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Database: PDB
Entry: 1C4A
LinkDB: 1C4A
Original site: 1C4A 
HEADER    OXIDOREDUCTASE                          13-AUG-99   1C4A              
TITLE     BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE            
TITLE    2 SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM               
TITLE    3 PASTEURIANUM                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (FE-ONLY HYDROGENASE);                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CPI;                                                        
COMPND   5 EC: 1.18.99.1                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PASTEURIANUM;                       
SOURCE   3 ORGANISM_TAXID: 1501;                                                
SOURCE   4 CELLULAR_LOCATION: CYTOPLASM                                         
KEYWDS    METALLOPROTEINS, [FES] CLUSTERS, HYDROGEN OXIDATION, PROTON           
KEYWDS   2 REDUCTION, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.LEMON,J.W.PETERS                                                  
REVDAT   3   31-MAR-09 1C4A    1       LINK   ATOM   CONECT                     
REVDAT   2   24-FEB-09 1C4A    1       VERSN                                    
REVDAT   1   22-DEC-99 1C4A    0                                                
JRNL        AUTH   B.J.LEMON,J.W.PETERS                                         
JRNL        TITL   BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT              
JRNL        TITL 2 THE ACTIVE SITE OF THE IRON-ONLY HYDROGENASE (CPI)           
JRNL        TITL 3 FROM CLOSTRIDIUM PASTEURIANUM.                               
JRNL        REF    BIOCHEMISTRY                  V.  38 12969 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10529166                                                     
JRNL        DOI    10.1021/BI9913193                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.857                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 23019                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4461                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 327                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 2.540                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.01                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1C4A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB001287.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1FEH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       66.85000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.85000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.00000            
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 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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   608     O    HOH A   618     4456     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  94   NE2   HIS A  94   CD2    -0.108                       
REMARK 500    HIS A 210   NE2   HIS A 210   CD2    -0.074                       
REMARK 500    HIS A 492   NE2   HIS A 492   CD2    -0.075                       
REMARK 500    HIS A 511   NE2   HIS A 511   CD2    -0.068                       
REMARK 500    HIS A 536   NE2   HIS A 536   CD2    -0.068                       
REMARK 500    HIS A 543   NE2   HIS A 543   CD2    -0.068                       
REMARK 500    HIS A 565   NE2   HIS A 565   CD2    -0.067                       
REMARK 500    HIS A 569   NE2   HIS A 569   CD2    -0.070                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PHE A  96   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    PHE A  96   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LEU A 148   CA  -  CB  -  CG  ANGL. DEV. =  21.2 DEGREES          
