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Database: PDB
Entry: 2BS3
LinkDB: 2BS3
Original site: 2BS3 
HEADER    OXIDOREDUCTASE                          14-MAY-05   2BS3              
TITLE     GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM                
TITLE    2 WOLINELLA SUCCINOGENES                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: QUINOL-FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT A;          
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 EC: 1.3.99.1;                                                        
COMPND   5 OTHER_DETAILS: FAD COVALENTLY BOUND TO HIS A43 BY AN 8-              
COMPND   6  ALPHA-(N-EPSILON-HISTIDYL) BOND;                                    
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: QUINOL-FUMARATE REDUCTASE IRON-SULFUR SUBUNIT B;           
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 EC: 1.3.99.1;                                                        
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: QUINOL-FUMARATE REDUCTASE DIHEME CYTOCHROME B              
COMPND  13  SUBUNIT C;                                                          
COMPND  14 CHAIN: C, F;                                                         
COMPND  15 EC: 1.3.99.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: WOLINELLA SUCCINOGENES;                         
SOURCE   3 ORGANISM_TAXID: 844;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: WOLINELLA SUCCINOGENES;                         
SOURCE   6 ORGANISM_TAXID: 844;                                                 
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: WOLINELLA SUCCINOGENES;                         
SOURCE   9 ORGANISM_TAXID: 844                                                  
KEYWDS    OXIDOREDUCTASE, 2FE-2S, 3D-STRUCTURE, 3FE-4S, 4FE-4S,                 
KEYWDS   2 CITRIC ACID CYCLE, DIHAEM CYTOCHROME B, ELECTRON                     
KEYWDS   3 TRANSPORT, FAD, FLAVOPROTEIN, FUMARATE REDUCTASE, HEME,              
KEYWDS   4 ION-SULPHUR PROTEIN, IRON, IRON- SULFUR, METAL-BINDING,              
KEYWDS   5 RESPIRATORY CHAIN, SUCCINATE DEHYDROGENASE, TRANSMEMBRANE,           
KEYWDS   6 TRICARBOXYLIC ACID CYCLE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.D.LANCASTER                                                       
REVDAT   2   24-FEB-09 2BS3    1       VERSN                                    
REVDAT   1   13-DEC-05 2BS3    0                                                
JRNL        AUTH   C.R.D.LANCASTER,U.S.SAUER,R.GROSS,A.H.HAAS,J.GRAF,           
JRNL        AUTH 2 H.SCHWALBE,W.MAENTELE,J.SIMON,G.MADEJ                        
JRNL        TITL   EXPERIMENTAL SUPPORT FOR THE E-PATHWAY HYPOTHESIS            
JRNL        TITL 2 OF COUPLED TRANSMEMBRANE ELECTRON AND PROTON                 
JRNL        TITL 3 TRANSFER IN DIHEMIC QUINOL:FUMARATE REDUCTASE                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102 18860 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16380425                                                     
JRNL        DOI    10.1073/PNAS.0509711102                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.R.D.LANCASTER                                              
REMARK   1  TITL   WOLINELLA SUCCINOGENES QUINOL:FUMARATE REDUCTASE             
REMARK   1  TITL 2 AND ITS COMPARISON TO E. COLI SUCCINATE:QUINONE              
REMARK   1  TITL 3 REDUCTASE                                                    
REMARK   1  REF    FEBS LETT.                    V. 555    21 2003              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1  PMID   14630313                                                     
REMARK   1  DOI    10.1016/S0014-5793(03)01100-1                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.R.D.LANCASTER                                              
REMARK   1  TITL   WOLINELLA SUCCINOGENES QUINOL:FUMARATE REDUCTASE -           
REMARK   1  TITL 2 2.2 ANGSTROM RESOLUTION CRYSTAL STRUCTURE AND THE            
REMARK   1  TITL 3 E-PATHWAY HYPOTHESIS OF COUPLED TRANSMEMBRANE                
REMARK   1  TITL 4 PROTON AND ELECTRON TRANSFER                                 
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1565   215 2002              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1  PMID   12409197                                                     
REMARK   1  DOI    10.1016/S0005-2736(02)00571-0                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.R.D.LANCASTER,R.GROSS,J.SIMON                              
REMARK   1  TITL   A THIRD CRYSTAL FORM OF WOLINELLA SUCCINOGENES               
REMARK   1  TITL 2 QUINOL:FUMARATE REDUCTASE REVEALS DOMAIN CLOSURE             
REMARK   1  TITL 3 AT THE SITE OF FUMARATE REDUCTION                            
REMARK   1  REF    EUR.J.BIOCHEM.                V. 268  1820 2001              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   11248702                                                     
REMARK   1  DOI    10.1046/J.1432-1327.2001.02053.X                             
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   C.R.D.LANCASTER,R.GROSS,A.HAAS,M.RITTER,W.MAENTELE,          
REMARK   1  AUTH 2 J.SIMON,A.KROEGER                                            
REMARK   1  TITL   ESSENTIAL ROLE OF GLU-C66 FOR MENAQUINOL OXIDATION           
REMARK   1  TITL 2 INDICATES TRANSMEMBRANE ELECTROCHEMICAL POTENTIAL            
REMARK   1  TITL 3 GENERATION BY WOLINELLA SUCCINOGENES FUMARATE                
REMARK   1  TITL 4 REDUCTASE                                                    
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  97 13051 2000              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   11186225                                                     
REMARK   1  DOI    10.1073/PNAS.220425797                                       
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   C.R.D.LANCASTER,A.KROEGER,M.AUER,H.MICHEL                    
REMARK   1  TITL   STRUCTURE OF FUMARATE REDUCTASE FROM WOLINELLA               
REMARK   1  TITL 2 SUCCINOGENES AT 2.2 ANGSTROMS RESOLUTION                     
REMARK   1  REF    NATURE                        V. 402   377 1999              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   10586875                                                     
REMARK   1  DOI    10.1038/46483                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2855917.81                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 182197                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : SHELLS                          
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.5                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1000                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.4                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10372                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.220                        
REMARK   3   BIN FREE R VALUE                    : 0.257                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 0.6                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 58                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.034                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18306                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 440                                     
REMARK   3   SOLVENT ATOMS            : 991                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.0                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64                                                 
REMARK   3    B22 (A**2) : -2.93                                                
REMARK   3    B33 (A**2) : 2.29                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 2.80                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.3                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.3                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.63                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.309923                                             
REMARK   3   BSOL        : 48.4032                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : PARHEM.ROY                                     
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : CIT.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : TOPHEM.ROY                                     
REMARK   3  TOPOLOGY FILE  4   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  5   : CIT.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BS3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-23965.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 277.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 182229                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2BS2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       94.38300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, E, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  FUNCTION: ESSENTIAL FOR FUMARATE RESPIRATION                        
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     ARG C   256                                                      
