HEADER    METALLOTHIONEIN                         14-MAY-90   1MRT              
TITLE     CONFORMATION OF CD-7 METALLOTHIONEIN-2 FROM RAT LIVER IN AQUEOUS      
TITLE    2 SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD7 METALLOTHIONEIN-2;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;                                  
SOURCE   3 ORGANISM_COMMON: BLACK RAT;                                          
SOURCE   4 ORGANISM_TAXID: 10117                                                
KEYWDS    METALLOTHIONEIN                                                       
EXPDTA    SOLUTION NMR                                                          
AUTHOR    W.BRAUN,P.SCHULTZE,E.WOERGOETTER,G.WAGNER,M.VASAK,J.H.R.KAEGI,        
AUTHOR   2 K.WUTHRICH                                                           
REVDAT   6   23-FEB-22 1MRT    1       REMARK LINK                              
REVDAT   5   24-FEB-09 1MRT    1       VERSN                                    
REVDAT   4   01-APR-03 1MRT    1       JRNL                                     
REVDAT   3   15-JUL-92 1MRT    1       HET                                      
REVDAT   2   15-JUL-91 1MRT    1       HEADER COMPND EXPDTA AUTHOR              
REVDAT   1   15-APR-91 1MRT    0                                                
JRNL        AUTH   P.SCHULTZE,E.WORGOTTER,W.BRAUN,G.WAGNER,M.VASAK,J.H.KAGI,    
JRNL        AUTH 2 K.WUTHRICH                                                   
JRNL        TITL   CONFORMATION OF [CD7]-METALLOTHIONEIN-2 FROM RAT LIVER IN    
JRNL        TITL 2 AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE    
JRNL        TITL 3 SPECTROSCOPY.                                                
JRNL        REF    J.MOL.BIOL.                   V. 203   251 1988              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   3184190                                                      
JRNL        DOI    10.1016/0022-2836(88)90106-4                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.ARSENIEV,P.SCHULTZE,E.WOERGOETTER,W.BRAUN,G.WAGNER,        
REMARK   1  AUTH 2 M.VASAK,J.H.R.KAEGI,K.WUTHRICH                               
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7             
REMARK   1  TITL 2 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR 
REMARK   1  TITL 3 MAGNETIC RESONANCE.                                          
REMARK   1  REF    J.MOL.BIOL.                   V. 201   637 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.WOERGOETTER,G.WAGNER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH        
REMARK   1  TITL   SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS IN RAT-LIVER            
REMARK   1  TITL 2 METALLOTHIONEIN-2                                            
REMARK   1  REF    EUR.J.BIOCHEM.                V. 167   457 1987              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.VASAK,E.WOERGOETTER,G.WAGNER,J.H.R.KAEGI,K.WUTHRICH        
REMARK   1  TITL   METAL CO-ORDINATION IN RAT LIVER METALLOTHIONEIN-2 PREPARED  
REMARK   1  TITL 2 WITH OR WITHOUT RECONSTITUTION OF THE METAL CLUSTERS, AND    
REMARK   1  TITL 3 COMPARISON WITH RABBIT LIVER METALLOTHIONEIN-2.              
REMARK   1  REF    J.MOL.BIOL.                   V. 196   711 1987              
REMARK   1  REFN                   ISSN 0022-2836                               
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 1MRT 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_1000175138.                                   
