GenomeNet

Database: PDB
Entry: 2C3P
LinkDB: 2C3P
Original site: 2C3P 
HEADER    OXIDOREDUCTASE                          11-OCT-05   2C3P              
TITLE     CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF                 
TITLE    2 PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO                
TITLE    3 AFRICANUS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE-FERREDOXIN OXIDOREDUCTASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.2.7.1;                                                         
COMPND   5 OTHER_DETAILS: COMPLEXED WITH IRON/SULFUR CLUSTER, THIAMIN           
COMPND   6  DIPHOSPHATE, CRYSTAL SOAKED 40 MINUTES WITH PYRUVATE                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO AFRICANUS;                        
SOURCE   3 ORGANISM_TAXID: 873                                                  
KEYWDS    OXIDOREDUCTASE, 4FE-4S, IRON, IRON-SULFUR, IRON-SULFUR                
KEYWDS   2 CLUSTER, PYRUVATE CATABOLISM, TPP-DEPENDENT ENZYME,                  
KEYWDS   3 METAL-BINDING, ELECTRON TRANSPORT                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CAVAZZA,C.CONTRERAS-MARTEL,L.PIEULLE,E.CHABRIERE,                   
AUTHOR   2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS                                  
REVDAT   2   24-FEB-09 2C3P    1       VERSN                                    
REVDAT   1   15-FEB-06 2C3P    0                                                
JRNL        AUTH   C.CAVAZZA,C.CONTRERAS-MARTEL,L.PIEULLE,E.CHABRIERE,          
JRNL        AUTH 2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS                          
JRNL        TITL   FLEXIBILITY OF THIAMINE DIPHOSPHATE REVEALED BY              
JRNL        TITL 2 KINETIC CRYSTALLOGRAPHIC STUDIES OF THE REACTION             
JRNL        TITL 3 OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE WITH                   
JRNL        TITL 4 PYRUVATE.                                                    
JRNL        REF    STRUCTURE                     V.  14   217 2006              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   16472741                                                     
JRNL        DOI    10.1016/J.STR.2005.10.013                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.CHABRIERE,X.VERNEDE,B.GUIGLIARELLI,M.-H.CHARON,            
REMARK   1  AUTH 2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE           
REMARK   1  TITL 2 OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE.                       
REMARK   1  REF    SCIENCE                       V.2559   294 2001              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1  PMID   11752578                                                     
REMARK   1  DOI    10.1126/SCIENCE.1066198                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5206462.79                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 111926                         
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) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5637                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 2.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.6                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17357                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.198                        
REMARK   3   BIN FREE R VALUE                    : 0.264                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.0                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 907                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18766                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 116                                     
REMARK   3   SOLVENT ATOMS            : 851                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.4                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.91                                                
REMARK   3    B22 (A**2) : 1.59                                                 
REMARK   3    B33 (A**2) : 2.33                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.6                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.2                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.96                            
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) : 2.40  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.38  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.03  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.31  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.379681                                             
REMARK   3   BSOL        : 33.4579                                              
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  : PARA_FES.PAR                                   
REMARK   3  PARAMETER FILE  3  : ITP.PAR                                        
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : PARA_FES.TOP                                   
REMARK   3  TOPOLOGY FILE  3   : ITP.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2C3P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25960.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 287.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979273                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 524442                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.01000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.03000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1KEK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG6000, 100MM MGCL2, 100MM          
REMARK 280  NA CACODYLATE PH 6                                                  
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       42.98300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.41100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.92000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.41100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.98300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.92000            
REMARK 290   SMTRY3   4  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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 125   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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   4      129.38   -178.42                                   
REMARK 500    SER A  87     -118.32     30.79                                   
REMARK 500    ALA A 118      -98.07   -132.62                                   
REMARK 500    PHE A 174      -59.33     62.58                                   
REMARK 500    ASN A 209      128.69   -175.37                                   
REMARK 500    ARG A 303      -64.69    -98.88                                   
REMARK 500    ARG A 329       53.54    -95.46                                   
REMARK 500    GLU A 353     -129.65   -140.50                                   
REMARK 500    LYS A 386       40.68     71.52                                   
REMARK 500    PRO A 414      155.80    -49.96                                   
REMARK 500    LYS A 589      -73.82    -52.59                                   
REMARK 500    ALA A 590     -172.05    -64.47                                   
REMARK 500    LYS A 593     -129.29    -75.82                                   
REMARK 500    ASP A 624       49.20   -146.41                                   
REMARK 500    ALA A 627      105.10    -57.65                                   
REMARK 500    GLU A 628      164.91    -48.11                                   
REMARK 500    THR A 629     -115.24    -73.08                                   
REMARK 500    LYS A 630       81.83    178.46                                   
REMARK 500    PRO A 633      177.80    -58.01                                   
REMARK 500    THR A 635     -151.32   -146.98                                   
REMARK 500    VAL A 642      -62.70   -121.80                                   
REMARK 500    LYS A 674       56.25     36.40                                   
REMARK 500    ALA A 846       49.74   -159.21                                   
REMARK 500    SER A 867      -91.10    -90.99                                   
REMARK 500    GLU A 899       48.11    -99.34                                   
REMARK 500    ASP A 968      -94.36   -115.46                                   
REMARK 500    ALA A1014       40.83   -158.51                                   
REMARK 500    LYS A1181     -102.30     74.62                                   
REMARK 500    ALA A1182      113.98     60.34                                   
REMARK 500    LYS A1231      -71.45    -21.73                                   
REMARK 500    SER B  87     -126.65     41.20                                   
REMARK 500    ALA B 118      -96.52   -126.16                                   
REMARK 500    PHE B 174      -61.91     68.54                                   
REMARK 500    HIS B 212       67.03   -159.24                                   
REMARK 500    ARG B 303      -62.12    -97.90                                   
REMARK 500    ARG B 329       57.93    -95.13                                   
REMARK 500    GLU B 353     -137.17   -103.72                                   
REMARK 500    THR B 629     -137.13    -70.35                                   
REMARK 500    GLU B 632      109.23    -51.85                                   
REMARK 500    VAL B 642      -50.87   -131.08                                   
REMARK 500    LYS B 674       58.20     28.76                                   