REMARK 465     ARG F   256                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 656    CA   C    O    CB   CG   CD   CE   NZ               
REMARK 470     HIS C 255    CA   C    O    CB   CG   ND1  CD2  CE1  NE2         
REMARK 470     LYS D 656    CA   C    O    CB   CG   CD   CE   NZ               
REMARK 470     HIS F 255    CA   C    O    CB   CG   ND1  CD2  CE1  NE2         
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A 145    CE   NZ                                             
REMARK 480     LYS A 336    CD   CE   NZ                                        
REMARK 480     ARG A 343    CZ  NH1  NH2                                        
REMARK 480     GLU A 359    CG   CD  OE1  OE2                                   
REMARK 480     LYS A 445    CE   NZ                                             
REMARK 480     LYS A 492    CD   CE   NZ                                        
REMARK 480     LYS A 507    CD   CE   NZ                                        
REMARK 480     LYS A 554    CD   CE   NZ                                        
REMARK 480     ALA A 599    CB                                                  
REMARK 480     LYS A 618    CD   CE   NZ                                        
REMARK 480     LYS B 126    CD   CE   NZ                                        
REMARK 480     LYS B 132    CD   CE   NZ                                        
REMARK 480     PHE C  47    CG  CD1  CD2  CE1  CE2   CZ                         
REMARK 480     ILE C  70   CD1                                                  
REMARK 480     LYS C 112    CE   NZ                                             
REMARK 480     ARG C 119    CZ  NH1  NH2                                        
REMARK 480     LYS C 204    CG   CD   CE   NZ                                   
REMARK 480     LYS D   2    CE   NZ                                             
REMARK 480     LYS D 145    CE   NZ                                             
REMARK 480     ARG D 273    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     LYS D 336    CG   CD   CE   NZ                                   
REMARK 480     ARG D 343    CZ  NH1  NH2                                        
REMARK 480     GLU D 359    CG   CD  OE1  OE2                                   
REMARK 480     LYS D 445    CE   NZ                                             
REMARK 480     LYS D 492    CD   CE   NZ                                        
REMARK 480     LYS D 502    CE   NZ                                             
REMARK 480     LYS D 507    CD   CE   NZ                                        
REMARK 480     LYS D 554    CD   CE   NZ                                        
REMARK 480     ALA D 599    CB                                                  
REMARK 480     LYS D 618    CD   CE   NZ                                        
REMARK 480     LYS E 126    CD   CE   NZ                                        
REMARK 480     LYS E 132    CD   CE   NZ                                        
REMARK 480     ILE F  70   CD1                                                  
REMARK 480     LYS F 112    CE   NZ                                             
REMARK 480     LYS F 204    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE C  47   CB  -  CG  -  CD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    PHE C  47   CB  -  CG  -  CD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 121      -10.95   -165.34                                   
REMARK 500    GLN A 122       65.77    175.59                                   
REMARK 500    LYS A 123       72.30    -59.42                                   
REMARK 500    THR A 124     -143.91   -104.13                                   
REMARK 500    ALA A 153     -126.39     51.87                                   
REMARK 500    ALA A 155       52.15   -144.79                                   
REMARK 500    ASN A 250       51.58     33.73                                   
REMARK 500    THR A 269      145.89    -29.02                                   
REMARK 500    ASP A 281     -163.72   -100.24                                   
REMARK 500    GLU A 294      -71.30    -77.84                                   
REMARK 500    LYS A 296     -135.86     59.12                                   
REMARK 500    PHE A 352      -50.30   -122.19                                   
REMARK 500    GLU A 359      -52.71   -134.17                                   
REMARK 500    HIS A 369      -46.47   -135.06                                   
REMARK 500    ASP A 398       72.72     67.64                                   
REMARK 500    ASN A 403      105.85   -170.53                                   
REMARK 500    ALA A 513       61.10     27.84                                   
REMARK 500    TYR A 552       67.88   -150.33                                   
REMARK 500    MET A 638       92.05   -161.41                                   
REMARK 500    ARG B   3      146.34     52.12                                   
REMARK 500    VAL B  56      -73.92   -136.40                                   
REMARK 500    LYS B 101      137.46   -172.46                                   
REMARK 500    ASP B 102     -109.57     52.26                                   
REMARK 500    ILE C  70      -31.33   -139.67                                   
REMARK 500    ARG C 252      -33.39   -135.14                                   
REMARK 500    THR C 253       29.64   -153.83                                   
REMARK 500    ALA D 121      -10.77   -165.39                                   
REMARK 500    GLN D 122       65.64    175.54                                   
REMARK 500    LYS D 123       72.30    -59.31                                   
REMARK 500    THR D 124     -143.79   -104.08                                   
REMARK 500    ALA D 153     -125.76     52.05                                   
REMARK 500    ALA D 155       52.96   -144.09                                   
REMARK 500    ASN D 250       50.17     34.30                                   
REMARK 500    THR D 269      145.94    -28.94                                   
REMARK 500    ASP D 281     -164.73   -100.66                                   
REMARK 500    GLU D 294      -70.93    -78.06                                   
REMARK 500    LYS D 296     -140.27     60.03                                   
REMARK 500    PHE D 352      -50.37   -122.51                                   
REMARK 500    GLU D 359      -52.99   -134.23                                   
REMARK 500    HIS D 369      -46.00   -134.85                                   
REMARK 500    ASP D 398       73.31     67.55                                   
REMARK 500    ASN D 403      106.36   -170.44                                   
REMARK 500    ALA D 513       61.57     27.96                                   
REMARK 500    TYR D 552       67.69   -150.36                                   
REMARK 500    MET D 638       92.40   -161.04                                   
REMARK 500    ARG E   3      146.41     51.80                                   
REMARK 500    VAL E  56      -74.46   -135.44                                   
REMARK 500    LYS E 101      136.89   -171.44                                   
REMARK 500    ASP E 102     -109.01     53.11                                   
REMARK 500    ILE F  70      -31.36   -139.60                                   
REMARK 500    VAL F 164      -60.17    -97.15                                   
REMARK 500    ARG F 252      -33.20   -134.93                                   
REMARK 500    THR F 253       29.78   -154.28                                   
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 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    ASP A 398        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PRO C 102        46.8      L          L   OUTSIDE RANGE           
REMARK 500    PRO F 102        46.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     LMT C 1257                                                       
REMARK 615     LMT F 1257                                                       
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                              NA A1658  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 393   O                                                      
REMARK 620 2 ALA A 395   O    92.4                                              
REMARK 620 3 HOH A2156   O   101.5  80.4                                        
REMARK 620 4 SER A 371   O    91.8 175.5 100.3                                  
REMARK 620 5 GLY A 373   O    92.6  98.5 165.9  79.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1658  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY D 373   O                                                      
REMARK 620 2 GLU D 393   O    91.0                                              
REMARK 620 3 SER D 371   O    78.9  91.5                                        
REMARK 620 4 ALA D 395   O    97.1  91.7 174.9                                  
REMARK 620 5 HOH D2162   O   164.8 104.1 101.2  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B1240  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 CYS B  77   SG   98.7                                              
REMARK 620 3 FES B1240  FE2  142.2 119.1                                        