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: 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    ALA A    42     H    SER A    45              1.57            
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    CYS A  33      -48.35   -144.78                                   
REMARK 500    VAL A  39       62.99    179.68                                   
REMARK 500    CYS A  41      153.87    -37.60                                   
REMARK 500    SER A  45      -78.15    -38.13                                   
REMARK 500    CYS A  48       81.67    -57.17                                   
REMARK 500    GLU A  52      102.14    179.09                                   
REMARK 500    ALA A  53       89.25    169.22                                   
REMARK 500    SER A  54       36.06    -88.32                                   
REMARK 500    ASP A  55      -13.85    148.96                                   
REMARK 500    LYS A  56      148.04   -170.48                                   
REMARK 500    CYS A  60      -91.96   -134.38                                   
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  125.2                                              
REMARK 620 3 CYS A  44   SG  105.2 101.4                                        
REMARK 620 4 CYS A  48   SG   88.8 111.2 127.2                                  
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  116.0                                              
REMARK 620 3 CYS A  37   SG   95.4 126.8                                        
REMARK 620 4 CYS A  37   N    68.8  87.8  63.9                                  
REMARK 620 5 CYS A  50   SG  127.4  94.0  99.4 159.5                            
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  101.3                                              
REMARK 620 3 CYS A  44   SG  116.3 113.7                                        
REMARK 620 4 CYS A  60   SG   93.1 101.3 126.7                                  
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  108.2                                              
REMARK 620 3 CYS A  59   SG   98.3 108.5                                        
REMARK 620 4 CYS A  60   SG  103.9 109.9 126.1                                  
REMARK 620 5 CYS A  60   N   167.1  72.5  93.5  64.6                            
REMARK 620 N                    1     2     3     4                             
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  1MRT A   31    61  UNP    P04355   MT2_RAT         31     61             
SEQRES   1 A   31  LYS SER CYS CYS SER CYS CYS PRO VAL GLY CYS ALA LYS          
SEQRES   2 A   31  CYS SER GLN GLY CYS ILE CYS LYS GLU 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  2.56  
LINK         SG  CYS A  34                CD    CD A 105     1555   1555  2.48  
LINK         SG  CYS A  34                CD    CD A 107     1555   1555  2.48  
LINK         SG  CYS A  36                CD    CD A 107     1555   1555  2.48  
LINK         SG  CYS A  37                CD    CD A 106     1555   1555  2.81  
LINK         SG  CYS A  37                CD    CD A 107     1555   1555  2.53  
LINK         N   CYS A  37                CD    CD A 107     1555   1555  3.15  
LINK         SG  CYS A  41                CD    CD A 106     1555   1555  2.53  
LINK         SG  CYS A  44                CD    CD A 105     1555   1555  2.53  
LINK         SG  CYS A  44                CD    CD A 106     1555   1555  2.50  
LINK         SG  CYS A  48                CD    CD A 105     1555   1555  2.51  
LINK         SG  CYS A  50                CD    CD A 101     1555   1555  2.56  
LINK         SG  CYS A  50                CD    CD A 107     1555   1555  2.65  
LINK         SG  CYS A  57                CD    CD A 101     1555   1555  2.50  
LINK         SG  CYS A  59                CD    CD A 101     1555   1555  2.53  
LINK         SG  CYS A  60                CD    CD A 101     1555   1555  2.60  
