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Entry: 1IDS
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HEADER    SUPEROXIDE DISMUTASE                    29-SEP-94   1IDS              
TITLE     X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE             
TITLE    2 DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS           
TITLE    3 RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON SUPEROXIDE DISMUTASE;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773                                                 
KEYWDS    SUPEROXIDE DISMUTASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.COOPER,K.MCINTYRE,S.P.WOOD,Y.ZHANG,D.YOUNG                        
REVDAT   2   24-FEB-09 1IDS    1       VERSN                                    
REVDAT   1   20-DEC-94 1IDS    0                                                
JRNL        AUTH   J.B.COOPER,K.MCINTYRE,M.O.BADASSO,S.P.WOOD,Y.ZHANG,          
JRNL        AUTH 2 T.R.GARBE,D.YOUNG                                            
JRNL        TITL   X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT               
JRNL        TITL 2 SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM                      
JRNL        TITL 3 TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTION REVEALS             
JRNL        TITL 4 NOVEL DIMER-DIMER INTERACTIONS.                              
JRNL        REF    J.MOL.BIOL.                   V. 246   531 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7877174                                                      
JRNL        DOI    10.1006/JMBI.1994.0105                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.B.COOPER,H.P.C.DRIESSEN,S.P.WOOD,Y.ZHANG,D.YOUNG           
REMARK   1  TITL   CRYSTALLISATION AND PRELIMINARY X-RAY ANALYSIS OF            
REMARK   1  TITL 2 THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM                 
REMARK   1  TITL 3 MYCOBACTERIUM TUBERCULOSIS                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 235  1156 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : RESTRAIN                                             
REMARK   3   AUTHORS     : MOSS,DRIESSEN,HANEEF,HOWLIN,HARRIS                   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 40396                          
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 + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6272                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 656                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.61                          
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.005 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.019 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.008 ; 0.017               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : 0.030 ; 0.050               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IDS 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40396                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       42.70000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLN A   200                                                      
REMARK 465     THR A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ILE A   205                                                      
REMARK 465     PHE A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     LEU B   204                                                      
REMARK 465     ILE B   205                                                      
REMARK 465     PHE B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C   200                                                      
REMARK 465     THR C   201                                                      
REMARK 465     LYS C   202                                                      
REMARK 465     GLY C   203                                                      
REMARK 465     LEU C   204                                                      
REMARK 465     ILE C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D   200                                                      
REMARK 465     THR D   201                                                      
REMARK 465     LYS D   202                                                      
REMARK 465     GLY D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     ILE D   205                                                      
REMARK 465     PHE D   206                                                      
REMARK 465     GLY D   207                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
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    HOH D  1314     O    HOH D  1642              2.03            
REMARK 500   O    HOH C  1332     O    HOH D  1324              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 B 161   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    VAL B 175   CA  -  CB  -  CG2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    TYR C 170   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    VAL D 175   CA  -  CB  -  CG2 ANGL. DEV. =   9.0 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    LYS A  31      -63.11   -108.83                                   
REMARK 500    ASP A  89     -147.66     54.46                                   
REMARK 500    ASP A 144     -116.00     53.53                                   
REMARK 500    ASN A 148       40.95     85.88                                   
REMARK 500    PHE A 166      -10.01   -142.23                                   
REMARK 500    LYS A 171     -135.51     56.12                                   
REMARK 500    LYS B  31      -71.11   -111.99                                   
REMARK 500    ASP B  89     -145.30     75.58                                   
REMARK 500    ASP B 144     -115.56     57.39                                   
REMARK 500    ASN B 148       45.13     84.09                                   
REMARK 500    LYS B 171     -127.04     59.63                                   
REMARK 500    LYS C  31      -62.96   -108.62                                   
REMARK 500    ASP C  89     -105.06     68.62                                   
REMARK 500    ASP C 144     -116.22     57.14                                   
