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Database: PDB
Entry: 1DXO
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HEADER    OXIDOREDUCTASE                          12-JAN-00   1DXO              
TITLE     CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,
TITLE    2 5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM         
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: QUINONE REDUCTASE;                                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DT-DIAPHORASE;                                              
COMPND   5 EC: 1.6.99.2;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FLAVOPROTEIN, ROSSMANN FOLD, OXIDOREDUCTASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FAIG,M.A.BIANCHET,S.CHEN,S.WINSKI,D.ROSS,L.M.AMZEL                  
REVDAT   5   05-JUL-17 1DXO    1       REMARK                                   
REVDAT   4   12-NOV-14 1DXO    1       HEADER KEYWDS JRNL   REMARK              
REVDAT   4 2                   1       VERSN  FORMUL SHEET  MASTER              
REVDAT   3   24-FEB-09 1DXO    1       VERSN                                    
REVDAT   2   21-OCT-05 1DXO    1       HETATM                                   
REVDAT   1   23-APR-00 1DXO    0                                                
JRNL        AUTH   M.FAIG,M.A.BIANCHET,S.CHEN,S.WINSKI,D.ROSS,P.TALALAY,        
JRNL        AUTH 2 L.M.AMZEL                                                    
JRNL        TITL   STRUCTURES OF RECOMBINANT MOUSE AND HUMAN NAD(P)H:QUINONE    
JRNL        TITL 2 OXIDOREDUCTASES:SPECIES COMPARISON AND STRUCTURAL CHANGES    
JRNL        TITL 3 WITH SUBSTRATE BINDING AND RELEASE                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  97  3177 2000              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   10706635                                                     
JRNL        DOI    10.1073/PNAS.050585797                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.A.BIANCHET,C.FOSTER,M.FAIG,P.TALALAY,L.M.AMZEL             
REMARK   1  TITL   STRUCTURE AND MECHANISM OF CYTOSOLIC QUINONE REDUCTASE       
REMARK   1  REF    BIOCHEM.SOC.TRANS.            V.  27   610 1999              
REMARK   1  REFN                   ISSN 0300-5127                               
REMARK   1  PMID   10917652                                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.FOSTER,M.A.BIANCHET,P.TALALAY,Q.ZHAO,L.M.AMZEL             
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN QUINONE REDUCTASE TYPE 2, A       
REMARK   1  TITL 2 METALLOPROTEIN                                               
REMARK   1  REF    BIOCHEMISTRY                  V.  38  9881 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   10433694                                                     
REMARK   1  DOI    10.1021/BI990799V                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.LI,M.A.BIANCHET,P.TALALAY,L.M.AMZEL                        
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF NAD(P)H:QUINONE           
REMARK   1  TITL 2 REDUCTASE, A FLAVOPROTEIN INVOLVED IN CANCER CHEMOPROTECTION 
REMARK   1  TITL 3 AND CHEMOTHERAPY: MECHANISM OF TWO-ELECTRON REDUCTION        
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  92  8846 1995              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   7568029                                                      
REMARK   1  DOI    10.1073/PNAS.92.19.8846                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 411877.160                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 70.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27730                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2802                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 30.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1784                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 190                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 260                                     
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.35000                                              
REMARK   3    B22 (A**2) : -1.82000                                             
REMARK   3    B33 (A**2) : 0.46000                                              
REMARK   3    B12 (A**2) : -2.88000                                             
REMARK   3    B13 (A**2) : 3.50000                                              
REMARK   3    B23 (A**2) : -0.02000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.930                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 19.00                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NEWPARAM.DQN                                   
