3.40           N  
ATOM    105  H   LYS A  43       4.504  11.960   6.038  1.00  1.13           H  
ATOM    106  HA  LYS A  43       5.680  14.394   5.086  1.00  1.02           H  
ATOM    107  N   CYS A  44       5.188  11.784   3.848  1.00  0.73           N  
ATOM    108  CA  CYS A  44       5.346  10.858   2.739  1.00  0.64           C  
ATOM    109  C   CYS A  44       4.047  10.851   1.931  1.00  0.82           C  
ATOM    110  O   CYS A  44       3.676   9.830   1.354  1.00  1.77           O  
ATOM    111  CB  CYS A  44       5.725   9.457   3.222  1.00  0.77           C  
ATOM    112  SG  CYS A  44       7.517   9.193   3.481  1.00  0.88           S  
ATOM    113  H   CYS A  44       4.260  11.853   4.212  1.00  1.31           H  
ATOM    114  HA  CYS A  44       6.174  11.229   2.137  1.00  0.65           H  
ATOM    115  N   ALA A  45       3.391  12.002   1.916  1.00  1.42           N  
ATOM    116  CA  ALA A  45       2.141  12.142   1.188  1.00  1.83           C  
ATOM    117  C   ALA A  45       2.394  12.917  -0.107  1.00  2.32           C  
ATOM    118  O   ALA A  45       1.455  13.401  -0.738  1.00  3.41           O  
ATOM    119  CB  ALA A  45       1.103  12.823   2.082  1.00  1.66           C  
ATOM    120  H   ALA A  45       3.699  12.828   2.388  1.00  2.24           H  
ATOM    121  HA  ALA A  45       1.788  11.141   0.940  1.00  2.22           H  
ATOM    122  N   GLN A  46       3.666  13.010  -0.465  1.00  2.11           N  
ATOM    123  CA  GLN A  46       4.054  13.717  -1.673  1.00  2.76           C  
ATOM    124  C   GLN A  46       5.328  13.107  -2.259  1.00  2.33           C  
ATOM    125  O   GLN A  46       6.224  13.830  -2.693  1.00  3.09           O  
ATOM    126  CB  GLN A  46       4.237  15.211  -1.399  1.00  3.78           C  
ATOM    127  CG  GLN A  46       3.717  16.051  -2.568  1.00  4.69           C  
ATOM    128  CD  GLN A  46       2.845  17.205  -2.069  1.00  5.20           C  
ATOM    129  OE1 GLN A  46       3.057  18.362  -2.392  1.00  6.44           O  
ATOM    130  NE2 GLN A  46       1.855  16.826  -1.266  1.00  4.86           N  
ATOM    131  H   GLN A  46       4.423  12.613   0.054  1.00  2.17           H  
ATOM    132  HA  GLN A  46       3.225  13.580  -2.368  1.00  3.14           H  
ATOM    133  N   GLY A  47       5.370  11.783  -2.253  1.00  1.75           N  
ATOM    134  CA  GLY A  47       6.520  11.067  -2.779  1.00  1.97           C  
ATOM    135  C   GLY A  47       7.535  10.773  -1.673  1.00  1.62           C  
ATOM    136  O   GLY A  47       8.210  11.679  -1.188  1.00  1.79           O  
ATOM    137  H   GLY A  47       4.637  11.202  -1.898  1.00  1.91           H  
ATOM    138  N   CYS A  48       7.611   9.502  -1.307  1.00  1.35           N  
ATOM    139  CA  CYS A  48       8.533   9.076  -0.267  1.00  1.11           C  
ATOM    140  C   CYS A  48       9.836   9.861  -0.430  1.00  1.13           C  
ATOM    141  O   CYS A  48      10.516   9.737  -1.448  1.00  1.24           O  
ATOM    142  CB  CYS A  48       8.767   7.565  -0.302  1.00  1.29           C  
ATOM    143  SG  CYS A  48       9.698   6.899   1.126  1.00  1.42           S  
ATOM    144  H   CYS A  48       7.058   8.770  -1.707  1.00  1.48           H  
ATOM    145  HA  CYS A  48       8.058   9.309   0.687  1.00  0.90           H  
ATOM    146  N   ILE A  49      10.146  10.650   0.588  1.00  1.10           N  
ATOM    147  CA  ILE A  49      11.356  11.454   0.570  1.00  1.15           C  
ATOM    148  C   ILE A  49      12.440  10.756   1.394  1.00  1.17           C  
