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Database: PDB
Entry: 1KF6
LinkDB: 1KF6
Original site: 1KF6 
HEADER    OXIDOREDUCTASE                          19-NOV-01   1KF6              
TITLE     E. COLI QUINOL-FUMARATE REDUCTASE WITH BOUND INHIBITOR HQNO           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUMARATE REDUCTASE FLAVOPROTEIN;                           
COMPND   3 CHAIN: A, M;                                                         
COMPND   4 EC: 1.3.99.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FUMARATE REDUCTASE IRON-SULFUR PROTEIN;                    
COMPND   8 CHAIN: B, N;                                                         
COMPND   9 EC: 1.3.99.1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: FUMARATE REDUCTASE 15 KDA HYDROPHOBIC PROTEIN;             
COMPND  13 CHAIN: C, O;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: FUMARATE REDUCTASE 13 KDA HYDROPHOBIC PROTEIN;             
COMPND  17 CHAIN: D, P;                                                         
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PFA;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  10 ORGANISM_TAXID: 562;                                                 
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PFA;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  17 ORGANISM_TAXID: 562;                                                 
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PFA;                                      
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  24 ORGANISM_TAXID: 562;                                                 
SOURCE  25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PFA                                       
KEYWDS    RESPIRATION, FUMARATE REDUCTACE, SUCCINATE DEHYDROGENASE, COMPLEX II, 
KEYWDS   2 QUINOL, QUINONE, OXIDOREDUCTASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.IVERSON,C.LUNA-CHAVEZ,L.R.CROAL,G.CECCHINI,D.C.REES               
REVDAT   5   13-JUL-11 1KF6    1       VERSN                                    
REVDAT   4   31-MAR-09 1KF6    1       LINK   ATOM   CONECT                     
REVDAT   3   24-FEB-09 1KF6    1       VERSN                                    
REVDAT   2   19-JUN-02 1KF6    1       JRNL                                     
REVDAT   1   13-MAR-02 1KF6    0                                                
JRNL        AUTH   T.M.IVERSON,C.LUNA-CHAVEZ,L.R.CROAL,G.CECCHINI,D.C.REES      
JRNL        TITL   CRYSTALLOGRAPHIC STUDIES OF THE ESCHERICHIA COLI             
JRNL        TITL 2 QUINOL-FUMARATE REDUCTASE WITH INHIBITORS BOUND TO THE       
JRNL        TITL 3 QUINOL-BINDING SITE.                                         
JRNL        REF    J.BIOL.CHEM.                  V. 277 16124 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11850430                                                     
JRNL        DOI    10.1074/JBC.M200815200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.M.IVERSON,C.LUNA-CHAVEZ,G.CECCHINI,D.C.REES                
REMARK   1  TITL   STRUCTURE OF THE ESCHERICHIA COLI FUMARATE REDUCTASE         
REMARK   1  TITL 2 RESPIRATORY COMPLEX                                          
REMARK   1  REF    SCIENCE                       V. 284  1961 1999              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1  DOI    10.1126/SCIENCE.284.5422.1961                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS, REFMAC                                          
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,MURSHUDOV,                 
REMARK   3               : VAGIN,DODSON                                         
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 292370                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1953                            
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            : 16640                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 415                                     
REMARK   3   SOLVENT ATOMS            : 16                                      
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) : 0.019                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.95                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1KF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014889.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : 0.87                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 292370                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FUM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5K MME, MGOAC, NACITRATE, EDTA,      
REMARK 280  DTT, HQNO, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K  
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       48.25250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      136.72550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.91800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      136.72550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.25250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.91800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21210 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, M, N, O, P                
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   577                                                      
REMARK 465     ARG A   578                                                      
REMARK 465     VAL A   579                                                      
REMARK 465     TYR A   580                                                      
REMARK 465     GLY A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     GLU A   583                                                      
REMARK 465     ALA A   584                                                      
REMARK 465     ASP A   585                                                      
REMARK 465     ALA A   586                                                      
REMARK 465     ALA A   587                                                      
REMARK 465     ASP A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     ALA A   590                                                      
REMARK 465     GLU A   591                                                      
REMARK 465     ALA A   592                                                      
REMARK 465     ALA A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     LYS A   595                                                      
REMARK 465     LYS A   596                                                      
REMARK 465     GLU A   597                                                      
REMARK 465     LYS A   598                                                      
REMARK 465     ALA A   599                                                      
REMARK 465     ASN A   600                                                      
REMARK 465     GLY A   601                                                      
REMARK 465     LYS M   577                                                      
REMARK 465     ARG M   578                                                      
REMARK 465     VAL M   579                                                      
REMARK 465     TYR M   580                                                      
REMARK 465     GLY M   581                                                      
REMARK 465     GLY M   582                                                      
REMARK 465     GLU M   583                                                      
REMARK 465     ALA M   584                                                      
REMARK 465     ASP M   585                                                      
REMARK 465     ALA M   586                                                      
