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Database: PDB
Entry: 2B76
LinkDB: 2B76
Original site: 2B76 
HEADER    OXIDOREDUCTASE                          03-OCT-05   2B76              
TITLE     E. COLI QUINOL FUMARATE REDUCTASE FRDA E49Q MUTATION                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT;                   
COMPND   3 CHAIN: A, M;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FUMARATE REDUCTASE IRON-SULFUR PROTEIN;                    
COMPND   8 CHAIN: B, N;                                                         
COMPND   9 EC: 1.3.99.1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: FUMARATE REDUCTASE SUBUNIT C;                              
COMPND  13 CHAIN: C, O;                                                         
COMPND  14 SYNONYM: FUMARATE REDUCTASE 15 KDA HYDROPHOBIC PROTEIN;              
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: FUMARATE REDUCTASE SUBUNIT D;                              
COMPND  18 CHAIN: D, P;                                                         
COMPND  19 SYNONYM: FUMARATE REDUCTASE 13 KDA HYDROPHOBIC PROTEIN;              
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: FRDA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PH3;                                      
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 GENE: FRDB;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PH3;                                      
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 562;                                                 
SOURCE  22 GENE: FRDC;                                                          
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  25 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PH3;                                      
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  30 ORGANISM_TAXID: 562;                                                 
SOURCE  31 GENE: FRDD;                                                          
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  34 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PH3                                       
KEYWDS    FUMARATE REDUCTASE, SUCCINATE DEHYDROGENASE, ELECTRON TRANSFER,       
KEYWDS   2 RESPIRATION, KREBS CYCLE, MEMBRANE PROTEIN, OXIDOREDUCTASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MAKLASHINA,T.M.IVERSON,Y.SHER,V.KOTLYAR,O.MIRZA,J.ANDRELL,          
AUTHOR   2 J.M.HUDSON,F.A.ARMSTRONG,G.CECCHINI                                  
REVDAT   4   13-JUL-11 2B76    1       VERSN                                    
REVDAT   3   24-FEB-09 2B76    1       VERSN                                    
REVDAT   2   02-MAY-06 2B76    1       JRNL                                     
REVDAT   1   21-FEB-06 2B76    0                                                
JRNL        AUTH   E.MAKLASHINA,T.M.IVERSON,Y.SHER,V.KOTLYAR,J.ANDRELL,O.MIRZA, 
JRNL        AUTH 2 J.M.HUDSON,F.A.ARMSTRONG,R.A.ROTHERY,J.H.WEINER,G.CECCHINI   
JRNL        TITL   FUMARATE REDUCTASE AND SUCCINATE OXIDASE ACTIVITY OF         
JRNL        TITL 2 ESCHERICHIA COLI COMPLEX II HOMOLOGS ARE PERTURBED           
JRNL        TITL 3 DIFFERENTLY BY MUTATION OF THE FLAVIN BINDING DOMAIN         
JRNL        REF    J.BIOL.CHEM.                  V. 281 11357 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16484232                                                     
JRNL        DOI    10.1074/JBC.M512544200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 47106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : SELECTED TO BE IDENTICAL TO     
REMARK   3                                      1KFY, 1KF6, 1L0V                
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 921                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16606                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 234                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.42700                                              
REMARK   3    B22 (A**2) : -0.24100                                             
REMARK   3    B33 (A**2) : -4.18600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 10.00                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : QFR.PAR                                        
REMARK   3  PARAMETER FILE  3  : MQ7.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2B76 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034759.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1KF6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MG ACETATE, PEG 5000 MME, NA CITRATE,    
REMARK 280  EDTA, DTT, PH 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       48.40100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      136.98600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.76350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      136.98600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.40100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.76350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: THE BIOLOGICAL UNIT IS A SINGLE HETEROTETRAMER. THERE ARE    
REMARK 300 TWO HETEROTETRAMERS IN EACH ASYMMETRIC UNIT                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 18510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 18420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   577                                                      
REMARK 465     ARG A   578                                                      
REMARK 465     VAL A   579                                                      
REMARK 465     TYR A   580                                                      
REMARK 465     GLY A   581                                                      
REMARK 465     GLY A   582                                                      
REMARK 465     GLU A   583                                                      
REMARK 465     ALA A   584                                                      
REMARK 465     ASP A   585                                                      
REMARK 465     ALA A   586                                                      
REMARK 465     ALA A   587                                                      
REMARK 465     ASP A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     ALA A   590                                                      
REMARK 465     GLU A   591                                                      
REMARK 465     ALA A   592                                                      
REMARK 465     ALA A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     LYS A   595                                                      
REMARK 465     LYS A   596                                                      
REMARK 465     GLU A   597                                                      
REMARK 465     LYS A   598                                                      
REMARK 465     ALA A   599                                                      
REMARK 465     ASN A   600                                                      
REMARK 465     GLY A   601                                                      
REMARK 465     THR M   572                                                      
REMARK 465     LEU M   573                                                      
REMARK 465     PRO M   574                                                      
REMARK 465     PRO M   575                                                      
REMARK 465     ALA M   576                                                      
REMARK 465     LYS M   577                                                      
REMARK 465     ARG M   578                                                      
REMARK 465     VAL M   579                                                      
REMARK 465     TYR M   580                                                      