REMARK   3  PARAMETER FILE  3  : NEWFAD_XPLOR.PAR                               
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  4   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004539.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36969                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09300                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS 0.9                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.50                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   1    CG1  CG2                                            
REMARK 470     VAL B   1    CG1  CG2                                            
REMARK 470     VAL C   1    CG1  CG2                                            
REMARK 470     VAL D   1    CG1  CG2                                            
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    GLU A 123      -46.85     78.59                                   
REMARK 500    TYR A 132     -126.70     45.91                                   
REMARK 500    ASP A 133      -13.41    -47.51                                   
REMARK 500    SER A 191       59.14     28.59                                   
REMARK 500    HIS A 257       53.29   -101.69                                   
REMARK 500    GLU B 123      -44.27     78.94                                   
REMARK 500    TYR B 132     -134.41     49.59                                   
REMARK 500    ASP B 133      -22.90    -39.63                                   
REMARK 500    ILE B 175      -63.38   -102.44                                   
REMARK 500    SER B 191       63.69     29.61                                   
REMARK 500    LEU B 230       35.78    -69.39                                   
REMARK 500    GLN B 233      -74.70    -56.56                                   
REMARK 500    ALA B 234       -1.92    -55.10                                   
REMARK 500    PHE B 236       38.31     36.55                                   
REMARK 500    HIS B 257       53.85   -101.92                                   
REMARK 500    LEU B 259       17.13     56.58                                   
REMARK 500    LYS B 261     -164.05   -105.09                                   
REMARK 500    ASP B 266       50.15     38.19                                   
REMARK 500    ARG B 272      150.39    -48.80                                   
REMARK 500    PHE C 106       27.47     47.41                                   
REMARK 500    GLU C 123      -46.86     78.37                                   
REMARK 500    TYR C 132     -128.12     45.93                                   
REMARK 500    ASP C 133      -19.39    -45.30                                   
REMARK 500    ILE C 175      -65.17   -103.40                                   
REMARK 500    SER C 191       56.56     31.94                                   
REMARK 500    HIS C 257       52.86   -101.18                                   
REMARK 500    LEU C 259       18.42     52.74                                   
REMARK 500    ASP C 266       48.77     37.19                                   
REMARK 500    GLU D 123      -35.52     80.70                                   
REMARK 500    TYR D 126     -167.50   -115.30                                   
REMARK 500    THR D 127      -11.56   -168.10                                   
REMARK 500    TYR D 128      -51.02     64.46                                   
REMARK 500    TYR D 132     -126.01     50.52                                   
REMARK 500    ILE D 175      -64.42   -103.76                                   
REMARK 500    SER D 191       62.69     21.42                                   
REMARK 500    LEU D 230       49.58    -70.87                                   
REMARK 500    SER D 254     -168.78   -161.89                                   
REMARK 500    HIS D 257       54.14   -103.53                                   
REMARK 500    LEU D 259       14.79     54.52                                   
REMARK 500    LYS D 261     -168.47   -100.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE.               
REMARK 700 EACH IS REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE             
REMARK 700 IDENTICAL STRANDS.                                                   
REMARK 700 SHEETS A AND A1 REPRESENT ONE BIFURCATED SHEET IN CHAIN A            
REMARK 700 SHEETS B AND B1 REPRESENT ONE BIFURCATED SHEET IN CHAIN D            
REMARK 700 SHEETS C AND C1 REPRESENT ONE BIFURCATED SHEET IN CHAIN C            
