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Database: PDB
Entry: 2LXP
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Original site: 2LXP 
HEADER    LIGASE                                  30-AUG-12   2LXP              
TITLE     NMR STRUCTURE OF TWO DOMAINS IN UBIQUITIN LIGASE GP78, RING AND G2BR, 
TITLE    2 BOUND TO ITS CONJUGATING ENZYME UBE2G                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 G2;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2-165;                                        
COMPND   5 SYNONYM: UBIQUITIN CARRIER PROTEIN G2, UBIQUITIN-PROTEIN LIGASE G2;  
COMPND   6 EC: 6.3.2.19;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE AMFR;                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 574-600;                                      
COMPND  12 SYNONYM: AUTOCRINE MOTILITY FACTOR RECEPTOR, ISOFORM 2, AMF RECEPTOR,
COMPND  13 ISOFORM 2, RING FINGER PROTEIN 45, GP78;                             
COMPND  14 EC: 6.3.2.-;                                                         
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE AMFR;                          
COMPND  18 CHAIN: C;                                                            
COMPND  19 FRAGMENT: UNP RESIDUES 327-384;                                      
COMPND  20 SYNONYM: AUTOCRINE MOTILITY FACTOR RECEPTOR, ISOFORM 2, AMF RECEPTOR,
COMPND  21 ISOFORM 2, RING FINGER PROTEIN 45, GP78;                             
COMPND  22 EC: 6.3.2.-;                                                         
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: UBE2G2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET3A;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: AMFR, RNF45;                                                   
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR: PET3A;                                     
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: AMFR, RNF45;                                                   
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 EXPRESSION_SYSTEM_VECTOR: PET3A                                      
KEYWDS    RING DOMAIN, UBIQUITIN, LIGASE                                        
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    R.DAS,Y.LINAG,J.MARIANO,J.LI,T.HUANG,A.KING,A.WEISSMAN,X.JI,R.BYRD    
REVDAT   2   02-OCT-13 2LXP    1       JRNL                                     
REVDAT   1   28-AUG-13 2LXP    0                                                
JRNL        AUTH   R.DAS,Y.H.LIANG,J.MARIANO,J.LI,T.HUANG,A.KING,S.G.TARASOV,   
JRNL        AUTH 2 A.M.WEISSMAN,X.JI,R.A.BYRD                                   
JRNL        TITL   ALLOSTERIC REGULATION OF E2:E3 INTERACTIONS PROMOTE A        
JRNL        TITL 2 PROCESSIVE UBIQUITINATION MACHINE.                           
JRNL        REF    EMBO J.                       V.  32  2504 2013              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   23942235                                                     
JRNL        DOI    10.1038/EMBOJ.2013.174                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR_NIH                                           
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2LXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB102962.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.2                                
REMARK 210  IONIC STRENGTH                 : 0                                  
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.7-1 MM [U-100% 13C; U-100%       
REMARK 210                                   15N] GP78RING, 50 MM TRIS, 2 MM    
REMARK 210                                   TCEP, 0.2 MM SODIUM AZIDE, 90%     
REMARK 210                                   H2O/10% D2O                        
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 2D 1H-13C HSQC;    
REMARK 210                                   3D CBCA(CO)NH; 3D HNCACB; 3D       
REMARK 210                                   C(CO)NH; 3D H(CCO)NH; 3D 1H-15N    
REMARK 210                                   NOESY; 3D 1H-15N TOCSY; 3D HNCO;   
REMARK 210                                   3D 1H-13C NOESY; 3D 1H-13C NOESY   
REMARK 210                                   AROMATIC                           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ; 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : X-PLOR_NIH, SPARKY, NMRDRAW, CNS   
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LOWEST HADDOCK SCORES              
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     ASP A    98                                                      
REMARK 465     ASP A    99                                                      
REMARK 465     PRO A   100                                                      
REMARK 465     MET A   101                                                      
REMARK 465     GLY A   102                                                      
REMARK 465     TYR A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     SER A   105                                                      
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   OE1  GLU A    38     HZ3  LYS B   586              1.58            
REMARK 500   HZ3  LYS A     7     OD2  ASP C   346              1.59            
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  1 ASN A  33       87.51   -157.07                                   