REMARK 465     ALA M   587                                                      
REMARK 465     ASP M   588                                                      
REMARK 465     LYS M   589                                                      
REMARK 465     ALA M   590                                                      
REMARK 465     GLU M   591                                                      
REMARK 465     ALA M   592                                                      
REMARK 465     ALA M   593                                                      
REMARK 465     ASN M   594                                                      
REMARK 465     LYS M   595                                                      
REMARK 465     LYS M   596                                                      
REMARK 465     GLU M   597                                                      
REMARK 465     LYS M   598                                                      
REMARK 465     ALA M   599                                                      
REMARK 465     ASN M   600                                                      
REMARK 465     GLY M   601                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  HIS A    44     C8M  FAD A   721              1.89            
REMARK 500   NE2  HIS M    44     C8M  FAD M   821              1.98            
REMARK 500   O    ALA P   104     OG1  THR P   108              2.08            
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    CYS B  65   CB    CYS B  65   SG     -0.130                       
REMARK 500    ASN C  65   C     ASN C  65   O      -0.141                       
REMARK 500    TRP C 130   C     TRP C 130   OXT     0.119                       
REMARK 500    ILE D 118   C     ILE D 118   OXT     0.221                       
REMARK 500    GLY O 104   C     GLY O 104   O      -0.105                       
REMARK 500    TRP O 130   CA    TRP O 130   CB      0.136                       
REMARK 500    ILE P 118   CA    ILE P 118   CB      0.145                       
REMARK 500    ILE P 118   C     ILE P 118   OXT     0.152                       
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    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP A 477   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 485   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    CYS B  65   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ARG B 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG D   7   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG M 151   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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                                                                      
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    ALA A  54      121.89   -174.18                                   
REMARK 500    ALA A  56      -40.78   -144.05                                   
REMARK 500    ARG A 123       17.31   -157.69                                   
REMARK 500    ALA A 128     -145.43     56.13                                   
REMARK 500    THR A 244      144.61    -35.75                                   
REMARK 500    LYS A 280      -25.54     79.37                                   
REMARK 500    MET A 282     -120.26     34.81                                   
REMARK 500    HIS A 318       12.46    -58.73                                   
REMARK 500    PRO A 343       12.30    -60.79                                   
REMARK 500    HIS A 355      -49.19   -131.38                                   
REMARK 500    ASN A 389      108.73    179.52                                   
REMARK 500    GLU A 537      120.65    -39.62                                   
REMARK 500    THR A 571      -65.33   -124.64                                   
REMARK 500    LEU A 573       78.14   -117.17                                   
REMARK 500    TYR B  13      117.39   -164.59                                   
REMARK 500    VAL B  17      -52.30   -134.22                                   
REMARK 500    ALA B  48       88.84   -158.44                                   
REMARK 500    SER B  56      -71.01   -171.14                                   
REMARK 500    MET B  59       29.34   -143.51                                   
REMARK 500    ARG B 100      131.74   -170.25                                   
REMARK 500    ASP B 101     -120.29     39.97                                   
REMARK 500    LYS B 117       71.03     48.48                                   
REMARK 500    PRO B 165        1.42    -60.81                                   
REMARK 500    LYS B 241       76.88   -107.46                                   
REMARK 500    LYS C  18      -93.44    -58.66                                   
REMARK 500    ASN C  65      -84.01      4.28                                   
REMARK 500    LYS C  99       67.91     60.90                                   
REMARK 500    MET C 103     -147.81    -88.48                                   
REMARK 500    ILE D  37      -58.17   -129.18                                   
REMARK 500    LEU D  43       58.26    -64.66                                   
REMARK 500    VAL D  99      -72.16    -59.98                                   
REMARK 500    THR D 117      142.78     69.80                                   
REMARK 500    GLN M   1     -179.80    171.59                                   
REMARK 500    ASP M   6      -78.81    -67.78                                   
REMARK 500    PRO M  28      -16.33    -47.60                                   
REMARK 500    ALA M  54      122.68   -175.63                                   
REMARK 500    ALA M  56      -65.43   -126.67                                   
REMARK 500    HIS M  59       36.17    -77.05                                   
REMARK 500    TRP M  75       16.79     50.40                                   
REMARK 500    GLU M  78       68.52    -67.94                                   
REMARK 500    GLN M  79      -37.34    -24.96                                   
REMARK 500    CYS M 101      117.00    -24.73                                   
REMARK 500    MET M 119      132.51    -28.26                                   
REMARK 500    ARG M 123       31.85   -140.47                                   
REMARK 500    ALA M 127       79.69   -116.11                                   
REMARK 500    ALA M 128     -161.45     53.94                                   
REMARK 500    ASP M 129       50.09    -98.09                                   
REMARK 500    HIS M 134        5.07    -63.13                                   
REMARK 500    ASP M 159      163.76    179.44                                   
REMARK 500    ALA M 187      101.85   -160.86                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     116 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN C   65     PRO C   66                   32.74                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASN C  65         16.14                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR D 117        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                               K A 720   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 357   O                                                      
REMARK 620 2 MET A 358   O    83.5                                              
REMARK 620 3 GLY A 359   O    80.8  72.7                                        
REMARK 620 4 GLU A 379   O    91.4 166.5  94.2                                  
REMARK 620 5 SER A 381   O   169.7  89.9  89.7  93.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 244  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  57   SG                                                     