REMARK 500    ASN C 148       42.30     83.96                                   
REMARK 500    PHE C 166       -7.46   -146.02                                   
REMARK 500    LYS C 171     -130.74     60.32                                   
REMARK 500    LYS D  31      -69.42   -105.96                                   
REMARK 500    ASP D  89     -141.52     53.41                                   
REMARK 500    ASP D 144     -119.75     57.68                                   
REMARK 500    ASN D 148       34.27     92.73                                   
REMARK 500    PHE D 166      -13.70   -145.69                                   
REMARK 500    LYS D 171     -125.70     66.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1021        DISTANCE =  9.07 ANGSTROMS                       
REMARK 525    HOH C1213        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A1023        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B1131        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH D1304        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH C1224        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH C1226        DISTANCE =  7.89 ANGSTROMS                       
REMARK 525    HOH A1041        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH D1333        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH A1098        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH D1378        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH D1379        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH C1323        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH D1465        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH C1522        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH B1471        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH D1511        DISTANCE =  8.69 ANGSTROMS                       
REMARK 525    HOH D1547        DISTANCE =  9.25 ANGSTROMS                       
REMARK 525    HOH D1548        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH D1552        DISTANCE =  5.00 ANGSTROMS                       
REMARK 525    HOH D1554        DISTANCE = 12.55 ANGSTROMS                       
REMARK 525    HOH A1413        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH D1560        DISTANCE =  7.86 ANGSTROMS                       
REMARK 525    HOH D1568        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH A1422        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH B1502        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH D1571        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH A1424        DISTANCE =  8.69 ANGSTROMS                       
REMARK 525    HOH C1605        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH C1606        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH B1519        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH C1627        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH B1562        DISTANCE =  8.53 ANGSTROMS                       
REMARK 525    HOH C1628        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH B1563        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH B1564        DISTANCE =  8.99 ANGSTROMS                       
REMARK 525    HOH B1586        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B1587        DISTANCE =  9.10 ANGSTROMS                       
REMARK 525    HOH A1458        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A1516        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B1619        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A1533        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH B1620        DISTANCE =  8.03 ANGSTROMS                       
REMARK 525    HOH B1621        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH A1545        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A1603        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH A1607        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH A1608        DISTANCE =  8.34 ANGSTROMS                       
REMARK 525    HOH A1629        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH A1644        DISTANCE = 10.29 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600  HETATMS 1001-1004 ARE PUTATIVE OH(-) IONS.                          
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                              FE A 208  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  76   NE2                                                    
REMARK 620 2 HIS A  28   NE2  86.9                                              
REMARK 620 3 ASP A 160   OD2 107.2  84.6                                        
REMARK 620 4 HIS A 164   NE2 134.5  88.5 117.4                                  
REMARK 620 5 HOH A1001   O    95.0 175.4  90.9  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 208  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 164   NE2                                                    
REMARK 620 2 HIS B  28   NE2  86.0                                              
REMARK 620 3 HOH B1002   O    97.8 172.8                                        
REMARK 620 4 HIS B  76   NE2 133.7  97.3  84.6                                  
REMARK 620 5 ASP B 160   OD2 111.8  86.0  86.9 114.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 208  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 160   OD2                                                    
REMARK 620 2 HOH C1003   O    79.2                                              
REMARK 620 3 HIS C  28   NE2  97.6 176.3                                        
REMARK 620 4 HIS C 164   NE2 118.9  89.3  94.0                                  
REMARK 620 5 HIS C  76   NE2 112.3  92.7  86.6 128.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 208  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  76   NE2                                                    
REMARK 620 2 ASP D 160   OD2 111.0                                              
REMARK 620 3 HIS D 164   NE2 131.4 117.2                                        
REMARK 620 4 HOH D1004   O    79.4  90.4  94.2                                  
REMARK 620 5 HIS D  28   NE2 103.2  82.8  88.8 173.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 SHEET                                                                