REMARK 500  1 ASP A  46       17.44     80.64                                   
REMARK 500  1 PRO A  65       31.30    -95.99                                   
REMARK 500  1 PHE A  78       52.68   -140.09                                   
REMARK 500  1 PRO A  96       33.72    -85.38                                   
REMARK 500  1 PRO A 130       88.50    -64.80                                   
REMARK 500  1 ASP C 339       37.87    -78.81                                   
REMARK 500  1 ILE C 343      -69.40    -99.94                                   
REMARK 500  1 TRP C 345     -161.91     62.16                                   
REMARK 500  1 ASP C 346     -168.01     60.57                                   
REMARK 500  1 CYS C 378      -38.76   -135.51                                   
REMARK 500  2 PRO A  65       36.91    -98.73                                   
REMARK 500  2 THR A  74       49.85    -97.38                                   
REMARK 500  2 CYS A  75     -165.29   -162.73                                   
REMARK 500  2 ALA A 107      -65.09   -108.25                                   
REMARK 500  2 ASP A 132      102.25    -57.12                                   
REMARK 500  2 GLU A 133      -71.48   -114.83                                   
REMARK 500  2 ASP A 146      -79.20   -100.18                                   
REMARK 500  2 ALA C 342       35.68    -75.83                                   
REMARK 500  2 ILE C 343      -62.70   -138.13                                   
REMARK 500  2 TRP C 345     -159.58     60.65                                   
REMARK 500  2 ASP C 346     -146.70     58.50                                   
REMARK 500  2 PRO C 376      -70.67    -42.64                                   
REMARK 500  2 THR C 377       40.33    -79.16                                   
REMARK 500  2 CYS C 378      -39.04   -148.10                                   
REMARK 500  3 ASP A  46       36.41     70.31                                   
REMARK 500  3 PRO A  65       34.54    -96.76                                   
REMARK 500  3 THR A  74       55.43   -110.97                                   
REMARK 500  3 PHE A  78       56.85   -145.78                                   
REMARK 500  3 PRO A  96      101.26    -57.97                                   
REMARK 500  3 ASP A 146      -81.64   -112.22                                   
REMARK 500  3 ALA C 342       38.09    -76.31                                   
REMARK 500  3 ILE C 343      -54.18   -140.32                                   
REMARK 500  3 TRP C 345     -147.03     61.04                                   
REMARK 500  3 ASP C 346     -153.86     59.81                                   
REMARK 500  3 PRO C 376      -75.74    -42.46                                   
REMARK 500  4 ASN A  33       86.92   -150.57                                   
REMARK 500  4 PRO A  65       33.09    -95.95                                   
REMARK 500  4 PHE A  78       55.55   -111.11                                   
REMARK 500  4 ARG A 109     -161.02   -111.19                                   
REMARK 500  4 ASP A 132       83.45    -67.05                                   
REMARK 500  4 ASP A 146      -76.27   -138.32                                   
REMARK 500  4 ASN C 338       78.57   -109.95                                   
REMARK 500  4 ASP C 339       42.71    -83.40                                   
REMARK 500  4 ALA C 342       23.23    -76.01                                   
REMARK 500  4 ILE C 343      -54.96   -133.40                                   
REMARK 500  4 TRP C 345     -168.98     65.46                                   
REMARK 500  4 ASP C 346     -147.61     57.64                                   
REMARK 500  4 GLN C 349       32.56    -85.35                                   
REMARK 500  4 PRO C 376      -70.37    -44.32                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     267 RAMACHANDRAN OUTLIERS.                        
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                           1  ZN C 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 358   ND1                                                    
REMARK 620 2 CYS C 378   SG  114.9                                              
REMARK 620 3 CYS C 375   SG  114.3 101.7                                        
REMARK 620 4 CYS C 356   SG  121.6 107.9  92.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN C 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 361   ND1                                                    
REMARK 620 2 CYS C 344   SG  138.8                                              
REMARK 620 3 CYS C 364   SG  123.1  90.6                                        
REMARK 620 4 CYS C 341   SG   93.0 101.5 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 901                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 18688   RELATED DB: BMRB                                 
DBREF  2LXP A    2   165  UNP    P60604   UB2G2_HUMAN      2    165             
DBREF  2LXP B  574   600  UNP    Q9UKV5   AMFR2_HUMAN    574    600             
DBREF  2LXP C  327   384  UNP    Q9UKV5   AMFR2_HUMAN    327    384             
SEQRES   1 A  164  ALA GLY THR ALA LEU LYS ARG LEU MET ALA GLU TYR LYS          
SEQRES   2 A  164  GLN LEU THR LEU ASN PRO PRO GLU GLY ILE VAL ALA GLY          
SEQRES   3 A  164  PRO MET ASN GLU GLU ASN PHE PHE GLU TRP GLU ALA LEU          