REMARK 500    ALA B 846       50.01   -159.04                                   
REMARK 500    SER B 867      -85.76    -92.04                                   
REMARK 500    SER B 900     -169.97   -121.21                                   
REMARK 500    ASP B 968      -95.78   -116.81                                   
REMARK 500    ALA B1014       44.11   -157.12                                   
REMARK 500    LYS B1181      -46.37     57.90                                   
REMARK 500    ALA B1182       81.62     45.97                                   
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                              MG A2237  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 963   OD1                                                    
REMARK 620 2 THR A 991   OG1  90.1                                              
REMARK 620 3 VAL A 993   O    92.7  78.7                                        
REMARK 620 4 1TP A2236   O13  95.8 171.1  94.3                                  
REMARK 620 5 1TP A2236   O23 169.1  90.5  98.1  84.9                            
REMARK 620 6 HOH A2308   O    83.3  85.3 163.6 101.9  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2237  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2379   O                                                      
REMARK 620 2 ASP B 963   OD1  81.9                                              
REMARK 620 3 THR B 991   OG1  89.5  92.9                                        
REMARK 620 4 VAL B 993   O   167.1  91.9  79.5                                  
REMARK 620 5 1TP B2236   O13 100.9  91.4 169.2  90.4                            
REMARK 620 6 1TP B2236   O22  91.0 167.8  97.0  97.0  80.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2238  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 985   OD1                                                    
REMARK 620 2 ALA A1056   O    71.4                                              
REMARK 620 3 SER A1063   OG   84.7  51.2                                        
REMARK 620 4 ASP A 983   OD2 107.7 147.8 159.4                                  
REMARK 620 5 PHE A1059   O   146.3  86.6 101.2  77.7                            
REMARK 620 6 GLY A1061   O   139.3 128.6  85.9  74.0  74.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2238  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B1061   O                                                      
REMARK 620 2 ASP B 983   OD2  78.4                                              
REMARK 620 3 ALA B1056   O   118.9 146.5                                        
REMARK 620 4 PHE B1059   O    68.0  74.1  85.8                                  
REMARK 620 5 ASN B 985   OD1 134.3 118.9  71.3 153.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2233  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 689   SG                                                     
REMARK 620 2 SF4 A2233  FE3  140.7                                              
REMARK 620 3 SF4 A2233  FE4  150.0  61.3                                        
REMARK 620 4 SF4 A2233   S2  114.6  54.7  55.4                                  
REMARK 620 5 SF4 A2233   S3  115.3 103.6  54.4 107.1                            
REMARK 620 6 SF4 A2233   S4  107.2  54.1 102.8 106.2 105.7                      
REMARK 620 7 SF4 A2233  FE2  142.4  59.7  59.8 102.4  55.1  53.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2233  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 A2233  FE1                                                     
REMARK 620 2 SF4 A2233  FE3   60.6                                              
REMARK 620 3 SF4 A2233  FE4   59.8  61.6                                        
REMARK 620 4 SF4 A2233   S1  102.4  54.6  54.9                                  
REMARK 620 5 SF4 A2233   S3   54.3 103.7  54.2 106.4                            
REMARK 620 6 SF4 A2233   S4   55.4  54.8 104.0 106.7 106.4                      
REMARK 620 7 CYS A 695   SG  151.6 140.8 139.9 105.9 114.9 115.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2233  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 A2233  FE1                                                     
REMARK 620 2 SF4 A2233  FE4   58.7                                              
REMARK 620 3 SF4 A2233   S1  101.6  53.8                                        
REMARK 620 4 SF4 A2233   S2   53.6  54.0 104.7                                  
REMARK 620 5 SF4 A2233   S4   54.9 101.3 105.8 105.8                            
REMARK 620 6 SF4 A2233  FE2   59.7  59.0  54.4 101.6  54.1                      
REMARK 620 7 CYS A 692   SG  154.4 140.4 104.0 117.9 117.2 139.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2233  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 755   SG                                                     
REMARK 620 2 SF4 A2233  FE1  144.3                                              
REMARK 620 3 SF4 A2233  FE3  142.2  60.0                                        
REMARK 620 4 SF4 A2233   S1  112.8 102.6  53.6                                  
REMARK 620 5 SF4 A2233   S2  110.5  54.1  53.9 104.5                            
REMARK 620 6 SF4 A2233   S3  114.9  54.8 102.9 107.2 106.2                      
REMARK 620 7 SF4 A2233  FE2  147.6  60.4  59.4  54.6 101.8  55.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2234  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 699   SG                                                     
REMARK 620 2 SF4 A2234  FE2  146.7                                              
REMARK 620 3 SF4 A2234  FE3  144.6  59.4                                        
REMARK 620 4 SF4 A2234  FE4  142.1  60.8  60.9                                  
REMARK 620 5 SF4 A2234   S2  110.7 102.6  54.5  54.9                            
REMARK 620 6 SF4 A2234   S3  113.2  54.4 102.1  54.1 106.6                      
REMARK 620 7 SF4 A2234   S4  114.3  54.1  54.4 103.6 105.9 105.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2234  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 751   SG                                                     
REMARK 620 2 SF4 A2234  FE1  145.6                                              
REMARK 620 3 SF4 A2234  FE3  147.4  60.7                                        
REMARK 620 4 SF4 A2234  FE4  139.7  59.9  61.0                                  
REMARK 620 5 SF4 A2234   S1  111.5 102.4  54.7  54.1                            
REMARK 620 6 SF4 A2234   S3  109.3  54.3 103.1  53.7 104.9                      
REMARK 620 7 SF4 A2234   S4  116.5  55.1  55.2 103.7 107.4 106.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2234  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 745   SG                                                     
REMARK 620 2 SF4 A2234  FE1  149.2                                              
REMARK 620 3 SF4 A2234  FE2  144.5  59.9                                        
REMARK 620 4 SF4 A2234  FE4  140.3  59.5  60.5                                  
REMARK 620 5 SF4 A2234   S1  109.0 101.7  54.6  53.9                            
REMARK 620 6 SF4 A2234   S2  112.6  54.1 102.6  54.1 105.2                      
REMARK 620 7 SF4 A2234   S4  117.1  54.6  54.3 102.6 106.5 105.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2234  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 748   SG                                                     
REMARK 620 2 SF4 A2234  FE1  140.0                                              
REMARK 620 3 SF4 A2234  FE2  139.1  59.3                                        
REMARK 620 4 SF4 A2234  FE3  155.1  59.6  58.5                                  
REMARK 620 5 SF4 A2234   S1  117.2 101.6  53.7  53.6                            
REMARK 620 6 SF4 A2234   S2  119.3  54.1 100.7  53.8 104.6                      
REMARK 620 7 SF4 A2234   S3  103.8  54.0  53.8 101.1 104.6 105.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2235  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 812   SG                                                     
REMARK 620 2 SF4 A2235  FE3  140.1                                              
REMARK 620 3 SF4 A2235  FE4  146.3  60.9                                        
REMARK 620 4 SF4 A2235   S2  111.1  54.2  54.2                                  
REMARK 620 5 SF4 A2235  FE2  148.9  60.1  57.0 100.0                            
REMARK 620 6 SF4 A2235   S3  115.9 104.0  53.8 104.7  54.2                      
REMARK 620 7 SF4 A2235   S4  112.4  54.8 101.2 107.4  54.2 104.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2235  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 A2235  FE3                                                     
REMARK 620 2 SF4 A2235  FE4   62.9                                              
REMARK 620 3 CYS A 840   SG  147.5 138.3                                        
REMARK 620 4 SF4 A2235  FE1   60.5  62.4 144.5                                  
REMARK 620 5 SF4 A2235   S1   54.8  55.5 111.4 103.9                            
REMARK 620 6 SF4 A2235   S3  104.4  56.0 108.1  54.2 109.7                      
REMARK 620 7 SF4 A2235   S4   55.3 106.8 114.9  55.5 106.7 105.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2235  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 A2235  FE4                                                     
REMARK 620 2 SF4 A2235   S2   53.8                                              
REMARK 620 3 SF4 A2235  FE1   59.7  54.4                                        
REMARK 620 4 SF4 A2235  FE2   56.3  99.5  59.3                                  
REMARK 620 5 SF4 A2235   S1   52.8 102.8 102.7  54.6                            
REMARK 620 6 SF4 A2235   S4  100.1 107.4  54.6  53.9 105.1                      