REMARK 465     GLY M   581                                                      
REMARK 465     GLY M   582                                                      
REMARK 465     GLU M   583                                                      
REMARK 465     ALA M   584                                                      
REMARK 465     ASP M   585                                                      
REMARK 465     ALA M   586                                                      
REMARK 465     ALA M   587                                                      
REMARK 465     ASP M   588                                                      
REMARK 465     LYS M   589                                                      
REMARK 465     ALA M   590                                                      
REMARK 465     GLU M   591                                                      
REMARK 465     ALA M   592                                                      
REMARK 465     ALA M   593                                                      
REMARK 465     ASN M   594                                                      
REMARK 465     LYS M   595                                                      
REMARK 465     LYS M   596                                                      
REMARK 465     GLU M   597                                                      
REMARK 465     LYS M   598                                                      
REMARK 465     ALA M   599                                                      
REMARK 465     ASN M   600                                                      
REMARK 465     GLY M   601                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   543     ND2  ASN A   546              1.85            
REMARK 500   NH1  ARG A    18     OE1  GLU A    92              1.88            
REMARK 500   NE   ARG A   542     OD2  ASP A   544              2.00            
REMARK 500   N    ASN B    14     OD2  ASP B    18              2.06            
REMARK 500   O    HIS B   143     OG   SER B   146              2.07            
REMARK 500   NH2  ARG B    12     OD1  ASP B   101              2.10            
REMARK 500   O    LYS B   241     N    ARG B   243              2.11            
REMARK 500   O    ALA M    24     N    ALA M    26              2.13            
REMARK 500   O    GLY A   118     NZ   LYS A   280              2.14            
REMARK 500   N    VAL N    69     O    VAL N    72              2.14            
REMARK 500   OD1  ASN B    14     N    GLU B    16              2.17            
REMARK 500   OG   SER O    39     O    ILE P    71              2.18            
REMARK 500   NH2  ARG M    42     OG   SER N    64              2.18            
REMARK 500   O    ALA B    32     NH1  ARG B    82              2.18            
REMARK 500   O    GLY A   275     CD   PRO A   277              2.19            
REMARK 500   OG   SER A   496     OE1  GLU B    16              2.19            
REMARK 500   O    LEU A   324     N    LEU A   328              2.19            
REMARK 500   OE2  GLU B    99     NH1  ARG C     4              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A  22   CA    ALA A  22   CB     -0.142                       
REMARK 500    SER A  36   CA    SER A  36   CB     -0.099                       
REMARK 500    GLU A  63   C     GLU A  63   O      -0.143                       
REMARK 500    TYR A  64   CE2   TYR A  64   CD2     0.095                       
REMARK 500    CYS A  77   CB    CYS A  77   SG     -0.108                       
REMARK 500    PHE A  85   CZ    PHE A  85   CE2    -0.126                       
REMARK 500    PRO A  90   CA    PRO A  90   CB     -0.136                       
REMARK 500    PRO A  90   CD    PRO A  90   N      -0.084                       
REMARK 500    VAL A 113   CB    VAL A 113   CG1    -0.137                       
REMARK 500    ASP A 129   CB    ASP A 129   CG      0.177                       
REMARK 500    GLN A 145   C     GLN A 145   O      -0.120                       
REMARK 500    ALA A 172   CA    ALA A 172   CB     -0.131                       
REMARK 500    GLU A 177   CD    GLU A 177   OE2     0.068                       
REMARK 500    GLY A 220   C     GLY A 220   O      -0.113                       
REMARK 500    VAL A 221   CA    VAL A 221   CB     -0.139                       
REMARK 500    VAL A 229   C     VAL A 229   O      -0.118                       
REMARK 500    GLY A 240   C     GLY A 240   O      -0.135                       
REMARK 500    GLY A 269   N     GLY A 269   CA     -0.118                       
REMARK 500    PRO A 270   CA    PRO A 270   C       0.156                       
REMARK 500    GLU A 276   N     GLU A 276   CA     -0.127                       
REMARK 500    GLU A 276   CA    GLU A 276   CB      0.136                       
REMARK 500    PRO A 277   CA    PRO A 277   C       0.184                       
REMARK 500    ARG A 287   C     ARG A 287   O      -0.125                       
REMARK 500    ARG A 327   CG    ARG A 327   CD      0.152                       
REMARK 500    PHE A 330   CB    PHE A 330   CG      0.102                       
REMARK 500    GLU A 333   CG    GLU A 333   CD      0.101                       
REMARK 500    PRO A 352   CA    PRO A 352   C       0.160                       
REMARK 500    LYS A 372   CB    LYS A 372   CG      0.262                       
REMARK 500    LYS A 372   CG    LYS A 372   CD      0.212                       
REMARK 500    LYS A 372   CD    LYS A 372   CE      0.155                       
REMARK 500    ALA A 424   CA    ALA A 424   CB      0.138                       
REMARK 500    LYS A 450   CD    LYS A 450   CE      0.269                       
REMARK 500    ILE A 465   CA    ILE A 465   CB     -0.150                       
REMARK 500    PRO A 469   CA    PRO A 469   C      -0.131                       
REMARK 500    GLU A 484   CG    GLU A 484   CD      0.132                       
REMARK 500    CYS A 517   CB    CYS A 517   SG     -0.131                       
REMARK 500    ASP A 543   CA    ASP A 543   CB      0.154                       
REMARK 500    ALA A 576   CA    ALA A 576   CB      0.175                       
REMARK 500    SER B  56   C     SER B  56   O      -0.117                       
REMARK 500    THR O   1   C     THR O   1   O       0.126                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  18   CG  -  CD  -  NE  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    PRO A  28   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR A  64   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD1 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A 106   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    GLY A 118   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    LYS A 120   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU A 136   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. = -20.5 DEGREES          
REMARK 500    ASP A 164   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP A 164   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    GLY A 194   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 225   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    VAL A 229   O   -  C   -  N   ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ARG A 248   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR A 266   N   -  CA  -  CB  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    GLY A 269   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
REMARK 500    PRO A 270   CB  -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO A 270   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    GLY A 269   CA  -  C   -  N   ANGL. DEV. = -24.8 DEGREES          
REMARK 500    GLY A 269   O   -  C   -  N   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO A 270   C   -  N   -  CA  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO A 270   C   -  N   -  CD  ANGL. DEV. = -37.3 DEGREES          