REMARK 500    TYR A 254   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TRP A 303   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A 303   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    LEU A 548   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    MET A 551   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    MET A 551   CA  -  CB  -  CG  ANGL. DEV. =  16.5 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                                                                      
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    ASN A  27       72.47    -43.52                                   
REMARK 500    ASP A  29       61.99   -102.22                                   
REMARK 500    LEU A  33      -61.69   -145.35                                   
REMARK 500    LEU A  36      148.73   -170.96                                   
REMARK 500    ASN A  38       18.77     56.51                                   
REMARK 500    ASN A  44       82.88     43.71                                   
REMARK 500    ASP A  63       15.41   -140.52                                   
REMARK 500    SER A  76     -176.19    -54.76                                   
REMARK 500    ASP A  77      -64.03    -92.36                                   
REMARK 500    SER A  88       43.07    -98.33                                   
REMARK 500    GLN A  89      -28.58   -144.02                                   
REMARK 500    ASP A  92      -12.67    169.95                                   
REMARK 500    PHE A  96       83.29    -66.98                                   
REMARK 500    PRO A 100       53.50   -101.50                                   
REMARK 500    ASN A 106       52.73   -145.10                                   
REMARK 500    CYS A 107      -84.38    -71.07                                   
REMARK 500    GLU A 108      -40.41    132.66                                   
REMARK 500    LEU A 149       70.32      1.70                                   
REMARK 500    GLU A 162       17.91     54.88                                   
REMARK 500    VAL A 202     -167.38   -125.72                                   
REMARK 500    SER A 236      -25.75   -142.62                                   
REMARK 500    PHE A 266     -161.18   -106.07                                   
REMARK 500    ASN A 289      -66.22     79.21                                   
REMARK 500    ASN A 290      -51.19   -140.99                                   
REMARK 500    THR A 334      -71.11   -124.82                                   
REMARK 500    SER A 340       86.35     55.04                                   
REMARK 500    TYR A 445       70.01   -116.63                                   
REMARK 500    ASN A 513      115.32     78.60                                   
REMARK 500    TYR A 555      -52.24   -136.79                                   
REMARK 500    LYS A 558      117.61     47.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 603        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH A 617        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 674        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 692        DISTANCE =  8.45 ANGSTROMS                       
REMARK 525    HOH A 767        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 820        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 821        DISTANCE =  5.00 ANGSTROMS                       
REMARK 525    HOH A 873        DISTANCE =  5.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC1 A 580                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 581                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 582                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 583                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 584                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 585                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FEH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1C4C   RELATED DB: PDB                                   
DBREF  1C4A A    1   574  UNP    P29166   PHF1_CLOPA       1    574             
SEQRES   1 A  574  MET LYS THR ILE ILE ILE ASN GLY VAL GLN PHE ASN THR          
SEQRES   2 A  574  ASP GLU ASP THR THR ILE LEU LYS PHE ALA ARG ASP ASN          