REMARK 620 4 FES B1240   S1  121.3 102.9  52.0                                  
REMARK 620 5 FES B1240   S2  115.7 112.5  52.9 104.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B1240  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  62   SG                                                     
REMARK 620 2 FES B1240  FE1  143.2                                              
REMARK 620 3 FES B1240   S1  120.7  52.0                                        
REMARK 620 4 CYS B  57   SG   98.0 118.7 102.7                                  
REMARK 620 5 FES B1240   S2  117.4  52.6 104.5 112.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES E1240  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E  77   SG                                                     
REMARK 620 2 CYS E  65   SG   98.6                                              
REMARK 620 3 FES E1240  FE2  118.4 142.9                                        
REMARK 620 4 FES E1240   S1  102.1 121.0  51.7                                  
REMARK 620 5 FES E1240   S2  112.6 116.8  52.9 104.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES E1240  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E  62   SG                                                     
REMARK 620 2 FES E1240  FE1  142.7                                              
REMARK 620 3 FES E1240   S1  121.8  51.9                                        
REMARK 620 4 FES E1240   S2  116.3  52.2 104.1                                  
REMARK 620 5 CYS E  57   SG   98.5 118.8 103.5 111.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1241  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S B1241  FE3                                                     
REMARK 620 2 F3S B1241   S3   54.7                                              
REMARK 620 3 F3S B1241   S1   53.0 105.9                                        
REMARK 620 4 F3S B1241  FE4   61.8  50.6 103.6                                  
REMARK 620 5 F3S B1241   S2  103.6 100.2 109.5  52.7                            
REMARK 620 6 CYS B 161   SG  147.0 115.9 114.9 141.5 109.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1241  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 208   SG                                                     
REMARK 620 2 F3S B1241   S3  124.1                                              
REMARK 620 3 F3S B1241   S1  116.4 105.9                                        
REMARK 620 4 F3S B1241  FE4  139.0  50.0 102.3                                  
REMARK 620 5 F3S B1241   S4  101.9  97.8 107.9  50.7                            
REMARK 620 6 F3S B1241  FE1  157.8  54.7  53.0  60.3 100.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1241  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S B1241  FE3                                                     
REMARK 620 2 F3S B1241   S3   53.9                                              
REMARK 620 3 F3S B1241   S4   51.7 102.5                                        
REMARK 620 4 CYS B 214   SG  148.1 120.4 110.7                                  
REMARK 620 5 F3S B1241  FE1   58.0  54.6  98.9 150.0                            
REMARK 620 6 F3S B1241   S2  101.0 104.6 107.3 110.4  53.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S E1241  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 161   SG                                                     
REMARK 620 2 F3S E1241   S1  114.5                                              
REMARK 620 3 F3S E1241  FE3  147.5  53.2                                        
REMARK 620 4 F3S E1241  FE4  141.8 103.6  61.7                                  
REMARK 620 5 F3S E1241   S2  108.8 109.8 103.6  52.6                            
REMARK 620 6 F3S E1241   S3  116.5 106.0  54.7  50.8 100.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S E1241  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S E1241  FE1                                                     
REMARK 620 2 F3S E1241   S1   52.6                                              
REMARK 620 3 F3S E1241  FE4   60.5 102.1                                        
REMARK 620 4 F3S E1241   S3   55.0 105.7  50.4                                  
REMARK 620 5 F3S E1241   S4  100.3 108.4  50.4  97.7                            
REMARK 620 6 CYS E 208   SG  157.5 116.0 139.5 124.3 102.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S E1241  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S E1241  FE1                                                     
REMARK 620 2 CYS E 214   SG  149.2                                              
REMARK 620 3 F3S E1241  FE3   57.9 148.3                                        
REMARK 620 4 F3S E1241   S2   53.5 110.1 101.2                                  
REMARK 620 5 F3S E1241   S3   54.6 119.6  53.9 104.7                            
REMARK 620 6 F3S E1241   S4   99.6 110.8  52.2 108.2 102.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1242  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 157   SG                                                     
REMARK 620 2 SF4 B1242  FE2  139.0                                              
REMARK 620 3 SF4 B1242  FE3  150.2  58.2                                        
REMARK 620 4 SF4 B1242  FE4  144.1  60.7  60.9                                  
REMARK 620 5 SF4 B1242   S2  121.4  99.5  51.8  54.3                            
REMARK 620 6 SF4 B1242   S4  114.8  52.5  50.5 100.6  99.6                      
REMARK 620 7 SF4 B1242   S3  110.0  51.9  99.1  53.2 106.6 102.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1242  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B1242  FE1                                                     
REMARK 620 2 SF4 B1242  FE3   60.6                                              
REMARK 620 3 SF4 B1242  FE4   58.7  61.1                                        
REMARK 620 4 SF4 B1242   S1   99.1  51.6  53.2                                  
REMARK 620 5 SF4 B1242   S4   53.9  51.8 100.1 101.7                            
REMARK 620 6 CYS B 154   SG  134.2 159.0 136.8 124.6 120.1                      
REMARK 620 7 SF4 B1242   S3   53.1 102.1  52.6 103.9 105.0  98.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1242  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 151   SG                                                     
REMARK 620 2 SF4 B1242  FE1  136.1                                              
REMARK 620 3 SF4 B1242  FE2  141.6  61.2                                        
REMARK 620 4 SF4 B1242  FE4  153.9  58.9  61.0                                  
REMARK 620 5 SF4 B1242   S1  121.4 102.3  55.2  53.9                            
REMARK 620 6 SF4 B1242   S2  113.7  53.1 103.0  53.6 104.5                      
REMARK 620 7 SF4 B1242   S4  103.1  54.8  54.8 102.4 108.0 104.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1242  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B1242  FE1                                                     
REMARK 620 2 SF4 B1242  FE2   60.6                                              
REMARK 620 3 SF4 B1242  FE3   60.2  57.9                                        
REMARK 620 4 SF4 B1242   S1  100.4  53.0  50.3                                  
REMARK 620 5 SF4 B1242   S2   53.1  98.6  51.3  98.8                            
REMARK 620 6 CYS B 218   SG  146.1 139.3 148.8 113.3 122.0                      
REMARK 620 7 SF4 B1242   S3   53.8  52.0  99.0 103.1 106.1 111.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E1242  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 E1242  FE2                                                     
REMARK 620 2 SF4 E1242   S3   51.8                                              
REMARK 620 3 SF4 E1242   S4   52.6 102.4                                        
REMARK 620 4 SF4 E1242  FE4   60.7  53.2 100.6                                  
REMARK 620 5 CYS E 157   SG  139.7 111.4 114.1 144.9                            
REMARK 620 6 SF4 E1242  FE3   58.3  99.1  50.4  61.0 148.8                      
REMARK 620 7 SF4 E1242   S2   99.6 106.8  99.4  54.4 120.7  51.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E1242  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 154   SG                                                     
REMARK 620 2 SF4 E1242  FE1  133.8                                              
REMARK 620 3 SF4 E1242   S3   98.7  53.2                                        
REMARK 620 4 SF4 E1242   S4  119.7  53.9 105.1                                  
REMARK 620 5 SF4 E1242  FE4  137.2  58.6  52.5  99.9                            
REMARK 620 6 SF4 E1242   S1  125.1  99.1 104.1 101.5  53.5                      
REMARK 620 7 SF4 E1242  FE3  158.9  60.6 102.2  51.6  61.0  51.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E1242  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 E1242  FE1                                                     
REMARK 620 2 SF4 E1242  FE2   61.2                                              
REMARK 620 3 SF4 E1242   S4   54.8  54.9                                        
REMARK 620 4 SF4 E1242  FE4   58.7  60.9 102.3                                  
REMARK 620 5 SF4 E1242   S1  102.3  55.2 108.0  54.2                            
REMARK 620 6 CYS E 151   SG  136.2 140.8 102.5 154.8 121.1                      