LINK         N   CYS A  60                CD    CD A 101     1555   1555  3.11  
LINK         SG  CYS A  60                CD    CD A 106     1555   1555  2.50  
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  4 CYS A  50  CYS A  57  CYS A  59  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  CYS A  44  CYS A  50                    
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  6.15           N  
ATOM      2  CA  LYS A  31       1.453   0.000   0.000  1.00  4.95           C  
ATOM      3  C   LYS A  31       1.959   1.421   0.255  1.00  2.72           C  
ATOM      4  O   LYS A  31       1.421   2.383  -0.292  1.00  2.64           O  
ATOM      5  CB  LYS A  31       1.989  -0.621  -1.291  1.00  5.93           C  
ATOM      6  CG  LYS A  31       1.411  -2.022  -1.507  1.00  7.38           C  
ATOM      7  CD  LYS A  31       2.419  -3.099  -1.101  1.00  8.69           C  
ATOM      8  CE  LYS A  31       2.466  -4.224  -2.136  1.00 10.32           C  
ATOM      9  NZ  LYS A  31       3.328  -3.843  -3.277  1.00 10.15           N  
ATOM     10  H   LYS A  31      -0.338   0.478   0.828  1.00  5.83           H  
ATOM     11  HA  LYS A  31       1.780  -0.636   0.823  1.00  5.73           H  
ATOM     12  N   SER A  32       2.987   1.510   1.085  1.00  2.40           N  
ATOM     13  CA  SER A  32       3.572   2.797   1.419  1.00  2.52           C  
ATOM     14  C   SER A  32       5.074   2.780   1.131  1.00  2.16           C  
ATOM     15  O   SER A  32       5.622   3.752   0.613  1.00  3.02           O  
ATOM     16  CB  SER A  32       3.315   3.155   2.884  1.00  5.00           C  
ATOM     17  OG  SER A  32       3.205   4.563   3.078  1.00  6.58           O  
ATOM     18  H   SER A  32       3.419   0.723   1.526  1.00  3.54           H  
ATOM     19  HA  SER A  32       3.067   3.518   0.775  1.00  2.70           H  
ATOM     20  N   CYS A  33       5.699   1.665   1.480  1.00  1.15           N  
ATOM     21  CA  CYS A  33       7.127   1.509   1.266  1.00  0.95           C  
ATOM     22  C   CYS A  33       7.402   0.048   0.906  1.00  0.98           C  
ATOM     23  O   CYS A  33       8.105  -0.235  -0.063  1.00  1.64           O  
ATOM     24  CB  CYS A  33       7.934   1.957   2.487  1.00  1.09           C  
ATOM     25  SG  CYS A  33       9.750   1.849   2.287  1.00  2.35           S  
ATOM     26  H   CYS A  33       5.246   0.879   1.901  1.00  1.06           H  
ATOM     27  HA  CYS A  33       7.394   2.168   0.440  1.00  1.21           H  
ATOM     28  N   CYS A  34       6.833  -0.843   1.705  1.00  1.00           N  
ATOM     29  CA  CYS A  34       7.008  -2.268   1.482  1.00  0.97           C  
ATOM     30  C   CYS A  34       5.664  -2.960   1.722  1.00  1.24           C  
ATOM     31  O   CYS A  34       4.650  -2.298   1.934  1.00  2.59           O  
ATOM     32  CB  CYS A  34       8.114  -2.847   2.366  1.00  0.76           C  
ATOM     33  SG  CYS A  34       8.309  -2.026   3.989  1.00  0.93           S  
ATOM     34  H   CYS A  34       6.262  -0.605   2.491  1.00  1.52           H  
ATOM     35  HA  CYS A  34       7.324  -2.386   0.446  1.00  1.18           H  
ATOM     36  N   SER A  35       5.701  -4.284   1.681  1.00  0.81           N  
ATOM     37  CA  SER A  35       4.500  -5.073   1.892  1.00  0.91           C  
ATOM     38  C   SER A  35       4.402  -5.497   3.359  1.00  0.86           C  
ATOM     39  O   SER A  35       3.388  -6.049   3.783  1.00  1.12           O  
ATOM     40  CB  SER A  35       4.482  -6.303   0.982  1.00  1.23           C  
ATOM     41  OG  SER A  35       4.672  -5.957  -0.387  1.00  2.18           O  
ATOM     42  H   SER A  35       6.531  -4.815   1.508  1.00  1.68           H  
ATOM     43  HA  SER A  35       3.672  -4.415   1.628  1.00  0.93           H  
ATOM     44  N   CYS A  36       5.470  -5.223   4.093  1.00  0.71           N  
ATOM     45  CA  CYS A  36       5.518  -5.569   5.503  1.00  0.81           C  