ATOM    149  O   ILE A  49      13.586  11.202   1.424  1.00  1.36           O  
ATOM    150  CB  ILE A  49      11.058  12.882   1.031  1.00  1.17           C  
ATOM    151  CG1 ILE A  49      11.321  13.040   2.530  1.00  1.76           C  
ATOM    152  CG2 ILE A  49       9.633  13.294   0.653  1.00  1.43           C  
ATOM    153  CD1 ILE A  49      10.304  12.247   3.353  1.00  1.83           C  
ATOM    154  H   ILE A  49       9.588  10.745   1.412  1.00  1.09           H  
ATOM    155  HA  ILE A  49      11.694  11.514  -0.465  1.00  1.19           H  
ATOM    156  HB  ILE A  49      11.737  13.558   0.512  1.00  1.15           H  
ATOM    157  N   CYS A  50      12.039   9.672   2.042  1.00  1.08           N  
ATOM    158  CA  CYS A  50      12.962   8.907   2.864  1.00  1.14           C  
ATOM    159  C   CYS A  50      13.865   8.090   1.939  1.00  1.33           C  
ATOM    160  O   CYS A  50      13.418   7.122   1.325  1.00  2.33           O  
ATOM    161  CB  CYS A  50      12.223   8.021   3.869  1.00  1.14           C  
ATOM    162  SG  CYS A  50      10.582   8.647   4.383  1.00  2.04           S  
ATOM    163  H   CYS A  50      11.105   9.316   2.012  1.00  1.09           H  
ATOM    164  HA  CYS A  50      13.545   9.630   3.435  1.00  1.10           H  
ATOM    165  N   LYS A  51      15.120   8.509   1.868  1.00  1.02           N  
ATOM    166  CA  LYS A  51      16.091   7.828   1.028  1.00  1.16           C  
ATOM    167  C   LYS A  51      17.503   8.189   1.492  1.00  2.07           C  
ATOM    168  O   LYS A  51      17.792   9.353   1.765  1.00  3.52           O  
ATOM    169  CB  LYS A  51      15.831   8.136  -0.448  1.00  1.88           C  
ATOM    170  CG  LYS A  51      15.441   6.868  -1.212  1.00  3.77           C  
ATOM    171  CD  LYS A  51      13.922   6.692  -1.243  1.00  5.30           C  
ATOM    172  CE  LYS A  51      13.438   6.346  -2.653  1.00  6.93           C  
ATOM    173  NZ  LYS A  51      13.363   7.566  -3.488  1.00  7.35           N  
ATOM    174  H   LYS A  51      15.476   9.297   2.371  1.00  1.50           H  
ATOM    175  HA  LYS A  51      15.946   6.756   1.164  1.00  2.19           H  
ATOM    176  N   GLY A  52      18.346   7.169   1.568  1.00  2.43           N  
ATOM    177  CA  GLY A  52      19.721   7.365   1.994  1.00  3.76           C  
ATOM    178  C   GLY A  52      19.929   6.859   3.423  1.00  3.51           C  
ATOM    179  O   GLY A  52      21.047   6.876   3.935  1.00  4.62           O  
ATOM    180  H   GLY A  52      18.102   6.226   1.344  1.00  2.69           H  
ATOM    181  N   ALA A  53      18.834   6.421   4.027  1.00  2.54           N  
ATOM    182  CA  ALA A  53      18.882   5.912   5.387  1.00  2.27           C  
ATOM    183  C   ALA A  53      17.830   4.814   5.553  1.00  1.89           C  
ATOM    184  O   ALA A  53      16.644   5.044   5.319  1.00  2.56           O  
ATOM    185  CB  ALA A  53      18.682   7.065   6.372  1.00  2.95           C  
ATOM    186  H   ALA A  53      17.928   6.411   3.604  1.00  2.55           H  
ATOM    187  HA  ALA A  53      19.871   5.483   5.546  1.00  2.43           H  
ATOM    188  N   SER A  54      18.301   3.643   5.957  1.00  1.90           N  
ATOM    189  CA  SER A  54      17.415   2.509   6.158  1.00  2.18           C  
ATOM    190  C   SER A  54      17.182   2.285   7.653  1.00  1.83           C  
ATOM    191  O   SER A  54      18.114   2.372   8.450  1.00  2.67           O  