SEQRES   3 A  574  ASN ILE ASP ILE SER ALA LEU CYS PHE LEU ASN ASN CYS          
SEQRES   4 A  574  ASN ASN ASP ILE ASN LYS CYS GLU ILE CYS THR VAL GLU          
SEQRES   5 A  574  VAL GLU GLY THR GLY LEU VAL THR ALA CYS ASP THR LEU          
SEQRES   6 A  574  ILE GLU ASP GLY MET ILE ILE ASN THR ASN SER ASP ALA          
SEQRES   7 A  574  VAL ASN GLU LYS ILE LYS SER ARG ILE SER GLN LEU LEU          
SEQRES   8 A  574  ASP ILE HIS GLU PHE LYS CYS GLY PRO CYS ASN ARG ARG          
SEQRES   9 A  574  GLU ASN CYS GLU PHE LEU LYS LEU VAL ILE LYS TYR LYS          
SEQRES  10 A  574  ALA ARG ALA SER LYS PRO PHE LEU PRO LYS ASP LYS THR          
SEQRES  11 A  574  GLU TYR VAL ASP GLU ARG SER LYS SER LEU THR VAL ASP          
SEQRES  12 A  574  ARG THR LYS CYS LEU LEU CYS GLY ARG CYS VAL ASN ALA          
SEQRES  13 A  574  CYS GLY LYS ASN THR GLU THR TYR ALA MET LYS PHE LEU          
SEQRES  14 A  574  ASN LYS ASN GLY LYS THR ILE ILE GLY ALA GLU ASP GLU          
SEQRES  15 A  574  LYS CYS PHE ASP ASP THR ASN CYS LEU LEU CYS GLY GLN          
SEQRES  16 A  574  CYS ILE ILE ALA CYS PRO VAL ALA ALA LEU SER GLU LYS          
SEQRES  17 A  574  SER HIS MET ASP ARG VAL LYS ASN ALA LEU ASN ALA PRO          
SEQRES  18 A  574  GLU LYS HIS VAL ILE VAL ALA MET ALA PRO SER VAL ARG          
SEQRES  19 A  574  ALA SER ILE GLY GLU LEU PHE ASN MET GLY PHE GLY VAL          
SEQRES  20 A  574  ASP VAL THR GLY LYS ILE TYR THR ALA LEU ARG GLN LEU          
SEQRES  21 A  574  GLY PHE ASP LYS ILE PHE ASP ILE ASN PHE GLY ALA ASP          
SEQRES  22 A  574  MET THR ILE MET GLU GLU ALA THR GLU LEU VAL GLN ARG          
SEQRES  23 A  574  ILE GLU ASN ASN GLY PRO PHE PRO MET PHE THR SER CYS          
SEQRES  24 A  574  CYS PRO GLY TRP VAL ARG GLN ALA GLU ASN TYR TYR PRO          
SEQRES  25 A  574  GLU LEU LEU ASN ASN LEU SER SER ALA LYS SER PRO GLN          
SEQRES  26 A  574  GLN ILE PHE GLY THR ALA SER LYS THR TYR TYR PRO SER          
SEQRES  27 A  574  ILE SER GLY LEU ASP PRO LYS ASN VAL PHE THR VAL THR          
SEQRES  28 A  574  VAL MET PRO CYS THR SER LYS LYS PHE GLU ALA ASP ARG          
SEQRES  29 A  574  PRO GLN MET GLU LYS ASP GLY LEU ARG ASP ILE ASP ALA          
SEQRES  30 A  574  VAL ILE THR THR ARG GLU LEU ALA LYS MET ILE LYS ASP          
SEQRES  31 A  574  ALA LYS ILE PRO PHE ALA LYS LEU GLU ASP SER GLU ALA          
SEQRES  32 A  574  ASP PRO ALA MET GLY GLU TYR SER GLY ALA GLY ALA ILE          
SEQRES  33 A  574  PHE GLY ALA THR GLY GLY VAL MET GLU ALA ALA LEU ARG          
SEQRES  34 A  574  SER ALA LYS ASP PHE ALA GLU ASN ALA GLU LEU GLU ASP          
SEQRES  35 A  574  ILE GLU TYR LYS GLN VAL ARG GLY LEU ASN GLY ILE LYS          
SEQRES  36 A  574  GLU ALA GLU VAL GLU ILE ASN ASN ASN LYS TYR ASN VAL          
SEQRES  37 A  574  ALA VAL ILE ASN GLY ALA SER ASN LEU PHE LYS PHE MET          
SEQRES  38 A  574  LYS SER GLY MET ILE ASN GLU LYS GLN TYR HIS PHE ILE          
SEQRES  39 A  574  GLU VAL MET ALA CYS HIS GLY GLY CYS VAL ASN GLY GLY          
SEQRES  40 A  574  GLY GLN PRO HIS VAL ASN PRO LYS ASP LEU GLU LYS VAL          
SEQRES  41 A  574  ASP ILE LYS LYS VAL ARG ALA SER VAL LEU TYR ASN GLN          
SEQRES  42 A  574  ASP GLU HIS LEU SER LYS ARG LYS SER HIS GLU ASN THR          
SEQRES  43 A  574  ALA LEU VAL LYS MET TYR GLN ASN TYR PHE GLY LYS PRO          
SEQRES  44 A  574  GLY GLU GLY ARG ALA HIS GLU ILE LEU HIS PHE LYS TYR          
SEQRES  45 A  574  LYS LYS                                                      
HET    HC1  A 580      16                                                       
HET    SF4  A 581       8                                                       
HET    SF4  A 582       8                                                       
HET    SF4  A 583       8                                                       
HET    SF4  A 584       8                                                       
HET    FES  A 585       4                                                       
HETNAM     HC1 2 IRON/2 SULFUR/5 CARBONYL/2 WATER INORGANIC CLUSTER             
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
