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Database: PDB
Entry: 2BKB
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Original site: 2BKB 
HEADER    OXIDOREDUCTASE                          14-FEB-05   2BKB              
TITLE     Q69E-FESOD                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [FE];                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: REDUCED STATE                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUPEROXIDE DISMUTASE, IRON REDOX TUNING, H-BOND NETWORK,              
KEYWDS   2 MUTANT, OXIDOREDUCTASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.YIKILMAZ,D.W.RODGERS,A.-F.MILLER                                    
REVDAT   2   24-FEB-09 2BKB    1       VERSN                                    
REVDAT   1   03-JAN-07 2BKB    0                                                
JRNL        AUTH   E.YIKILMAZ,D.W.RODGERS,A.-F.MILLER                           
JRNL        TITL   THE CRUCIAL IMPORTANCE OF CHEMISTRY IN THE                   
JRNL        TITL 2 STRUCTURE-FUNCTION LINK: MANIPULATING HYDROGEN               
JRNL        TITL 3 BONDING IN IRON-CONTAINING SUPEROXIDE DISMUTASE.             
JRNL        REF    BIOCHEMISTRY                  V.  45  1151 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16430211                                                     
JRNL        DOI    10.1021/BI051495D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.7  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 847928.80                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 79134                          
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) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 7776                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.6                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8140                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.253                        
REMARK   3   BIN FREE R VALUE                    : 0.298                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.9                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 891                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6012                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 629                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.7                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.327                                                
REMARK   3    B22 (A**2) : -3.918                                               
REMARK   3    B33 (A**2) : 2.591                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -2.697                                               
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.2                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.2                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.00  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.41  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.94  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.63  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.362302                                             
REMARK   3   BSOL        : 38.0928                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BKB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-22970.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5                                
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : GRADED MULTILAYER                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS IV)             
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87786                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07000                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: WT-FESOD 1ISB.PDB                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
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       53.85000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLN 69 TO GLU                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLN 69 TO GLU                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLN 69 TO GLU                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLN 69 TO GLU                         
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 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    SER A  58       26.04   -143.72                                   
REMARK 500    ASN A 117      107.53    -59.41                                   
REMARK 500    ASN A 140     -111.25     51.71                                   
REMARK 500    ARG A 167     -130.02     53.46                                   
REMARK 500    ASN B 340     -112.79     55.06                                   
REMARK 500    TYR B 362       -7.55   -141.67                                   
REMARK 500    ARG B 367     -130.61     49.20                                   
REMARK 500    SER C  58       18.90   -143.02                                   
REMARK 500    ASN C 140     -114.47     56.35                                   
REMARK 500    TYR C 162       -9.88   -140.20                                   
REMARK 500    ARG C 167     -129.67     53.44                                   
REMARK 500    SER D 258       25.76   -144.44                                   
REMARK 500    ASN D 340     -113.08     55.40                                   
REMARK 500    ARG D 367     -134.06     57.24                                   
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 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                             FE2 A1193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2081   O                                                      
REMARK 620 2 HIS A  73   NE2  90.7                                              
REMARK 620 3 ASP A 156   OD1  94.0 115.4                                        
REMARK 620 4 HIS A 160   NE2  89.9 128.0 116.4                                  
REMARK 620 5 HIS A  26   NE2 177.8  90.1  87.5  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B1393  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 356   OD2                                                    
REMARK 620 2 HIS B 226   NE2  86.1                                              
REMARK 620 3 HIS B 273   NE2 111.8  88.9                                        
REMARK 620 4 HIS B 360   NE2 118.9  91.6 129.3                                  
REMARK 620 5 HOH B2078   O    93.4 174.7  86.4  93.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 C1193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 160   NE2                                                    
