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Entry: 1UER
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HEADER    OXIDOREDUCTASE                          20-MAY-03   1UER              
TITLE     CRYSTAL STRUCTURE OF PORPHYROMONAS GINGIVALIS SOD                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: SOD;                                                        
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;                       
SOURCE   3 ORGANISM_TAXID: 837;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: TB-1;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PMAL-C2                                   
KEYWDS    METAL-SPECIFIC, CAMBIALISTIC, SUPEROXIDE DISMUTASE, SOD,              
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.YAMAKURA,S.SUGIO,B.Y.HIRAOKA,T.YOKOTA,D.OHMORI                      
REVDAT   2   24-FEB-09 1UER    1       VERSN                                    
REVDAT   1   20-MAY-04 1UER    0                                                
JRNL        AUTH   F.YAMAKURA,S.SUGIO,B.Y.HIRAOKA,D.OHMORI,T.YOKOTA             
JRNL        TITL   PRONOUNCED CONVERSION OF THE METAL-SPECIFIC                  
JRNL        TITL 2 ACTIVITY OF SUPEROXIDE DISMUTASE FROM                        
JRNL        TITL 3 PORPHYROMONAS GINGIVALIS BY THE MUTATION OF A                
JRNL        TITL 4 SINGLE AMINO ACID (GLY155THR) LOCATED APART FROM             
JRNL        TITL 5 THE ACTIVE SITE                                              
JRNL        REF    BIOCHEMISTRY                  V.  42 10790 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12962504                                                     
JRNL        DOI    10.1021/BI0349625                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.SUGIO,B.Y.HIRAOKA,F.YAMAKURA                               
REMARK   1  TITL   CRYSTAL STRUCTURE OF CAMBIALISTIC SUPEROXIDE                 
REMARK   1  TITL 2 DISMUTASE FROM PORPHYROMONAS GINGIVALIS                      
REMARK   1  REF    EUR.J.BIOCHEM.                V. 267  3487 2000              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   10848964                                                     
REMARK   1  DOI    10.1046/J.1432-1327.2000.01373.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98.1                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 91058                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 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            : 6104                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 504                                     
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) : 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  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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UER COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005742.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL24XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.836                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108296                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.07100                            
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, POTASSIUM PHOSPHATE, PH         
REMARK 280  5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       37.66000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.69500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.96500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.69500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.66000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.96500            
REMARK 290   SMTRY3   4  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 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
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 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  85     -120.03   -123.02                                   
REMARK 500    ASN A 141     -109.35     48.15                                   
REMARK 500    TYR A 163       -4.50   -143.60                                   
REMARK 500    GLN A 168     -127.76     48.73                                   
REMARK 500    LYS B 285     -115.97   -117.00                                   
REMARK 500    ASN B 341     -111.64     49.57                                   
REMARK 500    TYR B 363       -6.96   -142.42                                   
REMARK 500    GLN B 368     -129.01     49.04                                   
REMARK 500    LYS C 430      -52.15   -120.87                                   
REMARK 500    LYS C 485     -129.95   -114.74                                   
REMARK 500    ASP C 529     -165.53   -101.99                                   
REMARK 500    ASN C 541     -111.42     51.99                                   
REMARK 500    TYR C 563       -8.15   -145.77                                   
REMARK 500    GLN C 568     -129.48     50.42                                   
REMARK 500    THR D 602       74.77   -108.23                                   
REMARK 500    LYS D 685     -122.96    -94.21                                   
REMARK 500    ASN D 741     -107.95     44.72                                   
REMARK 500    TYR D 763       -4.51   -142.03                                   
REMARK 500    GLN D 768     -127.96     49.18                                   
REMARK 500    SER D 789       31.36    -80.74                                   
REMARK 500    ARG D 790       38.12   -142.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 277         0.07    SIDE_CHAIN                              
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 C 695        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH B 504        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 529        DISTANCE =  6.25 ANGSTROMS                       
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 192  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  74   NE2                                                    
REMARK 620 2 ASP A 157   OD2 111.9                                              
REMARK 620 3 HOH A 193   O    99.2  89.3                                        
REMARK 620 4 HIS A  27   NE2  83.2  88.4 177.2                                  
REMARK 620 5 HIS A 161   NE2 130.8 117.2  85.3  94.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 392  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 274   NE2                                                    
REMARK 620 2 ASP B 357   OD2 112.8                                              
REMARK 620 3 HOH B 393   O    95.4  91.0                                        