ATOM     46  C   CYS A  36       5.427  -4.277   6.318  1.00  0.92           C  
ATOM     47  O   CYS A  36       5.019  -4.298   7.478  1.00  1.22           O  
ATOM     48  CB  CYS A  36       6.773  -6.373   5.847  1.00  0.75           C  
ATOM     49  SG  CYS A  36       8.158  -6.175   4.667  1.00  1.93           S  
ATOM     50  H   CYS A  36       6.291  -4.773   3.740  1.00  0.71           H  
ATOM     51  HA  CYS A  36       4.658  -6.210   5.698  1.00  1.01           H  
ATOM     52  N   CYS A  37       5.815  -3.183   5.679  1.00  0.95           N  
ATOM     53  CA  CYS A  37       5.782  -1.884   6.330  1.00  1.23           C  
ATOM     54  C   CYS A  37       5.193  -0.869   5.348  1.00  1.39           C  
ATOM     55  O   CYS A  37       5.778   0.187   5.116  1.00  2.07           O  
ATOM     56  CB  CYS A  37       7.169  -1.463   6.821  1.00  1.41           C  
ATOM     57  SG  CYS A  37       8.141  -2.798   7.611  1.00  1.07           S  
ATOM     58  H   CYS A  37       6.146  -3.174   4.735  1.00  1.01           H  
ATOM     59  HA  CYS A  37       5.145  -1.990   7.207  1.00  1.46           H  
ATOM     60  N   PRO A  38       4.011  -1.236   4.783  1.00  1.91           N  
ATOM     61  CA  PRO A  38       3.335  -0.370   3.832  1.00  2.35           C  
ATOM     62  C   PRO A  38       2.670   0.811   4.543  1.00  1.53           C  
ATOM     63  O   PRO A  38       1.444   0.909   4.577  1.00  2.85           O  
ATOM     64  CB  PRO A  38       2.341  -1.270   3.117  1.00  3.91           C  
ATOM     65  CG  PRO A  38       2.168  -2.490   4.008  1.00  4.29           C  
ATOM     66  CD  PRO A  38       3.289  -2.480   5.035  1.00  2.96           C  
ATOM     67  HA  PRO A  38       4.058   0.060   3.138  1.00  2.74           H  
ATOM     68  N   VAL A  39       3.507   1.678   5.092  1.00  1.24           N  
ATOM     69  CA  VAL A  39       3.016   2.849   5.799  1.00  1.53           C  
ATOM     70  C   VAL A  39       4.203   3.656   6.328  1.00  1.56           C  
ATOM     71  O   VAL A  39       4.362   3.813   7.538  1.00  2.70           O  
ATOM     72  CB  VAL A  39       2.043   2.423   6.901  1.00  3.28           C  
ATOM     73  CG1 VAL A  39       0.592   2.588   6.446  1.00  3.67           C  
ATOM     74  CG2 VAL A  39       2.317   0.986   7.350  1.00  5.03           C  
ATOM     75  H   VAL A  39       4.503   1.592   5.059  1.00  2.44           H  
ATOM     76  HA  VAL A  39       2.467   3.460   5.082  1.00  1.97           H  
ATOM     77  HB  VAL A  39       2.202   3.078   7.759  1.00  4.23           H  
ATOM     78  N   GLY A  40       5.006   4.147   5.396  1.00  1.61           N  
ATOM     79  CA  GLY A  40       6.174   4.934   5.753  1.00  2.45           C  
ATOM     80  C   GLY A  40       6.702   4.537   7.133  1.00  2.07           C  
ATOM     81  O   GLY A  40       7.052   5.398   7.939  1.00  2.52           O  
ATOM     82  H   GLY A  40       4.870   4.015   4.414  1.00  2.08           H  
ATOM     83  N   CYS A  41       6.742   3.233   7.363  1.00  1.47           N  
ATOM     84  CA  CYS A  41       7.221   2.711   8.632  1.00  1.15           C  
ATOM     85  C   CYS A  41       8.391   3.580   9.098  1.00  1.06           C  
ATOM     86  O   CYS A  41       9.076   4.194   8.281  1.00  1.39           O  
ATOM     87  CB  CYS A  41       7.613   1.236   8.525  1.00  1.20           C  
ATOM     88  SG  CYS A  41       9.128   0.776   9.443  1.00  1.67           S  
ATOM     89  H   CYS A  41       6.456   2.539   6.702  1.00  1.47           H  
ATOM     90  HA  CYS A  41       6.388   2.776   9.332  1.00  1.21           H  
ATOM     91  N   ALA A  42       8.584   3.604  10.408  1.00  1.24           N  
ATOM     92  CA  ALA A  42       9.659   4.387  10.992  1.00  1.33           C  
ATOM     93  C   ALA A  42      10.983   4.006  10.326  1.00  0.94           C  
ATOM     94  O   ALA A  42      11.589   4.820   9.631  1.00  0.90           O  