REMARK 620 2 FES B 244   S1  114.0                                              
REMARK 620 3 FES B 244   S2  111.7 102.0                                        
REMARK 620 4 CYS B  62   SG  104.6 113.1 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 244  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 FES B 244   S1  118.3                                              
REMARK 620 3 FES B 244   S2  109.5 104.9                                        
REMARK 620 4 CYS B  77   SG   97.0 114.0 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 245  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 F3S B 245   S2  113.1                                              
REMARK 620 3 F3S B 245   S3  109.5 102.8                                        
REMARK 620 4 F3S B 245   S4  114.6 110.2 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 245  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 204   SG                                                     
REMARK 620 2 F3S B 245   S1  110.3                                              
REMARK 620 3 F3S B 245   S2  112.3 105.8                                        
REMARK 620 4 F3S B 245   S3  119.4 100.8 106.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 245  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 210   SG                                                     
REMARK 620 2 F3S B 245   S1  113.6                                              
REMARK 620 3 F3S B 245   S3  118.6 102.4                                        
REMARK 620 4 F3S B 245   S4  107.6 107.3 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 151   SG                                                     
REMARK 620 2 SF4 B 246   S2  106.2                                              
REMARK 620 3 SF4 B 246   S3  122.9 104.7                                        
REMARK 620 4 SF4 B 246   S4  119.6  98.0 101.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 148   SG                                                     
REMARK 620 2 SF4 B 246   S1  116.2                                              
REMARK 620 3 SF4 B 246   S3  119.8 102.1                                        
REMARK 620 4 SF4 B 246   S4  109.6 106.8 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 154   SG                                                     
REMARK 620 2 SF4 B 246   S1  119.2                                              
REMARK 620 3 SF4 B 246   S2  111.2 107.1                                        
REMARK 620 4 SF4 B 246   S4  107.7 109.8 100.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 214   SG                                                     
REMARK 620 2 SF4 B 246   S1  112.8                                              
REMARK 620 3 SF4 B 246   S2  128.7 102.3                                        
REMARK 620 4 SF4 B 246   S3  107.1 103.4  99.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K M 820   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR M 357   O                                                      
REMARK 620 2 MET M 358   O    88.4                                              
REMARK 620 3 GLY M 359   O    78.7  69.3                                        
REMARK 620 4 GLU M 379   O    81.2 155.9  87.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES N 244  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  57   SG                                                     
REMARK 620 2 FES N 244   S1  110.9                                              
REMARK 620 3 FES N 244   S2  114.0 105.5                                        
REMARK 620 4 CYS N  62   SG  101.8 111.3 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES N 244  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  65   SG                                                     
REMARK 620 2 FES N 244   S1  118.4                                              
REMARK 620 3 FES N 244   S2  114.9 106.1                                        
REMARK 620 4 CYS N  77   SG   95.1 109.1 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S N 245  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 158   SG                                                     
REMARK 620 2 F3S N 245   S2  114.7                                              
REMARK 620 3 F3S N 245   S3  113.1 104.1                                        
REMARK 620 4 F3S N 245   S4  108.2 112.3 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S N 245  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 204   SG                                                     
REMARK 620 2 F3S N 245   S1  105.0                                              
REMARK 620 3 F3S N 245   S2  120.1 103.4                                        
REMARK 620 4 F3S N 245   S3  116.1 100.6 108.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S N 245  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 210   SG                                                     
REMARK 620 2 F3S N 245   S1  108.4                                              
REMARK 620 3 F3S N 245   S3  116.8 103.4                                        
REMARK 620 4 F3S N 245   S4  109.7 113.5 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 151   SG                                                     
REMARK 620 2 SF4 N 246   S2  130.9                                              
REMARK 620 3 SF4 N 246   S3  119.0  89.0                                        
REMARK 620 4 SF4 N 246   S4  117.6  65.7 120.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 148   SG                                                     
REMARK 620 2 SF4 N 246   S1  131.2                                              
REMARK 620 3 SF4 N 246   S3  116.6  74.4                                        
REMARK 620 4 SF4 N 246   S4  116.1  93.6 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 154   SG                                                     
REMARK 620 2 SF4 N 246   S1  128.9                                              
REMARK 620 3 SF4 N 246   S2  107.0  93.3                                        
REMARK 620 4 SF4 N 246   S4  117.7 111.9  79.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 214   SG                                                     
REMARK 620 2 SF4 N 246   S1   96.6                                              
REMARK 620 3 SF4 N 246   S2  156.1  81.8                                        
REMARK 620 4 SF4 N 246   S3  104.3  92.5  99.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 720                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K M 820                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA M 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT N 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES N 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S N 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 N 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD M 821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQO C 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE1 P 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE1 P 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE1 O 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE1 O 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE1 O 813                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQO N 800                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FUM   RELATED DB: PDB                                   
REMARK 900 E. COLI QUINOL-FUMARATE REDUCTASE                                    
DBREF  1KF6 A    0   601  UNP    P00363   FRDA_ECOLI       0    601             
DBREF  1KF6 M    0   601  UNP    P00363   FRDA_ECOLI       0    601             
DBREF  1KF6 B    1   243  UNP    P0AC47   FRDB_ECOLI       1    243             