SEQRES   4 A  164  ILE MET GLY PRO GLU ASP THR CYS PHE GLU PHE GLY VAL          
SEQRES   5 A  164  PHE PRO ALA ILE LEU SER PHE PRO LEU ASP TYR PRO LEU          
SEQRES   6 A  164  SER PRO PRO LYS MET ARG PHE THR CYS GLU MET PHE HIS          
SEQRES   7 A  164  PRO ASN ILE TYR PRO ASP GLY ARG VAL CYS ILE SER ILE          
SEQRES   8 A  164  LEU HIS ALA PRO GLY ASP ASP PRO MET GLY TYR GLU SER          
SEQRES   9 A  164  SER ALA GLU ARG TRP SER PRO VAL GLN SER VAL GLU LYS          
SEQRES  10 A  164  ILE LEU LEU SER VAL VAL SER MET LEU ALA GLU PRO ASN          
SEQRES  11 A  164  ASP GLU SER GLY ALA ASN VAL ASP ALA SER LYS MET TRP          
SEQRES  12 A  164  ARG ASP ASP ARG GLU GLN PHE TYR LYS ILE ALA LYS GLN          
SEQRES  13 A  164  ILE VAL GLN LYS SER LEU GLY LEU                              
SEQRES   1 B   27  SER ALA ASP GLU ARG GLN ARG MET LEU VAL GLN ARG LYS          
SEQRES   2 B   27  ASP GLU LEU LEU GLN GLN ALA ARG LYS ARG PHE LEU ASN          
SEQRES   3 B   27  LYS                                                          
SEQRES   1 C   58  ALA VAL ALA THR PRO GLU GLU LEU ALA VAL ASN ASN ASP          
SEQRES   2 C   58  ASP CYS ALA ILE CYS TRP ASP SER MET GLN ALA ALA ARG          
SEQRES   3 C   58  LYS LEU PRO CYS GLY HIS LEU PHE HIS ASN SER CYS LEU          
SEQRES   4 C   58  ARG SER TRP LEU GLU GLN ASP THR SER CYS PRO THR CYS          
SEQRES   5 C   58  ARG MET SER LEU ASN ILE                                      
HET     ZN  C 900       1                                                       
HET     ZN  C 901       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    2(ZN 2+)                                                     
HELIX    1   1 GLY A    3  THR A   17  1                                  15    
HELIX    2   2 ILE A   90  HIS A   94  5                                   5    
HELIX    3   3 SER A  115  GLU A  129  1                                  15    
HELIX    4   4 ASN A  137  ASP A  147  1                                  11    
HELIX    5   5 ASP A  147  GLY A  164  1                                  18    
HELIX    6   6 ASP B  576  LYS B  600  1                                  25    
HELIX    7   7 PRO C  331  ASN C  338  1                                   8    
HELIX    8   8 ASN C  362  ASP C  372  1                                  11    
SHEET    1   A 4 ILE A  24  ASN A  30  0                                        
SHEET    2   A 4 ASN A  33  MET A  42 -1  O  GLU A  38   N  GLY A  27           
SHEET    3   A 4 VAL A  53  SER A  59 -1  O  ALA A  56   N  ALA A  39           
SHEET    4   A 4 LYS A  70  PHE A  73 -1  O  ARG A  72   N  ILE A  57           
SHEET    1   B 2 ALA C 351  LEU C 354  0                                        
SHEET    2   B 2 HIS C 358  HIS C 361 -1  O  HIS C 358   N  LEU C 354           
LINK         ND1 HIS C 358                ZN    ZN C 901     1555   1555  1.80  
LINK         ND1 HIS C 361                ZN    ZN C 900     1555   1555  1.84  
LINK         SG  CYS C 378                ZN    ZN C 901     1555   1555  2.14  
LINK         SG  CYS C 344                ZN    ZN C 900     1555   1555  2.15  
LINK         SG  CYS C 375                ZN    ZN C 901     1555   1555  2.23  
LINK         SG  CYS C 364                ZN    ZN C 900     1555   1555  2.24  
LINK         SG  CYS C 356                ZN    ZN C 901     1555   1555  2.26  
LINK         SG  CYS C 341                ZN    ZN C 900     1555   1555  2.48  
CISPEP   1 TYR A   64    PRO A   65          1         0.82                     
CISPEP   2 TYR A   64    PRO A   65          2         0.55                     
CISPEP   3 TYR A   64    PRO A   65          3         0.56                     
CISPEP   4 TYR A   64    PRO A   65          4         0.40                     
CISPEP   5 TYR A   64    PRO A   65          5         0.94                     
CISPEP   6 TYR A   64    PRO A   65          6         0.42                     
CISPEP   7 TYR A   64    PRO A   65          7         0.22                     
CISPEP   8 TYR A   64    PRO A   65          8         0.42                     
CISPEP   9 TYR A   64    PRO A   65          9         0.06                     
CISPEP  10 TYR A   64    PRO A   65         10         0.08                     
CISPEP  11 TYR A   64    PRO A   65         11         0.57                     
CISPEP  12 TYR A   64    PRO A   65         12         0.57                     
CISPEP  13 TYR A   64    PRO A   65         13        -0.30                     
CISPEP  14 TYR A   64    PRO A   65         14         0.75                     
CISPEP  15 TYR A   64    PRO A   65         15         0.71                     
CISPEP  16 TYR A   64    PRO A   65         16         0.93                     
CISPEP  17 TYR A   64    PRO A   65         17         0.36                     
CISPEP  18 TYR A   64    PRO A   65         18         0.04                     
CISPEP  19 TYR A   64    PRO A   65         19         0.27                     
CISPEP  20 TYR A   64    PRO A   65         20         0.80                     
SITE     1 AC1  4 CYS C 341  CYS C 344  HIS C 361  CYS C 364                    
SITE     1 AC2  4 CYS C 356  HIS C 358  CYS C 375  CYS C 378                    
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                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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