REMARK 700 SHEETS D AND D1 REPRESENT ONE BIFURCATED SHEET IN CHAIN D            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DQN A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DQN B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DQN C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DQN D 302                 
DBREF  1DXO A    1   273  UNP    P15559   DHQU_HUMAN       2    274             
DBREF  1DXO B    1   273  UNP    P15559   DHQU_HUMAN       2    274             
DBREF  1DXO C    1   273  UNP    P15559   DHQU_HUMAN       2    274             
DBREF  1DXO D    1   273  UNP    P15559   DHQU_HUMAN       2    274             
SEQRES   1 A  273  VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER GLU          
SEQRES   2 A  273  ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA ALA          
SEQRES   3 A  273  ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU SER          
SEQRES   4 A  273  ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER ARG          
SEQRES   5 A  273  LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN PHE          
SEQRES   6 A  273  GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU GLY          
SEQRES   7 A  273  HIS LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS LEU          
SEQRES   8 A  273  GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU GLN          
SEQRES   9 A  273  TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE GLU          
SEQRES  10 A  273  ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA ALA          
SEQRES  11 A  273  MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA VAL          
SEQRES  12 A  273  LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR SER          
SEQRES  13 A  273  LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU TRP          
SEQRES  14 A  273  PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE GLN          
SEQRES  15 A  273  VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS THR          
SEQRES  16 A  273  PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP LYS          
SEQRES  17 A  273  LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU TYR          
SEQRES  18 A  273  PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN ALA          
SEQRES  19 A  273  GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU LYS          
SEQRES  20 A  273  ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU GLY          
SEQRES  21 A  273  LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG LYS          
SEQRES   1 B  273  VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER GLU          
SEQRES   2 B  273  ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA ALA          
SEQRES   3 B  273  ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU SER          
SEQRES   4 B  273  ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER ARG          
SEQRES   5 B  273  LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN PHE          
SEQRES   6 B  273  GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU GLY          
SEQRES   7 B  273  HIS LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS LEU          
SEQRES   8 B  273  GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU GLN          
SEQRES   9 B  273  TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE GLU          
SEQRES  10 B  273  ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA ALA          
SEQRES  11 B  273  MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA VAL          
SEQRES  12 B  273  LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR SER          
SEQRES  13 B  273  LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU TRP          
SEQRES  14 B  273  PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE GLN          
SEQRES  15 B  273  VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS THR          
SEQRES  16 B  273  PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP LYS          
SEQRES  17 B  273  LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU TYR          
SEQRES  18 B  273  PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN ALA          
SEQRES  19 B  273  GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU LYS          
SEQRES  20 B  273  ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU GLY          
SEQRES  21 B  273  LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG LYS          
SEQRES   1 C  273  VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER GLU          
SEQRES   2 C  273  ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA ALA          
SEQRES   3 C  273  ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU SER          
SEQRES   4 C  273  ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER ARG          
SEQRES   5 C  273  LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN PHE          
SEQRES   6 C  273  GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU GLY          
