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Database: PDB
Entry: 1BS3
LinkDB: 1BS3
Original site: 1BS3 
HEADER    OXIDOREDUCTASE                          31-AUG-98   1BS3              
TITLE     P.SHERMANII SOD(FE+3) FLUORIDE                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SOD;                                                        
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 OTHER_DETAILS: COMPETITIVELY INHIBITED BY FLOURIDE. FLUORIDE OCCUPIES
COMPND   7 SUBSTRATE BINDING SITE.                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PROPIONIBACTERIUM FREUDENREICHII SUBSP.         
SOURCE   3 SHERMANII;                                                           
SOURCE   4 ORGANISM_TAXID: 1752;                                                
SOURCE   5 STRAIN: PZ3;                                                         
SOURCE   6 ATCC: GERMAN COLLECTION OF MICROORGANISMS (DSM) 4902;                
SOURCE   7 COLLECTION: GERMAN COLLECTION OF MICROORGANISMS (DSM) 4902;          
SOURCE   8 CELLULAR_LOCATION: CYTOPLASM                                         
KEYWDS    SUPEROXIDE DISMUTASE, FLUORIDE, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SCHMIDT                                                             
REVDAT   4   13-JUL-11 1BS3    1       VERSN                                    
REVDAT   3   24-FEB-09 1BS3    1       VERSN                                    
REVDAT   2   01-APR-03 1BS3    1       JRNL                                     
REVDAT   1   15-JUN-99 1BS3    0                                                
JRNL        AUTH   M.SCHMIDT                                                    
JRNL        TITL   MANIPULATING THE COORDINATION MUMBER OF THE FERRIC IRON      
JRNL        TITL 2 WITHIN THE CAMBIALISTIC SUPEROXIDE DISMUTASE OF              
JRNL        TITL 3 PROPIONIBACTERIUM SHERMANII BY CHANGING THE PH-VALUE A       
JRNL        TITL 4 CRYSTALLOGRAPHIC ANALYSIS                                    
JRNL        REF    EUR.J.BIOCHEM.                V. 262   117 1999              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   10231372                                                     
JRNL        DOI    10.1046/J.1432-1327.1999.00359.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 41693                          
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) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4178                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.62                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3691                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE                    : 0.2410                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 439                          
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            : 3208                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 478                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.10                          
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) : 0.15                            
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) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.25                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88                            
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) : 1.000 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.500 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.200 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.300 ; 2.500                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.PEP                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IRON AND FLUORIDE REFINED UNRESTRAINED    
REMARK   4                                                                      
REMARK   4 1BS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 6.1                                
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          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45799                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.1                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.14800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1AR5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.1                                   
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       54.20000            
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       54.20000            
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       39.71000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.64000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.71000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.64000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.20000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.71000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.64000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.71000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.64000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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   BIOMT1   2 -1.000000  0.000000  0.000000       79.42000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       54.20000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   433     O    HOH B   433     3655     0.66            
REMARK 500   O    HOH A   334     O    HOH A   334     3655     1.13            
REMARK 500   O    HOH B   347     O    HOH B   347     3555     1.33            