ATOM     95  CB  ALA A  42       9.685   4.170  12.507  1.00  2.16           C  
ATOM     96  H   ALA A  42       8.022   3.101  11.065  1.00  1.65           H  
ATOM     97  HA  ALA A  42       9.450   5.438  10.792  1.00  1.56           H  
ATOM     98  N   LYS A  43      11.392   2.768  10.562  1.00  1.38           N  
ATOM     99  CA  LYS A  43      12.632   2.269   9.993  1.00  1.74           C  
ATOM    100  C   LYS A  43      12.610   2.470   8.476  1.00  1.47           C  
ATOM    101  O   LYS A  43      13.656   2.457   7.829  1.00  2.08           O  
ATOM    102  CB  LYS A  43      12.872   0.819  10.418  1.00  2.43           C  
ATOM    103  CG  LYS A  43      14.299   0.628  10.936  1.00  3.82           C  
ATOM    104  CD  LYS A  43      14.363  -0.507  11.960  1.00  4.25           C  
ATOM    105  CE  LYS A  43      15.803  -0.984  12.160  1.00  5.90           C  
ATOM    106  NZ  LYS A  43      15.923  -1.755  13.417  1.00  6.84           N  
ATOM    107  H   LYS A  43      10.893   2.113  11.128  1.00  1.77           H  
ATOM    108  HA  LYS A  43      13.445   2.865  10.408  1.00  2.02           H  
ATOM    109  N   CYS A  44      11.406   2.650   7.953  1.00  0.91           N  
ATOM    110  CA  CYS A  44      11.233   2.853   6.525  1.00  1.28           C  
ATOM    111  C   CYS A  44      10.735   4.282   6.299  1.00  1.89           C  
ATOM    112  O   CYS A  44      10.079   4.563   5.297  1.00  2.96           O  
ATOM    113  CB  CYS A  44      10.288   1.816   5.916  1.00  1.07           C  
ATOM    114  SG  CYS A  44      11.003   0.142   5.729  1.00  1.39           S  
ATOM    115  H   CYS A  44      10.560   2.659   8.486  1.00  0.70           H  
ATOM    116  HA  CYS A  44      12.212   2.708   6.067  1.00  1.80           H  
ATOM    117  N   SER A  45      11.064   5.146   7.247  1.00  1.48           N  
ATOM    118  CA  SER A  45      10.658   6.539   7.165  1.00  2.19           C  
ATOM    119  C   SER A  45      10.743   7.024   5.716  1.00  1.97           C  
ATOM    120  O   SER A  45       9.727   7.122   5.030  1.00  2.42           O  
ATOM    121  CB  SER A  45      11.521   7.419   8.070  1.00  3.00           C  
ATOM    122  OG  SER A  45      11.131   7.323   9.438  1.00  3.94           O  
ATOM    123  H   SER A  45      11.598   4.909   8.059  1.00  1.07           H  
ATOM    124  HA  SER A  45       9.626   6.560   7.515  1.00  2.86           H  
ATOM    125  N   GLN A  46      11.965   7.313   5.293  1.00  2.00           N  
ATOM    126  CA  GLN A  46      12.196   7.785   3.938  1.00  2.32           C  
ATOM    127  C   GLN A  46      13.271   6.937   3.257  1.00  1.52           C  
ATOM    128  O   GLN A  46      14.236   7.472   2.713  1.00  2.58           O  
ATOM    129  CB  GLN A  46      12.579   9.266   3.932  1.00  3.82           C  
ATOM    130  CG  GLN A  46      12.785   9.773   2.503  1.00  4.40           C  
ATOM    131  CD  GLN A  46      11.552   9.496   1.640  1.00  6.16           C  
ATOM    132  OE1 GLN A  46      10.489  10.062   1.832  1.00  7.64           O  
ATOM    133  NE2 GLN A  46      11.754   8.597   0.681  1.00  6.56           N  
ATOM    134  H   GLN A  46      12.786   7.230   5.857  1.00  2.30           H  
ATOM    135  HA  GLN A  46      11.244   7.661   3.422  1.00  2.86           H  
ATOM    136  N   GLY A  47      13.069   5.629   3.309  1.00  0.97           N  
ATOM    137  CA  GLY A  47      14.009   4.701   2.703  1.00  1.37           C  
ATOM    138  C   GLY A  47      13.689   3.259   3.100  1.00  1.42           C  
ATOM    139  O   GLY A  47      13.959   2.847   4.227  1.00  2.89           O  
ATOM    140  H   GLY A  47      12.281   5.202   3.753  1.00  1.82           H  
ATOM    141  N   CYS A  48      13.119   2.530   2.151  1.00  1.29           N  
ATOM    142  CA  CYS A  48      12.759   1.143   2.388  1.00  1.21           C  
ATOM    143  C   CYS A  48      14.020   0.385   2.811  1.00  1.07           C  