REMARK 620 7 SF4 E1242   S2   53.4 103.3 105.1  53.7 104.7 114.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E1242  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 E1242  FE1                                                     
REMARK 620 2 SF4 E1242  FE2   60.7                                              
REMARK 620 3 SF4 E1242   S3   54.0  51.9                                        
REMARK 620 4 CYS E 218   SG  146.0 139.0 111.1                                  
REMARK 620 5 SF4 E1242   S1  100.5  53.0 103.0 113.2                            
REMARK 620 6 SF4 E1242  FE3   60.3  58.0  99.2 148.9  50.3                      
REMARK 620 7 SF4 E1242   S2   53.5  99.0 106.7 122.0  98.8  51.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1255  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  93   NE2                                                    
REMARK 620 2 HIS C 182   NE2 177.9                                              
REMARK 620 3 HEM C1255   NB   89.1  88.9                                        
REMARK 620 4 HEM C1255   NC   88.0  91.2  88.7                                  
REMARK 620 5 HEM C1255   NA   88.5  92.3  91.4 176.6                            
REMARK 620 6 HEM C1255   ND   94.7  87.2 175.7  89.7  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1256  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM C1256   NB                                                     
REMARK 620 2 HIS C  44   NE2  90.9                                              
REMARK 620 3 HIS C 143   NE2  86.5 177.4                                        
REMARK 620 4 HEM C1256   NA   89.0  90.8  89.2                                  
REMARK 620 5 HEM C1256   NC   88.6  90.0  90.0 177.5                            
REMARK 620 6 HEM C1256   ND  179.8  89.3  93.3  90.8  91.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F1255  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  93   NE2                                                    
REMARK 620 2 HIS F 182   NE2 177.5                                              
REMARK 620 3 HEM F1255   NA   87.3  91.2                                        
REMARK 620 4 HEM F1255   NB   89.3  88.8  90.1                                  
REMARK 620 5 HEM F1255   NC   89.3  92.1 176.7  90.1                            
REMARK 620 6 HEM F1255   ND   94.4  87.5  89.0 176.1  91.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F1256  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM F1256   NA                                                     
REMARK 620 2 HIS F  44   NE2  90.3                                              
REMARK 620 3 HIS F 143   NE2  89.5 179.2                                        
REMARK 620 4 HEM F1256   NB   90.6  92.6  88.2                                  
REMARK 620 5 HEM F1256   NC  178.5  89.3  90.9  90.8                            
REMARK 620 6 HEM F1256   ND   88.7  87.4  91.8 179.3  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1658                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA D1658                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1656                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A1657                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B1240                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B1241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B1242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C1255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C1256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT C1257                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D1656                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT D1657                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E1240                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S E1241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E1242                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F1255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F1256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT F1257                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E7P   RELATED DB: PDB                                   
REMARK 900  QUINOL:FUMARATE REDUCTASE FROM WOLINELLA                            
REMARK 900  SUCCINOGENES                                                        
REMARK 900 RELATED ID: 1QLA   RELATED DB: PDB                                   
REMARK 900  RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE                      
REMARK 900   FROM WOLINELLA SUCCINOGENES                                        
REMARK 900 RELATED ID: 1QLB   RELATED DB: PDB                                   
REMARK 900  RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE                      
REMARK 900   FROM WOLINELLA SUCCINOGENES                                        
REMARK 900 RELATED ID: 2BS2   RELATED DB: PDB                                   
REMARK 900  QUINOL:FUMARATE REDUCTASE FROM WOLINELLA                            
REMARK 900  SUCCINOGENES                                                        
REMARK 900 RELATED ID: 2BS4   RELATED DB: PDB                                   
REMARK 900  GLU C180 -> ILE VARIANT QUINOL:FUMARATE                             
REMARK 900  REDUCTASE FROM WOLINELLA SUCCINOGENES                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS SAY CONFLICT GLN 180 GLU FOR CHAINS C, F IS A VARIANT        
DBREF  2BS3 A    1   656  UNP    P17412   FRDA_WOLSU       1    656             
DBREF  2BS3 B    1   239  UNP    P17596   FRDB_WOLSU       1    239             
DBREF  2BS3 C    1   256  UNP    P17413   FRDC_WOLSU       1    256             
DBREF  2BS3 D    1   656  UNP    P17412   FRDA_WOLSU       1    656             
DBREF  2BS3 E    1   239  UNP    P17596   FRDB_WOLSU       1    239             
DBREF  2BS3 F    1   256  UNP    P17413   FRDC_WOLSU       1    256             
SEQADV 2BS3 GLN C  180  UNP  P17413    GLU   180 CONFLICT SEE REMARK 999        
SEQADV 2BS3 GLN F  180  UNP  P17413    GLU   180 CONFLICT SEE REMARK 999        
SEQRES   1 A  656  MET LYS VAL GLN TYR CYS ASP SER LEU VAL ILE GLY GLY          
SEQRES   2 A  656  GLY LEU ALA GLY LEU ARG ALA ALA VAL ALA THR GLN GLN          
SEQRES   3 A  656  LYS GLY LEU SER THR ILE VAL LEU SER LEU ILE PRO VAL          
SEQRES   4 A  656  LYS ARG SER HIS SER ALA ALA ALA GLN GLY GLY MET GLN          
SEQRES   5 A  656  ALA SER LEU GLY ASN SER LYS MET SER ASP GLY ASP ASN          
SEQRES   6 A  656  GLU ASP LEU HIS PHE MET ASP THR VAL LYS GLY SER ASP          
SEQRES   7 A  656  TRP GLY CYS ASP GLN LYS VAL ALA ARG MET PHE VAL ASN          
SEQRES   8 A  656  THR ALA PRO LYS ALA ILE ARG GLU LEU ALA ALA TRP GLY          
SEQRES   9 A  656  VAL PRO TRP THR ARG ILE HIS LYS GLY ASP ARG MET ALA          
SEQRES  10 A  656  ILE ILE ASN ALA GLN LYS THR THR ILE THR GLU GLU ASP          
SEQRES  11 A  656  PHE ARG HIS GLY LEU ILE HIS SER ARG ASP PHE GLY GLY          
SEQRES  12 A  656  THR LYS LYS TRP ARG THR CYS TYR THR ALA ASP ALA THR          
SEQRES  13 A  656  GLY HIS THR MET LEU PHE ALA VAL ALA ASN GLU CYS LEU          
SEQRES  14 A  656  LYS LEU GLY VAL SER ILE GLN ASP ARG LYS GLU ALA ILE          
SEQRES  15 A  656  ALA LEU ILE HIS GLN ASP GLY LYS CYS TYR GLY ALA VAL          
SEQRES  16 A  656  VAL ARG ASP LEU VAL THR GLY ASP ILE ILE ALA TYR VAL          
SEQRES  17 A  656  ALA LYS GLY THR LEU ILE ALA THR GLY GLY TYR GLY ARG          
SEQRES  18 A  656  ILE TYR LYS ASN THR THR ASN ALA VAL VAL CYS GLU GLY          
SEQRES  19 A  656  THR GLY THR ALA ILE ALA LEU GLU THR GLY ILE ALA GLN          
SEQRES  20 A  656  LEU GLY ASN MET GLU ALA VAL GLN PHE HIS PRO THR PRO          
SEQRES  21 A  656  LEU PHE PRO SER GLY ILE LEU LEU THR GLU GLY CYS ARG          
SEQRES  22 A  656  GLY ASP GLY GLY ILE LEU ARG ASP VAL ASP GLY HIS ARG          
SEQRES  23 A  656  PHE MET PRO ASP TYR GLU PRO GLU LYS LYS GLU LEU ALA          
SEQRES  24 A  656  SER ARG ASP VAL VAL SER ARG ARG MET ILE GLU HIS ILE          
SEQRES  25 A  656  ARG LYS GLY LYS GLY VAL GLN SER PRO TYR GLY GLN HIS          
SEQRES  26 A  656  LEU TRP LEU ASP ILE SER ILE LEU GLY ARG LYS HIS ILE          
SEQRES  27 A  656  GLU THR ASN LEU ARG ASP VAL GLN GLU ILE CYS GLU TYR          
SEQRES  28 A  656  PHE ALA GLY ILE ASP PRO ALA GLU LYS TRP ALA PRO VAL          
SEQRES  29 A  656  LEU PRO MET GLN HIS TYR SER MET GLY GLY ILE ARG THR          
SEQRES  30 A  656  ASP TYR ARG GLY GLU ALA LYS LEU LYS GLY LEU PHE SER          
SEQRES  31 A  656  ALA GLY GLU ALA ALA CYS TRP ASP MET HIS GLY PHE ASN          
SEQRES  32 A  656  ARG LEU GLY GLY ASN SER VAL SER GLU ALA VAL VAL ALA          
SEQRES  33 A  656  GLY MET ILE VAL GLY GLU TYR PHE ALA GLU HIS CYS ALA          
SEQRES  34 A  656  ASN THR GLN VAL ASP LEU GLU THR LYS THR LEU GLU LYS          
SEQRES  35 A  656  PHE VAL LYS GLY GLN GLU ALA TYR MET LYS SER LEU VAL          
SEQRES  36 A  656  GLU SER LYS GLY THR GLU ASP VAL PHE LYS ILE LYS ASN          
SEQRES  37 A  656  ARG MET LYS ASP VAL MET ASP ASP ASN VAL GLY ILE PHE          
SEQRES  38 A  656  ARG ASP GLY PRO HIS LEU GLU LYS ALA VAL LYS GLU LEU          
SEQRES  39 A  656  GLU GLU LEU TYR LYS LYS SER LYS ASN VAL GLY ILE LYS          
SEQRES  40 A  656  ASN LYS ARG LEU HIS ALA ASN PRO GLU LEU GLU GLU ALA          