ATOM    192  CB  SER A  54      17.986   1.244   5.514  1.00  3.45           C  
ATOM    193  OG  SER A  54      19.308   0.964   5.967  1.00  3.97           O  
ATOM    194  H   SER A  54      19.266   3.464   6.146  1.00  2.47           H  
ATOM    195  HA  SER A  54      16.483   2.779   5.661  1.00  2.51           H  
ATOM    196  N   ASP A  55      15.932   2.000   7.988  1.00  1.65           N  
ATOM    197  CA  ASP A  55      15.565   1.763   9.374  1.00  1.50           C  
ATOM    198  C   ASP A  55      15.317   3.103  10.068  1.00  1.36           C  
ATOM    199  O   ASP A  55      14.852   3.141  11.207  1.00  1.73           O  
ATOM    200  CB  ASP A  55      16.685   1.041  10.125  1.00  2.00           C  
ATOM    201  CG  ASP A  55      17.593   1.948  10.959  1.00  3.12           C  
ATOM    202  OD1 ASP A  55      17.127   2.675  11.849  1.00  3.59           O  
ATOM    203  OD2 ASP A  55      18.847   1.889  10.659  1.00  4.69           O  
ATOM    204  H   ASP A  55      15.179   1.931   7.334  1.00  2.38           H  
ATOM    205  HA  ASP A  55      14.669   1.143   9.331  1.00  1.57           H  
ATOM    206  N   LYS A  56      15.638   4.172   9.354  1.00  1.45           N  
ATOM    207  CA  LYS A  56      15.456   5.511   9.887  1.00  1.37           C  
ATOM    208  C   LYS A  56      15.673   6.534   8.770  1.00  1.36           C  
ATOM    209  O   LYS A  56      16.345   6.245   7.780  1.00  1.83           O  
ATOM    210  CB  LYS A  56      16.356   5.730  11.104  1.00  1.85           C  
ATOM    211  CG  LYS A  56      16.666   7.216  11.297  1.00  2.79           C  
ATOM    212  CD  LYS A  56      15.552   7.910  12.084  1.00  3.13           C  
ATOM    213  CE  LYS A  56      15.103   7.055  13.270  1.00  3.13           C  
ATOM    214  NZ  LYS A  56      13.937   6.222  12.897  1.00  4.17           N  
ATOM    215  H   LYS A  56      16.016   4.133   8.428  1.00  1.91           H  
ATOM    216  HA  LYS A  56      14.425   5.589  10.230  1.00  1.18           H  
ATOM    217  N   CYS A  57      15.092   7.708   8.965  1.00  1.13           N  
ATOM    218  CA  CYS A  57      15.214   8.776   7.987  1.00  1.13           C  
ATOM    219  C   CYS A  57      15.456  10.088   8.735  1.00  1.18           C  
ATOM    220  O   CYS A  57      15.671  10.086   9.946  1.00  1.63           O  
ATOM    221  CB  CYS A  57      13.984   8.854   7.080  1.00  1.13           C  
ATOM    222  SG  CYS A  57      12.514   9.629   7.845  1.00  2.12           S  
ATOM    223  H   CYS A  57      14.548   7.936   9.773  1.00  1.24           H  
ATOM    224  HA  CYS A  57      16.067   8.527   7.356  1.00  1.40           H  
ATOM    225  N   SER A  58      15.412  11.178   7.982  1.00  1.27           N  
ATOM    226  CA  SER A  58      15.624  12.495   8.559  1.00  1.34           C  
ATOM    227  C   SER A  58      14.655  13.501   7.936  1.00  1.24           C  
ATOM    228  O   SER A  58      14.827  14.710   8.086  1.00  1.62           O  
ATOM    229  CB  SER A  58      17.069  12.957   8.361  1.00  1.85           C  
ATOM    230  OG  SER A  58      17.781  13.027   9.594  1.00  1.73           O  
ATOM    231  H   SER A  58      15.237  11.171   6.998  1.00  1.64           H  
ATOM    232  HA  SER A  58      15.423  12.379   9.624  1.00  1.26           H  
ATOM    233  N   CYS A  59      13.657  12.965   7.248  1.00  1.16           N  
ATOM    234  CA  CYS A  59      12.660  13.802   6.602  1.00  1.45           C  
ATOM    235  C   CYS A  59      11.322  13.593   7.314  1.00  1.36           C  