REMARK 620 7 CYS A 815   SG  149.6 113.0 139.7 147.4 117.6 110.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A2235  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1071   SG                                                     
REMARK 620 2 SF4 A2235  FE3  152.3                                              
REMARK 620 3 SF4 A2235   S2  119.1  53.5                                        
REMARK 620 4 SF4 A2235  FE1  142.9  59.3  54.2                                  
REMARK 620 5 SF4 A2235  FE2  137.6  60.7 102.9  60.6                            
REMARK 620 6 SF4 A2235   S1  113.0  54.3 104.0 103.5  56.9                      
REMARK 620 7 SF4 A2235   S3  105.3 102.4 104.4  53.5  55.7 110.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2233  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 689   SG                                                     
REMARK 620 2 SF4 B2233  FE3  140.0                                              
REMARK 620 3 SF4 B2233  FE2  150.6  62.4                                        
REMARK 620 4 SF4 B2233  FE4  142.9  59.5  58.2                                  
REMARK 620 5 SF4 B2233   S3  115.9 103.4  53.6  53.6                            
REMARK 620 6 SF4 B2233   S2  106.5  54.0 102.9  54.5 104.3                      
REMARK 620 7 SF4 B2233   S4  116.0  54.6  55.4 100.7 106.7 106.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2233  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 692   SG                                                     
REMARK 620 2 SF4 B2233  FE1  154.9                                              
REMARK 620 3 SF4 B2233  FE2  139.3  59.2                                        
REMARK 620 4 SF4 B2233  FE4  138.5  61.6  57.8                                  
REMARK 620 5 SF4 B2233   S1  102.9 102.2  52.1  54.0                            
REMARK 620 6 SF4 B2233   S2  118.1  55.1 101.2  55.7 107.5                      
REMARK 620 7 SF4 B2233   S4  117.8  53.8  53.9 101.8 102.1 106.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2233  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2233  FE1                                                     
REMARK 620 2 SF4 B2233  FE3   58.4                                              
REMARK 620 3 SF4 B2233  FE4   61.8  59.4                                        
REMARK 620 4 SF4 B2233   S1  102.4  53.2  54.9                                  
REMARK 620 5 SF4 B2233   S3   55.4 101.5  55.5 108.5                            
REMARK 620 6 SF4 B2233   S4   53.1  52.4 101.9 101.8 106.2                      
REMARK 620 7 CYS B 755   SG  141.5 142.1 150.0 115.1 115.9 108.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2233  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 695   SG                                                     
REMARK 620 2 SF4 B2233  FE1  149.7                                              
REMARK 620 3 SF4 B2233  FE3  139.8  58.9                                        
REMARK 620 4 SF4 B2233  FE2  143.5  60.0  62.8                                  
REMARK 620 5 SF4 B2233   S1  109.8 100.4  54.5  54.2                            
REMARK 620 6 SF4 B2233   S3  116.7  54.4 103.5  54.5 106.8                      
REMARK 620 7 SF4 B2233   S2  112.8  53.5  53.5 103.5 105.9 104.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2234  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 699   SG                                                     
REMARK 620 2 SF4 B2234   S4  107.6                                              
REMARK 620 3 SF4 B2234  FE2  139.0  53.6                                        
REMARK 620 4 SF4 B2234  FE4  149.6 102.8  61.3                                  
REMARK 620 5 SF4 B2234   S2  113.3 106.5  55.3  53.8                            
REMARK 620 6 SF4 B2234  FE3  144.2  54.5  60.1  59.9 102.1                      
REMARK 620 7 SF4 B2234   S3  117.2 105.7 103.5  54.8 105.8  54.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2234  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2234   S4                                                     
REMARK 620 2 SF4 B2234  FE1   54.7                                              
REMARK 620 3 SF4 B2234  FE2   53.8  60.6                                        
REMARK 620 4 SF4 B2234  FE4  102.7  59.6  61.4                                  
REMARK 620 5 CYS B 745   SG  115.8 149.4 142.2 141.4                            
REMARK 620 6 SF4 B2234   S1  105.2 102.3  54.0  55.2 108.4                      
REMARK 620 7 SF4 B2234   S2  106.0  54.4 104.1  54.7 113.6 107.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2234  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 748   SG                                                     
REMARK 620 2 SF4 B2234   S4  118.7                                              
REMARK 620 3 SF4 B2234  FE1  135.9  54.3                                        
REMARK 620 4 SF4 B2234  FE4  137.9 100.9  58.3                                  
REMARK 620 5 SF4 B2234   S2  100.8 105.1  53.1  52.1                            
REMARK 620 6 SF4 B2234  FE3  159.4  54.3  59.3  58.7  99.7                      
REMARK 620 7 SF4 B2234   S1  120.9 105.6 101.0  54.0 103.3  53.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2234  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 751   SG                                                     
REMARK 620 2 SF4 B2234  FE1  144.1                                              
REMARK 620 3 SF4 B2234  FE2  142.9  60.4                                        
REMARK 620 4 SF4 B2234   S2  110.1  54.8  55.1                                  
REMARK 620 5 SF4 B2234  FE3  146.7  60.4  60.0 103.2                            
REMARK 620 6 SF4 B2234   S1  113.6 102.2  53.2 105.4  54.2                      
REMARK 620 7 SF4 B2234   S2  114.4  54.6 102.7 106.6  54.4 106.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2235  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2235   S4                                                     
REMARK 620 2 SF4 B2235  FE3   54.0                                              
REMARK 620 3 SF4 B2235  FE4  100.6  60.4                                        
REMARK 620 4 SF4 B2235  FE2   54.0  59.9  57.3                                  
REMARK 620 5 SF4 B2235   S3  104.2 103.9  55.0  53.9                            
REMARK 620 6 SF4 B2235   S2  106.1  53.9  53.8  99.8 105.8                      
REMARK 620 7 CYS B 812   SG  112.2 141.2 147.2 147.3 114.8 112.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2235  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2235   S4                                                     
REMARK 620 2 SF4 B2235  FE3   54.7                                              
REMARK 620 3 SF4 B2235  FE4  105.2  62.3                                        
REMARK 620 4 SF4 B2235   S1  105.5  54.0  55.9                                  
REMARK 620 5 CYS B 840   SG  116.1 147.5 138.7 111.5                            
REMARK 620 6 SF4 B2235  FE1   55.1  61.1  61.8 103.8 144.5                      
REMARK 620 7 SF4 B2235   S3  105.6 105.3  57.0 110.8 107.2  54.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2235  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B2235   S4                                                     
REMARK 620 2 CYS B 815   SG  106.7                                              
REMARK 620 3 SF4 B2235  FE4   99.5 153.6                                        
REMARK 620 4 SF4 B2235   S1  104.8 120.2  53.6                                  
REMARK 620 5 SF4 B2235  FE1   53.9 137.2  59.2 102.4                            
REMARK 620 6 SF4 B2235  FE2   53.6 145.6  56.6  54.4  59.0                      
REMARK 620 7 SF4 B2235   S2  107.0 113.8  53.5 103.3  54.8  99.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B2235  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1071   SG                                                     
REMARK 620 2 SF4 B2235  FE3  150.5                                              
REMARK 620 3 SF4 B2235   S1  112.8  53.6                                        
REMARK 620 4 SF4 B2235  FE1  143.3  60.4 103.5                                  
REMARK 620 5 SF4 B2235  FE2  138.1  61.1  56.3  60.9                            
REMARK 620 6 SF4 B2235   S3  106.6 102.8 109.3  53.6  55.0                      
REMARK 620 7 SF4 B2235   S2  117.5  54.3 104.1  55.6 104.2 106.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2237                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2237                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2234                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A2235                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1TP A2236                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2234                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B2235                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1TP B2236                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B0P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN                            
REMARK 900  OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS                         
REMARK 900 RELATED ID: 1KEK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE FREE RADICAL                               
REMARK 900  INTERMEDIATE OFPYRUVATE:FERREDOXIN OXIDOREDUCTASE                   
REMARK 900 RELATED ID: 2PDA   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  PYRUVATE- FERREDOXIN OXIDOREDUCTASE FROM                            
REMARK 900  DESULFOVIBRIO AFRICANUS AND PYRUVATE.                               