SEQRES  41 A  656  TYR ARG VAL PRO MET MET LEU LYS VAL ALA LEU CYS VAL          
SEQRES  42 A  656  ALA LYS GLY ALA LEU ASP ARG THR GLU SER ARG GLY ALA          
SEQRES  43 A  656  HIS ASN ARG GLU ASP TYR PRO LYS ARG ASP ASP ILE ASN          
SEQRES  44 A  656  TRP LEU ASN ARG THR LEU ALA SER TRP PRO ASN PRO GLU          
SEQRES  45 A  656  GLN THR LEU PRO THR LEU GLU TYR GLU ALA LEU ASP VAL          
SEQRES  46 A  656  ASN GLU MET GLU ILE ALA PRO GLY TYR ARG GLY TYR GLY          
SEQRES  47 A  656  ALA LYS GLY ASN TYR ILE GLU ASN PRO LEU SER VAL LYS          
SEQRES  48 A  656  ARG GLN GLU GLU ILE ASP LYS ILE GLN SER GLU LEU GLU          
SEQRES  49 A  656  ALA ALA GLY LYS ASP ARG HIS ALA ILE GLN GLU ALA LEU          
SEQRES  50 A  656  MET PRO TYR GLU LEU PRO ALA LYS TYR LYS ALA ARG ASN          
SEQRES  51 A  656  GLU ARG LEU GLY ASP LYS                                      
SEQRES   1 B  239  MET GLY ARG MET LEU THR ILE ARG VAL PHE LYS TYR ASP          
SEQRES   2 B  239  PRO GLN SER ALA VAL SER LYS PRO HIS PHE GLN GLU TYR          
SEQRES   3 B  239  LYS ILE GLU GLU ALA PRO SER MET THR ILE PHE ILE VAL          
SEQRES   4 B  239  LEU ASN MET ILE ARG GLU THR TYR ASP PRO ASP LEU ASN          
SEQRES   5 B  239  PHE ASP PHE VAL CYS ARG ALA GLY ILE CYS GLY SER CYS          
SEQRES   6 B  239  GLY MET MET ILE ASN GLY ARG PRO SER LEU ALA CYS ARG          
SEQRES   7 B  239  THR LEU THR LYS ASP PHE GLU ASP GLY VAL ILE THR LEU          
SEQRES   8 B  239  LEU PRO LEU PRO ALA PHE LYS LEU ILE LYS ASP LEU SER          
SEQRES   9 B  239  VAL ASP THR GLY ASN TRP PHE ASN GLY MET SER GLN ARG          
SEQRES  10 B  239  VAL GLU SER TRP ILE HIS ALA GLN LYS GLU HIS ASP ILE          
SEQRES  11 B  239  SER LYS LEU GLU GLU ARG ILE GLU PRO GLU VAL ALA GLN          
SEQRES  12 B  239  GLU VAL PHE GLU LEU ASP ARG CYS ILE GLU CYS GLY CYS          
SEQRES  13 B  239  CYS ILE ALA ALA CYS GLY THR LYS ILE MET ARG GLU ASP          
SEQRES  14 B  239  PHE VAL GLY ALA ALA GLY LEU ASN ARG VAL VAL ARG PHE          
SEQRES  15 B  239  MET ILE ASP PRO HIS ASP GLU ARG THR ASP GLU ASP TYR          
SEQRES  16 B  239  TYR GLU LEU ILE GLY ASP ASP ASP GLY VAL PHE GLY CYS          
SEQRES  17 B  239  MET THR LEU LEU ALA CYS HIS ASP VAL CYS PRO LYS ASN          
SEQRES  18 B  239  LEU PRO LEU GLN SER LYS ILE ALA TYR LEU ARG ARG LYS          
SEQRES  19 B  239  MET VAL SER VAL ASN                                          
SEQRES   1 C  256  MET THR ASN GLU SER ILE LEU GLU SER TYR SER GLY VAL          
SEQRES   2 C  256  THR PRO GLU ARG LYS LYS SER ARG MET PRO ALA LYS LEU          
SEQRES   3 C  256  ASP TRP TRP GLN SER ALA THR GLY LEU PHE LEU GLY LEU          
SEQRES   4 C  256  PHE MET ILE GLY HIS MET PHE PHE VAL SER THR ILE LEU          
SEQRES   5 C  256  LEU GLY ASP ASN VAL MET LEU TRP VAL THR LYS LYS PHE          
SEQRES   6 C  256  GLU LEU ASP PHE ILE PHE GLU GLY GLY LYS PRO ILE VAL          
SEQRES   7 C  256  VAL SER PHE LEU ALA ALA PHE VAL PHE ALA VAL PHE ILE          
SEQRES   8 C  256  ALA HIS ALA PHE LEU ALA MET ARG LYS PHE PRO ILE ASN          
SEQRES   9 C  256  TYR ARG GLN TYR LEU THR PHE LYS THR HIS LYS ASP LEU          
SEQRES  10 C  256  MET ARG HIS GLY ASP THR THR LEU TRP TRP ILE GLN ALA          
SEQRES  11 C  256  MET THR GLY PHE ALA MET PHE PHE LEU GLY SER VAL HIS          
SEQRES  12 C  256  LEU TYR ILE MET MET THR GLN PRO GLN THR ILE GLY PRO          
SEQRES  13 C  256  VAL SER SER SER PHE ARG MET VAL SER GLU TRP MET TRP          
SEQRES  14 C  256  PRO LEU TYR LEU VAL LEU LEU PHE ALA VAL GLN LEU HIS          
SEQRES  15 C  256  GLY SER VAL GLY LEU TYR ARG LEU ALA VAL LYS TRP GLY          
SEQRES  16 C  256  TRP PHE ASP GLY GLU THR PRO ASP LYS THR ARG ALA ASN          
SEQRES  17 C  256  LEU LYS LYS LEU LYS THR LEU MET SER ALA PHE LEU ILE          
SEQRES  18 C  256  VAL LEU GLY LEU LEU THR PHE GLY ALA TYR VAL LYS LYS          
SEQRES  19 C  256  GLY LEU GLU GLN THR ASP PRO ASN ILE ASP TYR LYS TYR          
SEQRES  20 C  256  PHE ASP TYR LYS ARG THR HIS HIS ARG                          
SEQRES   1 D  656  MET LYS VAL GLN TYR CYS ASP SER LEU VAL ILE GLY GLY          
SEQRES   2 D  656  GLY LEU ALA GLY LEU ARG ALA ALA VAL ALA THR GLN GLN          
SEQRES   3 D  656  LYS GLY LEU SER THR ILE VAL LEU SER LEU ILE PRO VAL          
SEQRES   4 D  656  LYS ARG SER HIS SER ALA ALA ALA GLN GLY GLY MET GLN          
SEQRES   5 D  656  ALA SER LEU GLY ASN SER LYS MET SER ASP GLY ASP ASN          
SEQRES   6 D  656  GLU ASP LEU HIS PHE MET ASP THR VAL LYS GLY SER ASP          
SEQRES   7 D  656  TRP GLY CYS ASP GLN LYS VAL ALA ARG MET PHE VAL ASN          
SEQRES   8 D  656  THR ALA PRO LYS ALA ILE ARG GLU LEU ALA ALA TRP GLY          
SEQRES   9 D  656  VAL PRO TRP THR ARG ILE HIS LYS GLY ASP ARG MET ALA          
SEQRES  10 D  656  ILE ILE ASN ALA GLN LYS THR THR ILE THR GLU GLU ASP          
SEQRES  11 D  656  PHE ARG HIS GLY LEU ILE HIS SER ARG ASP PHE GLY GLY          
SEQRES  12 D  656  THR LYS LYS TRP ARG THR CYS TYR THR ALA ASP ALA THR          
SEQRES  13 D  656  GLY HIS THR MET LEU PHE ALA VAL ALA ASN GLU CYS LEU          
SEQRES  14 D  656  LYS LEU GLY VAL SER ILE GLN ASP ARG LYS GLU ALA ILE          
SEQRES  15 D  656  ALA LEU ILE HIS GLN ASP GLY LYS CYS TYR GLY ALA VAL          
SEQRES  16 D  656  VAL ARG ASP LEU VAL THR GLY ASP ILE ILE ALA TYR VAL          
SEQRES  17 D  656  ALA LYS GLY THR LEU ILE ALA THR GLY GLY TYR GLY ARG          
SEQRES  18 D  656  ILE TYR LYS ASN THR THR ASN ALA VAL VAL CYS GLU GLY          
SEQRES  19 D  656  THR GLY THR ALA ILE ALA LEU GLU THR GLY ILE ALA GLN          
SEQRES  20 D  656  LEU GLY ASN MET GLU ALA VAL GLN PHE HIS PRO THR PRO          
SEQRES  21 D  656  LEU PHE PRO SER GLY ILE LEU LEU THR GLU GLY CYS ARG          
SEQRES  22 D  656  GLY ASP GLY GLY ILE LEU ARG ASP VAL ASP GLY HIS ARG          
SEQRES  23 D  656  PHE MET PRO ASP TYR GLU PRO GLU LYS LYS GLU LEU ALA          
SEQRES  24 D  656  SER ARG ASP VAL VAL SER ARG ARG MET ILE GLU HIS ILE          
SEQRES  25 D  656  ARG LYS GLY LYS GLY VAL GLN SER PRO TYR GLY GLN HIS          
SEQRES  26 D  656  LEU TRP LEU ASP ILE SER ILE LEU GLY ARG LYS HIS ILE          
SEQRES  27 D  656  GLU THR ASN LEU ARG ASP VAL GLN GLU ILE CYS GLU TYR          
SEQRES  28 D  656  PHE ALA GLY ILE ASP PRO ALA GLU LYS TRP ALA PRO VAL          
SEQRES  29 D  656  LEU PRO MET GLN HIS TYR SER MET GLY GLY ILE ARG THR          
SEQRES  30 D  656  ASP TYR ARG GLY GLU ALA LYS LEU LYS GLY LEU PHE SER          
SEQRES  31 D  656  ALA GLY GLU ALA ALA CYS TRP ASP MET HIS GLY PHE ASN          
SEQRES  32 D  656  ARG LEU GLY GLY ASN SER VAL SER GLU ALA VAL VAL ALA          
SEQRES  33 D  656  GLY MET ILE VAL GLY GLU TYR PHE ALA GLU HIS CYS ALA          
SEQRES  34 D  656  ASN THR GLN VAL ASP LEU GLU THR LYS THR LEU GLU LYS          
SEQRES  35 D  656  PHE VAL LYS GLY GLN GLU ALA TYR MET LYS SER LEU VAL          
SEQRES  36 D  656  GLU SER LYS GLY THR GLU ASP VAL PHE LYS ILE LYS ASN          
SEQRES  37 D  656  ARG MET LYS ASP VAL MET ASP ASP ASN VAL GLY ILE PHE          
SEQRES  38 D  656  ARG ASP GLY PRO HIS LEU GLU LYS ALA VAL LYS GLU LEU          
SEQRES  39 D  656  GLU GLU LEU TYR LYS LYS SER LYS ASN VAL GLY ILE LYS          
SEQRES  40 D  656  ASN LYS ARG LEU HIS ALA ASN PRO GLU LEU GLU GLU ALA          
SEQRES  41 D  656  TYR ARG VAL PRO MET MET LEU LYS VAL ALA LEU CYS VAL          
SEQRES  42 D  656  ALA LYS GLY ALA LEU ASP ARG THR GLU SER ARG GLY ALA          
SEQRES  43 D  656  HIS ASN ARG GLU ASP TYR PRO LYS ARG ASP ASP ILE ASN          
SEQRES  44 D  656  TRP LEU ASN ARG THR LEU ALA SER TRP PRO ASN PRO GLU          
SEQRES  45 D  656  GLN THR LEU PRO THR LEU GLU TYR GLU ALA LEU ASP VAL          
SEQRES  46 D  656  ASN GLU MET GLU ILE ALA PRO GLY TYR ARG GLY TYR GLY          
SEQRES  47 D  656  ALA LYS GLY ASN TYR ILE GLU ASN PRO LEU SER VAL LYS          
SEQRES  48 D  656  ARG GLN GLU GLU ILE ASP LYS ILE GLN SER GLU LEU GLU          
SEQRES  49 D  656  ALA ALA GLY LYS ASP ARG HIS ALA ILE GLN GLU ALA LEU          
SEQRES  50 D  656  MET PRO TYR GLU LEU PRO ALA LYS TYR LYS ALA ARG ASN          
SEQRES  51 D  656  GLU ARG LEU GLY ASP LYS                                      
SEQRES   1 E  239  MET GLY ARG MET LEU THR ILE ARG VAL PHE LYS TYR ASP          
SEQRES   2 E  239  PRO GLN SER ALA VAL SER LYS PRO HIS PHE GLN GLU TYR          
SEQRES   3 E  239  LYS ILE GLU GLU ALA PRO SER MET THR ILE PHE ILE VAL          
SEQRES   4 E  239  LEU ASN MET ILE ARG GLU THR TYR ASP PRO ASP LEU ASN          
SEQRES   5 E  239  PHE ASP PHE VAL CYS ARG ALA GLY ILE CYS GLY SER CYS          
SEQRES   6 E  239  GLY MET MET ILE ASN GLY ARG PRO SER LEU ALA CYS ARG          
SEQRES   7 E  239  THR LEU THR LYS ASP PHE GLU ASP GLY VAL ILE THR LEU          
SEQRES   8 E  239  LEU PRO LEU PRO ALA PHE LYS LEU ILE LYS ASP LEU SER          
SEQRES   9 E  239  VAL ASP THR GLY ASN TRP PHE ASN GLY MET SER GLN ARG          
SEQRES  10 E  239  VAL GLU SER TRP ILE HIS ALA GLN LYS GLU HIS ASP ILE          
SEQRES  11 E  239  SER LYS LEU GLU GLU ARG ILE GLU PRO GLU VAL ALA GLN          
SEQRES  12 E  239  GLU VAL PHE GLU LEU ASP ARG CYS ILE GLU CYS GLY CYS          
SEQRES  13 E  239  CYS ILE ALA ALA CYS GLY THR LYS ILE MET ARG GLU ASP          
SEQRES  14 E  239  PHE VAL GLY ALA ALA GLY LEU ASN ARG VAL VAL ARG PHE          
SEQRES  15 E  239  MET ILE ASP PRO HIS ASP GLU ARG THR ASP GLU ASP TYR          