REMARK 500    PRO A 270   CA  -  C   -  N   ANGL. DEV. =  13.9 DEGREES          
REMARK 500    GLU A 276   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PRO A 277   N   -  CA  -  C   ANGL. DEV. = -19.2 DEGREES          
REMARK 500    GLU A 321   N   -  CA  -  C   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    GLU A 326   C   -  N   -  CA  ANGL. DEV. = -21.1 DEGREES          
REMARK 500    ARG A 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    CYS A 332   CA  -  CB  -  SG  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A 351   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 370   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    LYS A 372   CB  -  CG  -  CD  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU A 391   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    LEU A 391   CB  -  CG  -  CD1 ANGL. DEV. = -12.7 DEGREES          
REMARK 500    GLY A 418   N   -  CA  -  C   ANGL. DEV. = -16.1 DEGREES          
REMARK 500    TRP A 448   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    GLU A 460   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    TYR A 466   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 467   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    LEU A 479   CB  -  CG  -  CD2 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    ARG A 485   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 488   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 501   CB  -  CG  -  OD1 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   5      148.07   -172.39                                   
REMARK 500    ASN A  27      104.32   -163.66                                   
REMARK 500    ALA A  54      112.21   -174.67                                   
REMARK 500    ALA A  56      -36.83   -154.19                                   
REMARK 500    SER A  61      142.65   -176.04                                   
REMARK 500    ASP A  83      -70.15    -38.55                                   
REMARK 500    PRO A 102       47.96    -66.17                                   
REMARK 500    PRO A 107      -22.47    -38.78                                   
REMARK 500    ARG A 123       25.79   -149.62                                   
REMARK 500    ALA A 128     -154.65     49.32                                   
REMARK 500    GLU A 154       53.48     35.64                                   
REMARK 500    MET A 268       34.43   -144.63                                   
REMARK 500    GLU A 271      165.21    -47.03                                   
REMARK 500    MET A 282     -104.05     30.85                                   
REMARK 500    ARG A 287      -84.10    -38.06                                   
REMARK 500    GLU A 321      -88.70    -19.17                                   
REMARK 500    VAL A 339       -4.77   -144.06                                   
REMARK 500    PRO A 343       17.83    -49.40                                   
REMARK 500    HIS A 355      -53.22   -135.23                                   
REMARK 500    ASN A 389      110.71    171.83                                   
REMARK 500    SER A 393      -13.16     85.92                                   
REMARK 500    GLN A 442      127.83    -39.63                                   
REMARK 500    THR A 571      -65.38   -134.18                                   
REMARK 500    PRO A 575      107.09    -34.69                                   
REMARK 500    VAL B  17      -79.17   -116.18                                   
REMARK 500    ALA B  32        4.34    -54.54                                   
REMARK 500    ALA B  48       86.48   -150.53                                   
REMARK 500    SER B  56      -68.79   -157.89                                   
REMARK 500    ALA B  94      160.55    -47.09                                   
REMARK 500    ASP B 101     -119.84     34.19                                   
REMARK 500    LYS B 117       71.86     47.02                                   
REMARK 500    ALA B 140      -37.28    -35.28                                   
REMARK 500    PRO B 170      -74.33    -39.91                                   
REMARK 500    HIS B 186       36.83   -140.80                                   
REMARK 500    ALA B 193      -38.58    -36.33                                   
REMARK 500    HIS B 217       61.50     36.69                                   
REMARK 500    ASP B 219       70.87     61.73                                   
REMARK 500    PRO B 242      -34.73    -17.47                                   
REMARK 500    PRO C   6       94.51    -61.58                                   
REMARK 500    THR C  12     -178.08    -62.28                                   
REMARK 500    LYS C  18      -74.47    -71.61                                   
REMARK 500    PRO C  20        4.88    -68.53                                   
REMARK 500    ARG C  28      -34.22    -37.89                                   
REMARK 500    THR C  31      -16.19    -35.86                                   
REMARK 500    LEU C  49       26.64    -69.04                                   
REMARK 500    LYS C  50      -38.09   -141.72                                   
REMARK 500    PRO C  53      -32.48    -33.35                                   
REMARK 500    LYS C  99     -137.25     62.92                                   
REMARK 500    GLU C 106      -49.41    -28.69                                   
REMARK 500    TYR C 129      -61.21   -106.10                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     274 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR O 129         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 118        -17.24                                           
REMARK 500    GLU A 276         12.40                                           
REMARK 500    VAL A 341         13.65                                           
REMARK 500    GLU A 422        -10.42                                           
REMARK 500    PRO B  15         12.12                                           
REMARK 500    GLU B  16         10.79                                           
REMARK 500    ASP B 185        -10.09                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A  29        21.2      L          L   OUTSIDE RANGE           
REMARK 500    ALA A  30        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR A 131        24.4      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 266        49.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 276        23.3      L          L   OUTSIDE RANGE           
REMARK 500    PRO A 277        47.2      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 321        24.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 341        23.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 547        17.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN B  46        21.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FAD A  703                                                       
REMARK 610     MQ7 D  700                                                       
REMARK 610     FAD M  803                                                       
REMARK 610     MQ7 P  800                                                       
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                             FES B 244  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  57   SG                                                     
REMARK 620 2 FES B 244   S1  116.8                                              
REMARK 620 3 FES B 244   S2  117.8 103.1                                        
REMARK 620 4 CYS B  62   SG   93.2 115.5 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 244  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 FES B 244   S1  108.2                                              