REMARK 900 RELATED ID: 2C3M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN                            
REMARK 900  OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS                         
REMARK 900 RELATED ID: 2C3O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE FREE RADICAL                               
REMARK 900  INTERMEDIATE OF PYRUVATE:FERREDOXIN                                 
REMARK 900  OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS                         
REMARK 900 RELATED ID: 2C3U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN                            
REMARK 900  OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS,                        
REMARK 900  OXYGEN INHIBITED FORM                                               
REMARK 900 RELATED ID: 2C3Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE RADICAL FORM OF                            
REMARK 900  PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM                             
REMARK 900  DESULFOVIBRIO AFRICANUS                                             
REMARK 900 RELATED ID: 2C42   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN                            
REMARK 900  OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS                         
DBREF  2C3P A    2  1232  UNP    P94692   P94692_DESAF     2   1232             
DBREF  2C3P B    2  1232  UNP    P94692   P94692_DESAF     2   1232             
SEQRES   1 A 1231  GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR          
SEQRES   2 A 1231  ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE          
SEQRES   3 A 1231  TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA          
SEQRES   4 A 1231  ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY          
SEQRES   5 A 1231  GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY          
SEQRES   6 A 1231  ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA          
SEQRES   7 A 1231  LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU          
SEQRES   8 A 1231  MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU          
SEQRES   9 A 1231  PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA          
SEQRES  10 A 1231  HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR          
SEQRES  11 A 1231  ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER          
SEQRES  12 A 1231  SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS          
SEQRES  13 A 1231  LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE          
SEQRES  14 A 1231  PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE          
SEQRES  15 A 1231  GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN          
SEQRES  16 A 1231  GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN          
SEQRES  17 A 1231  PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO          
SEQRES  18 A 1231  ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR          
SEQRES  19 A 1231  TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN          
SEQRES  20 A 1231  LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE          
SEQRES  21 A 1231  ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL          
SEQRES  22 A 1231  SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE          
SEQRES  23 A 1231  ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE          
SEQRES  24 A 1231  LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE          
SEQRES  25 A 1231  PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL          
SEQRES  26 A 1231  LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO          
SEQRES  27 A 1231  LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY          
SEQRES  28 A 1231  GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU          
SEQRES  29 A 1231  GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL          
SEQRES  30 A 1231  TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR          
SEQRES  31 A 1231  VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO          
SEQRES  32 A 1231  VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR          
SEQRES  33 A 1231  ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR          
SEQRES  34 A 1231  VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP          
SEQRES  35 A 1231  ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP          
SEQRES  36 A 1231  SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG          
SEQRES  37 A 1231  PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN          
SEQRES  38 A 1231  ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL          
SEQRES  39 A 1231  GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY          
SEQRES  40 A 1231  THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP          
SEQRES  41 A 1231  MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE          
SEQRES  42 A 1231  ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL          
SEQRES  43 A 1231  LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN          
SEQRES  44 A 1231  MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL          
SEQRES  45 A 1231  LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER          
SEQRES  46 A 1231  ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL          
SEQRES  47 A 1231  LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER          
SEQRES  48 A 1231  LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA          
SEQRES  49 A 1231  PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE          
SEQRES  50 A 1231  PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY          
SEQRES  51 A 1231  ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG          
SEQRES  52 A 1231  PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL          
SEQRES  53 A 1231  ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE          
SEQRES  54 A 1231  GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA          
SEQRES  55 A 1231  ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY          
SEQRES  56 A 1231  ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS          
SEQRES  57 A 1231  GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR          
SEQRES  58 A 1231  LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS          
SEQRES  59 A 1231  PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP          
SEQRES  60 A 1231  THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA          
SEQRES  61 A 1231  ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP          
SEQRES  62 A 1231  SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU          
SEQRES  63 A 1231  PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR          
SEQRES  64 A 1231  VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE          
SEQRES  65 A 1231  ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA          
SEQRES  66 A 1231  SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY          
SEQRES  67 A 1231  GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA          
SEQRES  68 A 1231  ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA          
SEQRES  69 A 1231  ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU          
SEQRES  70 A 1231  GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN          
SEQRES  71 A 1231  GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS          
SEQRES  72 A 1231  GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN          
SEQRES  73 A 1231  LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP          
SEQRES  74 A 1231  LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP          
SEQRES  75 A 1231  GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS          
SEQRES  76 A 1231  VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET          
SEQRES  77 A 1231  ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER          
SEQRES  78 A 1231  LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA          
SEQRES  79 A 1231  ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET          
SEQRES  80 A 1231  VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER          
SEQRES  81 A 1231  MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS          