SEQRES  16 E  239  TYR GLU LEU ILE GLY ASP ASP ASP GLY VAL PHE GLY CYS          
SEQRES  17 E  239  MET THR LEU LEU ALA CYS HIS ASP VAL CYS PRO LYS ASN          
SEQRES  18 E  239  LEU PRO LEU GLN SER LYS ILE ALA TYR LEU ARG ARG LYS          
SEQRES  19 E  239  MET VAL SER VAL ASN                                          
SEQRES   1 F  256  MET THR ASN GLU SER ILE LEU GLU SER TYR SER GLY VAL          
SEQRES   2 F  256  THR PRO GLU ARG LYS LYS SER ARG MET PRO ALA LYS LEU          
SEQRES   3 F  256  ASP TRP TRP GLN SER ALA THR GLY LEU PHE LEU GLY LEU          
SEQRES   4 F  256  PHE MET ILE GLY HIS MET PHE PHE VAL SER THR ILE LEU          
SEQRES   5 F  256  LEU GLY ASP ASN VAL MET LEU TRP VAL THR LYS LYS PHE          
SEQRES   6 F  256  GLU LEU ASP PHE ILE PHE GLU GLY GLY LYS PRO ILE VAL          
SEQRES   7 F  256  VAL SER PHE LEU ALA ALA PHE VAL PHE ALA VAL PHE ILE          
SEQRES   8 F  256  ALA HIS ALA PHE LEU ALA MET ARG LYS PHE PRO ILE ASN          
SEQRES   9 F  256  TYR ARG GLN TYR LEU THR PHE LYS THR HIS LYS ASP LEU          
SEQRES  10 F  256  MET ARG HIS GLY ASP THR THR LEU TRP TRP ILE GLN ALA          
SEQRES  11 F  256  MET THR GLY PHE ALA MET PHE PHE LEU GLY SER VAL HIS          
SEQRES  12 F  256  LEU TYR ILE MET MET THR GLN PRO GLN THR ILE GLY PRO          
SEQRES  13 F  256  VAL SER SER SER PHE ARG MET VAL SER GLU TRP MET TRP          
SEQRES  14 F  256  PRO LEU TYR LEU VAL LEU LEU PHE ALA VAL GLN LEU HIS          
SEQRES  15 F  256  GLY SER VAL GLY LEU TYR ARG LEU ALA VAL LYS TRP GLY          
SEQRES  16 F  256  TRP PHE ASP GLY GLU THR PRO ASP LYS THR ARG ALA ASN          
SEQRES  17 F  256  LEU LYS LYS LEU LYS THR LEU MET SER ALA PHE LEU ILE          
SEQRES  18 F  256  VAL LEU GLY LEU LEU THR PHE GLY ALA TYR VAL LYS LYS          
SEQRES  19 F  256  GLY LEU GLU GLN THR ASP PRO ASN ILE ASP TYR LYS TYR          
SEQRES  20 F  256  PHE ASP TYR LYS ARG THR HIS HIS ARG                          
HET     NA  A1658       1                                                       
HET     NA  D1658       1                                                       
HET    FAD  A1656      53                                                       
HET    CIT  A1657      26                                                       
HET    FES  B1240       4                                                       
HET    F3S  B1241       7                                                       
HET    SF4  B1242       8                                                       
HET    HEM  C1255      43                                                       
HET    HEM  C1256      43                                                       
HET    LMT  C1257      35                                                       
HET    FAD  D1656      53                                                       
HET    CIT  D1657      26                                                       
HET    FES  E1240       4                                                       
HET    F3S  E1241       7                                                       
HET    SF4  E1242       8                                                       
HET    HEM  F1255      43                                                       
HET    HEM  F1256      43                                                       
HET    LMT  F1257      35                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     CIT CITRIC ACID                                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETSYN     LMT LAURYL-BETA-D-MALTOSIDE                                          
HETSYN     HEM [DIHYDROGEN 3,7,12,17-TETRAMETHYL-8,13-                          
HETSYN   2 HEM  DIVINYL-2,18-PORPHINEDIPROPIONATO(2-)]IRON                      
FORMUL   7   NA    2(NA 1+)                                                     
FORMUL   9  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  10  CIT    2(C6 H8 O7)                                                  
FORMUL  11  FES    2(FE2 S2)                                                    
FORMUL  12  F3S    2(FE3 S4 1+)                                                 
FORMUL  13  SF4    2(FE4 S4 2+)                                                 
FORMUL  14  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  16  LMT    2(C24 H46 O11)                                               
FORMUL  25  HOH   *991(H2 O1)                                                   
HELIX    1   1 GLY A   14  GLN A   26  1                                  13    
HELIX    2   2 PRO A   38  SER A   42  5                                   5    
HELIX    3   3 SER A   42  ALA A   47  5                                   6    
HELIX    4   4 SER A   58  ASP A   62  5                                   5    
HELIX    5   5 ASN A   65  SER A   77  1                                  13    
HELIX    6   6 ASP A   82  TRP A  103  1                                  22    
HELIX    7   7 GLU A  129  HIS A  133  5                                   5    
HELIX    8   8 ALA A  155  GLY A  172  1                                  18    
HELIX    9   9 TYR A  219  TYR A  223  5                                   5    
HELIX   10  10 GLY A  234  GLU A  242  1                                   9    
HELIX   11  11 GLU A  270  GLY A  276  1                                   7    
HELIX   12  12 PHE A  287  GLU A  292  1                                   6    
HELIX   13  13 LYS A  295  ALA A  299  5                                   5    
HELIX   14  14 SER A  300  LYS A  314  1                                  15    
HELIX   15  15 ILE A  330  LEU A  333  5                                   4    
HELIX   16  16 GLY A  334  LEU A  342  1                                   9    
HELIX   17  17 LEU A  342  PHE A  352  1                                  11    
HELIX   18  18 ASN A  408  THR A  431  1                                  24    
HELIX   19  19 THR A  437  SER A  457  1                                  21    
HELIX   20  20 ASP A  462  VAL A  478  1                                  17    
HELIX   21  21 ASP A  483  LYS A  502  1                                  20    
HELIX   22  22 ASN A  514  ARG A  540  1                                  27    
HELIX   23  23 ASP A  584  MET A  588  5                                   5    
HELIX   24  24 ASN A  606  ALA A  626  1                                  21    
HELIX   25  25 ASP A  629  MET A  638  1                                  10    
HELIX   26  26 PRO A  643  LYS A  647  5                                   5    
HELIX   27  27 THR B   35  TYR B   47  1                                  13    
HELIX   28  28 CYS B   77  THR B   79  5                                   3    
HELIX   29  29 THR B   81  PHE B   84  5                                   4    
HELIX   30  30 THR B  107  VAL B  118  1                                  12    
HELIX   31  31 GLU B  138  ARG B  150  1                                  13    
HELIX   32  32 GLY B  155  ALA B  160  1                                   6    
HELIX   33  33 CYS B  161  ARG B  167  1                                   7    
HELIX   34  34 VAL B  171  ILE B  184  1                                  14    
HELIX   35  35 THR B  191  GLY B  200  1                                  10    
HELIX   36  36 GLY B  204  CYS B  208  5                                   5    
HELIX   37  37 LEU B  212  CYS B  218  1                                   7    
HELIX   38  38 PRO B  223  SER B  237  1                                  15    
HELIX   39  39 THR C    2  GLY C   12  1                                  11    
HELIX   40  40 ARG C   21  SER C   49  1                                  29    
HELIX   41  41 THR C   50  LEU C   53  5                                   4    
HELIX   42  42 GLY C   54  GLU C   66  1                                  13    
HELIX   43  43 PRO C   76  MET C   98  1                                  23    
HELIX   44  44 ARG C   99  PHE C  101  5                                   3    
HELIX   45  45 ASN C  104  ARG C  119  1                                  16    
HELIX   46  46 HIS C  120  GLN C  150  1                                  31    
HELIX   47  47 PRO C  151  ILE C  154  5                                   4    
HELIX   48  48 VAL C  157  SER C  165  1                                   9    
HELIX   49  49 MET C  168  GLY C  195  1                                  28    
HELIX   50  50 THR C  201  LEU C  236  1                                  36    
HELIX   51  51 GLY D   14  GLN D   26  1                                  13    
HELIX   52  52 PRO D   38  SER D   42  5                                   5    
HELIX   53  53 SER D   42  ALA D   47  5                                   6    
HELIX   54  54 SER D   58  ASP D   62  5                                   5    
HELIX   55  55 ASN D   65  SER D   77  1                                  13    
HELIX   56  56 ASP D   82  TRP D  103  1                                  22    
HELIX   57  57 GLU D  129  HIS D  133  5                                   5    
HELIX   58  58 ALA D  155  GLY D  172  1                                  18    
HELIX   59  59 TYR D  219  TYR D  223  5                                   5    
HELIX   60  60 GLY D  234  GLU D  242  1                                   9    
HELIX   61  61 GLU D  270  GLY D  276  1                                   7    