REMARK 620 2 HOH C2052   O    89.4                                              
REMARK 620 3 ASP C 156   OD1 115.3  96.8                                        
REMARK 620 4 HIS C  73   NE2 128.7  89.8 115.7                                  
REMARK 620 5 HIS C  26   NE2  87.5 176.8  84.8  92.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 D1393  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 356   OD1                                                    
REMARK 620 2 HIS D 226   NE2  81.6                                              
REMARK 620 3 HIS D 273   NE2 115.7  90.0                                        
REMARK 620 4 HIS D 360   NE2 120.0  88.3 123.3                                  
REMARK 620 5 HOH D2058   O    98.1 179.5  90.5  91.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B1393                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 C1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 D1393                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ISA   RELATED DB: PDB                                   
REMARK 900  IRON(II) SUPEROXIDE DISMUTASE                                       
REMARK 900 RELATED ID: 1ISB   RELATED DB: PDB                                   
REMARK 900  IRON(III) SUPEROXIDE DISMUTASE                                      
REMARK 900 RELATED ID: 1ISC   RELATED DB: PDB                                   
REMARK 900  IRON(III) SUPEROXIDE DISMUTASE COMPLEXED WITH                       
REMARK 900   AZIDE                                                              
DBREF  2BKB A    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2BKB B  201   392  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2BKB C    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  2BKB D  201   392  UNP    P0AGD3   SODF_ECOLI       1    192             
SEQADV 2BKB GLU A   69  UNP  P0AGD3    GLN    69 ENGINEERED MUTATION            
SEQADV 2BKB GLU B  269  UNP  P0AGD3    GLN    69 ENGINEERED MUTATION            
SEQADV 2BKB GLU C   69  UNP  P0AGD3    GLN    69 ENGINEERED MUTATION            
SEQADV 2BKB GLU D  269  UNP  P0AGD3    GLN    69 ENGINEERED MUTATION            
SEQRES   1 A  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 A  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 A  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 A  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 A  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 A  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 A  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 A  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 A  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 A  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 A  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 A  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 A  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 A  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 A  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 B  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 B  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 B  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 B  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 B  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 B  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 B  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 B  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 B  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 B  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 B  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 B  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 B  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 B  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 B  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 C  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 C  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 C  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 C  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 C  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 C  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 C  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 C  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 C  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 C  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 C  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 C  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 C  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 C  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 C  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 D  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 D  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 D  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 D  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 D  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 D  192  ASN ALA ALA GLU VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 D  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 D  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 D  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 D  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 D  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 D  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 D  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 D  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 D  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
HET    FE2  A1193       1                                                       
HET    FE2  B1393       1                                                       
HET    FE2  C1193       1                                                       
HET    FE2  D1393       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   5  FE2    4(FE 2+)                                                     
FORMUL   9  HOH   *629(H2 O1)                                                   
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  ARG A   57  1                                   7    
HELIX    4   4 GLU A   60  CYS A   79  1                                  20    
HELIX    5   5 THR A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ASN A  117  1                                  16    
HELIX    7   7 THR A  143  THR A  147  5                                   5    
HELIX    8   8 TRP A  158  ALA A  161  5                                   4    
HELIX    9   9 TYR A  162  ARG A  167  1                                   6    