REMARK 620 3 FES B 244   S2  102.7 101.5                                        
REMARK 620 4 CYS B  77   SG  110.9 112.0 120.6                                  
REMARK 620 5 CYS B  77   CB   66.8 126.1 132.4  44.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 148   SG                                                     
REMARK 620 2 SF4 B 246   S1  112.0                                              
REMARK 620 3 SF4 B 246   S2  118.2 107.6                                        
REMARK 620 4 SF4 B 246   S4  107.0 109.0 102.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 151   SG                                                     
REMARK 620 2 SF4 B 246   S2  117.3                                              
REMARK 620 3 SF4 B 246   S3  108.8 106.9                                        
REMARK 620 4 SF4 B 246   S4  113.8 103.0 106.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 154   SG                                                     
REMARK 620 2 SF4 B 246   S1  113.6                                              
REMARK 620 3 SF4 B 246   S3  114.4 107.0                                        
REMARK 620 4 SF4 B 246   S4  106.1 108.6 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 245  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 F3S B 245   S1  115.2                                              
REMARK 620 3 F3S B 245   S3   92.4 104.6                                        
REMARK 620 4 F3S B 245   S4  124.1 110.3 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 245  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 204   SG                                                     
REMARK 620 2 F3S B 245   S1  111.9                                              
REMARK 620 3 F3S B 245   S2  108.5 104.1                                        
REMARK 620 4 F3S B 245   S3  120.0 105.7 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 246  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 214   SG                                                     
REMARK 620 2 SF4 B 246   S1  115.1                                              
REMARK 620 3 SF4 B 246   S2  110.7 105.8                                        
REMARK 620 4 SF4 B 246   S3  112.4 106.4 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES N 244  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  57   SG                                                     
REMARK 620 2 FES N 244   S1  110.6                                              
REMARK 620 3 FES N 244   S2  111.1 103.9                                        
REMARK 620 4 CYS N  62   SG  110.2 111.6 109.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES N 244  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  65   SG                                                     
REMARK 620 2 FES N 244   S1  114.2                                              
REMARK 620 3 FES N 244   S2  113.0 103.3                                        
REMARK 620 4 CYS N  77   SG  105.3 110.9 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 148   SG                                                     
REMARK 620 2 SF4 N 246   S1  110.4                                              
REMARK 620 3 SF4 N 246   S2  115.7 106.6                                        
REMARK 620 4 SF4 N 246   S4  115.7 104.3 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 151   SG                                                     
REMARK 620 2 SF4 N 246   S2  118.1                                              
REMARK 620 3 SF4 N 246   S3  109.2 104.2                                        
REMARK 620 4 SF4 N 246   S4  114.7 103.2 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 154   SG                                                     
REMARK 620 2 SF4 N 246   S1  113.2                                              
REMARK 620 3 SF4 N 246   S3  113.1 105.3                                        
REMARK 620 4 SF4 N 246   S4  115.9 103.3 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S N 245  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 158   SG                                                     
REMARK 620 2 F3S N 245   S1  131.5                                              
REMARK 620 3 F3S N 245   S3   80.9 103.0                                        
REMARK 620 4 F3S N 245   S4  123.9 102.3 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S N 245  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 204   SG                                                     
REMARK 620 2 F3S N 245   S1  124.7                                              
REMARK 620 3 F3S N 245   S2   74.2 103.6                                        
REMARK 620 4 F3S N 245   S3  131.0 103.2 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 N 246  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N 214   SG                                                     
REMARK 620 2 SF4 N 246   S1  112.8                                              
REMARK 620 3 SF4 N 246   S2  115.5 104.9                                        
REMARK 620 4 SF4 N 246   S3  113.9 105.2 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC M 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQ7 D 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES N 244                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S N 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 N 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD M 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQ7 P 800                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KF6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1L0V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KFY   RELATED DB: PDB                                   
DBREF  2B76 A    0   601  GB     P00363   FRDA_ECOLI       0    601             
DBREF  2B76 M    0   601  GB     P00363   FRDA_ECOLI       0    601             
DBREF  2B76 B    1   243  UNP    P00364   FRDB_ECOLI       1    243             
DBREF  2B76 N    1   243  UNP    P00364   FRDB_ECOLI       1    243             
DBREF  2B76 C    1   130  UNP    P0A8Q0   FRDC_ECOLI       2    131             
DBREF  2B76 O    1   130  UNP    P0A8Q0   FRDC_ECOLI       2    131             
DBREF  2B76 D    0   118  UNP    P0A8Q3   FRDD_ECOLI       1    119             
DBREF  2B76 P    0   118  UNP    P0A8Q3   FRDD_ECOLI       1    119             
SEQADV 2B76 GLN A   49  GB   P00363    GLU    49 ENGINEERED                     
SEQADV 2B76 GLN M   49  GB   P00363    GLU    49 ENGINEERED                     
SEQRES   1 A  602  MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA          
SEQRES   2 A  602  GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN          
SEQRES   3 A  602  ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL          
SEQRES   4 A  602  TYR PRO MET ARG SER HIS THR VAL ALA ALA GLN GLY GLY          
SEQRES   5 A  602  SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR          
SEQRES   6 A  602  HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS          
SEQRES   7 A  602  GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO          
SEQRES   8 A  602  THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP          
SEQRES   9 A  602  SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE          
SEQRES  10 A  602  GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP          
SEQRES  11 A  602  LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR          
SEQRES  12 A  602  SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS          
SEQRES  13 A  602  PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG          
SEQRES  14 A  602  GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL          
SEQRES  15 A  602  GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY          
SEQRES  16 A  602  ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE          
