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Database: PDB
Entry: 1ESO
LinkDB: 1ESO
Original site: 1ESO 
HEADER    OXIDOREDUCTASE                          27-JUN-97   1ESO              
TITLE     MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CU, ZN SUPEROXIDE DISMUTASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SOD;                                                        
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: BMH 71-18;                                                   
SOURCE   5 CELLULAR_LOCATION: PERIPLASM;                                        
SOURCE   6 GENE: SODC;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, CU,ZN SUPEROXIDE DISMUTASE, MONOMERIC                 
KEYWDS   2 SUPEROXIDE DISMUTASE, COPPER ENZYMES, ENZYME EVOLUTION, X-           
KEYWDS   3 RAY CRYSTAL STRUCTURE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PESCE,C.CAPASSO,A.BATTISTONI,S.FOLCARELLI,G.ROTILIO,                
AUTHOR   2 A.DESIDERI,M.BOLOGNESI                                               
REVDAT   2   24-FEB-09 1ESO    1       VERSN                                    
REVDAT   1   01-JUL-98 1ESO    0                                                
JRNL        AUTH   A.PESCE,C.CAPASSO,A.BATTISTONI,S.FOLCARELLI,                 
JRNL        AUTH 2 G.ROTILIO,A.DESIDERI,M.BOLOGNESI                             
JRNL        TITL   UNIQUE STRUCTURAL FEATURES OF THE MONOMERIC CU,ZN            
JRNL        TITL 2 SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI,                  
JRNL        TITL 3 REVEALED BY X-RAY CRYSTALLOGRAPHY.                           
JRNL        REF    J.MOL.BIOL.                   V. 274   408 1997              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9405149                                                      
JRNL        DOI    10.1006/JMBI.1997.1400                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-B                                           
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 9057                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 433                             
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1680                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.263                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 433                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 8624                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1103                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.018 ; 6.000 ; 1125            
REMARK   3   BOND ANGLES            (DEGREES) : 2.780 ; 10.500; 1510            
REMARK   3   TORSION ANGLES         (DEGREES) : 19.360; 0.000 ; 695             
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.018 ; 8.500 ; 32              
REMARK   3   GENERAL PLANES               (A) : 0.019 ; 28.000; 165             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 4.700 ; 7.000 ; 1125            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.062 ; 0.062 ; 13              
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : TNT                                                  
REMARK   3   KSOL        : 0.76                                                 
REMARK   3   BSOL        : 103.30                                               
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT: ENGH-HUBER                                  
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ESO 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        : 07-APR-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 8.5                                
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                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : PINHOLE COLLIMATOR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9044                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED       
REMARK 200  BY SIRAS IN THE DEPOSITORS' LAB                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 30%        
REMARK 280  PEG 4000, 0.2 M MGCL2, 0.1 M TRIS, PH 8.5                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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       26.20000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     LYS A   54A                                                      
REMARK 475     ASP A   54B                                                      
REMARK 475     GLY A   54C                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A    4   CG    CD    OE1   OE2                               
REMARK 480     LYS A    5   CG    CD    CE    NZ                                
REMARK 480     GLU A    7   CG    CD    OE1   OE2                               
REMARK 480     GLN A   10D  CG    CD    OE1   NE2                               
REMARK 480     GLU A   40   CG    CD    OE1   OE2                               
REMARK 480     LYS A   48   CE    NZ                                            
REMARK 480     THR A   54   CA    C     O     CB    OG1   CG2                   
REMARK 480     LYS A   54D  CB    CG    CD    CE    NZ                          
REMARK 480     GLN A   65   CD    OE1   NE2                                     
REMARK 480     ASN A   66   OD1                                                 
REMARK 480     ASN A   89   OD1                                                 
REMARK 480     ASP A  108   OD2                                                 
REMARK 480     LYS A  113   NZ                                                  
REMARK 480     LYS A  133   CD    CE    NZ                                      
