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Entry: 1MMM
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HEADER    OXIDOREDUCTASE                          26-AUG-98   1MMM              
TITLE     DISTINCT METAL ENVIRONMENT IN IRON-SUBSTITUTED MANGANESE              
TITLE    2 SUPEROXIDE DISMUTASE PROVIDES A STRUCTURAL BASIS OF METAL            
TITLE    3 SPECIFICITY                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (IRON-SUBSTITUTED MANGANESE SUPEROXIDE             
COMPND   3 DISMUTASE);                                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: FE-MNSOD, FE-MNSD;                                          
COMPND   6 EC: 1.15.1.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: AB2463/PDT1-5                                                
KEYWDS    IRON-SUBSTITUTED MANGANESE SUPEROXIDE DISMUTASE,                      
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,G.B.JAMESON,                  
AUTHOR   2 E.N.BAKER                                                            
REVDAT   3   24-FEB-09 1MMM    1       VERSN                                    
REVDAT   2   29-DEC-99 1MMM    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   02-SEP-98 1MMM    0                                                
JRNL        AUTH   R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,                     
JRNL        AUTH 2 G.B.JAMESON,E.N.BAKER                                        
JRNL        TITL   DISTINCT METAL ENVIRONMENT IN FE-SUBSTITUTED                 
JRNL        TITL 2 MANGANESE SUPEROXIDE DISMUTASE PROVIDES A                    
JRNL        TITL 3 STRUCTURAL BASIS OF METAL SPECIFICITY                        
JRNL        REF    J.AM.CHEM.SOC.                V. 120  9684 1998              
JRNL        REFN                   ISSN 0002-7863                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3C                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20683                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1563                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 3256                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 284                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.26300                                             
REMARK   3    B22 (A**2) : 0.62900                                              
REMARK   3    B33 (A**2) : 1.63400                                              
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  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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MMM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008360.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.75                               
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20726                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1VEW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.75                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.33550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.33550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       23.09500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.52000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       23.09500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.52000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      103.33550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       23.09500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.52000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      103.33550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       23.09500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.52000            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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     GLN B   21   CG    CD    OE1   NE2                               
REMARK 480     GLU B   47   CG    CD    OE1   OE2                               
REMARK 480     ASN B   50   CG    OD1   ND2                                     
REMARK 480     LYS B  137   CG    CD    CE    NZ                                
REMARK 480     LYS B  205   CB    CG    CD    CE    NZ                          
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    PRO A  16       30.05    -93.96                                   
REMARK 500    LYS A  29      -64.54   -107.96                                   
REMARK 500    LYS A  89      142.09   -178.42                                   
REMARK 500    ASN A 145     -116.82     47.43                                   
REMARK 500    GLN A 178     -133.25     50.50                                   
REMARK 500    PRO B  16       31.48    -82.07                                   
REMARK 500    HIS B  17      -61.53    -99.71                                   
REMARK 500    LYS B  89      143.12   -178.58                                   
REMARK 500    ASN B 145     -121.78     45.81                                   
REMARK 500    TYR B 173       -1.84   -142.48                                   
REMARK 500    GLN B 178     -130.14     51.94                                   
REMARK 500    LYS B 204        3.32     59.00                                   
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                              FE A 206  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  81   NE2  88.5                                              
REMARK 620 3 ASP A 167   OD2  85.3 106.7                                        
REMARK 620 4 HIS A 171   NE2  90.0 146.7 106.3                                  
REMARK 620 5  OH A 207   O   171.8  98.2  88.3  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 206  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  81   NE2  92.8                                              
REMARK 620 3 ASP B 167   OD2  89.4 113.5                                        
REMARK 620 4 HIS B 171   NE2  90.0 146.5  99.8                                  
REMARK 620 5  OH B 207   O   178.2  86.5  92.3  89.7                            
REMARK 620 6  OH B 208   O    89.4  68.5 177.7  78.2  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: FE1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: IRON-SUBSTITUTED ACTIVE SITE CHAIN A.              
REMARK 800  CONTAINS ONE EXOGENOUS LIGAND MODELLED AS HYDROXIDE.                
REMARK 800 SITE_IDENTIFIER: FE2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: IRON-SUBSTITUTED ACTIVE SITE CHAIN B.              
REMARK 800  CONTAINS TWO EXOGENOUS LIGANDS BOTH MODELLED AS HYDROXIDES.         