DBREF  1KF6 N    1   243  UNP    P0AC47   FRDB_ECOLI       1    243             
DBREF  1KF6 C    1   130  UNP    P0A8Q0   FRDC_ECOLI       2    131             
DBREF  1KF6 O    1   130  UNP    P0A8Q0   FRDC_ECOLI       2    131             
DBREF  1KF6 D    0   118  UNP    P0A8Q3   FRDD_ECOLI       1    119             
DBREF  1KF6 P    0   118  UNP    P0A8Q3   FRDD_ECOLI       1    119             
SEQRES   1 A  602  MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA          
SEQRES   2 A  602  GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN          
SEQRES   3 A  602  ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL          
SEQRES   4 A  602  TYR PRO MET ARG SER HIS THR VAL ALA ALA GLU GLY GLY          
SEQRES   5 A  602  SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR          
SEQRES   6 A  602  HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS          
SEQRES   7 A  602  GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO          
SEQRES   8 A  602  THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP          
SEQRES   9 A  602  SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE          
SEQRES  10 A  602  GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP          
SEQRES  11 A  602  LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR          
SEQRES  12 A  602  SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS          
SEQRES  13 A  602  PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG          
SEQRES  14 A  602  GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL          
SEQRES  15 A  602  GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY          
SEQRES  16 A  602  ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE          
SEQRES  17 A  602  VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY          
SEQRES  18 A  602  VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO          
SEQRES  19 A  602  THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY          
SEQRES  20 A  602  CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY          
SEQRES  21 A  602  TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR          
SEQRES  22 A  602  PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY          
SEQRES  23 A  602  PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP          
SEQRES  24 A  602  ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL          
SEQRES  25 A  602  VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU          
SEQRES  26 A  602  HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA          
SEQRES  27 A  602  TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL          
SEQRES  28 A  602  ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR          
SEQRES  29 A  602  ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA          
SEQRES  30 A  602  VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN          
SEQRES  31 A  602  ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE          
SEQRES  32 A  602  GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA          
SEQRES  33 A  602  THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN          
SEQRES  34 A  602  ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN          
SEQRES  35 A  602  GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU          
SEQRES  36 A  602  MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG          
SEQRES  37 A  602  THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA          
SEQRES  38 A  602  GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP          
SEQRES  39 A  602  THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE          
SEQRES  40 A  602  GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA          
SEQRES  41 A  602  HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS          
SEQRES  42 A  602  GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL          
SEQRES  43 A  602  ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP          
SEQRES  44 A  602  GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR          
SEQRES  45 A  602  THR LEU PRO PRO ALA LYS ARG VAL TYR GLY GLY GLU ALA          
SEQRES  46 A  602  ASP ALA ALA ASP LYS ALA GLU ALA ALA ASN LYS LYS GLU          
SEQRES  47 A  602  LYS ALA ASN GLY                                              
SEQRES   1 B  243  ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR          
SEQRES   2 B  243  ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR          
SEQRES   3 B  243  GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA          
SEQRES   4 B  243  LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER          
SEQRES   5 B  243  TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS          
SEQRES   6 B  243  GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS          
SEQRES   7 B  243  THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU          
SEQRES   8 B  243  ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL          
SEQRES   9 B  243  ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS          
SEQRES  10 B  243  PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY          
SEQRES  11 B  243  THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS          
SEQRES  12 B  243  GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA          
SEQRES  13 B  243  ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY          
SEQRES  14 B  243  PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP          
SEQRES  15 B  243  SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU          
SEQRES  16 B  243  ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY          
SEQRES  17 B  243  TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA          
SEQRES  18 B  243  ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP          
SEQRES  19 B  243  PHE LEU ILE ALA THR LEU LYS PRO ARG                          
SEQRES   1 C  130  THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER          
SEQRES   2 C  130  THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET          
SEQRES   3 C  130  LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER          
SEQRES   4 C  130  ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY          
SEQRES   5 C  130  PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN          
SEQRES   6 C  130  PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA          
SEQRES   7 C  130  ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO          
SEQRES   8 C  130  LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY          
SEQRES   9 C  130  PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL          
SEQRES  10 C  130  VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP          
SEQRES   1 D  119  MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL          
SEQRES   2 D  119  PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA          
SEQRES   3 D  119  ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU          
SEQRES   4 D  119  LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR          
SEQRES   5 D  119  GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG          
SEQRES   6 D  119  VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS          
SEQRES   7 D  119  GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS          
SEQRES   8 D  119  ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU          
SEQRES   9 D  119  ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL          
SEQRES  10 D  119  THR ILE                                                      
SEQRES   1 M  602  MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA          