ATOM    144  O   CYS A  48      14.654  -0.277   1.992  1.00  1.75           O  
ATOM    145  CB  CYS A  48      12.100   0.512   1.160  1.00  1.44           C  
ATOM    146  SG  CYS A  48      11.411  -1.161   1.433  1.00  1.24           S  
ATOM    147  H   CYS A  48      12.903   2.873   1.237  1.00  2.47           H  
ATOM    148  HA  CYS A  48      12.020   1.143   3.189  1.00  1.16           H  
ATOM    149  N   ILE A  49      14.344   0.509   4.090  1.00  1.07           N  
ATOM    150  CA  ILE A  49      15.517  -0.155   4.632  1.00  1.05           C  
ATOM    151  C   ILE A  49      15.122  -1.543   5.142  1.00  1.02           C  
ATOM    152  O   ILE A  49      15.873  -2.172   5.885  1.00  1.16           O  
ATOM    153  CB  ILE A  49      16.188   0.721   5.692  1.00  1.14           C  
ATOM    154  CG1 ILE A  49      15.353   0.769   6.972  1.00  1.15           C  
ATOM    155  CG2 ILE A  49      16.477   2.120   5.143  1.00  1.23           C  
ATOM    156  CD1 ILE A  49      15.787  -0.323   7.952  1.00  1.08           C  
ATOM    157  H   ILE A  49      13.823   1.050   4.749  1.00  1.69           H  
ATOM    158  HA  ILE A  49      16.230  -0.277   3.816  1.00  1.15           H  
ATOM    159  HB  ILE A  49      17.147   0.272   5.949  1.00  1.26           H  
ATOM    160  N   CYS A  50      13.944  -1.979   4.722  1.00  0.99           N  
ATOM    161  CA  CYS A  50      13.440  -3.280   5.127  1.00  1.03           C  
ATOM    162  C   CYS A  50      13.310  -4.155   3.878  1.00  1.04           C  
ATOM    163  O   CYS A  50      12.383  -3.983   3.089  1.00  1.47           O  
ATOM    164  CB  CYS A  50      12.115  -3.164   5.882  1.00  1.43           C  
ATOM    165  SG  CYS A  50      11.276  -4.757   6.210  1.00  1.73           S  
ATOM    166  H   CYS A  50      13.339  -1.461   4.117  1.00  1.06           H  
ATOM    167  HA  CYS A  50      14.172  -3.698   5.818  1.00  1.05           H  
ATOM    168  N   LYS A  51      14.254  -5.075   3.738  1.00  1.12           N  
ATOM    169  CA  LYS A  51      14.257  -5.976   2.599  1.00  1.39           C  
ATOM    170  C   LYS A  51      14.383  -7.418   3.095  1.00  1.38           C  
ATOM    171  O   LYS A  51      15.377  -8.089   2.820  1.00  2.31           O  
ATOM    172  CB  LYS A  51      15.343  -5.573   1.599  1.00  2.24           C  
ATOM    173  CG  LYS A  51      15.219  -4.096   1.221  1.00  3.92           C  
ATOM    174  CD  LYS A  51      13.804  -3.770   0.739  1.00  6.02           C  
ATOM    175  CE  LYS A  51      13.695  -3.911  -0.780  1.00  7.21           C  
ATOM    176  NZ  LYS A  51      12.384  -4.485  -1.155  1.00  8.43           N  
ATOM    177  H   LYS A  51      15.005  -5.208   4.384  1.00  1.35           H  
ATOM    178  HA  LYS A  51      13.297  -5.868   2.093  1.00  1.58           H  
ATOM    179  N   GLU A  52      13.361  -7.852   3.818  1.00  1.34           N  
ATOM    180  CA  GLU A  52      13.345  -9.202   4.356  1.00  1.55           C  
ATOM    181  C   GLU A  52      12.068  -9.436   5.166  1.00  1.40           C  
ATOM    182  O   GLU A  52      11.961  -8.988   6.306  1.00  2.50           O  
ATOM    183  CB  GLU A  52      14.589  -9.469   5.205  1.00  2.63           C  
ATOM    184  CG  GLU A  52      14.544 -10.870   5.819  1.00  2.81           C  
ATOM    185  CD  GLU A  52      15.916 -11.543   5.751  1.00  3.82           C  
ATOM    186  OE1 GLU A  52      16.393 -11.868   4.654  1.00  4.49           O  
ATOM    187  OE2 GLU A  52      16.491 -11.725   6.891  1.00  4.68           O  
ATOM    188  H   GLU A  52      12.556  -7.301   4.037  1.00  1.95           H  
ATOM    189  HA  GLU A  52      13.358  -9.860   3.487  1.00  1.83           H  
ATOM    190  N   ALA A  53      11.131 -10.137   4.544  1.00  1.11           N  
ATOM    191  CA  ALA A  53       9.866 -10.436   5.192  1.00  1.58           C  
ATOM    192  C   ALA A  53       8.893 -11.012   4.161  1.00  1.55           C  