REMARK 700  SHEET_ID: EA, SHEET IN A SUBUNIT. N-CENTERED OVERHAND               
REMARK 700  TOPOLOGY.                                                           
REMARK 700  SHEET_ID: EB, SHEET IN B SUBUNIT. N-CENTERED OVERHAND               
REMARK 700  TOPOLOGY.                                                           
REMARK 700  SHEET_ID: EC, SHEET IN C SUBUNIT. N-CENTERED OVERHAND               
REMARK 700  TOPOLOGY.                                                           
REMARK 700  SHEET_ID: ED, SHEET IN D SUBUNIT. N-CENTERED OVERHAND               
REMARK 700  TOPOLOGY.                                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: A1                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE OF CHAIN A                          
REMARK 800 SITE_IDENTIFIER: A2                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE OF CHAIN B                          
REMARK 800 SITE_IDENTIFIER: A3                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE OF CHAIN C                          
REMARK 800 SITE_IDENTIFIER: A4                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE OF CHAIN D                          
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 208                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 208                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 208                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 208                  
DBREF  1IDS A    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1IDS B    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1IDS C    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1IDS D    1   207  UNP    P17670   SODF_MYCTU       1    207             
SEQRES   1 A  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 A  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 A  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 A  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 A  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 A  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 A  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 A  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 A  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 A  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 A  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 A  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 A  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 A  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 A  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 A  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 B  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 B  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 B  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 B  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 B  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 B  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 B  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 B  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 B  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 B  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 B  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 B  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 B  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 B  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 B  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 B  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 C  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 C  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 C  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 C  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 C  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 C  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 C  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 C  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 C  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 C  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 C  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 C  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 C  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 C  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 C  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 C  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 D  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 D  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 D  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 D  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 D  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 D  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 D  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 D  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 D  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 D  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 D  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 D  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 D  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 D  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 D  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 D  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
HET     FE  A 208       1                                                       
HET     FE  B 208       1                                                       
HET     FE  C 208       1                                                       
HET     FE  D 208       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   9  HOH   *656(H2 O)                                                    
HELIX    1 H1A GLY A   22  ALA A   52  1                                  31    
HELIX    2 H2A ILE A   59  ASN A   82  1                                  24    
HELIX    3 H3A GLY A   93  PHE A  103  1                                  11    
HELIX    4 H4A PHE A  106  THR A  118  1                                  13    
HELIX    5 H5A LYS A  174  ASN A  183  1                                  10    
HELIX    6 H6A TRP A  187  THR A  198  1                                  12    