FORMUL   2  HC1    C5 H8 FE2 O7 S2                                              
FORMUL   3  SF4    4(FE4 S4)                                                    
FORMUL   7  FES    FE2 S2                                                       
FORMUL   8  HOH   *327(H2 O)                                                    
HELIX    1   1 THR A   18  ASN A   26  1                                   9    
HELIX    2   2 ASP A   77  LEU A   91  1                                  15    
HELIX    3   3 ARG A  103  CYS A  107  5                                   5    
HELIX    4   4 LEU A  110  LYS A  117  1                                   8    
HELIX    5   5 GLY A  151  THR A  161  1                                  11    
HELIX    6   6 ALA A  179  LYS A  183  5                                   5    
HELIX    7   7 CYS A  184  THR A  188  5                                   5    
HELIX    8   8 GLY A  194  CYS A  200  1                                   7    
HELIX    9   9 HIS A  210  ALA A  220  1                                  11    
HELIX   10  10 PRO A  231  SER A  236  5                                   6    
HELIX   11  11 SER A  236  ASN A  242  5                                   7    
HELIX   12  12 VAL A  249  LEU A  260  1                                  12    
HELIX   13  13 ILE A  268  GLU A  288  1                                  21    
HELIX   14  14 CYS A  300  TYR A  311  1                                  12    
HELIX   15  15 PRO A  312  LEU A  315  5                                   4    
HELIX   16  16 SER A  323  LYS A  333  1                                  11    
HELIX   17  17 THR A  334  ILE A  339  1                                   6    
HELIX   18  18 ASP A  343  LYS A  345  5                                   3    
HELIX   19  19 THR A  356  ASP A  363  1                                   8    
HELIX   20  20 THR A  381  ALA A  391  1                                  11    
HELIX   21  21 PRO A  394  LEU A  398  5                                   5    
HELIX   22  22 ASP A  404  GLY A  408  5                                   5    
HELIX   23  23 SER A  411  ILE A  416  1                                   6    
HELIX   24  24 PHE A  417  ALA A  419  5                                   3    
HELIX   25  25 GLY A  421  ASN A  437  1                                  17    
HELIX   26  26 TYR A  445  ARG A  449  5                                   5    
HELIX   27  27 GLY A  473  SER A  483  1                                  11    
HELIX   28  28 GLY A  484  GLU A  488  5                                   5    
HELIX   29  29 GLY A  502  GLY A  506  5                                   5    
HELIX   30  30 ASN A  513  VAL A  520  1                                   8    
HELIX   31  31 ASP A  521  LEU A  537  1                                  17    
HELIX   32  32 LYS A  541  GLU A  544  5                                   4    
HELIX   33  33 ASN A  545  TYR A  555  1                                  11    
HELIX   34  34 GLU A  561  LEU A  568  1                                   8    
SHEET    1   A 5 VAL A   9  THR A  13  0                                        
SHEET    2   A 5 LYS A   2  ILE A   6 -1  N  LYS A   2   O  THR A  13           
SHEET    3   A 5 MET A  70  ASN A  73  1  O  MET A  70   N  ILE A   5           
SHEET    4   A 5 THR A  50  VAL A  53 -1  N  GLU A  52   O  ASN A  73           
SHEET    5   A 5 GLY A  57  THR A  60 -1  N  GLY A  57   O  VAL A  53           
SHEET    1   B 3 VAL A 133  ASP A 134  0                                        
SHEET    2   B 3 LEU A 140  ASP A 143 -1  O  VAL A 142   N  ASP A 134           
SHEET    3   B 3 LEU A 205  GLU A 207 -1  O  SER A 206   N  THR A 141           
SHEET    1   C 2 LYS A 167  LYS A 171  0                                        
SHEET    2   C 2 LYS A 174  GLY A 178 -1  O  LYS A 174   N  LYS A 171           
SHEET    1   D 4 LYS A 264  ASP A 267  0                                        
SHEET    2   D 4 HIS A 224  MET A 229  1  O  VAL A 225   N  LYS A 264           