SEQRES   7 C  273  HIS LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS LEU          
SEQRES   8 C  273  GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU GLN          
SEQRES   9 C  273  TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE GLU          
SEQRES  10 C  273  ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA ALA          
SEQRES  11 C  273  MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA VAL          
SEQRES  12 C  273  LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR SER          
SEQRES  13 C  273  LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU TRP          
SEQRES  14 C  273  PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE GLN          
SEQRES  15 C  273  VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS THR          
SEQRES  16 C  273  PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP LYS          
SEQRES  17 C  273  LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU TYR          
SEQRES  18 C  273  PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN ALA          
SEQRES  19 C  273  GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU LYS          
SEQRES  20 C  273  ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU GLY          
SEQRES  21 C  273  LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG LYS          
SEQRES   1 D  273  VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER GLU          
SEQRES   2 D  273  ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA ALA          
SEQRES   3 D  273  ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU SER          
SEQRES   4 D  273  ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER ARG          
SEQRES   5 D  273  LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN PHE          
SEQRES   6 D  273  GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU GLY          
SEQRES   7 D  273  HIS LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS LEU          
SEQRES   8 D  273  GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU GLN          
SEQRES   9 D  273  TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE GLU          
SEQRES  10 D  273  ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA ALA          
SEQRES  11 D  273  MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA VAL          
SEQRES  12 D  273  LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR SER          
SEQRES  13 D  273  LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU TRP          
SEQRES  14 D  273  PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE GLN          
SEQRES  15 D  273  VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS THR          
SEQRES  16 D  273  PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP LYS          
SEQRES  17 D  273  LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU TYR          
SEQRES  18 D  273  PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN ALA          
SEQRES  19 D  273  GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU LYS          
SEQRES  20 D  273  ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU GLY          
SEQRES  21 D  273  LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG LYS          
HET    FAD  A 301      53                                                       
HET    DQN  A 302      12                                                       
HET    FAD  B 301      53                                                       
HET    DQN  B 302      12                                                       
HET    FAD  C 301      53                                                       
HET    DQN  C 302      12                                                       
HET    FAD  D 301      53                                                       
HET    DQN  D 302      12                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     DQN DUROQUINONE                                                      
FORMUL   5  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   6  DQN    4(C10 H12 O2)                                                
FORMUL  13  HOH   *105(H2 O)                                                    
HELIX    1   1 SER A   16  LYS A   32  1                                  17    
HELIX    2   2 SER A   51  ASP A   54  5                                   4    
HELIX    3   3 ASP A   61  PHE A   65  5                                   5    
HELIX    4   4 GLN A   66  GLY A   78  1                                  13    
HELIX    5   5 SER A   81  ALA A   94  1                                  14    
HELIX    6   6 PRO A  109  PHE A  120  1                                  12    
HELIX    7   7 MET A  131  GLY A  135  5                                   5    