HELIX   62  62 PHE D  287  GLU D  292  1                                   6    
HELIX   63  63 LYS D  295  ALA D  299  5                                   5    
HELIX   64  64 SER D  300  LYS D  314  1                                  15    
HELIX   65  65 ILE D  330  LEU D  333  5                                   4    
HELIX   66  66 GLY D  334  LEU D  342  1                                   9    
HELIX   67  67 LEU D  342  PHE D  352  1                                  11    
HELIX   68  68 ASN D  408  THR D  431  1                                  24    
HELIX   69  69 THR D  437  SER D  457  1                                  21    
HELIX   70  70 ASP D  462  VAL D  478  1                                  17    
HELIX   71  71 ASP D  483  LYS D  502  1                                  20    
HELIX   72  72 ASN D  514  ARG D  540  1                                  27    
HELIX   73  73 ASP D  584  MET D  588  5                                   5    
HELIX   74  74 ASN D  606  ALA D  626  1                                  21    
HELIX   75  75 ASP D  629  MET D  638  1                                  10    
HELIX   76  76 PRO D  643  LYS D  647  5                                   5    
HELIX   77  77 THR E   35  TYR E   47  1                                  13    
HELIX   78  78 CYS E   77  THR E   79  5                                   3    
HELIX   79  79 THR E   81  PHE E   84  5                                   4    
HELIX   80  80 THR E  107  VAL E  118  1                                  12    
HELIX   81  81 GLU E  138  ARG E  150  1                                  13    
HELIX   82  82 GLY E  155  ALA E  160  1                                   6    
HELIX   83  83 CYS E  161  ARG E  167  1                                   7    
HELIX   84  84 VAL E  171  ILE E  184  1                                  14    
HELIX   85  85 THR E  191  GLY E  200  1                                  10    
HELIX   86  86 GLY E  204  CYS E  208  5                                   5    
HELIX   87  87 LEU E  212  CYS E  218  1                                   7    
HELIX   88  88 PRO E  223  SER E  237  1                                  15    
HELIX   89  89 THR F    2  GLY F   12  1                                  11    
HELIX   90  90 ARG F   21  SER F   49  1                                  29    
HELIX   91  91 THR F   50  LEU F   53  5                                   4    
HELIX   92  92 GLY F   54  GLU F   66  1                                  13    
HELIX   93  93 PRO F   76  MET F   98  1                                  23    
HELIX   94  94 ARG F   99  PHE F  101  5                                   3    
HELIX   95  95 ASN F  104  ARG F  119  1                                  16    
HELIX   96  96 HIS F  120  GLN F  150  1                                  31    
HELIX   97  97 PRO F  151  ILE F  154  5                                   4    
HELIX   98  98 VAL F  157  SER F  165  1                                   9    
HELIX   99  99 MET F  168  GLY F  195  1                                  28    
HELIX  100 100 THR F  201  GLU F  237  1                                  37    
SHEET    1  AA 4 VAL A   3  TYR A   5  0                                        
SHEET    2  AA 4 ILE A 204  VAL A 208  1  O  ALA A 206   N  GLN A   4           
SHEET    3  AA 4 LYS A 190  ASP A 198 -1  O  ALA A 194   N  TYR A 207           
SHEET    4  AA 4 LYS A 179  GLN A 187 -1  O  GLU A 180   N  ARG A 197           
SHEET    1  AB 5 SER A 174  GLN A 176  0                                        
SHEET    2  AB 5 THR A  31  LEU A  34  1  O  THR A  31   N  SER A 174           
SHEET    3  AB 5 SER A   8  ILE A  11  1  O  SER A   8   N  ILE A  32           
SHEET    4  AB 5 GLY A 211  ILE A 214  1  O  GLY A 211   N  LEU A   9           
SHEET    5  AB 5 LEU A 388  SER A 390  1  O  PHE A 389   N  ILE A 214           
SHEET    1  AC 2 MET A  51  GLN A  52  0                                        
SHEET    2  AC 2 THR A 149  CYS A 150 -1  O  CYS A 150   N  MET A  51           
SHEET    1  AD 2 GLY A 113  MET A 116  0                                        
SHEET    2  AD 2 THR A 125  GLU A 128 -1  O  ILE A 126   N  ARG A 115           
SHEET    1  AE 5 ALA A 395  CYS A 396  0                                        
SHEET    2  AE 5 GLY A 374  ARG A 376  1  O  ILE A 375   N  CYS A 396           
SHEET    3  AE 5 LEU A 248  GLY A 249 -1  O  GLY A 249   N  GLY A 374           
SHEET    4  AE 5 ASN A 562  SER A 567 -1  O  ALA A 566   N  LEU A 248           
SHEET    5  AE 5 THR A 577  ALA A 582 -1  O  THR A 577   N  SER A 567           
SHEET    1  AF 2 VAL A 254  HIS A 257  0                                        
SHEET    2  AF 2 MET A 367  SER A 371 -1  O  MET A 367   N  HIS A 257           
SHEET    1  AG 3 ILE A 278  ARG A 280  0                                        
SHEET    2  AG 3 LEU A 326  ASP A 329 -1  O  TRP A 327   N  ARG A 280           
SHEET    3  AG 3 ALA A 362  VAL A 364 -1  O  ALA A 362   N  LEU A 328           
SHEET    1  AH 2 ASP A 434  GLU A 436  0                                        
SHEET    2  AH 2 ASP D 434  GLU D 436 -1  O  LEU D 435   N  LEU A 435           
SHEET    1  AI 2 ARG A 555  ASP A 556  0                                        
SHEET    2  AI 2 TYR A 603  ILE A 604  1  N  ILE A 604   O  ARG A 555           
SHEET    1  BA 5 HIS B  22  GLU B  29  0                                        
SHEET    2  BA 5 MET B   4  LYS B  11 -1  O  LEU B   5   N  ILE B  28           
SHEET    3  BA 5 VAL B  88  LEU B  92  1  O  ILE B  89   N  ARG B   8           
SHEET    4  BA 5 GLY B  66  ILE B  69 -1  O  MET B  68   N  LEU B  92           
SHEET    5  BA 5 ARG B  72  LEU B  75 -1  O  ARG B  72   N  ILE B  69           
SHEET    1  BB 2 LYS B  98  LYS B 101  0                                        
SHEET    2  BB 2 SER B 104  ASP B 106 -1  O  SER B 104   N  ILE B 100           
SHEET    1  DA 4 VAL D   3  TYR D   5  0                                        
SHEET    2  DA 4 ILE D 204  VAL D 208  1  O  ALA D 206   N  GLN D   4           
SHEET    3  DA 4 LYS D 190  ASP D 198 -1  O  ALA D 194   N  TYR D 207           
SHEET    4  DA 4 LYS D 179  GLN D 187 -1  O  GLU D 180   N  ARG D 197           
SHEET    1  DB 5 SER D 174  GLN D 176  0                                        
SHEET    2  DB 5 THR D  31  LEU D  34  1  O  THR D  31   N  SER D 174           
SHEET    3  DB 5 SER D   8  ILE D  11  1  O  SER D   8   N  ILE D  32           
SHEET    4  DB 5 GLY D 211  ILE D 214  1  O  GLY D 211   N  LEU D   9           
SHEET    5  DB 5 LEU D 388  SER D 390  1  O  PHE D 389   N  ILE D 214           
SHEET    1  DC 2 MET D  51  GLN D  52  0                                        
SHEET    2  DC 2 THR D 149  CYS D 150 -1  O  CYS D 150   N  MET D  51           
SHEET    1  DD 2 GLY D 113  MET D 116  0                                        
SHEET    2  DD 2 THR D 125  GLU D 128 -1  O  ILE D 126   N  ARG D 115           
SHEET    1  DE 5 ALA D 395  CYS D 396  0                                        
SHEET    2  DE 5 GLY D 374  ARG D 376  1  O  ILE D 375   N  CYS D 396           
SHEET    3  DE 5 LEU D 248  GLY D 249 -1  O  GLY D 249   N  GLY D 374           
SHEET    4  DE 5 ASN D 562  SER D 567 -1  O  ALA D 566   N  LEU D 248           
SHEET    5  DE 5 THR D 577  ALA D 582 -1  O  THR D 577   N  SER D 567           
SHEET    1  DF 2 VAL D 254  HIS D 257  0                                        
SHEET    2  DF 2 MET D 367  SER D 371 -1  O  MET D 367   N  HIS D 257           
SHEET    1  DG 3 ILE D 278  ARG D 280  0                                        
SHEET    2  DG 3 LEU D 326  ASP D 329 -1  O  TRP D 327   N  ARG D 280           
SHEET    3  DG 3 ALA D 362  VAL D 364 -1  O  ALA D 362   N  LEU D 328           
SHEET    1  DH 2 ARG D 555  ASP D 556  0                                        
SHEET    2  DH 2 TYR D 603  ILE D 604  1  N  ILE D 604   O  ARG D 555           
SHEET    1  EA 5 HIS E  22  GLU E  29  0                                        
SHEET    2  EA 5 MET E   4  LYS E  11 -1  O  LEU E   5   N  ILE E  28           
SHEET    3  EA 5 VAL E  88  LEU E  92  1  O  ILE E  89   N  ARG E   8           
SHEET    4  EA 5 GLY E  66  ILE E  69 -1  O  MET E  68   N  LEU E  92           
SHEET    5  EA 5 ARG E  72  LEU E  75 -1  O  ARG E  72   N  ILE E  69           
SHEET    1  EB 2 LYS E  98  LYS E 101  0                                        
SHEET    2  EB 2 SER E 104  ASP E 106 -1  O  SER E 104   N  ILE E 100           
LINK         NE2 HIS A  43                 C8M FAD A1656     1555   1555  1.45  
LINK        NA    NA A1658                 O   ALA A 395     1555   1555  2.51  
LINK        NA    NA A1658                 O   HOH A2156     1555   1555  2.30  
LINK        NA    NA A1658                 O   SER A 371     1555   1555  2.44  
LINK        NA    NA A1658                 O   GLY A 373     1555   1555  2.48  
LINK        NA    NA A1658                 O   GLU A 393     1555   1555  2.41  
LINK        FE1  FES B1240                 SG  CYS B  65     1555   1555  2.14  
LINK        FE1  FES B1240                 SG  CYS B  77     1555   1555  2.21  
LINK        FE2  FES B1240                 SG  CYS B  62     1555   1555  2.16  
LINK        FE2  FES B1240                 SG  CYS B  57     1555   1555  2.20  
LINK        FE1  F3S B1241                 SG  CYS B 161     1555   1555  2.18  