SEQRES  82 A 1231  GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA          
SEQRES  83 A 1231  TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET          
SEQRES  84 A 1231  GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER          
SEQRES  85 A 1231  GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA          
SEQRES  86 A 1231  ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA          
SEQRES  87 A 1231  PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN          
SEQRES  88 A 1231  ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA          
SEQRES  89 A 1231  LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL          
SEQRES  90 A 1231  ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE          
SEQRES  91 A 1231  PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY          
SEQRES  92 A 1231  SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG          
SEQRES  93 A 1231  ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU          
SEQRES  94 A 1231  ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN          
SEQRES  95 A 1231  GLY ASP LEU SER LYS ARG THR LYS LYS                          
SEQRES   1 B 1231  GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR          
SEQRES   2 B 1231  ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE          
SEQRES   3 B 1231  TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA          
SEQRES   4 B 1231  ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY          
SEQRES   5 B 1231  GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY          
SEQRES   6 B 1231  ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA          
SEQRES   7 B 1231  LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU          
SEQRES   8 B 1231  MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU          
SEQRES   9 B 1231  PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA          
SEQRES  10 B 1231  HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR          
SEQRES  11 B 1231  ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER          
SEQRES  12 B 1231  SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS          
SEQRES  13 B 1231  LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE          
SEQRES  14 B 1231  PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE          
SEQRES  15 B 1231  GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN          
SEQRES  16 B 1231  GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN          
SEQRES  17 B 1231  PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO          
SEQRES  18 B 1231  ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR          
SEQRES  19 B 1231  TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN          
SEQRES  20 B 1231  LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE          
SEQRES  21 B 1231  ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL          
SEQRES  22 B 1231  SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE          
SEQRES  23 B 1231  ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE          
SEQRES  24 B 1231  LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE          
SEQRES  25 B 1231  PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL          
SEQRES  26 B 1231  LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO          
SEQRES  27 B 1231  LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY          
SEQRES  28 B 1231  GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU          
SEQRES  29 B 1231  GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL          
SEQRES  30 B 1231  TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR          
SEQRES  31 B 1231  VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO          
SEQRES  32 B 1231  VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR          
SEQRES  33 B 1231  ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR          
SEQRES  34 B 1231  VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP          
SEQRES  35 B 1231  ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP          
SEQRES  36 B 1231  SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG          
SEQRES  37 B 1231  PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN          
SEQRES  38 B 1231  ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL          
SEQRES  39 B 1231  GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY          
SEQRES  40 B 1231  THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP          
SEQRES  41 B 1231  MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE          
SEQRES  42 B 1231  ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL          
SEQRES  43 B 1231  LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN          
SEQRES  44 B 1231  MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL          
SEQRES  45 B 1231  LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER          
SEQRES  46 B 1231  ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL          
SEQRES  47 B 1231  LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER          
SEQRES  48 B 1231  LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA          
SEQRES  49 B 1231  PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE          
SEQRES  50 B 1231  PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY          
SEQRES  51 B 1231  ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG          
SEQRES  52 B 1231  PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL          
SEQRES  53 B 1231  ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE          
SEQRES  54 B 1231  GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA          
SEQRES  55 B 1231  ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY          
SEQRES  56 B 1231  ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS          
SEQRES  57 B 1231  GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR          
SEQRES  58 B 1231  LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS          
SEQRES  59 B 1231  PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP          
SEQRES  60 B 1231  THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA          
SEQRES  61 B 1231  ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP          
SEQRES  62 B 1231  SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU          
SEQRES  63 B 1231  PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR          
SEQRES  64 B 1231  VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE          
SEQRES  65 B 1231  ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA          
SEQRES  66 B 1231  SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY          
SEQRES  67 B 1231  GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA          
SEQRES  68 B 1231  ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA          
SEQRES  69 B 1231  ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU          
SEQRES  70 B 1231  GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN          
SEQRES  71 B 1231  GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS          
SEQRES  72 B 1231  GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN          
SEQRES  73 B 1231  LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP          
SEQRES  74 B 1231  LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP          
SEQRES  75 B 1231  GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS          
SEQRES  76 B 1231  VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET          
SEQRES  77 B 1231  ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER          
SEQRES  78 B 1231  LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA          
SEQRES  79 B 1231  ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET          
SEQRES  80 B 1231  VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER          
SEQRES  81 B 1231  MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS          
SEQRES  82 B 1231  GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA          
SEQRES  83 B 1231  TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET          
SEQRES  84 B 1231  GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER          
SEQRES  85 B 1231  GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA          