HELIX    8   8 SER A  151  SER A  156  5                                   6    
HELIX    9   9 ASP A  163  SER A  173  1                                  11    
HELIX   10  10 LEU A  176  GLY A  180  5                                   5    
HELIX   11  11 SER A  191  THR A  195  5                                   5    
HELIX   12  12 PRO A  196  LEU A  211  1                                  16    
HELIX   13  13 GLU A  212  GLU A  217  5                                   6    
HELIX   14  14 PRO A  224  LEU A  227  5                                   4    
HELIX   15  15 LYS A  239  LYS A  247  1                                   9    
HELIX   16  16 SER B   16  LYS B   32  1                                  17    
HELIX   17  17 LEU B   41  ASN B   45  1                                   5    
HELIX   18  18 SER B   51  ASP B   54  5                                   4    
HELIX   19  19 GLN B   66  GLY B   78  1                                  13    
HELIX   20  20 SER B   81  ALA B   94  1                                  14    
HELIX   21  21 PRO B  109  PHE B  120  1                                  12    
HELIX   22  22 THR B  127  MET B  131  5                                   5    
HELIX   23  23 MET B  131  GLY B  135  5                                   5    
HELIX   24  24 SER B  151  SER B  156  5                                   6    
HELIX   25  25 ASP B  163  SER B  173  1                                  11    
HELIX   26  26 LEU B  176  GLY B  180  5                                   5    
HELIX   27  27 SER B  191  THR B  195  5                                   5    
HELIX   28  28 PRO B  196  GLU B  212  1                                  17    
HELIX   29  29 ASN B  213  GLU B  217  5                                   5    
HELIX   30  30 PRO B  224  LEU B  227  5                                   4    
HELIX   31  31 LYS B  239  LYS B  247  1                                   9    
HELIX   32  32 SER C   16  LYS C   32  1                                  17    
HELIX   33  33 SER C   51  ASP C   54  5                                   4    
HELIX   34  34 GLN C   66  GLY C   78  1                                  13    
HELIX   35  35 SER C   81  ALA C   94  1                                  14    
HELIX   36  36 PRO C  109  PHE C  120  1                                  12    
HELIX   37  37 THR C  127  MET C  131  5                                   5    
HELIX   38  38 MET C  131  GLY C  135  5                                   5    
HELIX   39  39 SER C  151  SER C  156  5                                   6    
HELIX   40  40 ASP C  163  SER C  173  1                                  11    
HELIX   41  41 LEU C  176  GLY C  180  5                                   5    
HELIX   42  42 SER C  191  THR C  195  5                                   5    
HELIX   43  43 PRO C  196  GLU C  212  1                                  17    
HELIX   44  44 ASN C  213  GLU C  217  5                                   5    
HELIX   45  45 PRO C  224  LEU C  227  5                                   4    
HELIX   46  46 LYS C  239  LYS C  247  1                                   9    
HELIX   47  47 SER D   16  LYS D   32  1                                  17    
HELIX   48  48 SER D   51  ASP D   54  5                                   4    
HELIX   49  49 ASP D   61  PHE D   65  5                                   5    
HELIX   50  50 GLN D   66  GLY D   78  1                                  13    
HELIX   51  51 SER D   81  ALA D   94  1                                  14    
HELIX   52  52 PRO D  109  PHE D  120  1                                  12    
HELIX   53  53 MET D  131  GLY D  135  5                                   5    
HELIX   54  54 SER D  151  SER D  156  5                                   6    
HELIX   55  55 ASP D  163  SER D  173  1                                  11    
HELIX   56  56 LEU D  176  GLY D  180  5                                   5    
HELIX   57  57 SER D  191  THR D  195  5                                   5    
HELIX   58  58 PRO D  196  GLU D  212  1                                  17    
HELIX   59  59 ASN D  213  GLU D  217  5                                   5    
HELIX   60  60 PRO D  224  LEU D  227  5                                   4    
HELIX   61  61 LYS D  239  LYS D  247  1                                   9    
SHEET    1  AA 5 GLU A  35  ASP A  40  0                                        
SHEET    2  AA 5 ARG A   4  LEU A   9  1  O  ALA A   5   N  VAL A  37           
SHEET    3  AA 5 LEU A  96  PRO A 102  1  O  LEU A  96   N  LEU A   6           
SHEET    4  AA 5 LYS A 141  THR A 147  1  O  LYS A 141   N  VAL A  97           
SHEET    5  AA 5 GLN A 187  THR A 189 -1  O  GLN A 187   N  ILE A 146           