SHEET    3   D 4 VAL A 347  MET A 353  1  O  PHE A 348   N  ILE A 226           
SHEET    4   D 4 ALA A 377  THR A 380  1  O  ALA A 377   N  THR A 351           
SHEET    1   E 4 MET A 295  PHE A 296  0                                        
SHEET    2   E 4 PHE A 493  MET A 497  1  N  ILE A 494   O  MET A 295           
SHEET    3   E 4 ASN A 464  ASN A 472  1  O  ASN A 467   N  PHE A 493           
SHEET    4   E 4 ILE A 454  ILE A 461 -1  O  LYS A 455   N  VAL A 470           
SHEET    1   F 2 GLU A 368  LYS A 369  0                                        
SHEET    2   F 2 LEU A 372  ARG A 373 -1  O  LEU A 372   N  LYS A 369           
LINK        FE1  HC1 A 580                 SG  CYS A 503     1555   1555  2.37  
LINK        FE1  FES A 585                 SG  CYS A  49     1555   1555  2.28  
LINK        FE1  FES A 585                 SG  CYS A  62     1555   1555  2.30  
LINK        FE2  FES A 585                 SG  CYS A  34     1555   1555  2.31  
LINK        FE2  FES A 585                 SG  CYS A  46     1555   1555  2.35  
LINK         NE2 HIS A  94                FE1  SF4 A 584     1555   1555  1.97  
LINK         SG  CYS A  98                FE4  SF4 A 584     1555   1555  2.39  
LINK         SG  CYS A 101                FE3  SF4 A 584     1555   1555  2.26  
LINK         SG  CYS A 107                FE2  SF4 A 584     1555   1555  2.32  
LINK         SG  CYS A 147                FE3  SF4 A 583     1555   1555  2.39  
LINK         SG  CYS A 150                FE2  SF4 A 583     1555   1555  2.31  
LINK         SG  CYS A 153                FE4  SF4 A 583     1555   1555  2.27  
LINK         SG  CYS A 157                FE2  SF4 A 582     1555   1555  2.28  
LINK         SG  CYS A 190                FE4  SF4 A 582     1555   1555  2.30  
LINK         SG  CYS A 193                FE1  SF4 A 582     1555   1555  2.25  
LINK         SG  CYS A 196                FE3  SF4 A 582     1555   1555  2.29  
LINK         SG  CYS A 200                FE1  SF4 A 583     1555   1555  2.28  
LINK         SG  CYS A 300                FE3  SF4 A 581     1555   1555  2.28  
LINK         SG  CYS A 355                FE1  SF4 A 581     1555   1555  2.24  
LINK         SG  CYS A 499                FE2  SF4 A 581     1555   1555  2.26  
LINK         SG  CYS A 503                FE4  SF4 A 581     1555   1555  2.37  
CISPEP   1 GLY A   99    PRO A  100          0         5.09                     
CISPEP   2 GLY A  291    PRO A  292          0        25.93                     
CISPEP   3 PHE A  293    PRO A  294          0        -3.49                     
SITE     1 AC1 16 ALA A 230  PRO A 231  SER A 232  ALA A 272                    
SITE     2 AC1 16 CYS A 299  PRO A 324  GLN A 325  MET A 353                    
SITE     3 AC1 16 PRO A 354  CYS A 355  LYS A 358  PHE A 417                    
SITE     4 AC1 16 GLY A 418  MET A 497  CYS A 503  SF4 A 581                    
SITE     1 AC2  8 CYS A 300  PRO A 301  CYS A 355  ALA A 498                    
SITE     2 AC2  8 CYS A 499  CYS A 503  GLY A 506  HC1 A 580                    
SITE     1 AC3  8 CYS A 157  MET A 166  CYS A 190  LEU A 191                    
SITE     2 AC3  8 LEU A 192  CYS A 193  GLY A 194  CYS A 196                    
SITE     1 AC4 10 CYS A 147  LEU A 148  LEU A 149  CYS A 150                    
SITE     2 AC4 10 GLY A 151  CYS A 153  ILE A 177  CYS A 200                    
SITE     3 AC4 10 VAL A 202  LEU A 205                                          
SITE     1 AC5  9 HIS A  94  GLU A  95  LYS A  97  CYS A  98                    
SITE     2 AC5  9 CYS A 101  ARG A 104  CYS A 107  VAL A 202                    
SITE     3 AC5  9 ALA A 203                                                     
SITE     1 AC6  8 LEU A  33  CYS A  34  PHE A  35  LYS A  45                    
SITE     2 AC6  8 CYS A  46  GLU A  47  CYS A  49  CYS A  62                    
CRYST1  133.700   84.000   55.700  90.00  90.00  90.00 P 21 21 2     4          
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      0.007479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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