SEQRES  86 B 1231  ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA          
SEQRES  87 B 1231  PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN          
SEQRES  88 B 1231  ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA          
SEQRES  89 B 1231  LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL          
SEQRES  90 B 1231  ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE          
SEQRES  91 B 1231  PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY          
SEQRES  92 B 1231  SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG          
SEQRES  93 B 1231  ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU          
SEQRES  94 B 1231  ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN          
SEQRES  95 B 1231  GLY ASP LEU SER LYS ARG THR LYS LYS                          
HET     MG  A2237       1                                                       
HET     CA  A2238       1                                                       
HET     MG  B2237       1                                                       
HET     CA  B2238       1                                                       
HET    SF4  A2233       8                                                       
HET    SF4  A2234       8                                                       
HET    SF4  A2235       8                                                       
HET    1TP  A2236      32                                                       
HET    SF4  B2233       8                                                       
HET    SF4  B2234       8                                                       
HET    SF4  B2235       8                                                       
HET    1TP  B2236      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     1TP 1-(2-{(2S,4R,5R)-3-[(4-AMINO-2-                                  
HETNAM   2 1TP  METHYLPYRIMIDIN-5-YL)METHYL]-2-[(1S)-1-CARBOXY-1-               
HETNAM   3 1TP  HYDROXYETHYL]-4-METHYL-1,3-THIAZOLIDIN-5-YL}ETHOXY)-1,          
HETNAM   4 1TP  1,3,3-TETRAHYDROXY-1LAMBDA~5~-DIPHOSPHOX-1-EN-                  
HETNAM   5 1TP  2-IUM 3-OXIDE                                                   
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   7  SF4    6(FE4 S4 2+)                                                 
FORMUL  10  1TP    2()                                                          
FORMUL  15  HOH   *851(H2 O1)                                                   
HELIX    1   1 GLY A   10  SER A   22  1                                  13    
HELIX    2   2 SER A   33  GLY A   47  1                                  15    
HELIX    3   3 SER A   63  ALA A   77  1                                  15    
HELIX    4   4 ALA A   86  GLU A  103  1                                  18    
HELIX    5   5 HIS A  127  ALA A  133  1                                   7    
HELIX    6   6 SER A  145  ASN A  164  1                                  20    
HELIX    7   7 ASP A  187  VAL A  195  1                                   9    
HELIX    8   8 ASN A  196  SER A  207  1                                  12    
HELIX    9   9 ILE A  224  ALA A  231  1                                   8    
HELIX   10  10 ALA A  232  GLY A  255  1                                  24    
HELIX   11  11 SER A  278  ALA A  292  1                                  15    
HELIX   12  12 VAL A  309  ALA A  316  1                                   8    
HELIX   13  13 ASP A  338  GLY A  352  1                                  15    
HELIX   14  14 LEU A  365  LYS A  368  5                                   4    
HELIX   15  15 SER A  371  GLY A  384  1                                  14    
HELIX   16  16 GLY A  429  ASN A  444  1                                  16    
HELIX   17  17 ALA A  493  TYR A  498  1                                   6    
HELIX   18  18 SER A  518  LEU A  526  1                                   9    
HELIX   19  19 PRO A  527  LYS A  537  1                                  11    
HELIX   20  20 ASP A  545  VAL A  553  1                                   9    
HELIX   21  21 ILE A  559  ALA A  571  1                                  13    
HELIX   22  22 PRO A  575  ALA A  590  1                                  16    
HELIX   23  23 GLU A  596  LEU A  613  1                                  18    
HELIX   24  24 PRO A  619  ALA A  625  5                                   7    
HELIX   25  25 ASN A  636  VAL A  642  1                                   7    
HELIX   26  26 VAL A  642  THR A  648  1                                   7    
HELIX   27  27 GLN A  650  LEU A  654  5                                   5    
HELIX   28  28 PRO A  655  PHE A  659  5                                   5    
HELIX   29  29 GLY A  668  GLU A  673  5                                   6    
HELIX   30  30 ASN A  693  CYS A  699  1                                   7    
HELIX   31  31 LYS A  710  VAL A  715  5                                   6    
HELIX   32  32 GLY A  728  LYS A  732  5                                   5    
HELIX   33  33 GLY A  749  CYS A  755  1                                   7    
HELIX   34  34 LEU A  767  ARG A  783  1                                  17    
HELIX   35  35 SER A  795  GLN A  800  1                                   6    
HELIX   36  36 GLU A  817  GLY A  829  1                                  13    
HELIX   37  37 GLY A  839  SER A  847  1                                   9    
HELIX   38  38 ASP A  871  GLU A  899  1                                  29    
HELIX   39  39 SER A  903  GLY A  916  1                                  14    
HELIX   40  40 ASP A  919  LEU A  934  1                                  16    
HELIX   41  41 ASP A  939  ALA A  947  1                                   9    
HELIX   42  42 MET A  948  TYR A  952  5                                   5    
HELIX   43  43 ASP A  963  ASP A  968  1                                   6    
HELIX   44  44 GLY A  970  SER A  980  1                                  11    
HELIX   45  45 ASP A 1024  THR A 1031  1                                   8    
HELIX   46  46 SER A 1045  PHE A 1059  1                                  15    
HELIX   47  47 CYS A 1071  GLY A 1075  5                                   5    
HELIX   48  48 GLY A 1079  GLY A 1081  5                                   3    
HELIX   49  49 LYS A 1082  SER A 1093  1                                  12    
HELIX   50  50 ASP A 1102  ALA A 1107  1                                   6    
HELIX   51  51 SER A 1123  ALA A 1130  1                                   8    
HELIX   52  52 GLN A 1131  PHE A 1141  1                                  11    
HELIX   53  53 PHE A 1141  THR A 1169  1                                  29    
HELIX   54  54 THR A 1219  THR A 1230  1                                  12    
HELIX   55  55 GLY B   10  SER B   22  1                                  13    
HELIX   56  56 SER B   33  GLN B   46  1                                  14    
HELIX   57  57 SER B   63  ALA B   77  1                                  15    
HELIX   58  58 ALA B   86  GLU B  103  1                                  18    
HELIX   59  59 HIS B  127  ALA B  133  1                                   7    
HELIX   60  60 SER B  145  ASN B  164  1                                  20    
HELIX   61  61 ASP B  187  SER B  193  1                                   7    
HELIX   62  62 ASN B  196  LYS B  206  1                                  11    
HELIX   63  63 ILE B  224  ALA B  231  1                                   8    
HELIX   64  64 ALA B  232  GLY B  255  1                                  24    
HELIX   65  65 SER B  278  ALA B  292  1                                  15    
HELIX   66  66 VAL B  309  ALA B  315  1                                   7    
HELIX   67  67 ASP B  338  GLY B  352  1                                  15    
HELIX   68  68 GLY B  364  LYS B  368  5                                   5    
HELIX   69  69 SER B  371  MET B  382  1                                  12    
HELIX   70  70 GLY B  429  THR B  445  1                                  17    
HELIX   71  71 ASN B  491  VAL B  495  5                                   5    
HELIX   72  72 SER B  518  LEU B  526  1                                   9    