SEQRES  17 A  602  VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY          
SEQRES  18 A  602  VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO          
SEQRES  19 A  602  THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY          
SEQRES  20 A  602  CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY          
SEQRES  21 A  602  TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR          
SEQRES  22 A  602  PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY          
SEQRES  23 A  602  PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP          
SEQRES  24 A  602  ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL          
SEQRES  25 A  602  VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU          
SEQRES  26 A  602  HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA          
SEQRES  27 A  602  TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL          
SEQRES  28 A  602  ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR          
SEQRES  29 A  602  ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA          
SEQRES  30 A  602  VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN          
SEQRES  31 A  602  ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE          
SEQRES  32 A  602  GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA          
SEQRES  33 A  602  THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN          
SEQRES  34 A  602  ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN          
SEQRES  35 A  602  GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU          
SEQRES  36 A  602  MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG          
SEQRES  37 A  602  THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA          
SEQRES  38 A  602  GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP          
SEQRES  39 A  602  THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE          
SEQRES  40 A  602  GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA          
SEQRES  41 A  602  HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS          
SEQRES  42 A  602  GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL          
SEQRES  43 A  602  ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP          
SEQRES  44 A  602  GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR          
SEQRES  45 A  602  THR LEU PRO PRO ALA LYS ARG VAL TYR GLY GLY GLU ALA          
SEQRES  46 A  602  ASP ALA ALA ASP LYS ALA GLU ALA ALA ASN LYS LYS GLU          
SEQRES  47 A  602  LYS ALA ASN GLY                                              
SEQRES   1 B  243  ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR          
SEQRES   2 B  243  ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR          
SEQRES   3 B  243  GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA          
SEQRES   4 B  243  LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER          
SEQRES   5 B  243  TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS          
SEQRES   6 B  243  GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS          
SEQRES   7 B  243  THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU          
SEQRES   8 B  243  ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL          
SEQRES   9 B  243  ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS          
SEQRES  10 B  243  PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY          
SEQRES  11 B  243  THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS          
SEQRES  12 B  243  GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA          
SEQRES  13 B  243  ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY          
SEQRES  14 B  243  PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP          
SEQRES  15 B  243  SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU          
SEQRES  16 B  243  ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY          
SEQRES  17 B  243  TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA          
SEQRES  18 B  243  ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP          
SEQRES  19 B  243  PHE LEU ILE ALA THR LEU LYS PRO ARG                          
SEQRES   1 C  130  THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER          
SEQRES   2 C  130  THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET          
SEQRES   3 C  130  LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER          
SEQRES   4 C  130  ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY          
SEQRES   5 C  130  PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN          
SEQRES   6 C  130  PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA          
SEQRES   7 C  130  ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO          
SEQRES   8 C  130  LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY          
SEQRES   9 C  130  PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL          
SEQRES  10 C  130  VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP          
SEQRES   1 D  119  MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL          
SEQRES   2 D  119  PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA          
SEQRES   3 D  119  ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU          
SEQRES   4 D  119  LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR          
SEQRES   5 D  119  GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG          
SEQRES   6 D  119  VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS          
SEQRES   7 D  119  GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS          
SEQRES   8 D  119  ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU          
SEQRES   9 D  119  ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL          
SEQRES  10 D  119  THR ILE                                                      
SEQRES   1 M  602  MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA          
SEQRES   2 M  602  GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN          
SEQRES   3 M  602  ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL          
SEQRES   4 M  602  TYR PRO MET ARG SER HIS THR VAL ALA ALA GLN GLY GLY          
SEQRES   5 M  602  SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR          
SEQRES   6 M  602  HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS          
SEQRES   7 M  602  GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO          
SEQRES   8 M  602  THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP          
SEQRES   9 M  602  SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE          
SEQRES  10 M  602  GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP          
SEQRES  11 M  602  LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR          
SEQRES  12 M  602  SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS          
SEQRES  13 M  602  PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG          
SEQRES  14 M  602  GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL          
SEQRES  15 M  602  GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY          
SEQRES  16 M  602  ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE          
SEQRES  17 M  602  VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY          
SEQRES  18 M  602  VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO          
SEQRES  19 M  602  THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY          
SEQRES  20 M  602  CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY          
SEQRES  21 M  602  TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR          
SEQRES  22 M  602  PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY          
SEQRES  23 M  602  PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP          
SEQRES  24 M  602  ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL          