ATOM    193  O   ALA A  53       8.141 -10.272   3.529  1.00  2.40           O  
ATOM    194  CB  ALA A  53       9.324  -9.171   5.861  1.00  2.39           C  
ATOM    195  H   ALA A  53      11.226 -10.498   3.616  1.00  1.67           H  
ATOM    196  HA  ALA A  53      10.055 -11.186   5.960  1.00  2.02           H  
ATOM    197  N   SER A  54       8.939 -12.329   4.024  1.00  1.28           N  
ATOM    198  CA  SER A  54       8.071 -13.014   3.081  1.00  1.93           C  
ATOM    199  C   SER A  54       6.742 -13.365   3.753  1.00  2.08           C  
ATOM    200  O   SER A  54       6.162 -14.415   3.479  1.00  3.32           O  
ATOM    201  CB  SER A  54       8.739 -14.277   2.534  1.00  2.55           C  
ATOM    202  OG  SER A  54       8.646 -14.358   1.114  1.00  3.09           O  
ATOM    203  H   SER A  54       9.553 -12.925   4.542  1.00  1.38           H  
ATOM    204  HA  SER A  54       7.913 -12.306   2.267  1.00  2.15           H  
ATOM    205  N   ASP A  55       6.298 -12.467   4.619  1.00  1.45           N  
ATOM    206  CA  ASP A  55       5.048 -12.669   5.332  1.00  1.61           C  
ATOM    207  C   ASP A  55       5.136 -12.003   6.707  1.00  1.45           C  
ATOM    208  O   ASP A  55       4.123 -11.825   7.381  1.00  1.75           O  
ATOM    209  CB  ASP A  55       4.769 -14.158   5.545  1.00  1.95           C  
ATOM    210  CG  ASP A  55       3.587 -14.715   4.749  1.00  2.93           C  
ATOM    211  OD1 ASP A  55       3.727 -15.091   3.576  1.00  4.01           O  
ATOM    212  OD2 ASP A  55       2.469 -14.755   5.391  1.00  3.53           O  
ATOM    213  H   ASP A  55       6.775 -11.616   4.836  1.00  1.81           H  
ATOM    214  HA  ASP A  55       4.282 -12.219   4.700  1.00  1.76           H  
ATOM    215  N   LYS A  56       6.358 -11.654   7.082  1.00  1.07           N  
ATOM    216  CA  LYS A  56       6.593 -11.012   8.365  1.00  1.06           C  
ATOM    217  C   LYS A  56       8.038 -10.515   8.425  1.00  0.93           C  
ATOM    218  O   LYS A  56       8.932 -11.123   7.837  1.00  0.97           O  
ATOM    219  CB  LYS A  56       6.218 -11.953   9.511  1.00  1.40           C  
ATOM    220  CG  LYS A  56       6.716 -11.410  10.852  1.00  1.62           C  
ATOM    221  CD  LYS A  56       6.364 -12.364  11.995  1.00  2.08           C  
ATOM    222  CE  LYS A  56       7.563 -12.573  12.922  1.00  3.24           C  
ATOM    223  NZ  LYS A  56       7.161 -12.399  14.336  1.00  4.47           N  
ATOM    224  H   LYS A  56       7.177 -11.803   6.528  1.00  0.88           H  
ATOM    225  HA  LYS A  56       5.928 -10.150   8.425  1.00  1.05           H  
ATOM    226  N   CYS A  57       8.223  -9.415   9.140  1.00  1.10           N  
ATOM    227  CA  CYS A  57       9.545  -8.830   9.284  1.00  1.21           C  
ATOM    228  C   CYS A  57       9.877  -8.756  10.776  1.00  1.61           C  
ATOM    229  O   CYS A  57       8.986  -8.840  11.619  1.00  3.08           O  
ATOM    230  CB  CYS A  57       9.633  -7.459   8.611  1.00  1.07           C  
ATOM    231  SG  CYS A  57       9.685  -6.039   9.765  1.00  2.75           S  
ATOM    232  H   CYS A  57       7.491  -8.927   9.615  1.00  1.33           H  
ATOM    233  HA  CYS A  57      10.239  -9.491   8.766  1.00  1.30           H  
ATOM    234  N   SER A  58      11.163  -8.599  11.056  1.00  0.85           N  
ATOM    235  CA  SER A  58      11.624  -8.513  12.432  1.00  1.02           C  
ATOM    236  C   SER A  58      12.700  -7.433  12.556  1.00  0.88           C  
ATOM    237  O   SER A  58      13.455  -7.413  13.526  1.00  1.05           O  
ATOM    238  CB  SER A  58      12.165  -9.859  12.917  1.00  1.51           C  
ATOM    239  OG  SER A  58      13.006 -10.477  11.947  1.00  1.91           O  
ATOM    240  H   SER A  58      11.882  -8.532  10.365  1.00  1.53           H  
ATOM    241  HA  SER A  58      10.743  -8.244  13.015  1.00  1.09           H  