REMARK 620 4 HIS B 361   NE2 129.4 117.8  85.9                                  
REMARK 620 5 HIS B 227   NE2  84.0  85.4 175.8  97.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 592  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 557   OD2                                                    
REMARK 620 2 HOH C 593   O    91.8                                              
REMARK 620 3 HIS C 427   NE2  89.4 177.2                                        
REMARK 620 4 HIS C 474   NE2 111.9  96.4  80.8                                  
REMARK 620 5 HIS C 561   NE2 119.8  88.3  93.2 127.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 792  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 757   OD2                                                    
REMARK 620 2 HIS D 761   NE2 115.3                                              
REMARK 620 3 HIS D 674   NE2 113.9 130.9                                        
REMARK 620 4 HOH D   4   O    83.6  90.5  95.8                                  
REMARK 620 5 HIS D 627   NE2  88.1  98.0  82.6 170.1                            
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 FE A 192                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 392                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 592                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 792                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UES   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, G155T MUTANT                                       
DBREF  1UER A    1   191  UNP    P19665   SODF_PORGI       1    191             
DBREF  1UER B  201   391  UNP    P19665   SODF_PORGI       1    191             
DBREF  1UER C  401   591  UNP    P19665   SODF_PORGI       1    191             
DBREF  1UER D  601   791  UNP    P19665   SODF_PORGI       1    191             
SEQRES   1 A  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 A  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 A  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 A  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 A  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 A  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 A  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 A  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 A  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 A  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 A  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 A  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 A  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 A  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 A  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 B  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 B  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 B  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 B  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 B  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 B  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 B  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 B  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 B  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 B  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 B  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 B  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 B  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 B  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 B  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 C  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 C  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 C  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 C  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 C  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 C  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 C  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 C  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 C  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 C  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 C  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 C  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 C  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 C  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 C  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 D  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 D  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 D  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 D  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 D  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 D  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 D  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 D  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 D  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 D  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 D  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 D  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 D  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 D  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 D  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
HET     FE  A 192       1                                                       
HET     FE  B 392       1                                                       
HET     FE  C 592       1                                                       
HET     FE  D 792       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   9  HOH   *504(H2 O)                                                    
HELIX    1   1 SER A   20  HIS A   28  1                                   9    
HELIX    2   2 LYS A   30  ILE A   43  1                                  14    
HELIX    3   3 ASP A   52  SER A   60  1                                   9    
HELIX    4   4 GLU A   61  GLN A   80  1                                  20    
HELIX    5   5 LYS A   90  GLY A  102  1                                  13    
HELIX    6   6 SER A  103  LEU A  118  1                                  16    
HELIX    7   7 ASN A  144  GLY A  149  5                                   6    
HELIX    8   8 TRP A  159  ALA A  162  5                                   4    
HELIX    9   9 TYR A  163  GLN A  168  1                                   6    
HELIX   10  10 ARG A  170  TRP A  179  1                                  10    
HELIX   11  11 SER A  180  VAL A  182  5                                   3    
HELIX   12  12 ASP A  183  TYR A  191  1                                   9    
HELIX   13  13 SER B  220  HIS B  228  1                                   9    