SEQRES  25 M  602  VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU          
SEQRES  26 M  602  HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA          
SEQRES  27 M  602  TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL          
SEQRES  28 M  602  ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR          
SEQRES  29 M  602  ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA          
SEQRES  30 M  602  VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN          
SEQRES  31 M  602  ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE          
SEQRES  32 M  602  GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA          
SEQRES  33 M  602  THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN          
SEQRES  34 M  602  ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN          
SEQRES  35 M  602  GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU          
SEQRES  36 M  602  MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG          
SEQRES  37 M  602  THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA          
SEQRES  38 M  602  GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP          
SEQRES  39 M  602  THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE          
SEQRES  40 M  602  GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA          
SEQRES  41 M  602  HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS          
SEQRES  42 M  602  GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL          
SEQRES  43 M  602  ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP          
SEQRES  44 M  602  GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR          
SEQRES  45 M  602  THR LEU PRO PRO ALA LYS ARG VAL TYR GLY GLY GLU ALA          
SEQRES  46 M  602  ASP ALA ALA ASP LYS ALA GLU ALA ALA ASN LYS LYS GLU          
SEQRES  47 M  602  LYS ALA ASN GLY                                              
SEQRES   1 N  243  ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR          
SEQRES   2 N  243  ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR          
SEQRES   3 N  243  GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA          
SEQRES   4 N  243  LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER          
SEQRES   5 N  243  TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS          
SEQRES   6 N  243  GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS          
SEQRES   7 N  243  THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU          
SEQRES   8 N  243  ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL          
SEQRES   9 N  243  ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS          
SEQRES  10 N  243  PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY          
SEQRES  11 N  243  THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS          
SEQRES  12 N  243  GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA          
SEQRES  13 N  243  ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY          
SEQRES  14 N  243  PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP          
SEQRES  15 N  243  SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU          
SEQRES  16 N  243  ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY          
SEQRES  17 N  243  TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA          
SEQRES  18 N  243  ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP          
SEQRES  19 N  243  PHE LEU ILE ALA THR LEU LYS PRO ARG                          
SEQRES   1 O  130  THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER          
SEQRES   2 O  130  THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET          
SEQRES   3 O  130  LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER          
SEQRES   4 O  130  ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY          
SEQRES   5 O  130  PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN          
SEQRES   6 O  130  PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA          
SEQRES   7 O  130  ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO          
SEQRES   8 O  130  LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY          
SEQRES   9 O  130  PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL          
SEQRES  10 O  130  VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP          
SEQRES   1 P  119  MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL          
SEQRES   2 P  119  PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA          
SEQRES   3 P  119  ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU          
SEQRES   4 P  119  LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR          
SEQRES   5 P  119  GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG          
SEQRES   6 P  119  VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS          
SEQRES   7 P  119  GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS          
SEQRES   8 P  119  ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU          
SEQRES   9 P  119  ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL          
SEQRES  10 P  119  THR ILE                                                      
HET    FLC  A 702      13                                                       
HET    FLC  M 802      13                                                       
HET    FES  B 244       4                                                       
HET    F3S  B 245       7                                                       
HET    SF4  B 246       8                                                       
HET    FAD  A 703      52                                                       
HET    MQ7  D 700      33                                                       
HET    FES  N 244       4                                                       
HET    F3S  N 245       7                                                       
HET    SF4  N 246       8                                                       
HET    FAD  M 803      52                                                       
HET    MQ7  P 800      33                                                       
HETNAM     FLC CITRATE ANION                                                    
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MQ7 MENAQUINONE-7                                                    
FORMUL   9  FLC    2(C6 H5 O7 3-)                                               
FORMUL  11  FES    2(FE2 S2)                                                    
FORMUL  12  F3S    2(FE3 S4)                                                    
FORMUL  13  SF4    2(FE4 S4)                                                    
FORMUL  14  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  15  MQ7    2(C46 H64 O2)                                                
HELIX    1   1 GLY A   14  ASN A   27  1                                  14    
HELIX    2   2 TYR A   39  ALA A   48  5                                  10    
HELIX    3   3 SER A   61  ASP A   74  1                                  14    
HELIX    4   4 GLU A   78  TRP A   99  1                                  22    
HELIX    5   5 ALA A  127  ASP A  129  5                                   3    
HELIX    6   6 LYS A  130  SER A  143  1                                  14    
HELIX    7   7 LEU A  144  PHE A  146  5                                   3    
HELIX    8   8 ALA A  195  TYR A  199  5                                   5    
HELIX    9   9 GLY A  210  SER A  218  1                                   9    
HELIX   10  10 THR A  244  GLU A  250  1                                   7    
HELIX   11  11 ARG A  261  ASP A  265  5                                   5    
HELIX   12  12 TYR A  281  GLY A  285  5                                   5    
HELIX   13  13 PRO A  286  LYS A  300  1                                  15    