ATOM    236  O   CYS A  59      10.355  14.304   7.047  1.00  1.73           O  
ATOM    237  CB  CYS A  59      12.561  13.507   5.103  1.00  1.83           C  
ATOM    238  SG  CYS A  59      13.167  11.854   4.604  1.00  1.17           S  
ATOM    239  H   CYS A  59      13.524  11.981   7.130  1.00  1.28           H  
ATOM    240  HA  CYS A  59      12.999  14.832   6.708  1.00  1.58           H  
ATOM    241  N   CYS A  60      11.310  12.614   8.207  1.00  1.05           N  
ATOM    242  CA  CYS A  60      10.107  12.303   8.960  1.00  1.24           C  
ATOM    243  C   CYS A  60      10.517  11.925  10.385  1.00  1.51           C  
ATOM    244  O   CYS A  60       9.767  11.254  11.093  1.00  2.36           O  
ATOM    245  CB  CYS A  60       9.290  11.197   8.289  1.00  1.12           C  
ATOM    246  SG  CYS A  60       9.033  11.417   6.491  1.00  1.38           S  
ATOM    247  H   CYS A  60      12.101  12.040   8.419  1.00  0.88           H  
ATOM    248  HA  CYS A  60       9.495  13.205   8.960  1.00  1.66           H  
ATOM    249  N   ALA A  61      11.705  12.372  10.764  1.00  1.20           N  
ATOM    250  CA  ALA A  61      12.223  12.090  12.091  1.00  1.73           C  
ATOM    251  C   ALA A  61      11.666  13.115  13.081  1.00  2.22           C  
ATOM    252  O   ALA A  61      11.834  12.880  14.297  1.00  3.61           O  
ATOM    253  CB  ALA A  61      13.753  12.087  12.053  1.00  1.82           C  
ATOM    254  OXT ALA A  61      11.085  14.111  12.598  1.00  2.28           O  
ATOM    255  H   ALA A  61      12.309  12.917  10.182  1.00  1.11           H  
ATOM    256  HA  ALA A  61      11.878  11.096  12.378  1.00  2.37           H  
TER     257      ALA A  61                                                      
HETATM  258 CD    CD A 101      11.430  10.566   5.791  1.00  1.16          CD  
HETATM  259 CD    CD A 105       7.737   6.800   2.679  1.00  1.10          CD  
HETATM  260 CD    CD A 106       7.339   9.639   6.077  1.00  1.08          CD  
HETATM  261 CD    CD A 107      10.164   6.638   6.130  1.00  1.12          CD  
CONECT   25  259                                                                
CONECT   33  259  261                                                           
CONECT   49  261                                                                
CONECT   52  261                                                                
CONECT   57  260  261                                                           
CONECT   86  260                                                                
CONECT  112  259  260                                                           
CONECT  143  259                                                                
CONECT  162  258  261                                                           
CONECT  222  258                                                                
CONECT  238  258                                                                
CONECT  246  258  260                                                           
CONECT  258  162  222  238  246                                                 
CONECT  259   25   33  112  143                                                 
CONECT  260   57   86  112  246                                                 
CONECT  261   33   49   52   57                                                 
CONECT  261  162                                                                
MASTER      201    0    4    0    0    0   10    6  202    1   17    3          
END