HELIX   10  10 ALA A  169  ALA A  179  1                                  11    
HELIX   11  11 ASN A  182  ALA A  192  1                                  11    
HELIX   12  12 SER B  219  TYR B  227  1                                   9    
HELIX   13  13 LYS B  229  LYS B  243  1                                  15    
HELIX   14  14 SER B  251  ARG B  257  1                                   7    
HELIX   15  15 GLU B  260  CYS B  279  1                                  20    
HELIX   16  16 THR B  289  GLY B  301  1                                  13    
HELIX   17  17 SER B  302  LYS B  316  1                                  15    
HELIX   18  18 THR B  343  THR B  347  5                                   5    
HELIX   19  19 TRP B  358  ALA B  361  5                                   4    
HELIX   20  20 TYR B  362  ARG B  367  1                                   6    
HELIX   21  21 ALA B  369  TRP B  378  1                                  10    
HELIX   22  22 ASN B  382  ALA B  392  1                                  11    
HELIX   23  23 SER C   19  TYR C   27  1                                   9    
HELIX   24  24 LYS C   29  LYS C   43  1                                  15    
HELIX   25  25 SER C   51  ARG C   57  1                                   7    
HELIX   26  26 GLU C   60  LEU C   80  1                                  21    
HELIX   27  27 THR C   89  GLY C  101  1                                  13    
HELIX   28  28 SER C  102  LYS C  116  1                                  15    
HELIX   29  29 THR C  143  THR C  147  5                                   5    
HELIX   30  30 TRP C  158  ALA C  161  5                                   4    
HELIX   31  31 TYR C  162  ARG C  167  1                                   6    
HELIX   32  32 ALA C  169  TRP C  178  1                                  10    
HELIX   33  33 ASN C  182  ALA C  192  1                                  11    
HELIX   34  34 SER D  219  TYR D  227  1                                   9    
HELIX   35  35 LYS D  229  LYS D  243  1                                  15    
HELIX   36  36 SER D  251  ARG D  257  1                                   7    
HELIX   37  37 GLU D  260  CYS D  279  1                                  20    
HELIX   38  38 THR D  289  GLY D  301  1                                  13    
HELIX   39  39 SER D  302  ASN D  317  1                                  16    
HELIX   40  40 THR D  343  THR D  347  5                                   5    
HELIX   41  41 TRP D  358  ALA D  361  5                                   4    
HELIX   42  42 TYR D  362  ARG D  367  1                                   6    
HELIX   43  43 ALA D  369  TRP D  378  1                                  10    
HELIX   44  44 ASN D  382  ALA D  392  1                                  11    
SHEET    1  AA 3 LEU A 133  SER A 139  0                                        
SHEET    2  AA 3 GLY A 121  LYS A 127 -1  O  TRP A 122   N  THR A 138           
SHEET    3  AA 3 THR A 150  ASP A 156 -1  O  THR A 150   N  LYS A 127           
SHEET    1  BA 3 LEU B 333  SER B 339  0                                        
SHEET    2  BA 3 GLY B 321  LYS B 327 -1  O  TRP B 322   N  THR B 338           
SHEET    3  BA 3 THR B 350  ASP B 356 -1  O  THR B 350   N  LYS B 327           
SHEET    1  CA 3 LEU C 133  SER C 139  0                                        
SHEET    2  CA 3 GLY C 121  LYS C 127 -1  O  TRP C 122   N  THR C 138           
SHEET    3  CA 3 THR C 150  ASP C 156 -1  O  THR C 150   N  LYS C 127           
SHEET    1  DA 3 LEU D 333  SER D 339  0                                        
SHEET    2  DA 3 GLY D 321  LYS D 327 -1  O  TRP D 322   N  THR D 338           
SHEET    3  DA 3 THR D 350  ASP D 356 -1  O  THR D 350   N  LYS D 327           
LINK        FE   FE2 A1193                 O   HOH A2081     1555   1555  2.12  
LINK        FE   FE2 A1193                 NE2 HIS A  73     1555   1555  2.10  
LINK        FE   FE2 A1193                 OD1 ASP A 156     1555   1555  1.94  
LINK        FE   FE2 A1193                 NE2 HIS A 160     1555   1555  2.16  
LINK        FE   FE2 A1193                 NE2 HIS A  26     1555   1555  2.16  
LINK        FE   FE2 B1393                 OD2 ASP B 356     1555   1555  1.96  
LINK        FE   FE2 B1393                 NE2 HIS B 226     1555   1555  2.25  
LINK        FE   FE2 B1393                 NE2 HIS B 273     1555   1555  2.19  
LINK        FE   FE2 B1393                 NE2 HIS B 360     1555   1555  2.06  
LINK        FE   FE2 B1393                 O   HOH B2078     1555   1555  2.17  
LINK        FE   FE2 C1193                 O   HOH C2052     1555   1555  2.18  
LINK        FE   FE2 C1193                 OD1 ASP C 156     1555   1555  1.97  
LINK        FE   FE2 C1193                 NE2 HIS C  73     1555   1555  2.11  
LINK        FE   FE2 C1193                 NE2 HIS C  26     1555   1555  2.26  
LINK        FE   FE2 C1193                 NE2 HIS C 160     1555   1555  2.19  
LINK        FE   FE2 D1393                 NE2 HIS D 226     1555   1555  2.27  
LINK        FE   FE2 D1393                 NE2 HIS D 273     1555   1555  2.22  
LINK        FE   FE2 D1393                 NE2 HIS D 360     1555   1555  2.14  
LINK        FE   FE2 D1393                 O   HOH D2058     1555   1555  2.08  
LINK        FE   FE2 D1393                 OD1 ASP D 356     1555   1555  1.95  
CISPEP   1 ALA A   15    PRO A   16          0         0.27                     
CISPEP   2 ALA B  215    PRO B  216          0         0.12                     
CISPEP   3 ALA C   15    PRO C   16          0         0.06                     
CISPEP   4 ALA D  215    PRO D  216          0         0.06                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     2 AC1  5 HOH A2081                                                     
SITE     1 AC2  5 HIS B 226  HIS B 273  ASP B 356  HIS B 360                    
SITE     2 AC2  5 HOH B2078                                                     
SITE     1 AC3  5 HIS C  26  HIS C  73  ASP C 156  HIS C 160                    
SITE     2 AC3  5 HOH C2052                                                     
SITE     1 AC4  5 HIS D 226  HIS D 273  ASP D 356  HIS D 360                    
SITE     2 AC4  5 HOH D2058                                                     
CRYST1   43.500  107.700   84.200  90.00  95.02  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      0.022989  0.000000  0.002019        0.00000                         
SCALE2      0.000000  0.009285  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011922        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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