HELIX   14  14 GLY A  320  LEU A  328  1                                   9    
HELIX   15  15 PRO A  329  GLY A  340  1                                  12    
HELIX   16  16 SER A  393  ALA A  414  1                                  22    
HELIX   17  17 ASN A  421  ASN A  441  1                                  21    
HELIX   18  18 ASN A  447  CYS A  463  1                                  17    
HELIX   19  19 THR A  468  PHE A  486  1                                  19    
HELIX   20  20 LYS A  487  VAL A  489  5                                   3    
HELIX   21  21 ASN A  499  ARG A  525  1                                  27    
HELIX   22  22 SER B   35  LEU B   47  1                                  13    
HELIX   23  23 CYS B   77  THR B   79  5                                   3    
HELIX   24  24 PHE B   80  TYR B   84  5                                   5    
HELIX   25  25 MET B  106  ILE B  116  1                                  11    
HELIX   26  26 THR B  126  GLY B  130  5                                   5    
HELIX   27  27 THR B  135  HIS B  143  1                                   9    
HELIX   28  28 GLN B  144  GLY B  147  5                                   4    
HELIX   29  29 CYS B  158  LEU B  163  1                                   6    
HELIX   30  30 GLY B  169  ASP B  182  1                                  14    
HELIX   31  31 GLY B  187  ASN B  196  1                                  10    
HELIX   32  32 GLY B  200  CYS B  204  5                                   5    
HELIX   33  33 GLY B  208  CYS B  214  1                                   7    
HELIX   34  34 ASP B  219  ALA B  238  1                                  20    
HELIX   35  35 THR C   14  LYS C   18  5                                   5    
HELIX   36  36 LEU C   19  THR C   31  1                                  13    
HELIX   37  37 THR C   31  LEU C   49  1                                  19    
HELIX   38  38 GLY C   52  ASN C   65  1                                  14    
HELIX   39  39 ASN C   65  ALA C   90  1                                  26    
HELIX   40  40 PRO C   91  ALA C   94  5                                   4    
HELIX   41  41 PRO C  105  TYR C  129  1                                  25    
HELIX   42  42 VAL D   12  ILE D   27  1                                  16    
HELIX   43  43 ILE D   27  ILE D   37  1                                  11    
HELIX   44  44 SER D   50  SER D   60  1                                  11    
HELIX   45  45 GLY D   63  ASP D   88  1                                  26    
HELIX   46  46 ALA D   95  ILE D  118  1                                  24    
HELIX   47  47 ALA M   15  ALA M   22  1                                   8    
HELIX   48  48 SER M   61  GLY M   73  1                                  13    
HELIX   49  49 GLU M   78  GLY M  100  1                                  23    
HELIX   50  50 LYS M  130  LEU M  139  1                                  10    
HELIX   51  51 ALA M  195  TYR M  199  5                                   5    
HELIX   52  52 ASP M  211  ALA M  216  1                                   6    
HELIX   53  53 THR M  244  GLY M  249  1                                   6    
HELIX   54  54 ARG M  261  GLY M  267  5                                   7    
HELIX   55  55 PRO M  286  ALA M  293  1                                   8    
HELIX   56  56 PHE M  294  GLY M  301  1                                   8    
HELIX   57  57 GLY M  320  ARG M  327  1                                   8    
HELIX   58  58 LEU M  328  VAL M  339  1                                  12    
HELIX   59  59 LEU M  396  ALA M  415  1                                  20    
HELIX   60  60 ALA M  424  GLN M  442  1                                  19    
HELIX   61  61 ASN M  447  ALA M  458  1                                  12    
HELIX   62  62 THR M  468  ILE M  476  1                                   9    
HELIX   63  63 ASP M  477  GLU M  484  1                                   8    
HELIX   64  64 ASN M  499  GLY M  509  1                                  11    
HELIX   65  65 HIS M  510  LEU M  512  5                                   3    
HELIX   66  66 ASN M  513  ARG M  525  1                                  13    
HELIX   67  67 SER N   35  ASP N   45  1                                  11    
HELIX   68  68 PHE N   80  TYR N   84  5                                   5    
HELIX   69  69 MET N  106  ALA N  115  1                                  10    
HELIX   70  70 MET N  139  GLY N  147  1                                   9    
HELIX   71  71 GLN N  160  ASN N  164  5                                   5    
HELIX   72  72 GLY N  169  GLU N  181  1                                  13    
HELIX   73  73 LYS N  188  GLU N  190  5                                   3    
HELIX   74  74 ARG N  191  ASN N  196  1                                   6    
HELIX   75  75 TYR N  209  CYS N  214  1                                   6    
HELIX   76  76 ASP N  219  ASP N  234  1                                  16    
HELIX   77  77 THR O   14  LYS O   18  5                                   5    
HELIX   78  78 PHE O   21  THR O   31  1                                  11    
HELIX   79  79 ALA O   32  LEU O   49  1                                  18    
HELIX   80  80 GLY O   52  ASN O   65  1                                  14    
HELIX   81  81 ASN O   65  ALA O   90  1                                  26    
HELIX   82  82 PRO O   91  ALA O   94  5                                   4    
HELIX   83  83 PRO O  105  TYR O  129  1                                  25    
HELIX   84  84 ASP P    9  ILE P   27  1                                  19    
HELIX   85  85 ILE P   27  ILE P   37  1                                  11    
HELIX   86  86 SER P   50  GLN P   59  1                                  10    
HELIX   87  87 SER P   60  ILE P   62  5                                   3    
HELIX   88  88 GLY P   63  ASP P   88  1                                  26    
HELIX   89  89 ALA P   95  ILE P  118  1                                  24    
SHEET    1   A 4 GLN A   1  GLN A   4  0                                        
SHEET    2   A 4 LEU A 180  ARG A 184  1  O  ARG A 184   N  PHE A   3           
SHEET    3   A 4 HIS A 166  ASN A 174 -1  N  LEU A 170   O  ILE A 183           
SHEET    4   A 4 HIS A 155  ASP A 163 -1  N  LEU A 161   O  GLY A 169           
SHEET    1   B 5 ILE A 149  PHE A 152  0                                        
SHEET    2   B 5 ILE A  32  ILE A  35  1  N  LEU A  34   O  PHE A 152           
SHEET    3   B 5 LEU A   7  VAL A  10  1  N  ILE A   9   O  ALA A  33           
SHEET    4   B 5 VAL A 188  MET A 190  1  O  VAL A 189   N  VAL A  10           
SHEET    5   B 5 LEU A 374  ALA A 376  1  O  PHE A 375   N  MET A 190           
SHEET    1   C 3 SER A  52  ALA A  53  0                                        
SHEET    2   C 3 THR A 124  TRP A 125 -1  O  TRP A 125   N  SER A  52           
SHEET    3   C 3 VAL A 113  ARG A 114 -1  N  ARG A 114   O  THR A 124           
SHEET    1   D 5 SER A 381  SER A 382  0                                        
SHEET    2   D 5 GLY A 360  GLU A 362  1  N  ILE A 361   O  SER A 382           
SHEET    3   D 5 LEU A 223  ARG A 224 -1  N  ARG A 224   O  GLY A 360           
SHEET    4   D 5 LYS A 549  ARG A 555 -1  O  ALA A 553   N  LEU A 223           
SHEET    5   D 5 THR A 561  ASP A 567 -1  O  SER A 566   N  HIS A 550           
SHEET    1   E 4 VAL A 229  GLY A 235  0                                        
SHEET    2   E 4 ILE A 348  THR A 357 -1  O  ARG A 351   N  GLY A 235           
SHEET    3   E 4 ASP A 310  ASP A 315 -1  N  LEU A 314   O  ILE A 348           
SHEET    4   E 4 ILE A 253  VAL A 255 -1  N  ILE A 253   O  ASP A 315           
SHEET    1   F 4 VAL A 229  GLY A 235  0                                        