REMARK 500   O    HOH A   343     O    HOH A   343     4566     1.97            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  30      -60.11   -105.80                                   
REMARK 500    ASP A  94     -134.43     55.98                                   
REMARK 500    ASP A 145     -119.82     57.56                                   
REMARK 500    LYS A 172     -133.36     56.78                                   
REMARK 500    LYS B  30      -60.88   -104.06                                   
REMARK 500    ASP B  94     -140.87     53.43                                   
REMARK 500    ASP B 145     -116.41     57.31                                   
REMARK 500    ASN B 149       45.92     70.21                                   
REMARK 500    PHE B 167      -13.95   -144.92                                   
REMARK 500    LYS B 172     -132.78     57.32                                   
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 A 295        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 335        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A 405        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B 394        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B 423        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH B 448        DISTANCE =  5.95 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 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  27   NE2                                                    
REMARK 620 2 HIS A  75   NE2  89.1                                              
REMARK 620 3 ASP A 161   OD2  85.6 101.5                                        
REMARK 620 4 HIS A 165   NE2  89.8 145.3 113.0                                  
REMARK 620 5   F A 203   F    95.0  61.9 163.3  83.7                            
REMARK 620 6 HOH A 204   O   176.6  91.5  90.9  91.6  88.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  27   NE2                                                    
REMARK 620 2 HIS B  75   NE2  92.2                                              
REMARK 620 3 ASP B 161   OD2  84.3 104.7                                        
REMARK 620 4 HIS B 165   NE2  92.4 144.1 111.2                                  
REMARK 620 5   F B 203   F   100.2  68.6 171.9  75.5                            
REMARK 620 6 HOH B 204   O   176.3  90.2  92.4  87.2  83.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: FEA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: FERRIC IRON (FE(III)), SIX FOLD COORDINATED        
REMARK 800  FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY            
REMARK 800  COMPETITIVELY HAMPERED                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FEB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: FERRIC IRON (FE(III)), SIX FOLD COORDINATED        
REMARK 800  FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY            
REMARK 800  COMPETITIVELY HAMPERED                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F A 203                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F B 203                   
DBREF  1BS3 A    1   201  UNP    P80293   SODM_PROFR       1    201             
DBREF  1BS3 B    1   201  UNP    P80293   SODM_PROFR       1    201             
SEQRES   1 A  201  ALA VAL TYR THR LEU PRO GLU LEU PRO TYR ASP TYR SER          
SEQRES   2 A  201  ALA LEU GLU PRO TYR ILE SER GLY GLU ILE MET GLU LEU          
SEQRES   3 A  201  HIS HIS ASP LYS HIS HIS LYS ALA TYR VAL ASP GLY ALA          
SEQRES   4 A  201  ASN THR ALA LEU ASP LYS LEU ALA GLU ALA ARG ASP LYS          
SEQRES   5 A  201  ALA ASP PHE GLY ALA ILE ASN LYS LEU GLU LYS ASP LEU          
SEQRES   6 A  201  ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS SER VAL PHE          
SEQRES   7 A  201  TRP LYS ASN MET ALA PRO LYS GLY SER ALA PRO GLU ARG          
SEQRES   8 A  201  PRO THR ASP GLU LEU GLY ALA ALA ILE ASP GLU PHE PHE          
SEQRES   9 A  201  GLY SER PHE ASP ASN MET LYS ALA GLN PHE THR ALA ALA          
SEQRES  10 A  201  ALA THR GLY ILE GLN GLY SER GLY TRP ALA SER LEU VAL          
SEQRES  11 A  201  TRP ASP PRO LEU GLY LYS ARG ILE ASN THR LEU GLN PHE          
SEQRES  12 A  201  TYR ASP HIS GLN ASN ASN LEU PRO ALA GLY SER ILE PRO          
SEQRES  13 A  201  LEU LEU GLN LEU ASP MET TRP GLU HIS ALA PHE TYR LEU          
SEQRES  14 A  201  GLN TYR LYS ASN VAL LYS GLY ASP TYR VAL LYS SER TRP          
SEQRES  15 A  201  TRP ASN VAL VAL ASN TRP ASP ASP VAL ALA LEU ARG PHE          
SEQRES  16 A  201  SER GLU ALA ARG VAL ALA                                      
SEQRES   1 B  201  ALA VAL TYR THR LEU PRO GLU LEU PRO TYR ASP TYR SER          
SEQRES   2 B  201  ALA LEU GLU PRO TYR ILE SER GLY GLU ILE MET GLU LEU          
SEQRES   3 B  201  HIS HIS ASP LYS HIS HIS LYS ALA TYR VAL ASP GLY ALA          
SEQRES   4 B  201  ASN THR ALA LEU ASP LYS LEU ALA GLU ALA ARG ASP LYS          
SEQRES   5 B  201  ALA ASP PHE GLY ALA ILE ASN LYS LEU GLU LYS ASP LEU          
SEQRES   6 B  201  ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS SER VAL PHE          
SEQRES   7 B  201  TRP LYS ASN MET ALA PRO LYS GLY SER ALA PRO GLU ARG          
SEQRES   8 B  201  PRO THR ASP GLU LEU GLY ALA ALA ILE ASP GLU PHE PHE          
SEQRES   9 B  201  GLY SER PHE ASP ASN MET LYS ALA GLN PHE THR ALA ALA          
SEQRES  10 B  201  ALA THR GLY ILE GLN GLY SER GLY TRP ALA SER LEU VAL          
SEQRES  11 B  201  TRP ASP PRO LEU GLY LYS ARG ILE ASN THR LEU GLN PHE          
SEQRES  12 B  201  TYR ASP HIS GLN ASN ASN LEU PRO ALA GLY SER ILE PRO          
SEQRES  13 B  201  LEU LEU GLN LEU ASP MET TRP GLU HIS ALA PHE TYR LEU          