ATOM    242  N   CYS A  59      12.736  -6.561  11.559  1.00  0.83           N  
ATOM    243  CA  CYS A  59      13.708  -5.480  11.545  1.00  0.84           C  
ATOM    244  C   CYS A  59      12.974  -4.171  11.841  1.00  0.79           C  
ATOM    245  O   CYS A  59      13.605  -3.144  12.087  1.00  0.94           O  
ATOM    246  CB  CYS A  59      14.468  -5.421  10.218  1.00  0.94           C  
ATOM    247  SG  CYS A  59      13.651  -6.283   8.826  1.00  2.62           S  
ATOM    248  H   CYS A  59      12.118  -6.584  10.773  1.00  0.98           H  
ATOM    249  HA  CYS A  59      14.434  -5.702  12.326  1.00  0.97           H  
ATOM    250  N   CYS A  60      11.652  -4.250  11.807  1.00  0.77           N  
ATOM    251  CA  CYS A  60      10.826  -3.083  12.068  1.00  0.90           C  
ATOM    252  C   CYS A  60       9.705  -3.493  13.026  1.00  1.35           C  
ATOM    253  O   CYS A  60       9.875  -3.445  14.243  1.00  2.30           O  
ATOM    254  CB  CYS A  60      10.278  -2.476  10.775  1.00  0.85           C  
ATOM    255  SG  CYS A  60      11.506  -2.297   9.431  1.00  1.19           S  
ATOM    256  H   CYS A  60      11.147  -5.089  11.605  1.00  0.80           H  
ATOM    257  HA  CYS A  60      11.474  -2.337  12.528  1.00  1.11           H  
ATOM    258  N   ALA A  61       8.584  -3.888  12.439  1.00  2.05           N  
ATOM    259  CA  ALA A  61       7.436  -4.306  13.225  1.00  2.73           C  
ATOM    260  C   ALA A  61       7.257  -5.820  13.094  1.00  3.49           C  
ATOM    261  O   ALA A  61       6.814  -6.247  12.005  1.00  4.68           O  
ATOM    262  CB  ALA A  61       6.197  -3.531  12.772  1.00  4.21           C  
ATOM    263  OXT ALA A  61       7.568  -6.517  14.084  1.00  3.86           O  
ATOM    264  H   ALA A  61       8.454  -3.924  11.449  1.00  2.81           H  
ATOM    265  HA  ALA A  61       7.640  -4.062  14.268  1.00  2.77           H  
TER     266      ALA A  61                                                      
HETATM  267 CD    CD A 101      11.607  -4.799   8.748  1.00  1.04          CD  
HETATM  268 CD    CD A 105      10.102  -0.411   3.433  1.00  1.21          CD  
HETATM  269 CD    CD A 106      10.187  -0.883   7.855  1.00  1.38          CD  
HETATM  270 CD    CD A 107       8.863  -3.937   5.471  1.00  0.81          CD  
CONECT   25  268                                                                
CONECT   33  268  270                                                           
CONECT   49  270                                                                
CONECT   52  270                                                                
CONECT   57  269  270                                                           
CONECT   88  269                                                                
CONECT  114  268  269                                                           
CONECT  146  268                                                                
CONECT  165  267  270                                                           
CONECT  231  267                                                                
CONECT  247  267                                                                
CONECT  250  267                                                                
CONECT  255  267  269                                                           
CONECT  267  165  231  247  250                                                 
CONECT  267  255                                                                
CONECT  268   25   33  114  146                                                 
CONECT  269   57   88  114  255                                                 
CONECT  270   33   49   52   57                                                 
CONECT  270  165                                                                
MASTER      198    0    4    0    0    0    9    6  208    1   19    3          
END