SHEET    2   F 4 ILE A 348  THR A 357 -1  O  ARG A 351   N  GLY A 235           
SHEET    3   F 4 ASP A 310  ASP A 315 -1  N  LEU A 314   O  ILE A 348           
SHEET    4   F 4 ILE A 304  SER A 305 -1  N  ILE A 304   O  VAL A 311           
SHEET    1   G 2 TYR A 466  ARG A 467  0                                        
SHEET    2   G 2 GLN A 533  ARG A 534  1  O  GLN A 533   N  ARG A 467           
SHEET    1   H 5 PHE B  25  TYR B  30  0                                        
SHEET    2   H 5 LYS B   4  VAL B  10 -1  N  LEU B   6   O  VAL B  28           
SHEET    3   H 5 MET B  88  GLU B  91  1  O  VAL B  90   N  GLU B   9           
SHEET    4   H 5 GLY B  66  VAL B  69 -1  N  MET B  68   O  GLU B  91           
SHEET    5   H 5 VAL B  72  LEU B  75 -1  O  LYS B  74   N  MET B  67           
SHEET    1   I 2 ILE B  98  ARG B 100  0                                        
SHEET    2   I 2 VAL B 103  VAL B 104 -1  O  VAL B 103   N  ARG B 100           
SHEET    1   J 2 ILE C  97  VAL C  98  0                                        
SHEET    2   J 2 GLU C 101  LYS C 102 -1  O  GLU C 101   N  VAL C  98           
SHEET    1   K 4 THR M   2  PHE M   3  0                                        
SHEET    2   K 4 LEU M 180  ILE M 183  1  N  GLN M 182   O  PHE M   3           
SHEET    3   K 4 ALA M 172  ASN M 174 -1  N  ALA M 172   O  VAL M 181           
SHEET    4   K 4 HIS M 155  VAL M 157 -1  N  PHE M 156   O  MET M 173           
SHEET    1   L 3 LEU M   7  VAL M  10  0                                        
SHEET    2   L 3 ILE M  32  ILE M  35  1  O  ILE M  35   N  ILE M   9           
SHEET    3   L 3 ILE M 149  ARG M 151  1  O  GLN M 150   N  ILE M  32           
SHEET    1   M 4 TYR M 231  GLY M 235  0                                        
SHEET    2   M 4 ILE M 348  ALA M 354 -1  O  THR M 353   N  HIS M 232           
SHEET    3   M 4 GLY M 309  LEU M 314 -1  N  VAL M 312   O  VAL M 350           
SHEET    4   M 4 ILE M 304  THR M 306 -1  N  ILE M 304   O  VAL M 311           
SHEET    1   N 2 PHE M 554  ARG M 555  0                                        
SHEET    2   N 2 GLY M 559  THR M 560 -1  O  THR M 560   N  PHE M 554           
SHEET    1   O 3 VAL N  72  LYS N  74  0                                        
SHEET    2   O 3 MET N  67  VAL N  69 -1  N  VAL N  69   O  VAL N  72           
SHEET    3   O 3 VAL N  90  GLU N  91 -1  O  GLU N  91   N  MET N  68           
SHEET    1   P 2 ILE O  97  VAL O  98  0                                        
SHEET    2   P 2 GLU O 101  LYS O 102 -1  O  GLU O 101   N  VAL O  98           
LINK         SG  CYS B  57                FE2  FES B 244     1555   1555  2.21  
LINK         SG  CYS B  62                FE2  FES B 244     1555   1555  2.02  
LINK         SG  CYS B  65                FE1  FES B 244     1555   1555  2.33  
LINK         SG  CYS B  77                FE1  FES B 244     1555   1555  2.49  
LINK         SG  CYS B 148                FE3  SF4 B 246     1555   1555  2.19  
LINK         SG  CYS B 151                FE1  SF4 B 246     1555   1555  2.21  
LINK         SG  CYS B 154                FE2  SF4 B 246     1555   1555  2.21  
LINK         SG  CYS B 158                FE3  F3S B 245     1555   1555  2.02  
LINK         SG  CYS B 204                FE1  F3S B 245     1555   1555  2.19  
LINK         SG  CYS B 214                FE4  SF4 B 246     1555   1555  2.24  
LINK         SG  CYS N  57                FE2  FES N 244     1555   1555  2.28  
LINK         SG  CYS N  62                FE2  FES N 244     1555   1555  2.26  
LINK         SG  CYS N  65                FE1  FES N 244     1555   1555  2.26  
LINK         SG  CYS N  77                FE1  FES N 244     1555   1555  2.25  
LINK         SG  CYS N 148                FE3  SF4 N 246     1555   1555  2.25  
LINK         SG  CYS N 151                FE1  SF4 N 246     1555   1555  2.27  
LINK         SG  CYS N 154                FE2  SF4 N 246     1555   1555  2.27  
LINK         SG  CYS N 158                FE3  F3S N 245     1555   1555  2.54  
LINK         SG  CYS N 204                FE1  F3S N 245     1555   1555  2.40  
LINK         SG  CYS N 214                FE4  SF4 N 246     1555   1555  2.30  
LINK         NE2 HIS A  44                 C8M FAD A 703     1555   1555  1.86  
LINK         NE2 HIS M  44                 C8M FAD M 803     1555   1555  1.81  
LINK         CB  CYS B  77                FE1  FES B 244     1555   1555  2.30  
SITE     1 AC1 10 GLN A 230  HIS A 232  THR A 244  GLU A 245                    
SITE     2 AC1 10 ARG A 287  HIS A 355  ARG A 390  GLY A 392                    
SITE     3 AC1 10 SER A 393  FAD A 703                                          
SITE     1 AC2  9 PHE M 116  GLN M 230  HIS M 232  LEU M 242                    
SITE     2 AC2  9 GLU M 245  ARG M 287  HIS M 355  ARG M 390                    
SITE     3 AC2  9 ASN M 394                                                     
SITE     1 AC3  7 SER B  56  CYS B  57  ARG B  58  CYS B  62                    
SITE     2 AC3  7 GLY B  63  CYS B  65  CYS B  77                               
SITE     1 AC4 10 CYS B 158  GLN B 160  CYS B 204  THR B 205                    
SITE     2 AC4 10 PHE B 206  VAL B 207  GLY B 208  TYR B 209                    
SITE     3 AC4 10 CYS B 210  ALA B 221                                          
SITE     1 AC5  6 CYS B 148  ILE B 149  CYS B 151  GLY B 152                    
SITE     2 AC5  6 CYS B 154  CYS B 214                                          
SITE     1 AC6 31 GLY A  11  ALA A  12  GLY A  14  ALA A  15                    
SITE     2 AC6 31 SER A  36  LYS A  37  SER A  43  HIS A  44                    
SITE     3 AC6 31 THR A  45  ALA A  47  ALA A  48  GLN A  49                    
SITE     4 AC6 31 GLY A  50  GLY A  51  HIS A 155  VAL A 157                    
SITE     5 AC6 31 THR A 192  GLY A 193  THR A 203  ASN A 204                    
SITE     6 AC6 31 ASP A 211  MET A 215  LEU A 242  TYR A 356                    
SITE     7 AC6 31 GLY A 378  GLU A 379  SER A 393  SER A 395                    
SITE     8 AC6 31 LEU A 396  LEU A 399  FLC A 702                               
SITE     1 AC7  8 GLY C  45  TRP C  56  ILE C 123  ALA C 127                    
SITE     2 AC7  8 VAL D  35  LEU D  49  PHE D  57  LEU D  67                    
SITE     1 AC8  8 LEU N  37  CYS N  57  ILE N  61  CYS N  62                    
SITE     2 AC8  8 GLY N  63  SER N  64  CYS N  65  CYS N  77                    
SITE     1 AC9 11 CYS N 158  CYS N 204  THR N 205  PHE N 206                    
SITE     2 AC9 11 VAL N 207  GLY N 208  TYR N 209  CYS N 210                    
SITE     3 AC9 11 ALA N 221  ILE N 224  GLN N 225                               
SITE     1 BC1  8 CYS N 148  ILE N 149  CYS N 151  GLY N 152                    
SITE     2 BC1  8 CYS N 154  CYS N 214  PRO N 215  VAL N 218                    
SITE     1 BC2 32 VAL M  10  GLY M  11  ALA M  12  GLY M  13                    
SITE     2 BC2 32 GLY M  14  ALA M  15  SER M  36  LYS M  37                    
SITE     3 BC2 32 SER M  43  HIS M  44  THR M  45  ALA M  47                    
SITE     4 BC2 32 ALA M  48  GLN M  49  GLY M  50  GLY M  51                    
SITE     5 BC2 32 VAL M 157  ALA M 191  THR M 192  THR M 203                    
SITE     6 BC2 32 ASN M 204  ILE M 207  VAL M 208  ASP M 211                    
SITE     7 BC2 32 GLY M 212  LEU M 242  HIS M 355  TYR M 356                    
SITE     8 BC2 32 GLY M 378  GLU M 379  LEU M 396  LEU M 399                    
SITE     1 BC3  8 ILE O 123  VAL O 126  VAL P  35  LEU P  49                    
SITE     2 BC3  8 PHE P  57  ILE P  62  PHE P  66  LEU P  67                    
CRYST1   96.802  139.527  273.972  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010330  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007167  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003650        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system