SEQRES   2 M  602  GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN          
SEQRES   3 M  602  ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL          
SEQRES   4 M  602  TYR PRO MET ARG SER HIS THR VAL ALA ALA GLU GLY GLY          
SEQRES   5 M  602  SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR          
SEQRES   6 M  602  HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS          
SEQRES   7 M  602  GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO          
SEQRES   8 M  602  THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP          
SEQRES   9 M  602  SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE          
SEQRES  10 M  602  GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP          
SEQRES  11 M  602  LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR          
SEQRES  12 M  602  SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS          
SEQRES  13 M  602  PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG          
SEQRES  14 M  602  GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL          
SEQRES  15 M  602  GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY          
SEQRES  16 M  602  ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE          
SEQRES  17 M  602  VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY          
SEQRES  18 M  602  VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO          
SEQRES  19 M  602  THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY          
SEQRES  20 M  602  CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY          
SEQRES  21 M  602  TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR          
SEQRES  22 M  602  PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY          
SEQRES  23 M  602  PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP          
SEQRES  24 M  602  ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL          
SEQRES  25 M  602  VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU          
SEQRES  26 M  602  HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA          
SEQRES  27 M  602  TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL          
SEQRES  28 M  602  ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR          
SEQRES  29 M  602  ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA          
SEQRES  30 M  602  VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN          
SEQRES  31 M  602  ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE          
SEQRES  32 M  602  GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA          
SEQRES  33 M  602  THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN          
SEQRES  34 M  602  ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN          
SEQRES  35 M  602  GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU          
SEQRES  36 M  602  MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG          
SEQRES  37 M  602  THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA          
SEQRES  38 M  602  GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP          
SEQRES  39 M  602  THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE          
SEQRES  40 M  602  GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA          
SEQRES  41 M  602  HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS          
SEQRES  42 M  602  GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL          
SEQRES  43 M  602  ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP          
SEQRES  44 M  602  GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR          
SEQRES  45 M  602  THR LEU PRO PRO ALA LYS ARG VAL TYR GLY GLY GLU ALA          
SEQRES  46 M  602  ASP ALA ALA ASP LYS ALA GLU ALA ALA ASN LYS LYS GLU          
SEQRES  47 M  602  LYS ALA ASN GLY                                              
SEQRES   1 N  243  ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR          
SEQRES   2 N  243  ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR          
SEQRES   3 N  243  GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA          
SEQRES   4 N  243  LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER          
SEQRES   5 N  243  TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS          
SEQRES   6 N  243  GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS          
SEQRES   7 N  243  THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU          
SEQRES   8 N  243  ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL          
SEQRES   9 N  243  ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS          
SEQRES  10 N  243  PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY          
SEQRES  11 N  243  THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS          
SEQRES  12 N  243  GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA          
SEQRES  13 N  243  ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY          
SEQRES  14 N  243  PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP          
SEQRES  15 N  243  SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU          
SEQRES  16 N  243  ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY          
SEQRES  17 N  243  TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA          
SEQRES  18 N  243  ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP          
SEQRES  19 N  243  PHE LEU ILE ALA THR LEU LYS PRO ARG                          
SEQRES   1 O  130  THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER          
SEQRES   2 O  130  THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET          
SEQRES   3 O  130  LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER          
SEQRES   4 O  130  ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY          
SEQRES   5 O  130  PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN          
SEQRES   6 O  130  PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA          
SEQRES   7 O  130  ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO          
SEQRES   8 O  130  LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY          
SEQRES   9 O  130  PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL          
SEQRES  10 O  130  VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP          
SEQRES   1 P  119  MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL          
SEQRES   2 P  119  PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA          
SEQRES   3 P  119  ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU          
SEQRES   4 P  119  LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR          
SEQRES   5 P  119  GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG          
SEQRES   6 P  119  VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS          
SEQRES   7 P  119  GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS          
SEQRES   8 P  119  ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU          
SEQRES   9 P  119  ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL          
SEQRES  10 P  119  THR ILE                                                      
HET      K  A 720       1                                                       
HET      K  M 820       1                                                       
HET    OAA  A 702       9                                                       
HET    ACT  A 703       4                                                       
HET    ACT  B 704       4                                                       
HET    OAA  M 802       9                                                       
HET    ACT  N 803       4                                                       
HET    FES  B 244       4                                                       