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 207                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH B 207                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH B 208                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 206                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 206                  
DBREF  1MMM A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1MMM B    1   205  UNP    P00448   SODM_ECOLI       1    205             
SEQRES   1 A  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 A  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 A  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 A  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 A  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 A  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 A  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 A  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 A  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 A  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 A  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 A  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 A  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 A  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 A  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 B  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 B  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 B  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 B  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 B  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 B  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 B  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 B  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 B  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 B  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 B  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 B  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 B  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 B  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
HET     OH  A 207       1                                                       
HET     OH  B 207       1                                                       
HET     OH  B 208       1                                                       
HET     FE  A 206       1                                                       
HET     FE  B 206       1                                                       
HETNAM      OH HYDROXIDE ION                                                    
HETNAM      FE FE (III) ION                                                     
FORMUL   3   OH    3(H O 1-)                                                    
FORMUL   6   FE    2(FE 3+)                                                     
FORMUL   8  HOH   *284(H2 O)                                                    
HELIX    1   1 LYS A   20  THR A   28  1                                   9    
HELIX    2   2 HIS A   30  LEU A   42  1                                  13    
HELIX    3   3 PRO A   46  ASN A   50  1                                   5    
HELIX    4   4 VAL A   53  THR A   58  1                                   6    
HELIX    5   5 LEU A   60  GLN A   62  5                                   3    
HELIX    6   6 ALA A   65  LYS A   86  1                                  22    
HELIX    7   7 GLY A   96  PHE A  106  1                                  11    
HELIX    8   8 VAL A  109  SER A  122  1                                  14    
HELIX    9   9 PRO A  149  MET A  151  5                                   3    
HELIX   10  10 GLU A  153  SER A  156  1                                   4    
HELIX   11  11 GLU A  170  ALA A  172  5                                   3    
HELIX   12  12 TYR A  174  PHE A  177  1                                   4    
HELIX   13  13 ARG A  181  VAL A  191  1                                  11    
HELIX   14  14 TRP A  194  ALA A  203  1                                  10    
HELIX   15  15 LYS B   20  THR B   28  1                                   9    
HELIX   16  16 HIS B   30  SER B   44  1                                  15    
HELIX   17  17 PRO B   46  ALA B   49  1                                   4    
HELIX   18  18 VAL B   53  THR B   58  1                                   6    
HELIX   19  19 LEU B   60  GLN B   62  5                                   3    
HELIX   20  20 ALA B   65  LYS B   86  1                                  22    
HELIX   21  21 GLY B   96  PHE B  106  1                                  11    
HELIX   22  22 VAL B  109  SER B  122  1                                  14    
HELIX   23  23 PRO B  149  MET B  151  5                                   3    
HELIX   24  24 GLU B  153  SER B  156  1                                   4    
HELIX   25  25 GLU B  170  ALA B  172  5                                   3    
HELIX   26  26 TYR B  174  PHE B  177  1                                   4    
HELIX   27  27 ARG B  181  VAL B  191  1                                  11    
HELIX   28  28 TRP B  194  ALA B  203  1                                  10    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  N  LYS A 134   O  LYS A 137           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  N  LEU A 166   O  ALA A 129           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  N  LYS B 134   O  LYS B 137           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  N  LEU B 166   O  ALA B 129           
LINK         NE2 HIS A  26                FE    FE A 206     1555   1555  2.16  
LINK         NE2 HIS A  81                FE    FE A 206     1555   1555  2.06  
LINK         OD2 ASP A 167                FE    FE A 206     1555   1555  2.08  
LINK         NE2 HIS A 171                FE    FE A 206     1555   1555  2.27  
LINK         NE2 HIS B  26                FE    FE B 206     1555   1555  2.21  
LINK         NE2 HIS B  81                FE    FE B 206     1555   1555  2.19  
LINK         OD2 ASP B 167                FE    FE B 206     1555   1555  2.03  
LINK         NE2 HIS B 171                FE    FE B 206     1555   1555  2.32  
LINK         O    OH A 207                FE    FE A 206     1555   1555  2.22  
LINK         O    OH B 207                FE    FE B 206     1555   1555  2.23  
LINK         O    OH B 208                FE    FE B 206     1555   1555  1.99  
CISPEP   1 GLU A   15    PRO A   16          0        -0.23                     
CISPEP   2 GLU B   15    PRO B   16          0        -0.03                     
SITE     1 FE1  6  FE A 206  HIS A  26  HIS A  81  ASP A 167                    
SITE     2 FE1  6 HIS A 171   OH A 207                                          
SITE     1 FE2  7  FE B 206  HIS B  26  HIS B  81  ASP B 167                    
SITE     2 FE2  7 HIS B 171   OH B 207   OH B 208                               
SITE     1 AC1  6 HIS A  81  GLN A 146  ASP A 167  TRP A 169                    
SITE     2 AC1  6 HIS A 171   FE A 206                                          
SITE     1 AC2  8 TYR B  34  HIS B  81  GLN B 146  ASP B 167                    
SITE     2 AC2  8 TRP B 169  HIS B 171   FE B 206   OH B 208                    
SITE     1 AC3  7 HIS B  26  HIS B  30  TYR B  34  HIS B  81                    
SITE     2 AC3  7 HIS B 171   FE B 206   OH B 207                               
SITE     1 AC4  5 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC4  5  OH A 207                                                     
SITE     1 AC5  6 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC5  6  OH B 207   OH B 208                                          
CRYST1   46.190   89.040  206.671  90.00  90.00  90.00 C 2 2 21     16          
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      0.021650  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011231  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004839        0.00000                         
MTRIX1   1  0.729903  0.132591  0.670567      -17.32900    1                    
MTRIX2   1  0.126001 -0.990294  0.058660       51.12900    1                    
MTRIX3   1  0.671837  0.041676 -0.739526       34.36400    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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