LINK        FE3  F3S B1241                 SG  CYS B 208     1555   1555  2.19  
LINK        FE4  F3S B1241                 SG  CYS B 214     1555   1555  2.17  
LINK        FE1  SF4 B1242                 SG  CYS B 157     1555   1555  2.15  
LINK        FE2  SF4 B1242                 SG  CYS B 154     1555   1555  2.17  
LINK        FE3  SF4 B1242                 SG  CYS B 151     1555   1555  2.16  
LINK        FE4  SF4 B1242                 SG  CYS B 218     1555   1555  2.18  
LINK         NE2 HIS C  44                FE   HEM C1256     1555   1555  2.05  
LINK         NE2 HIS C  93                FE   HEM C1255     1555   1555  2.04  
LINK         NE2 HIS C 182                FE   HEM C1255     1555   1555  2.03  
LINK        FE   HEM C1256                 NE2 HIS C 143     1555   1555  2.06  
LINK         NE2 HIS D  43                 C8M FAD D1656     1555   1555  1.45  
LINK        NA    NA D1658                 O   SER D 371     1555   1555  2.46  
LINK        NA    NA D1658                 O   ALA D 395     1555   1555  2.50  
LINK        NA    NA D1658                 O   HOH D2162     1555   1555  2.23  
LINK        NA    NA D1658                 O   GLU D 393     1555   1555  2.43  
LINK        NA    NA D1658                 O   GLY D 373     1555   1555  2.52  
LINK        FE2  FES E1240                 SG  CYS E  57     1555   1555  2.19  
LINK        FE2  FES E1240                 SG  CYS E  62     1555   1555  2.18  
LINK        FE1  FES E1240                 SG  CYS E  65     1555   1555  2.15  
LINK        FE1  FES E1240                 SG  CYS E  77     1555   1555  2.19  
LINK        FE4  F3S E1241                 SG  CYS E 214     1555   1555  2.16  
LINK        FE3  F3S E1241                 SG  CYS E 208     1555   1555  2.15  
LINK        FE1  F3S E1241                 SG  CYS E 161     1555   1555  2.18  
LINK        FE4  SF4 E1242                 SG  CYS E 218     1555   1555  2.18  
LINK        FE3  SF4 E1242                 SG  CYS E 151     1555   1555  2.19  
LINK        FE2  SF4 E1242                 SG  CYS E 154     1555   1555  2.17  
LINK        FE1  SF4 E1242                 SG  CYS E 157     1555   1555  2.15  
LINK         NE2 HIS F  93                FE   HEM F1255     1555   1555  2.04  
LINK         NE2 HIS F 143                FE   HEM F1256     1555   1555  2.03  
LINK         NE2 HIS F 182                FE   HEM F1255     1555   1555  2.04  
LINK        FE   HEM F1256                 NE2 HIS F  44     1555   1555  2.08  
CISPEP   1 PHE A  262    PRO A  263          0         0.08                     
CISPEP   2 PHE D  262    PRO D  263          0         0.15                     
SITE     1 AC1  6 SER A 371  MET A 372  GLY A 373  GLU A 393                    
SITE     2 AC1  6 ALA A 395  HOH A2156                                          
SITE     1 AC2  6 SER D 371  MET D 372  GLY D 373  GLU D 393                    
SITE     2 AC2  6 ALA D 395  HOH D2162                                          
SITE     1 AC3 37 GLY A  12  GLY A  13  GLY A  14  LEU A  15                    
SITE     2 AC3 37 ALA A  16  SER A  35  LEU A  36  ILE A  37                    
SITE     3 AC3 37 SER A  42  HIS A  43  SER A  44  ALA A  47                    
SITE     4 AC3 37 GLY A  49  GLY A  50  LYS A 179  ALA A 181                    
SITE     5 AC3 37 ALA A 215  THR A 216  GLY A 217  THR A 227                    
SITE     6 AC3 37 ASN A 228  THR A 235  HIS A 369  TYR A 370                    
SITE     7 AC3 37 GLY A 392  GLU A 393  ARG A 404  GLY A 407                    
SITE     8 AC3 37 ASN A 408  SER A 409  VAL A 410  CIT A1657                    
SITE     9 AC3 37 HOH A2269  HOH A2270  HOH A2271  HOH A2272                    
SITE    10 AC3 37 HOH A2273                                                     
SITE     1 AC4 15 ALA A  46  GLN A  48  GLY A  49  PHE A 141                    
SITE     2 AC4 15 GLN A 255  HIS A 257  LEU A 267  THR A 269                    
SITE     3 AC4 15 GLU A 270  ARG A 301  HIS A 369  ARG A 404                    
SITE     4 AC4 15 GLY A 406  FAD A1656  HOH A2274                               
SITE     1 AC5  9 VAL B  56  CYS B  57  ARG B  58  GLY B  60                    
SITE     2 AC5  9 ILE B  61  CYS B  62  GLY B  63  CYS B  65                    
SITE     3 AC5  9 CYS B  77                                                     
SITE     1 AC6  9 CYS B 161  THR B 163  CYS B 208  MET B 209                    
SITE     2 AC6  9 THR B 210  LEU B 211  LEU B 212  ALA B 213                    
SITE     3 AC6  9 CYS B 214                                                     
SITE     1 AC7  9 CYS B 151  ILE B 152  GLU B 153  CYS B 154                    
SITE     2 AC7  9 GLY B 155  CYS B 157  CYS B 218  PRO B 219                    
SITE     3 AC7  9 LYS B 220                                                     
SITE     1 AC8 22 HOH B2142  GLN C  30  SER C  31  GLY C  34                    
SITE     2 AC8 22 LEU C  37  PHE C  90  HIS C  93  ALA C  94                    
SITE     3 AC8 22 ALA C  97  LYS C 100  PHE C 101  TRP C 126                    
SITE     4 AC8 22 GLY C 133  MET C 136  PHE C 137  HIS C 182                    
SITE     5 AC8 22 GLY C 186  LEU C 190  LYS C 193  HEM C1256                    
SITE     6 AC8 22 HOH C2046  HOH C2047                                          
SITE     1 AC9 15 PHE C  40  MET C  41  HIS C  44  LEU C  82                    
SITE     2 AC9 15 ALA C  83  HIS C 143  MET C 147  ILE C 154                    
SITE     3 AC9 15 SER C 159  ARG C 162  TYR C 172  LEU C 176                    
SITE     4 AC9 15 GLY C 224  PHE C 228  HEM C1255                               
SITE     1 BC1  8 PHE C 101  PRO C 102  ASN C 104  TYR C 108                    
SITE     2 BC1  8 MET C 131  PHE F  95  MET F  98  ARG F  99                    
SITE     1 BC2 38 GLY D  12  GLY D  13  GLY D  14  LEU D  15                    
SITE     2 BC2 38 ALA D  16  SER D  35  LEU D  36  ILE D  37                    
SITE     3 BC2 38 SER D  42  HIS D  43  SER D  44  ALA D  47                    
SITE     4 BC2 38 GLY D  49  GLY D  50  LYS D 179  GLU D 180                    
SITE     5 BC2 38 ALA D 181  ALA D 215  THR D 216  GLY D 217                    
SITE     6 BC2 38 THR D 227  ASN D 228  THR D 235  HIS D 369                    
SITE     7 BC2 38 TYR D 370  GLY D 392  GLU D 393  ARG D 404                    
SITE     8 BC2 38 GLY D 407  ASN D 408  SER D 409  VAL D 410                    
SITE     9 BC2 38 CIT D1657  HOH D2128  HOH D2285  HOH D2286                    
SITE    10 BC2 38 HOH D2287  HOH D2288                                          
SITE     1 BC3 15 ALA D  46  GLN D  48  GLY D  49  PHE D 141                    
SITE     2 BC3 15 GLN D 255  HIS D 257  LEU D 267  THR D 269                    
SITE     3 BC3 15 GLU D 270  ARG D 301  HIS D 369  ARG D 404                    
SITE     4 BC3 15 FAD D1656  HOH D2289  HOH D2291                               
SITE     1 BC4  9 VAL E  56  CYS E  57  ARG E  58  GLY E  60                    
SITE     2 BC4  9 ILE E  61  CYS E  62  GLY E  63  CYS E  65                    
SITE     3 BC4  9 CYS E  77                                                     
SITE     1 BC5  9 CYS E 161  THR E 163  CYS E 208  MET E 209                    
SITE     2 BC5  9 THR E 210  LEU E 211  LEU E 212  ALA E 213                    
SITE     3 BC5  9 CYS E 214                                                     
SITE     1 BC6  9 CYS E 151  ILE E 152  GLU E 153  CYS E 154                    
SITE     2 BC6  9 GLY E 155  CYS E 157  CYS E 218  PRO E 219                    
SITE     3 BC6  9 LYS E 220                                                     
SITE     1 BC7 23 GLN F  30  SER F  31  GLY F  34  LEU F  37                    
SITE     2 BC7 23 PHE F  90  HIS F  93  ALA F  94  ALA F  97                    
SITE     3 BC7 23 LYS F 100  PHE F 101  TRP F 126  GLY F 133                    
SITE     4 BC7 23 MET F 136  PHE F 137  VAL F 179  HIS F 182                    
SITE     5 BC7 23 GLY F 186  LEU F 190  LYS F 193  HEM F1256                    
SITE     6 BC7 23 HOH F2057  HOH F2058  HOH F2059                               
SITE     1 BC8 15 PHE F  40  MET F  41  HIS F  44  LEU F  82                    
SITE     2 BC8 15 ALA F  83  HIS F 143  MET F 147  ILE F 154                    
SITE     3 BC8 15 SER F 159  ARG F 162  TYR F 172  LEU F 176                    
SITE     4 BC8 15 GLY F 224  PHE F 228  HEM F1255                               
SITE     1 BC9  9 LEU C  26  PHE C  95  MET C  98  ARG C  99                    
SITE     2 BC9  9 PHE F 101  PRO F 102  ASN F 104  TYR F 108                    
SITE     3 BC9  9 MET F 131                                                     
CRYST1   85.104  188.766  117.817  90.00 104.47  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011750  0.000000  0.003032        0.00000                         
SCALE2      0.000000  0.005298  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008766        0.00000                         
MTRIX1   1 -0.999932 -0.011239  0.003138      174.44280    1                    
MTRIX2   1  0.010826 -0.793178  0.608894       -1.51400    1                    
MTRIX3   1 -0.004354  0.608886  0.793246        0.70450    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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