HET    F3S  B 245       7                                                       
HET    SF4  B 246       8                                                       
HET    FAD  A 721      53                                                       
HET    FES  N 244       4                                                       
HET    F3S  N 245       7                                                       
HET    SF4  N 246       8                                                       
HET    FAD  M 821      53                                                       
HET    HQO  C 700      19                                                       
HET    CE1  P 710      37                                                       
HET    CE1  P 810      37                                                       
HET    CE1  O 811      37                                                       
HET    CE1  O 812      37                                                       
HET    CE1  O 813      37                                                       
HET    1PE  A 705      16                                                       
HET    HQO  N 800      19                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     OAA OXALOACETATE ION                                                 
HETNAM     ACT ACETATE ION                                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     HQO 2-HEPTYL-4-HYDROXY QUINOLINE N-OXIDE                             
HETNAM     CE1 O-DODECANYL OCTAETHYLENE GLYCOL                                  
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     HQO 2-HEPTYL-1-OXY-QUINOLIN-4-OL                                     
HETSYN     CE1 THESIT                                                           
HETSYN     1PE PEG400                                                           
FORMUL   9    K    2(K 1+)                                                      
FORMUL  11  OAA    2(C4 H3 O5 1-)                                               
FORMUL  12  ACT    3(C2 H3 O2 1-)                                               
FORMUL  16  FES    2(FE2 S2)                                                    
FORMUL  17  F3S    2(FE3 S4)                                                    
FORMUL  18  SF4    2(FE4 S4)                                                    
FORMUL  19  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  24  HQO    2(C16 H21 N O2)                                              
FORMUL  25  CE1    5(C28 H58 O9)                                                
FORMUL  30  1PE    C10 H22 O6                                                   
FORMUL  32  HOH   *16(H2 O)                                                     
HELIX    1   1 GLY A   13  ASN A   27  1                                  15    
HELIX    2   2 TYR A   39  ALA A   48  5                                  10    
HELIX    3   3 SER A   61  GLY A   73  1                                  13    
HELIX    4   4 GLU A   78  TRP A   99  1                                  22    
HELIX    5   5 LYS A  130  LEU A  144  1                                  15    
HELIX    6   6 ALA A  195  TYR A  199  5                                   5    
HELIX    7   7 GLY A  210  SER A  218  1                                   9    
HELIX    8   8 GLU A  245  GLU A  250  1                                   6    
HELIX    9   9 ARG A  261  TYR A  266  5                                   6    
HELIX   10  10 TYR A  281  GLY A  285  5                                   5    
HELIX   11  11 PRO A  286  GLY A  301  1                                  16    
HELIX   12  12 LEU A  316  LEU A  319  5                                   4    
HELIX   13  13 GLY A  320  LEU A  328  1                                   9    
HELIX   14  14 LEU A  328  GLY A  340  1                                  13    
HELIX   15  15 SER A  393  THR A  416  1                                  24    
HELIX   16  16 ASN A  421  GLN A  442  1                                  22    
HELIX   17  17 ASN A  447  CYS A  463  1                                  17    
HELIX   18  18 THR A  468  LYS A  487  1                                  20    
HELIX   19  19 ASN A  499  ARG A  525  1                                  27    
HELIX   20  20 SER B   35  LEU B   47  1                                  13    
HELIX   21  21 CYS B   77  THR B   79  5                                   3    
HELIX   22  22 PHE B   80  TYR B   84  5                                   5    
HELIX   23  23 MET B  106  ILE B  116  1                                  11    
HELIX   24  24 THR B  126  GLY B  130  5                                   5    
HELIX   25  25 THR B  135  LYS B  141  1                                   7    
HELIX   26  26 TYR B  142  GLY B  147  5                                   6    
HELIX   27  27 GLY B  152  CYS B  158  1                                   7    
HELIX   28  28 CYS B  158  ASN B  164  1                                   7    
HELIX   29  29 GLY B  169  GLU B  181  1                                  13    
HELIX   30  30 LYS B  188  SER B  197  1                                  10    
HELIX   31  31 GLY B  200  CYS B  204  5                                   5    
HELIX   32  32 GLY B  208  CYS B  214  1                                   7    
HELIX   33  33 ASP B  219  LEU B  240  1                                  22    
HELIX   34  34 THR C   14  LYS C   18  5                                   5    
HELIX   35  35 LEU C   19  THR C   31  1                                  13    
HELIX   36  36 THR C   31  ASN C   51  1                                  21    
HELIX   37  37 ASN C   51  GLN C   64  1                                  14    
HELIX   38  38 PRO C   66  ALA C   90  1                                  25    
HELIX   39  39 PRO C   91  ALA C   94  5                                   4    
HELIX   40  40 PRO C  105  TYR C  129  1                                  25    
HELIX   41  41 ASP D    9  ILE D   27  1                                  19    
HELIX   42  42 ILE D   27  ILE D   37  1                                  11    
HELIX   43  43 LEU D   38  GLY D   42  5                                   5    
HELIX   44  44 SER D   50  GLN D   59  1                                  10    
HELIX   45  45 SER D   60  LEU D   89  1                                  30    
HELIX   46  46 ALA D   95  VAL D  116  1                                  22    
HELIX   47  47 GLY M   13  ASN M   27  1                                  15    
HELIX   48  48 TYR M   39  ALA M   48  5                                  10    
HELIX   49  49 SER M   61  ASP M   74  1                                  14    
HELIX   50  50 GLU M   78  HIS M   88  1                                  11    
HELIX   51  51 HIS M   88  TRP M   99  1                                  12    
HELIX   52  52 ALA M  127  THR M  131  5                                   5    
HELIX   53  53 GLY M  132  SER M  143  1                                  12    
HELIX   54  54 LEU M  144  PHE M  146  5                                   3    
HELIX   55  55 ALA M  195  TYR M  199  5                                   5    
HELIX   56  56 GLY M  210  HIS M  219  1                                  10    
HELIX   57  57 GLU M  245  GLU M  250  1                                   6    
HELIX   58  58 ARG M  261  GLY M  267  5                                   7    
HELIX   59  59 TYR M  281  GLY M  285  5                                   5    
HELIX   60  60 PRO M  286  GLY M  301  1                                  16    
HELIX   61  61 GLY M  320  LEU M  328  1                                   9    
HELIX   62  62 LEU M  328  VAL M  339  1                                  12    
HELIX   63  63 GLY M  378  SER M  381  5                                   4    
