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Database: PDB
Entry: 1XER
LinkDB: 1XER
Original site: 1XER 
HEADER    ELECTRON TRANSPORT                      28-AUG-96   1XER              
TITLE     STRUCTURE OF FERREDOXIN                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN;                                                
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII STR. 7;                     
SOURCE   3 ORGANISM_TAXID: 273063;                                              
SOURCE   4 STRAIN: STRAIN 7                                                     
KEYWDS    ELECTRON TRANSPORT, IRON-SULFUR, DUPLICATION                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.FUJII,Y.HATA,H.MORIYAMA,T.WAKAGI,N.TANAKA,T.OSHIMA                  
REVDAT   2   24-FEB-09 1XER    1       VERSN                                    
REVDAT   1   04-SEP-97 1XER    0                                                
JRNL        AUTH   T.FUJII,Y.HATA,T.WAKAGI,N.TANAKA,T.OSHIMA                    
JRNL        TITL   NOVEL ZINC-BINDING CENTRE IN THERMOACIDOPHILIC               
JRNL        TITL 2 ARCHAEAL FERREDOXINS.                                        
JRNL        REF    NAT.STRUCT.BIOL.              V.   3   834 1996              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   8836097                                                      
JRNL        DOI    10.1038/NSB1096-834                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.FUJII,H.MORIYAMA,A.TAKENAKA,N.TANAKA,T.WAKAGI,             
REMARK   1  AUTH 2 T.OSHIMA                                                     
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES ON             
REMARK   1  TITL 2 SULFOLOBUS ACIDOCALDARIUS FERREDOXIN                         
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V. 110   472 1991              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 5008                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 555                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE                    : 0.2290                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 71                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 772                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.74                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.89                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.41                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XER COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS IIC                         
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8689                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.76000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       25.06000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       25.06000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.14000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       25.06000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       25.06000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       17.38000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       25.06000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       25.06000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       52.14000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       25.06000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       25.06000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       17.38000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       34.76000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: DIMERIC                           
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       69.52000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MLZ A  29    CM                                                  
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 106  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  16   ND1                                                    
REMARK 620 2 HIS A  19   NE2 110.7                                              
REMARK 620 3 HIS A  34   ND1 105.1 109.1                                        
REMARK 620 4 ASP A  76   OD1 112.0 114.1 105.3                                  
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 A 106                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 104                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 105                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 BECAUSE OF THE ELECTRON DENSITY OF THE SIDE CHAIN OF LYS             
REMARK 999 29 IS NOT CLEAR, THE EXACT POSITION OF THE SIDE CHAIN OF             
REMARK 999 LYS 29 IS UNDEFINED.  ALTHOUGH IT IS KNOWN FROM CHEMICAL             
REMARK 999 ANALYSIS THAT THE N-ZETA ATOM OF LYS 29 IS MONOMETHYLATED,           
REMARK 999 THE COORDINATES CONTAIN ONLY NORMAL SIDE CHAIN                       
REMARK 999 COORDINATES FOR LYS 29.                                              
DBREF  1XER A    1   103  UNP    P55907   FER1_SULTO       2    104             
SEQADV 1XER MLZ A   29  UNP  P55907    LYS    30 MODIFIED RESIDUE               
SEQRES   1 A  103  GLY ILE ASP PRO ASN TYR ARG THR ASN ARG GLN VAL VAL          
SEQRES   2 A  103  GLY GLU HIS SER GLY HIS LYS VAL TYR GLY PRO VAL GLU          
SEQRES   3 A  103  PRO PRO MLZ VAL LEU GLY ILE HIS GLY THR ILE VAL GLY          
SEQRES   4 A  103  VAL ASP PHE ASP LEU CYS ILE ALA ASP GLY SER CYS ILE          
SEQRES   5 A  103  ASN ALA CYS PRO VAL ASN VAL PHE GLN TRP TYR ASP THR          
SEQRES   6 A  103  PRO GLY HIS PRO ALA SER GLU LYS LYS ALA ASP PRO VAL          
SEQRES   7 A  103  ASN GLU GLN ALA CYS ILE PHE CYS MET ALA CYS VAL ASN          
SEQRES   8 A  103  VAL CYS PRO VAL ALA ALA ILE ASP VAL LYS PRO PRO              
MODRES 1XER MLZ A   29  LYS  N-METHYL-LYSINE                                    
HET    MLZ  A  29       9                                                       
HET     ZN  A 106       1                                                       
HET    F3S  A 104       7                                                       
HET    F3S  A 105       7                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     F3S FE3-S4 CLUSTER                                                   
FORMUL   1  MLZ    C7 H16 N2 O2                                                 
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  F3S    2(FE3 S4)                                                    
FORMUL   5  HOH   *31(H2 O)                                                     
HELIX    1   1 TYR A    6  ASN A    9  1                                   4    
HELIX    2   2 SER A   50  ALA A   54  1                                   5    
HELIX    3   3 GLU A   80  ALA A   82  5                                   3    
HELIX    4   4 ALA A   88  VAL A   92  1                                   5    
SHEET    1   A 2 VAL A  38  VAL A  40  0                                        
SHEET    2   A 2 ILE A  98  VAL A 100 -1  N  ASP A  99   O  GLY A  39           
SHEET    1   B 2 GLN A  61  ASP A  64  0                                        
SHEET    2   B 2 LYS A  73  ASP A  76 -1  N  ASP A  76   O  GLN A  61           
SHEET    1   C 2 VAL A  12  HIS A  16  0                                        
SHEET    2   C 2 HIS A  19  TYR A  22 -1  N  VAL A  21   O  VAL A  13           
LINK         N   MLZ A  29                 C   PRO A  28     1555   1555  1.32  
LINK         C   MLZ A  29                 N   VAL A  30     1555   1555  1.33  
LINK        FE1  F3S A 104                 SG  CYS A  45     1555   1555  2.28  
LINK        FE3  F3S A 104                 SG  CYS A  93     1555   1555  2.30  
LINK        FE1  F3S A 105                 SG  CYS A  83     1555   1555  2.31  
LINK        FE3  F3S A 105                 SG  CYS A  55     1555   1555  2.31  
LINK        ZN    ZN A 106                 ND1 HIS A  16     1555   1555  2.07  
LINK        ZN    ZN A 106                 NE2 HIS A  19     1555   1555  1.95  
LINK        ZN    ZN A 106                 ND1 HIS A  34     1555   1555  1.96  
LINK        ZN    ZN A 106                 OD1 ASP A  76     1555   1555  1.85  
LINK         SG  CYS A  51                FE4  F3S A 104     1555   1555  2.30  
LINK         SG  CYS A  89                FE4  F3S A 105     1555   1555  2.31  
CISPEP   1 GLY A   23    PRO A   24          0         0.05                     
CISPEP   2 PRO A   27    PRO A   28          0         0.23                     
SITE     1 AC1  4 HIS A  16  HIS A  19  HIS A  34  ASP A  76                    
SITE     1 AC2 10 CYS A  45  ILE A  46  ALA A  47  ASP A  48                    
SITE     2 AC2 10 GLY A  49  SER A  50  CYS A  51  TRP A  62                    
SITE     3 AC2 10 CYS A  93  ILE A  98                                          
SITE     1 AC3  9 CYS A  55  VAL A  57  VAL A  59  PHE A  60                    
SITE     2 AC3  9 CYS A  83  ILE A  84  CYS A  86  MET A  87                    
SITE     3 AC3  9 CYS A  89                                                     
CRYST1   50.120   50.120   69.520  90.00  90.00  90.00 P 43 21 2     8          
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      0.019952  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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