SEQRES  14 B  201  GLN TYR LYS ASN VAL LYS GLY ASP TYR VAL LYS SER TRP          
SEQRES  15 B  201  TRP ASN VAL VAL ASN TRP ASP ASP VAL ALA LEU ARG PHE          
SEQRES  16 B  201  SER GLU ALA ARG VAL ALA                                      
HET     FE  A 202       1                                                       
HET      F  A 203       1                                                       
HET     FE  B 202       1                                                       
HET      F  B 203       1                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM       F FLUORIDE ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   4    F    2(F 1-)                                                      
FORMUL   7  HOH   *478(H2 O)                                                    
HELIX    1   1 GLY A   21  ASP A   29  1                                   9    
HELIX    2   2 HIS A   31  LYS A   52  1                                  22    
HELIX    3   3 ILE A   58  LYS A   80  1                                  23    
HELIX    4   4 ASP A   94  PHE A  104  1                                  11    
HELIX    5   5 PHE A  107  THR A  119  1                                  13    
HELIX    6   6 GLU A  164  ALA A  166  5                                   3    
HELIX    7   7 TYR A  168  TYR A  171  1                                   4    
HELIX    8   8 LYS A  175  VAL A  185  1                                  11    
HELIX    9   9 TRP A  188  ALA A  198  1                                  11    
HELIX   10  10 GLY B   21  ASP B   29  1                                   9    
HELIX   11  11 HIS B   31  LYS B   52  1                                  22    
HELIX   12  12 ILE B   58  LYS B   80  1                                  23    
HELIX   13  13 ASP B   94  PHE B  104  1                                  11    
HELIX   14  14 PHE B  107  THR B  119  1                                  13    
HELIX   15  15 GLU B  164  ALA B  166  5                                   3    
HELIX   16  16 TYR B  168  TYR B  171  1                                   4    
HELIX   17  17 LYS B  175  VAL B  185  1                                  11    
HELIX   18  18 TRP B  188  ARG B  199  1                                  12    
SHEET    1   A 3 ARG A 137  TYR A 144  0                                        
SHEET    2   A 3 GLY A 125  ASP A 132 -1  N  ASP A 132   O  ARG A 137           
SHEET    3   A 3 ILE A 155  ASP A 161 -1  N  LEU A 160   O  ALA A 127           
SHEET    1   B 3 ARG B 137  TYR B 144  0                                        
SHEET    2   B 3 GLY B 125  ASP B 132 -1  N  ASP B 132   O  ARG B 137           
SHEET    3   B 3 ILE B 155  ASP B 161 -1  N  LEU B 160   O  ALA B 127           
LINK        FE    FE A 202                 NE2 HIS A  27     1555   1555  2.17  
LINK        FE    FE A 202                 NE2 HIS A  75     1555   1555  2.15  
LINK        FE    FE A 202                 OD2 ASP A 161     1555   1555  1.83  
LINK        FE    FE A 202                 NE2 HIS A 165     1555   1555  2.09  
LINK        FE    FE A 202                 F     F A 203     1555   1555  1.89  
LINK        FE    FE A 202                 O   HOH A 204     1555   1555  2.10  
LINK         F     F A 203                 NE2 HIS A  75     1555   1555  2.09  
LINK        FE    FE B 202                 NE2 HIS B  27     1555   1555  2.15  
LINK        FE    FE B 202                 NE2 HIS B  75     1555   1555  2.18  
LINK        FE    FE B 202                 OD2 ASP B 161     1555   1555  1.85  
LINK        FE    FE B 202                 NE2 HIS B 165     1555   1555  2.16  
LINK        FE    FE B 202                 F     F B 203     1555   1555  1.80  
LINK        FE    FE B 202                 O   HOH B 204     1555   1555  2.10  
LINK         F     F B 203                 NE2 HIS B  75     1555   1555  2.26  
CISPEP   1 GLU A   16    PRO A   17          0         0.01                     
CISPEP   2 GLU B   16    PRO B   17          0        -0.07                     
SITE     1 FEA  7  FE A 202  HIS A  27  HIS A  75  ASP A 161                    
SITE     2 FEA  7 HIS A 165    F A 203  HOH A 204                               
SITE     1 FEB  7  FE B 202  HIS B  27  HIS B  75  ASP B 161                    
SITE     2 FEB  7 HIS B 165    F B 203  HOH B 204                               
SITE     1 AC1  6 HIS A  27  HIS A  75  ASP A 161  HIS A 165                    
SITE     2 AC1  6   F A 203  HOH A 204                                          
SITE     1 AC2  7 HIS A  27  TYR A  35  HIS A  75  ASP A 161                    
SITE     2 AC2  7 HIS A 165   FE A 202  HOH A 204                               
SITE     1 AC3  6 HIS B  27  HIS B  75  ASP B 161  HIS B 165                    
SITE     2 AC3  6   F B 203  HOH B 204                                          
SITE     1 AC4  7 HIS B  27  TYR B  35  HIS B  75  ASP B 161                    
SITE     2 AC4  7 HIS B 165   FE B 202  HOH B 204                               
CRYST1   79.420   85.280  108.400  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      0.012591  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011726  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009225        0.00000                         
MTRIX1   1  0.202800 -0.001900 -0.979200       58.19220    1                    
MTRIX2   1  0.003600 -1.000000  0.002700       32.91420    1                    
MTRIX3   1 -0.979200 -0.004000 -0.202800       71.53430    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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