HELIX   64  64 ASN M  394  THR M  416  1                                  23    
HELIX   65  65 ASN M  421  GLN M  442  1                                  22    
HELIX   66  66 ASN M  447  CYS M  463  1                                  17    
HELIX   67  67 THR M  468  LYS M  487  1                                  20    
HELIX   68  68 ASN M  499  ARG M  525  1                                  27    
HELIX   69  69 SER N   35  LEU N   47  1                                  13    
HELIX   70  70 CYS N   77  THR N   79  5                                   3    
HELIX   71  71 PHE N   80  TYR N   84  5                                   5    
HELIX   72  72 MET N  106  ILE N  116  1                                  11    
HELIX   73  73 THR N  126  GLY N  130  5                                   5    
HELIX   74  74 THR N  135  ALA N  140  1                                   6    
HELIX   75  75 LYS N  141  TYR N  142  5                                   2    
HELIX   76  76 HIS N  143  CYS N  148  5                                   6    
HELIX   77  77 GLY N  152  CYS N  158  1                                   7    
HELIX   78  78 CYS N  158  ASN N  164  1                                   7    
HELIX   79  79 GLY N  169  GLU N  181  1                                  13    
HELIX   80  80 LYS N  188  ASN N  196  1                                   9    
HELIX   81  81 GLY N  200  CYS N  204  5                                   5    
HELIX   82  82 GLY N  208  CYS N  214  1                                   7    
HELIX   83  83 ASP N  219  LEU N  240  1                                  22    
HELIX   84  84 LEU O   19  THR O   31  1                                  13    
HELIX   85  85 THR O   31  ASN O   51  1                                  21    
HELIX   86  86 ASN O   51  GLN O   64  1                                  14    
HELIX   87  87 ASN O   65  ALA O   90  1                                  26    
HELIX   88  88 PRO O   91  ALA O   94  5                                   4    
HELIX   89  89 PRO O  105  TYR O  129  1                                  25    
HELIX   90  90 ASP P    9  ILE P   27  1                                  19    
HELIX   91  91 ILE P   27  ILE P   37  1                                  11    
HELIX   92  92 LEU P   38  GLY P   42  5                                   5    
HELIX   93  93 SER P   50  GLN P   59  1                                  10    
HELIX   94  94 SER P   60  LEU P   89  1                                  30    
HELIX   95  95 ALA P   95  ILE P  118  1                                  24    
SHEET    1   A 4 GLN A   1  GLN A   4  0                                        
SHEET    2   A 4 THR A 179  ARG A 184  1  O  ARG A 184   N  PHE A   3           
SHEET    3   A 4 HIS A 166  ASN A 174 -1  N  ASN A 174   O  THR A 179           
SHEET    4   A 4 HIS A 155  ASP A 163 -1  N  LEU A 161   O  ARG A 168           
SHEET    1   B 5 ILE A 149  ASP A 153  0                                        
SHEET    2   B 5 ILE A  32  SER A  36  1  N  ILE A  32   O  GLN A 150           
SHEET    3   B 5 LEU A   7  VAL A  10  1  N  ILE A   9   O  ILE A  35           
SHEET    4   B 5 VAL A 188  MET A 190  1  O  VAL A 189   N  VAL A  10           
SHEET    5   B 5 LEU A 374  ALA A 376  1  O  PHE A 375   N  VAL A 188           
SHEET    1   C 2 SER A  52  ALA A  53  0                                        
SHEET    2   C 2 THR A 124  TRP A 125 -1  O  TRP A 125   N  SER A  52           
SHEET    1   D 5 SER A 381  SER A 382  0                                        
SHEET    2   D 5 GLY A 360  GLU A 362  1  N  ILE A 361   O  SER A 382           
SHEET    3   D 5 LEU A 223  ARG A 224 -1  N  ARG A 224   O  GLY A 360           
SHEET    4   D 5 LYS A 549  ARG A 555 -1  O  ALA A 553   N  LEU A 223           
SHEET    5   D 5 THR A 561  ASP A 567 -1  O  ARG A 562   N  PHE A 554           
SHEET    1   E 4 VAL A 229  GLY A 235  0                                        
SHEET    2   E 4 ILE A 348  THR A 357 -1  O  TYR A 356   N  GLN A 230           
SHEET    3   E 4 VAL A 312  ASP A 315 -1  N  LEU A 314   O  ILE A 348           
SHEET    4   E 4 ILE A 253  VAL A 255 -1  N  ILE A 253   O  ASP A 315           
SHEET    1   F 5 HIS B  22  TYR B  30  0                                        
SHEET    2   F 5 LYS B   4  ARG B  12 -1  N  ILE B   8   O  TYR B  26           
SHEET    3   F 5 MET B  88  ALA B  92  1  O  VAL B  90   N  GLU B   9           
SHEET    4   F 5 GLY B  66  VAL B  69 -1  N  MET B  68   O  GLU B  91           
SHEET    5   F 5 VAL B  72  LEU B  75 -1  O  LYS B  74   N  MET B  67           
SHEET    1   G 2 ILE B  98  ARG B 100  0                                        
SHEET    2   G 2 VAL B 103  VAL B 104 -1  O  VAL B 103   N  ARG B 100           
SHEET    1   H 4 PHE M   3  GLN M   4  0                                        
SHEET    2   H 4 THR M 179  ARG M 184  1  O  ARG M 184   N  PHE M   3           
SHEET    3   H 4 VAL M 167  ASN M 174 -1  N  ASN M 174   O  THR M 179           
SHEET    4   H 4 ASP M 159  VAL M 162 -1  N  ASP M 159   O  VAL M 171           
SHEET    1   I 3 ALA M   8  VAL M  10  0                                        
SHEET    2   I 3 VAL M 188  MET M 190  1  O  VAL M 189   N  VAL M  10           
SHEET    3   I 3 LEU M 374  ALA M 376  1  O  PHE M 375   N  MET M 190           
SHEET    1   J 2 ILE M  35  SER M  36  0                                        
SHEET    2   J 2 PHE M 152  ASP M 153  1  O  PHE M 152   N  SER M  36           
SHEET    1   K 3 SER M  52  ALA M  53  0                                        
SHEET    2   K 3 THR M 124  TRP M 125 -1  O  TRP M 125   N  SER M  52           
SHEET    3   K 3 VAL M 113  ARG M 114 -1  N  ARG M 114   O  THR M 124           
SHEET    1   L 4 GLY M 360  ILE M 361  0                                        
SHEET    2   L 4 LEU M 223  ARG M 224 -1  N  ARG M 224   O  GLY M 360           
SHEET    3   L 4 LYS M 549  ARG M 555 -1  O  ALA M 553   N  LEU M 223           
SHEET    4   L 4 THR M 561  ASP M 567 -1  O  SER M 566   N  HIS M 550           
SHEET    1   M 4 VAL M 229  GLY M 235  0                                        
SHEET    2   M 4 ILE M 348  THR M 357 -1  O  THR M 353   N  HIS M 232           
SHEET    3   M 4 GLY M 309  ASP M 315 -1  N  LEU M 314   O  ILE M 348           
SHEET    4   M 4 ILE M 253  VAL M 255 -1  N  VAL M 255   O  TYR M 313           
SHEET    1   N 4 VAL M 229  GLY M 235  0                                        
SHEET    2   N 4 ILE M 348  THR M 357 -1  O  THR M 353   N  HIS M 232           
SHEET    3   N 4 GLY M 309  ASP M 315 -1  N  LEU M 314   O  ILE M 348           
SHEET    4   N 4 ILE M 304  THR M 306 -1  N  ILE M 304   O  VAL M 311           
SHEET    1   O 5 HIS N  22  TYR N  30  0                                        
SHEET    2   O 5 LYS N   4  ARG N  12 -1  N  VAL N  10   O  ALA N  24           
SHEET    3   O 5 MET N  88  ALA N  92  1  O  VAL N  90   N  GLU N   9           
SHEET    4   O 5 GLY N  66  VAL N  69 -1  N  MET N  68   O  GLU N  91           
SHEET    5   O 5 VAL N  72  LEU N  75 -1  O  VAL N  72   N  VAL N  69           
SHEET    1   P 2 ILE N  98  ARG N 100  0                                        
SHEET    2   P 2 VAL N 103  VAL N 104 -1  O  VAL N 103   N  ARG N 100           
SHEET    1   Q 2 ILE O  97  VAL O  98  0                                        
SHEET    2   Q 2 GLU O 101  LYS O 102 -1  O  GLU O 101   N  VAL O  98           
LINK         O   THR A 357                 K     K A 720     1555   1555  2.71  
LINK         O   MET A 358                 K     K A 720     1555   1555  2.82  
LINK         O   GLY A 359                 K     K A 720     1555   1555  2.68  
LINK         O   GLU A 379                 K     K A 720     1555   1555  2.86  
LINK         O   SER A 381                 K     K A 720     1555   1555  2.77  