HELIX   14  14 LYS B  230  ILE B  244  1                                  15    
HELIX   15  15 ASP B  252  SER B  260  1                                   9    
HELIX   16  16 GLU B  261  GLN B  280  1                                  20    
HELIX   17  17 LYS B  290  GLY B  302  1                                  13    
HELIX   18  18 SER B  303  LEU B  318  1                                  16    
HELIX   19  19 ASN B  344  GLY B  349  5                                   6    
HELIX   20  20 TRP B  359  ALA B  362  5                                   4    
HELIX   21  21 TYR B  363  GLN B  368  1                                   6    
HELIX   22  22 ARG B  370  TRP B  379  1                                  10    
HELIX   23  23 SER B  380  VAL B  382  5                                   3    
HELIX   24  24 ASP B  383  TYR B  391  1                                   9    
HELIX   25  25 SER C  420  HIS C  428  1                                   9    
HELIX   26  26 LYS C  430  ILE C  443  1                                  14    
HELIX   27  27 ASP C  452  SER C  460  1                                   9    
HELIX   28  28 GLU C  461  GLN C  480  1                                  20    
HELIX   29  29 LYS C  490  GLY C  502  1                                  13    
HELIX   30  30 SER C  503  LEU C  518  1                                  16    
HELIX   31  31 ASN C  544  GLY C  549  5                                   6    
HELIX   32  32 TRP C  559  ALA C  562  5                                   4    
HELIX   33  33 TYR C  563  GLN C  568  1                                   6    
HELIX   34  34 ARG C  570  TRP C  579  1                                  10    
HELIX   35  35 SER C  580  VAL C  582  5                                   3    
HELIX   36  36 ASP C  583  SER C  589  1                                   7    
HELIX   37  37 SER D  620  LYS D  630  1                                  11    
HELIX   38  38 LYS D  630  ILE D  644  1                                  15    
HELIX   39  39 ASP D  652  SER D  660  1                                   9    
HELIX   40  40 GLU D  661  GLN D  680  1                                  20    
HELIX   41  41 LYS D  690  GLY D  702  1                                  13    
HELIX   42  42 SER D  703  LEU D  718  1                                  16    
HELIX   43  43 ASN D  744  GLY D  749  5                                   6    
HELIX   44  44 TRP D  759  ALA D  762  5                                   4    
HELIX   45  45 TYR D  763  GLN D  768  1                                   6    
HELIX   46  46 ARG D  770  TRP D  779  1                                  10    
HELIX   47  47 SER D  780  VAL D  782  5                                   3    
HELIX   48  48 ASP D  783  SER D  789  1                                   7    
SHEET    1   A 3 LEU A 134  PRO A 140  0                                        
SHEET    2   A 3 GLY A 122  SER A 128 -1  N  TRP A 125   O  GLU A 137           
SHEET    3   A 3 ASN A 151  ASP A 157 -1  O  ASN A 151   N  SER A 128           
SHEET    1   B 3 LEU B 334  PRO B 340  0                                        
SHEET    2   B 3 GLY B 322  SER B 328 -1  N  TRP B 323   O  GLU B 339           
SHEET    3   B 3 ASN B 351  ASP B 357 -1  O  ASN B 351   N  SER B 328           
SHEET    1   C 3 LEU C 534  PRO C 540  0                                        
SHEET    2   C 3 GLY C 522  SER C 528 -1  N  TRP C 523   O  GLU C 539           
SHEET    3   C 3 ASN C 551  ASP C 557 -1  O  ASN C 551   N  SER C 528           
SHEET    1   D 3 LEU D 734  PRO D 740  0                                        
SHEET    2   D 3 GLY D 722  SER D 728 -1  N  ALA D 727   O  SER D 735           
SHEET    3   D 3 ASN D 751  ASP D 757 -1  O  ASN D 751   N  SER D 728           
LINK        FE    FE A 192                 NE2 HIS A  74     1555   1555  2.17  
LINK        FE    FE A 192                 OD2 ASP A 157     1555   1555  1.98  
LINK        FE    FE B 392                 NE2 HIS B 274     1555   1555  2.19  
LINK        FE    FE B 392                 OD2 ASP B 357     1555   1555  2.04  
LINK        FE    FE C 592                 OD2 ASP C 557     1555   1555  1.97  
LINK        FE    FE D 792                 OD2 ASP D 757     1555   1555  2.05  
LINK        FE    FE D 792                 NE2 HIS D 761     1555   1555  2.19  
LINK        FE    FE A 192                 O   HOH A 193     1555   1555  2.04  
LINK        FE    FE A 192                 NE2 HIS A  27     1555   1555  2.24  
LINK        FE    FE A 192                 NE2 HIS A 161     1555   1555  2.24  
LINK        FE    FE B 392                 O   HOH B 393     1555   1555  2.09  
LINK        FE    FE B 392                 NE2 HIS B 361     1555   1555  2.25  
LINK        FE    FE B 392                 NE2 HIS B 227     1555   1555  2.26  
LINK        FE    FE C 592                 O   HOH C 593     1555   1555  2.01  
LINK        FE    FE C 592                 NE2 HIS C 427     1555   1555  2.25  
LINK        FE    FE C 592                 NE2 HIS C 474     1555   1555  2.23  
LINK        FE    FE C 592                 NE2 HIS C 561     1555   1555  2.21  
LINK        FE    FE D 792                 NE2 HIS D 674     1555   1555  2.23  
LINK        FE    FE D 792                 O   HOH D   4     1555   1555  2.18  
LINK        FE    FE D 792                 NE2 HIS D 627     1555   1555  2.26  
CISPEP   1 ALA A   16    PRO A   17          0         1.07                     
CISPEP   2 ALA B  216    PRO B  217          0         0.21                     
CISPEP   3 ALA C  416    PRO C  417          0         0.16                     
CISPEP   4 ALA D  616    PRO D  617          0         0.34                     
SITE     1 AC1  5 HIS A  27  HIS A  74  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A 193                                                     
SITE     1 AC2  5 HIS B 227  HIS B 274  ASP B 357  HIS B 361                    
SITE     2 AC2  5 HOH B 393                                                     
SITE     1 AC3  5 HIS C 427  HIS C 474  ASP C 557  HIS C 561                    
SITE     2 AC3  5 HOH C 593                                                     
SITE     1 AC4  5 HOH D   4  HIS D 627  HIS D 674  ASP D 757                    
SITE     2 AC4  5 HIS D 761                                                     
CRYST1   75.320   95.930  101.390  90.00  90.00  90.00 P 21 21 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      0.013277  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010424  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009863        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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