HELIX   73  73 PRO B  527  LYS B  537  1                                  11    
HELIX   74  74 ASP B  545  VAL B  553  1                                   9    
HELIX   75  75 ILE B  559  ALA B  571  1                                  13    
HELIX   76  76 PRO B  575  ALA B  590  1                                  16    
HELIX   77  77 GLY B  595  LEU B  613  1                                  19    
HELIX   78  78 PRO B  619  ALA B  625  5                                   7    
HELIX   79  79 ASN B  636  VAL B  642  1                                   7    
HELIX   80  80 VAL B  642  THR B  648  1                                   7    
HELIX   81  81 GLN B  650  LEU B  654  5                                   5    
HELIX   82  82 PRO B  655  PHE B  659  5                                   5    
HELIX   83  83 GLY B  668  GLU B  673  5                                   6    
HELIX   84  84 PRO B  686  CYS B  689  5                                   4    
HELIX   85  85 ASN B  693  CYS B  699  1                                   7    
HELIX   86  86 GLU B  712  VAL B  715  5                                   4    
HELIX   87  87 GLY B  728  LYS B  732  5                                   5    
HELIX   88  88 GLY B  749  CYS B  755  1                                   7    
HELIX   89  89 GLN B  770  ARG B  783  1                                  14    
HELIX   90  90 SER B  795  GLN B  800  1                                   6    
HELIX   91  91 GLU B  817  GLY B  829  1                                  13    
HELIX   92  92 GLY B  839  SER B  847  1                                   9    
HELIX   93  93 ASP B  871  GLU B  899  1                                  29    
HELIX   94  94 SER B  903  LYS B  917  1                                  15    
HELIX   95  95 ASP B  919  LEU B  934  1                                  16    
HELIX   96  96 ASP B  939  ALA B  947  1                                   9    
HELIX   97  97 MET B  948  TYR B  952  5                                   5    
HELIX   98  98 ASP B  963  ASP B  968  1                                   6    
HELIX   99  99 GLY B  970  SER B  980  1                                  11    
HELIX  100 100 ASP B 1024  THR B 1031  1                                   8    
HELIX  101 101 SER B 1045  PHE B 1059  1                                  15    
HELIX  102 102 CYS B 1071  GLY B 1075  5                                   5    
HELIX  103 103 GLY B 1079  GLY B 1081  5                                   3    
HELIX  104 104 LYS B 1082  SER B 1093  1                                  12    
HELIX  105 105 ASP B 1102  GLN B 1108  1                                   7    
HELIX  106 106 SER B 1123  ALA B 1130  1                                   8    
HELIX  107 107 GLN B 1131  PHE B 1141  1                                  11    
HELIX  108 108 PHE B 1141  THR B 1169  1                                  29    
HELIX  109 109 THR B 1219  THR B 1230  1                                  12    
SHEET    1  AA 8 MET A   5  ASP A   9  0                                        
SHEET    2  AA 8 ILE A 180  GLU A 184 -1  O  GLN A 181   N  THR A   8           
SHEET    3  AA 8 PHE A 448  SER A 454 -1  O  ALA A 449   N  LYS A 182           
SHEET    4  AA 8 ILE A 463  GLY A 471 -1  O  ILE A 465   N  SER A 454           
SHEET    5  AA 8 ILE A 418  LEU A 425 -1  O  ILE A 418   N  PHE A 470           
SHEET    6  AA 8 TYR A 486  CYS A 489  1  O  TYR A 486   N  GLN A 421           
SHEET    7  AA 8 THR A 509  ASN A 513  1  O  THR A 509   N  VAL A 487           
SHEET    8  AA 8 LYS A 540  ILE A 544  1  O  LYS A 540   N  PHE A 510           
SHEET    1  AB 7 THR A  57  GLU A  60  0                                        
SHEET    2  AB 7 VAL A  24  ILE A  27  1  O  ALA A  25   N  ARG A  59           
SHEET    3  AB 7 THR A  81  THR A  85  1  O  THR A  82   N  ALA A  26           
SHEET    4  AB 7 VAL A 108  ALA A 113  1  O  VAL A 108   N  THR A  83           
SHEET    5  AB 7 PHE A 167  ASP A 172  1  O  PHE A 167   N  PHE A 109           
SHEET    6  AB 7 ALA A 139  ALA A 142  1  O  ALA A 139   N  MET A 168           
SHEET    7  AB 7 LEU A 304  ARG A 306 -1  N  TYR A 305   O  MET A 140           
SHEET    1  AC 9 VAL A 215  ARG A 216  0                                        
SHEET    2  AC 9 ALA B 863  ASN B 866  1  O  TRP B 864   N  ARG A 216           
SHEET    3  AC 9 MET B 832  ASN B 836  1  O  MET B 832   N  ALA B 863           
SHEET    4  AC 9 SER B 956  GLY B 962  1  O  SER B 956   N  PHE B 833           
SHEET    5  AC 9 ASN B 985  ASP B 990  1  O  ASN B 985   N  ILE B 959           
SHEET    6  AC 9 SER B1063  TYR B1068  1  O  SER B1063   N  VAL B 986           
SHEET    7  AC 9 TYR B1036  VAL B1040  1  O  TYR B1036   N  LEU B1064           
SHEET    8  AC 9 PHE B1099  TYR B1101 -1  O  PHE B1099   N  THR B1039           
SHEET    9  AC 9 PHE B1113  LEU B1115 -1  O  GLN B1114   N  ARG B1100           
SHEET    1  AD 2 THR A 218  ALA A 219  0                                        
SHEET    2  AD 2 ALA B 120  LEU B 121  1  N  LEU B 121   O  THR A 218           
SHEET    1  AE 6 PHE A 261  GLY A 265  0                                        
SHEET    2  AE 6 ILE A 297  VAL A 302 -1  O  LEU A 299   N  VAL A 264           
SHEET    3  AE 6 ARG A 271  SER A 275  1  O  ARG A 271   N  GLY A 298           
SHEET    4  AE 6 VAL A 323  ASP A 328  1  O  VAL A 323   N  VAL A 272           
SHEET    5  AE 6 LYS A 357  TYR A 363  1  O  LYS A 357   N  ILE A 324           
SHEET    6  AE 6 PHE A 390  VAL A 392  1  O  PHE A 390   N  ARG A 362           
SHEET    1  AF 2 ASN A 680  TRP A 684  0                                        
SHEET    2  AF 2 LEU A 762  PRO A 766 -1  O  VAL A 763   N  GLN A 683           
SHEET    1  AG 3 ILE A 704  ALA A 709  0                                        
SHEET    2  AG 3 LYS A 735  ILE A 740 -1  O  LYS A 735   N  ALA A 709           
SHEET    3  AG 3 LEU A 724  GLU A 725 -1  O  LEU A 724   N  PHE A 736           
SHEET    1  AH 9 PHE A1113  LEU A1115  0                                        
SHEET    2  AH 9 PHE A1099  TYR A1101 -1  O  ARG A1100   N  GLN A1114           
SHEET    3  AH 9 TYR A1036  VAL A1040 -1  O  VAL A1037   N  TYR A1101           
SHEET    4  AH 9 SER A1063  TYR A1068  1  O  LEU A1064   N  ALA A1038           
SHEET    5  AH 9 ASN A 985  ASP A 990  1  O  VAL A 986   N  VAL A1065           
SHEET    6  AH 9 SER A 956  GLY A 962  1  O  VAL A 957   N  ASN A 985           
SHEET    7  AH 9 MET A 832  ASN A 836  1  O  PHE A 833   N  TRP A 958           
SHEET    8  AH 9 ALA A 863  ASN A 866  1  O  ALA A 863   N  ILE A 834           
SHEET    9  AH 9 VAL B 215  ARG B 216  1  O  ARG B 216   N  ASN A 866           
SHEET    1  BA 8 LYS B   3  ASP B   9  0                                        
SHEET    2  BA 8 ILE B 180  LEU B 186 -1  O  GLN B 181   N  THR B   8           
SHEET    3  BA 8 PHE B 448  SER B 454 -1  O  ALA B 449   N  LYS B 182           
SHEET    4  BA 8 ILE B 463  GLY B 471 -1  O  ILE B 465   N  SER B 454           
SHEET    5  BA 8 ILE B 418  LEU B 425 -1  O  ILE B 418   N  PHE B 470           
SHEET    6  BA 8 TYR B 486  CYS B 489  1  O  TYR B 486   N  GLN B 421           
SHEET    7  BA 8 THR B 509  ASN B 513  1  O  THR B 509   N  VAL B 487           
SHEET    8  BA 8 LYS B 540  ILE B 544  1  O  LYS B 540   N  PHE B 510           
SHEET    1  BB 7 THR B  57  GLU B  60  0                                        
SHEET    2  BB 7 VAL B  24  ILE B  27  1  O  ALA B  25   N  ARG B  59           
SHEET    3  BB 7 THR B  81  THR B  85  1  O  THR B  82   N  ALA B  26           
SHEET    4  BB 7 VAL B 108  ALA B 113  1  O  VAL B 108   N  THR B  83           
SHEET    5  BB 7 PHE B 167  ASP B 172  1  O  PHE B 167   N  PHE B 109           
SHEET    6  BB 7 ALA B 139  ALA B 142  1  O  ALA B 139   N  MET B 168           
SHEET    7  BB 7 LEU B 304  ARG B 306 -1  N  TYR B 305   O  MET B 140           
SHEET    1  BC 6 PHE B 261  GLY B 265  0                                        
SHEET    2  BC 6 ILE B 297  VAL B 302 -1  O  LEU B 299   N  VAL B 264           
SHEET    3  BC 6 ARG B 271  SER B 275  1  O  ARG B 271   N  GLY B 298           
SHEET    4  BC 6 VAL B 323  ASP B 328  1  O  VAL B 323   N  VAL B 272           
SHEET    5  BC 6 LYS B 357  ARG B 362  1  O  LYS B 357   N  ILE B 324           
SHEET    6  BC 6 PHE B 390  THR B 391  1  O  PHE B 390   N  ARG B 362           