LINK         SG  CYS B  57                FE2  FES B 244     1555   1555  2.23  
LINK         SG  CYS B  62                FE2  FES B 244     1555   1555  2.24  
LINK         SG  CYS B  65                FE1  FES B 244     1555   1555  2.26  
LINK         SG  CYS B  77                FE1  FES B 244     1555   1555  2.27  
LINK         SG  CYS B 158                FE4  F3S B 245     1555   1555  2.27  
LINK         SG  CYS B 204                FE1  F3S B 245     1555   1555  2.22  
LINK         SG  CYS B 210                FE3  F3S B 245     1555   1555  2.37  
LINK         SG  CYS B 151                FE1  SF4 B 246     1555   1555  2.24  
LINK         SG  CYS B 148                FE2  SF4 B 246     1555   1555  2.33  
LINK         SG  CYS B 154                FE3  SF4 B 246     1555   1555  2.24  
LINK         SG  CYS B 214                FE4  SF4 B 246     1555   1555  2.24  
LINK         O   THR M 357                 K     K M 820     1555   1555  2.70  
LINK         O   MET M 358                 K     K M 820     1555   1555  2.98  
LINK         O   GLY M 359                 K     K M 820     1555   1555  2.83  
LINK         O   GLU M 379                 K     K M 820     1555   1555  2.81  
LINK         SG  CYS N  57                FE2  FES N 244     1555   1555  2.31  
LINK         SG  CYS N  62                FE2  FES N 244     1555   1555  2.29  
LINK         SG  CYS N  65                FE1  FES N 244     1555   1555  2.26  
LINK         SG  CYS N  77                FE1  FES N 244     1555   1555  2.36  
LINK         SG  CYS N 158                FE4  F3S N 245     1555   1555  2.23  
LINK         SG  CYS N 204                FE1  F3S N 245     1555   1555  2.23  
LINK         SG  CYS N 210                FE3  F3S N 245     1555   1555  2.34  
LINK         SG  CYS N 151                FE1  SF4 N 246     1555   1555  2.04  
LINK         SG  CYS N 148                FE2  SF4 N 246     1555   1555  2.04  
LINK         SG  CYS N 154                FE3  SF4 N 246     1555   1555  2.33  
LINK         SG  CYS N 214                FE4  SF4 N 246     1555   1555  2.40  
CISPEP   1 GLY A  269    PRO A  270          0        -1.32                     
CISPEP   2 GLY C  104    PRO C  105          0         0.30                     
CISPEP   3 GLY M  269    PRO M  270          0        -0.72                     
SITE     1 AC1  5 THR A 357  MET A 358  GLY A 359  GLU A 379                    
SITE     2 AC1  5 SER A 381                                                     
SITE     1 AC2  5 THR M 357  MET M 358  GLY M 359  GLU M 379                    
SITE     2 AC2  5 SER M 381                                                     
SITE     1 AC3  9 HIS A 232  LEU A 242  THR A 244  GLU A 245                    
SITE     2 AC3  9 HIS A 355  ARG A 390  GLY A 392  SER A 393                    
SITE     3 AC3  9 FAD A 721                                                     
SITE     1 AC4  3 ASP A 556  ARG A 562  GLU A 564                               
SITE     1 AC5  3 ARG A 452  GLY B  41  ASP B  45                               
SITE     1 AC6 10 PHE M 116  HIS M 232  LEU M 242  THR M 244                    
SITE     2 AC6 10 GLU M 245  ARG M 287  HIS M 355  ARG M 390                    
SITE     3 AC6 10 SER M 393  FAD M 821                                          
SITE     1 AC7  6 TRP M 448  ARG M 452  GLY N  41  ASP N  45                    
SITE     2 AC7  6 TYR N  53  TRP N  55                                          
SITE     1 AC8  7 SER B  56  CYS B  57  ARG B  58  CYS B  62                    
SITE     2 AC8  7 GLY B  63  CYS B  65  CYS B  77                               
SITE     1 AC9 10 CYS B 158  GLN B 160  CYS B 204  THR B 205                    
SITE     2 AC9 10 PHE B 206  VAL B 207  GLY B 208  TYR B 209                    
SITE     3 AC9 10 CYS B 210  ILE B 224                                          
SITE     1 BC1  6 CYS B 148  ILE B 149  CYS B 151  GLY B 152                    
SITE     2 BC1  6 CYS B 154  CYS B 214                                          
SITE     1 BC2 32 GLY A  11  ALA A  12  GLY A  14  ALA A  15                    
SITE     2 BC2 32 SER A  36  LYS A  37  VAL A  38  SER A  43                    
SITE     3 BC2 32 HIS A  44  THR A  45  ALA A  48  GLU A  49                    
SITE     4 BC2 32 GLY A  50  GLY A  51  HIS A 155  VAL A 157                    
SITE     5 BC2 32 ALA A 191  THR A 192  GLY A 193  THR A 203                    
SITE     6 BC2 32 ASN A 204  ASP A 211  HIS A 355  TYR A 356                    
SITE     7 BC2 32 GLU A 379  ARG A 390  SER A 393  ASN A 394                    
SITE     8 BC2 32 SER A 395  LEU A 396  LEU A 399  OAA A 702                    
SITE     1 BC3  7 SER N  56  CYS N  57  ARG N  58  CYS N  62                    
SITE     2 BC3  7 GLY N  63  CYS N  65  CYS N  77                               
SITE     1 BC4  9 CYS N 158  GLN N 160  CYS N 204  THR N 205                    
SITE     2 BC4  9 PHE N 206  VAL N 207  GLY N 208  CYS N 210                    
SITE     3 BC4  9 ILE N 224                                                     
SITE     1 BC5  8 CYS N 148  ILE N 149  ASN N 150  CYS N 151                    
SITE     2 BC5  8 GLY N 152  CYS N 154  CYS N 214  VAL N 218                    
SITE     1 BC6 36 GLY M  11  ALA M  12  GLY M  13  GLY M  14                    
SITE     2 BC6 36 ALA M  15  SER M  36  LYS M  37  VAL M  38                    
SITE     3 BC6 36 SER M  43  HIS M  44  THR M  45  ALA M  48                    
SITE     4 BC6 36 GLU M  49  GLY M  50  GLY M  51  HIS M 155                    
SITE     5 BC6 36 PHE M 156  VAL M 157  ALA M 191  THR M 192                    
SITE     6 BC6 36 GLY M 193  THR M 203  ASN M 204  ASP M 211                    
SITE     7 BC6 36 LEU M 242  HIS M 355  TYR M 356  GLY M 378                    
SITE     8 BC6 36 GLU M 379  ARG M 390  SER M 393  ASN M 394                    
SITE     9 BC6 36 SER M 395  LEU M 396  LEU M 399  OAA M 802                    
SITE     1 BC7  9 THR B 205  PHE B 206  GLN B 225  LYS B 228                    
SITE     2 BC7  9 ARG C  28  GLU C  29  TRP D  14  PHE D  17                    
SITE     3 BC7  9 HIS D  80                                                     
SITE     1 BC8  8 THR B 239  TRP D  76  ASP P   9  LYS P  97                    
SITE     2 BC8  8 TRP P  98  TYR P 101  GLY P 102  CE1 P 810                    
SITE     1 BC9  6 ASP D   9  TRP D  98  ASP P   9  PHE P  13                    
SITE     2 BC9  6 TRP P  76  CE1 P 710                                          
SITE     1 CC1  7 TYR C 129  LEU D  43  PHE D  44  PRO D  45                    
SITE     2 CC1  7 GLY D  46  LEU O  73  CE1 O 813                               
SITE     1 CC2  8 VAL C  98  PRO C 107  SER C 111  ALA C 114                    
SITE     2 CC2  8 VAL C 118  LEU O 124  TYR O 129  PRO P  45                    
SITE     1 CC3  5 TYR C 129  ARG O  23  PHE O  24  GLY O  30                    
SITE     2 CC3  5 CE1 O 811                                                     
SITE     1 CC4  7 GLY A  72  ARG A 287  ASP A 288  LYS A 289                    
SITE     2 CC4  7 GLN A 292  TYR A 466  GLN A 533                               
SITE     1 CC5  9 THR N 205  PHE N 206  GLN N 225  LYS N 228                    
SITE     2 CC5  9 ARG O  28  GLU O  29  TRP P  14  PHE P  17                    
SITE     3 CC5  9 ARG P  81                                                     
CRYST1   96.505  137.836  273.451  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      0.010360  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007250  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003660        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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