REMARK 480     GLU A  140   CG    CD    OE1   OE2                               
REMARK 480     LYS A  148   CG    CD    CE    NZ                                
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A 124   CG  -  SD  -  CE  ANGL. DEV. =  10.0 DEGREES          
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    ASP A  54B      61.43    124.07                                   
REMARK 500    LYS A  54D    -170.12    161.97                                   
REMARK 500    ASP A  63       67.95   -158.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 149  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  61   ND1                                                    
REMARK 620 2 HIS A  69   ND1 108.8                                              
REMARK 620 3 HIS A  78   ND1 107.4 113.3                                        
REMARK 620 4 ASP A  81   OD1 115.3 106.9 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 150  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  44   ND1                                                    
REMARK 620 2 HIS A  46   NE2 148.8                                              
REMARK 620 3 HIS A  61   NE2  72.7  96.8                                        
REMARK 620 4 HIS A 118   NE2  97.6 111.7 126.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CUL                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CU LIGANDS.                                        
REMARK 800 SITE_IDENTIFIER: ZNL                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ZN LIGANDS.                                        
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 149                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 150                  
DBREF  1ESO A    2   148  UNP    P53635   SODC_ECOLI      20    173             
SEQRES   1 A  154  ALA SER GLU LYS VAL GLU MET ASN LEU VAL THR SER GLN          
SEQRES   2 A  154  GLY VAL GLY GLN SER ILE GLY SER VAL THR ILE THR GLU          
SEQRES   3 A  154  THR ASP LYS GLY LEU GLU PHE SER PRO ASP LEU LYS ALA          
SEQRES   4 A  154  LEU PRO PRO GLY GLU HIS GLY PHE HIS ILE HIS ALA LYS          
SEQRES   5 A  154  GLY SER CYS GLN PRO ALA THR LYS ASP GLY LYS ALA SER          
SEQRES   6 A  154  ALA ALA GLU SER ALA GLY GLY HIS LEU ASP PRO GLN ASN          
SEQRES   7 A  154  THR GLY LYS HIS GLU GLY PRO GLU GLY ALA GLY HIS LEU          
SEQRES   8 A  154  GLY ASP LEU PRO ALA LEU VAL VAL ASN ASN ASP GLY LYS          
SEQRES   9 A  154  ALA THR ASP ALA VAL ILE ALA PRO ARG LEU LYS SER LEU          
SEQRES  10 A  154  ASP GLU ILE LYS ASP LYS ALA LEU MET VAL HIS VAL GLY          
SEQRES  11 A  154  GLY ASP ASN MET SER ASP GLN PRO LYS PRO LEU GLY GLY          
SEQRES  12 A  154  GLY GLY GLU ARG TYR ALA CYS GLY VAL ILE LYS                  
HET     ZN  A 149       1                                                       
HET     CU  A 150       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CU COPPER (II) ION                                                  
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CU    CU 2+                                                        
FORMUL   4  HOH   *75(H2 O)                                                     
HELIX    1   1 ALA A   55  GLY A   59  5                                   5    
HELIX    2   2 SER A  104  LYS A  111  5                                   6    
HELIX    3   3 PRO A  134  GLY A  137  5                                   4    
SHEET    1   A 4 VAL A  97  ALA A  99  0                                        
SHEET    2   A 4 GLY A  26  LEU A  33 -1  N  PHE A  29   O  VAL A  97           
SHEET    3   A 4 GLY A  10E THR A  23 -1  N  THR A  23   O  GLY A  26           
SHEET    4   A 4 SER A   3  THR A  10B-1  N  MET A   8   O  ILE A  15           
SHEET    1   B 2 GLY A  39  HIS A  46  0                                        
SHEET    2   B 2 LEU A  85  VAL A  87 -1  N  VAL A  87   O  GLY A  39           
SHEET    1   C 2 LYS A 113  HIS A 118  0                                        
SHEET    2   C 2 ARG A 141  ILE A 147 -1  N  ILE A 147   O  LYS A 113           
SSBOND   1 CYS A   50A   CYS A  144                          1555   1555  1.99  
LINK        ZN    ZN A 149                 ND1 HIS A  61     1555   1555  2.14  
LINK        ZN    ZN A 149                 ND1 HIS A  69     1555   1555  1.98  
LINK        ZN    ZN A 149                 ND1 HIS A  78     1555   1555  1.93  
LINK        ZN    ZN A 149                 OD1 ASP A  81     1555   1555  2.07  
LINK        CU    CU A 150                 ND1 HIS A  44     1555   1555  2.19  
LINK        CU    CU A 150                 NE2 HIS A  46     1555   1555  2.09  
LINK        CU    CU A 150                 NE2 HIS A  61     1555   1555  2.65  
LINK        CU    CU A 150                 NE2 HIS A 118     1555   1555  2.11  
CISPEP   1 GLN A  131    PRO A  132          0         2.33                     
SITE     1 CUL  4 HIS A  44  HIS A  46  HIS A  61  HIS A 118                    
SITE     1 ZNL  4 HIS A  61  HIS A  69  HIS A  78  ASP A  81                    
SITE     1 AC1  4 HIS A  61  HIS A  69  HIS A  78  ASP A  81                    
SITE     1 AC2  4 HIS A  44  HIS A  46  HIS A  61  HIS A 118                    
CRYST1   33.000   52.400   43.200  90.00 111.20  90.00 P 1 21 1      2          
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      0.030303  0.000000  0.011754        0.00000                         
SCALE2      0.000000  0.019084  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024828        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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