SHEET    1  BD 2 ASN B 680  TRP B 684  0                                        
SHEET    2  BD 2 LEU B 762  PRO B 766 -1  O  VAL B 763   N  GLN B 683           
SHEET    1  BE 3 ILE B 704  LYS B 710  0                                        
SHEET    2  BE 3 TYR B 734  ILE B 740 -1  O  LYS B 735   N  ALA B 709           
SHEET    3  BE 3 LEU B 724  GLU B 725 -1  O  LEU B 724   N  PHE B 736           
SSBOND   1 CYS A 1195    CYS A 1212                          1555   1555  2.02  
SSBOND   2 CYS B 1195    CYS B 1212                          1555   1555  2.03  
LINK        FE1  SF4 A2233                 SG  CYS A 689     1555   1555  2.30  
LINK        FE2  SF4 A2233                 SG  CYS A 695     1555   1555  2.31  
LINK        FE3  SF4 A2233                 SG  CYS A 692     1555   1555  2.31  
LINK        FE4  SF4 A2233                 SG  CYS A 755     1555   1555  2.29  
LINK        FE1  SF4 A2234                 SG  CYS A 699     1555   1555  2.30  
LINK        FE2  SF4 A2234                 SG  CYS A 751     1555   1555  2.32  
LINK        FE3  SF4 A2234                 SG  CYS A 745     1555   1555  2.28  
LINK        FE4  SF4 A2234                 SG  CYS A 748     1555   1555  2.32  
LINK        FE1  SF4 A2235                 SG  CYS A 812     1555   1555  2.26  
LINK        FE2  SF4 A2235                 SG  CYS A 840     1555   1555  2.30  
LINK        FE3  SF4 A2235                 SG  CYS A 815     1555   1555  2.29  
LINK        FE4  SF4 A2235                 SG  CYS A1071     1555   1555  2.30  
LINK        MG    MG A2237                 OD1 ASP A 963     1555   1555  2.03  
LINK        MG    MG A2237                 OG1 THR A 991     1555   1555  2.27  
LINK        MG    MG A2237                 O   VAL A 993     1555   1555  2.14  
LINK        MG    MG A2237                 O13 1TP A2236     1555   1555  2.08  
LINK        MG    MG A2237                 O23 1TP A2236     1555   1555  2.09  
LINK        MG    MG A2237                 O   HOH A2308     1555   1555  2.11  
LINK        CA    CA A2238                 OD1 ASN A 985     1555   1555  2.78  
LINK        CA    CA A2238                 O   GLY A1061     1555   1555  2.97  
LINK        CA    CA A2238                 O   PHE A1059     1555   1555  2.80  
LINK        CA    CA A2238                 OD2 ASP A 983     1555   1555  2.84  
LINK        CA    CA A2238                 OG  SER A1063     1555   1555  3.13  
LINK        CA    CA A2238                 O   ALA A1056     1555   1555  2.93  
LINK        FE1  SF4 B2233                 SG  CYS B 689     1555   1555  2.29  
LINK        FE4  SF4 B2233                 SG  CYS B 695     1555   1555  2.30  
LINK        FE2  SF4 B2233                 SG  CYS B 755     1555   1555  2.29  
LINK        FE3  SF4 B2233                 SG  CYS B 692     1555   1555  2.30  
LINK        FE2  SF4 B2234                 SG  CYS B 748     1555   1555  2.31  
LINK        FE3  SF4 B2234                 SG  CYS B 745     1555   1555  2.29  
LINK        FE1  SF4 B2234                 SG  CYS B 699     1555   1555  2.34  
LINK        FE4  SF4 B2234                 SG  CYS B 751     1555   1555  2.30  
LINK        FE1  SF4 B2235                 SG  CYS B 812     1555   1555  2.27  
LINK        FE2  SF4 B2235                 SG  CYS B 840     1555   1555  2.27  
LINK        FE3  SF4 B2235                 SG  CYS B 815     1555   1555  2.31  
LINK        FE4  SF4 B2235                 SG  CYS B1071     1555   1555  2.28  
LINK        MG    MG B2237                 O22 1TP B2236     1555   1555  2.01  
LINK        MG    MG B2237                 O13 1TP B2236     1555   1555  2.19  
LINK        MG    MG B2237                 O   VAL B 993     1555   1555  2.14  
LINK        MG    MG B2237                 OG1 THR B 991     1555   1555  2.19  
LINK        MG    MG B2237                 OD1 ASP B 963     1555   1555  2.26  
LINK        MG    MG B2237                 O   HOH B2379     1555   1555  2.13  
LINK        CA    CA B2238                 OD1 ASN B 985     1555   1555  2.54  
LINK        CA    CA B2238                 O   PHE B1059     1555   1555  2.86  
LINK        CA    CA B2238                 O   ALA B1056     1555   1555  2.90  
LINK        CA    CA B2238                 OD2 ASP B 983     1555   1555  2.84  
LINK        CA    CA B2238                 O   GLY B1061     1555   1555  3.06  
CISPEP   1 THR A   31    PRO A   32          0         0.32                     
CISPEP   2 ARG A  306    PRO A  307          0        -0.37                     
CISPEP   3 ALA A  848    PRO A  849          0         0.47                     
CISPEP   4 THR B   31    PRO B   32          0        -0.47                     
CISPEP   5 ARG B  306    PRO B  307          0        -0.69                     
CISPEP   6 ALA B  848    PRO B  849          0         0.39                     
SITE     1 AC1  5 ASP A 963  THR A 991  VAL A 993  1TP A2236                    
SITE     2 AC1  5 HOH A2308                                                     
SITE     1 AC2  7 ASP A 983  VAL A 984  ASN A 985  ALA A1056                    
SITE     2 AC2  7 PHE A1059  GLY A1061  SER A1063                               
SITE     1 AC3  5 ASP B 963  THR B 991  VAL B 993  1TP B2236                    
SITE     2 AC3  5 HOH B2379                                                     
SITE     1 AC4  8 ASP B 983  VAL B 984  ASN B 985  ALA B1056                    
SITE     2 AC4  8 GLU B1057  PHE B1059  GLY B1061  SER B1063                    
SITE     1 AC5 10 TRP A 684  CYS A 689  ILE A 690  CYS A 692                    
SITE     2 AC5 10 ASN A 693  CYS A 695  CYS A 755  PRO A 756                    
SITE     3 AC5 10 ALA A 761  LEU A 762                                          
SITE     1 AC6  9 PRO A 682  CYS A 699  PRO A 700  ILE A 704                    
SITE     2 AC6  9 CYS A 745  MET A 746  CYS A 748  GLY A 749                    
SITE     3 AC6  9 CYS A 751                                                     
SITE     1 AC7  8 LYS A 459  CYS A 812  CYS A 815  GLU A 817                    
SITE     2 AC7  8 CYS A 840  CYS A1071  ILE A1072  MET B1203                    
SITE     1 AC8 29 PRO A  29  ILE A  30  THR A  31  GLU A  64                    
SITE     2 AC8 29 GLN A  88  ARG A 114  GLU A 817  THR A 838                    
SITE     3 AC8 29 CYS A 840  PHE A 869  GLU A 870  GLY A 962                    
SITE     4 AC8 29 ASP A 963  GLY A 964  TRP A 965  ILE A 969                    
SITE     5 AC8 29 THR A 991  VAL A 993  TYR A 994  SER A 995                    
SITE     6 AC8 29 ASN A 996  THR A 997   MG A2237  HOH A2255                    
SITE     7 AC8 29 HOH A2256  HOH A2275  HOH A2308  HOH A2379                    
SITE     8 AC8 29 MET B1202                                                     
SITE     1 AC9 10 TRP B 684  CYS B 689  ILE B 690  CYS B 692                    
SITE     2 AC9 10 ASN B 693  CYS B 695  CYS B 755  PRO B 756                    
SITE     3 AC9 10 ALA B 761  LEU B 762                                          
SITE     1 BC1  7 CYS B 699  ILE B 704  CYS B 745  MET B 746                    
SITE     2 BC1  7 CYS B 748  GLY B 749  CYS B 751                               
SITE     1 BC2  8 MET A1203  LYS B 459  CYS B 812  CYS B 815                    
SITE     2 BC2  8 GLU B 817  CYS B 840  CYS B1071  ILE B1072                    
SITE     1 BC3 30 MET A1202  PRO B  29  ILE B  30  THR B  31                    
SITE     2 BC3 30 GLU B  64  GLN B  88  LEU B  92  ARG B 114                    
SITE     3 BC3 30 GLU B 817  THR B 838  GLY B 839  CYS B 840                    
SITE     4 BC3 30 PHE B 869  GLU B 870  GLY B 962  ASP B 963                    
SITE     5 BC3 30 GLY B 964  TRP B 965  THR B 991  VAL B 993                    
SITE     6 BC3 30 TYR B 994  SER B 995  ASN B 996  THR B 997                    
SITE     7 BC3 30  MG B2237  HOH B2322  HOH B2323  HOH B2336                    
SITE     8 BC3 30 HOH B2379  HOH B2472                                          
CRYST1   85.966  145.840  210.822  90.00  90.00  90.00 P 21 21 21    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      0.011633  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006857  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004743        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system