HELIX    7 H7A GLU A  163  ALA A  165  5SINGLE TURN OF 3/10 HELIX          3    
HELIX    8 H8A TYR A  167  TYR A  170  1SINGLE TURN OF ALPHA HELIX         4    
HELIX    9 H1B GLY B   22  LYS B   53  1                                  32    
HELIX   10 H2B ILE B   59  ASN B   82  1                                  24    
HELIX   11 H3B GLU B   94  PHE B  103  1                                  10    
HELIX   12 H4B PHE B  106  THR B  118  1                                  13    
HELIX   13 H5B LYS B  174  ASN B  183  1                                  10    
HELIX   14 H6B TRP B  187  THR B  198  1                                  12    
HELIX   15 H7B GLU B  163  ALA B  165  5SINGLE TURN OF 3/10 HELIX          3    
HELIX   16 H8B TYR B  167  TYR B  170  1SINGLE TURN OF ALPHA HELIX         4    
HELIX   17 H1C GLY C   22  ALA C   52  1                                  31    
HELIX   18 H2C ILE C   59  LYS C   81  1                                  23    
HELIX   19 H3C GLY C   93  PHE C  103  1                                  11    
HELIX   20 H4C PHE C  106  ALA C  117  1                                  12    
HELIX   21 H5C LYS C  174  ASN C  183  1                                  10    
HELIX   22 H6C TRP C  187  THR C  198  1                                  12    
HELIX   23 H7C GLU C  163  ALA C  165  5SINGLE TURN OF 3/10 HELIX          3    
HELIX   24 H8C TYR C  167  TYR C  170  1SINGLE TURN OF ALPHA HELIX         4    
HELIX   25 H1D GLY D   22  ALA D   52  1                                  31    
HELIX   26 H2D ILE D   59  LYS D   81  1                                  23    
HELIX   27 H3D GLY D   93  PHE D  103  1                                  11    
HELIX   28 H4D PHE D  106  THR D  118  1                                  13    
HELIX   29 H5D LYS D  174  ASN D  183  1                                  10    
HELIX   30 H6D TRP D  187  THR D  198  1                                  12    
HELIX   31 H7D GLU D  163  ALA D  165  5SINGLE TURN OF 3/10 HELIX          3    
HELIX   32 H8D TYR D  167  TYR D  170  1SINGLE TURN OF ALPHA HELIX         4    
SHEET    1  EA 3 LYS A 136  TYR A 143  0                                        
SHEET    2  EA 3 GLY A 124  ASP A 131 -1  N  TRP A 125   O  VAL A 142           
SHEET    3  EA 3 ILE A 153  ASP A 160 -1  O  LEU A 159   N  ALA A 126           
SHEET    1  EB 3 LYS B 136  TYR B 143  0                                        
SHEET    2  EB 3 GLY B 124  ASP B 131 -1  N  TRP B 125   O  VAL B 142           
SHEET    3  EB 3 VAL B 154  ASP B 160 -1  O  LEU B 159   N  ALA B 126           
SHEET    1  EC 3 LYS C 136  TYR C 143  0                                        
SHEET    2  EC 3 GLY C 124  ASP C 131 -1  N  TRP C 125   O  VAL C 142           
SHEET    3  EC 3 VAL C 154  ASP C 160 -1  O  LEU C 159   N  ALA C 126           
SHEET    1  ED 3 LYS D 136  TYR D 143  0                                        
SHEET    2  ED 3 GLY D 124  ASP D 131 -1  N  TRP D 125   O  VAL D 142           
SHEET    3  ED 3 ILE D 153  ASP D 160 -1  O  LEU D 159   N  ALA D 126           
LINK        FE    FE A 208                 NE2 HIS A  76     1555   1555  2.19  
LINK        FE    FE A 208                 NE2 HIS A  28     1555   1555  2.25  
LINK        FE    FE A 208                 OD2 ASP A 160     1555   1555  1.99  
LINK        FE    FE A 208                 NE2 HIS A 164     1555   1555  2.21  
LINK        FE    FE A 208                 O   HOH A1001     1555   1555  2.38  
LINK        FE    FE B 208                 NE2 HIS B 164     1555   1555  2.31  
LINK        FE    FE B 208                 NE2 HIS B  28     1555   1555  2.23  
LINK        FE    FE B 208                 O   HOH B1002     1555   1555  2.27  
LINK        FE    FE B 208                 NE2 HIS B  76     1555   1555  2.09  
LINK        FE    FE B 208                 OD2 ASP B 160     1555   1555  2.04  
LINK        FE    FE C 208                 OD2 ASP C 160     1555   1555  2.00  
LINK        FE    FE C 208                 O   HOH C1003     1555   1555  2.31  
LINK        FE    FE C 208                 NE2 HIS C  28     1555   1555  2.17  
LINK        FE    FE C 208                 NE2 HIS C 164     1555   1555  2.31  
LINK        FE    FE C 208                 NE2 HIS C  76     1555   1555  2.11  
LINK        FE    FE D 208                 NE2 HIS D  76     1555   1555  2.39  
LINK        FE    FE D 208                 OD2 ASP D 160     1555   1555  2.00  
LINK        FE    FE D 208                 NE2 HIS D 164     1555   1555  2.20  
LINK        FE    FE D 208                 O   HOH D1004     1555   1555  2.19  
LINK        FE    FE D 208                 NE2 HIS D  28     1555   1555  2.31  
CISPEP   1 GLU A   17    PRO A   18          0         1.42                     
CISPEP   2 GLU B   17    PRO B   18          0         0.73                     
CISPEP   3 GLU C   17    PRO C   18          0         1.89                     
CISPEP   4 GLU D   17    PRO D   18          0         2.09                     
SITE     1  A1  1  FE A 208                                                     
SITE     1  A2  1  FE B 208                                                     
SITE     1  A3  1  FE C 208                                                     
SITE     1  A4  1  FE D 208                                                     
SITE     1 AC1  5 HIS A  28  HIS A  76  ASP A 160  HIS A 164                    
SITE     2 AC1  5 HOH A1001                                                     
SITE     1 AC2  5 HIS B  28  HIS B  76  ASP B 160  HIS B 164                    
SITE     2 AC2  5 HOH B1002                                                     
SITE     1 AC3  5 HIS C  28  HIS C  76  ASP C 160  HIS C 164                    
SITE     2 AC3  5 HOH C1003                                                     
SITE     1 AC4  5 HIS D  28  HIS D  76  ASP D 160  HIS D 164                    
SITE     2 AC4  5 HOH D1004                                                     
CRYST1   68.650   85.400   66.350  90.00  99.86  90.00 P 1 21 1      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      0.014567  0.000000  0.002532        0.00000                         
SCALE2      0.000000  0.011710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015298        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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