SHEET    1  AB 5 GLU A  35  ASP A  40  0                                        
SHEET    2  AB 5 ARG A   4  LEU A   9  1  O  ALA A   5   N  VAL A  37           
SHEET    3  AB 5 LEU A  96  PRO A 102  1  O  LEU A  96   N  LEU A   6           
SHEET    4  AB 5 LYS A 141  THR A 147  1  O  LYS A 141   N  VAL A  97           
SHEET    5  AB 5 GLN A 182  VAL A 183  1  O  GLN A 182   N  ALA A 142           
SHEET    1  AC 2 GLN A 187  THR A 189  0                                        
SHEET    2  AC 2 LYS A 141  THR A 147 -1  O  LEU A 144   N  GLN A 187           
SHEET    1  BA 5 GLU B  35  ASP B  40  0                                        
SHEET    2  BA 5 ARG B   4  LEU B   9  1  O  ALA B   5   N  VAL B  37           
SHEET    3  BA 5 LEU B  96  PRO B 102  1  O  LEU B  96   N  LEU B   6           
SHEET    4  BA 5 LYS B 141  THR B 147  1  O  LYS B 141   N  VAL B  97           
SHEET    5  BA 5 GLN B 187  THR B 189 -1  O  GLN B 187   N  ILE B 146           
SHEET    1  BB 5 GLU B  35  ASP B  40  0                                        
SHEET    2  BB 5 ARG B   4  LEU B   9  1  O  ALA B   5   N  VAL B  37           
SHEET    3  BB 5 LEU B  96  PRO B 102  1  O  LEU B  96   N  LEU B   6           
SHEET    4  BB 5 LYS B 141  THR B 147  1  O  LYS B 141   N  VAL B  97           
SHEET    5  BB 5 GLN B 182  VAL B 183  1  O  GLN B 182   N  ALA B 142           
SHEET    1  BC 2 GLN B 187  THR B 189  0                                        
SHEET    2  BC 2 LYS B 141  THR B 147 -1  O  LEU B 144   N  GLN B 187           
SHEET    1  CA 5 GLU C  35  ASP C  40  0                                        
SHEET    2  CA 5 ARG C   4  LEU C   9  1  O  ALA C   5   N  VAL C  37           
SHEET    3  CA 5 LEU C  96  PRO C 102  1  O  LEU C  96   N  LEU C   6           
SHEET    4  CA 5 LYS C 141  THR C 147  1  O  LYS C 141   N  VAL C  97           
SHEET    5  CA 5 GLN C 187  THR C 189 -1  O  GLN C 187   N  ILE C 146           
SHEET    1  CB 5 GLU C  35  ASP C  40  0                                        
SHEET    2  CB 5 ARG C   4  LEU C   9  1  O  ALA C   5   N  VAL C  37           
SHEET    3  CB 5 LEU C  96  PRO C 102  1  O  LEU C  96   N  LEU C   6           
SHEET    4  CB 5 LYS C 141  THR C 147  1  O  LYS C 141   N  VAL C  97           
SHEET    5  CB 5 GLN C 182  VAL C 183  1  O  GLN C 182   N  ALA C 142           
SHEET    1  CC 2 GLN C 187  THR C 189  0                                        
SHEET    2  CC 2 LYS C 141  THR C 147 -1  O  LEU C 144   N  GLN C 187           
SHEET    1  DA 5 GLU D  35  ASP D  40  0                                        
SHEET    2  DA 5 ARG D   4  LEU D   9  1  O  ALA D   5   N  VAL D  37           
SHEET    3  DA 5 LEU D  96  PRO D 102  1  O  LEU D  96   N  LEU D   6           
SHEET    4  DA 5 LYS D 141  THR D 147  1  O  LYS D 141   N  VAL D  97           
SHEET    5  DA 5 GLN D 187  THR D 189 -1  O  GLN D 187   N  ILE D 146           
SHEET    1  DB 5 GLU D  35  ASP D  40  0                                        
SHEET    2  DB 5 ARG D   4  LEU D   9  1  O  ALA D   5   N  VAL D  37           
SHEET    3  DB 5 LEU D  96  PRO D 102  1  O  LEU D  96   N  LEU D   6           
SHEET    4  DB 5 LYS D 141  THR D 147  1  O  LYS D 141   N  VAL D  97           
SHEET    5  DB 5 GLN D 182  VAL D 183  1  O  GLN D 182   N  ALA D 142           
SHEET    1  DC 2 GLN D 187  THR D 189  0                                        
SHEET    2  DC 2 LYS D 141  THR D 147 -1  O  LEU D 144   N  GLN D 187           
SITE     1 AC1 25 HIS A  11  THR A  15  SER A  16  PHE A  17                    
SITE     2 AC1 25 ASN A  18  ALA A  20  PRO A 102  LEU A 103                    
SITE     3 AC1 25 GLN A 104  TRP A 105  PHE A 106  THR A 147                    
SITE     4 AC1 25 THR A 148  GLY A 149  GLY A 150  TYR A 155                    
SITE     5 AC1 25 ILE A 192  ARG A 200  LEU A 204  DQN A 302                    
SITE     6 AC1 25 HOH A2021  HOH A2022  GLN C  66  TYR C  67                    
SITE     7 AC1 25 PRO C  68                                                     
SITE     1 AC2 23 HIS B  11  THR B  15  SER B  16  PHE B  17                    
SITE     2 AC2 23 ASN B  18  ALA B  20  PRO B 102  LEU B 103                    
SITE     3 AC2 23 GLN B 104  TRP B 105  PHE B 106  THR B 147                    
SITE     4 AC2 23 THR B 148  GLY B 149  GLY B 150  TYR B 155                    
SITE     5 AC2 23 ILE B 192  ARG B 200  LEU B 204  DQN B 302                    
SITE     6 AC2 23 ASN D  64  GLN D  66  TYR D  67                               
SITE     1 AC3 22 GLN A  66  TYR A  67  HIS C  11  THR C  15                    
SITE     2 AC3 22 SER C  16  PHE C  17  ASN C  18  ALA C  20                    
SITE     3 AC3 22 PRO C 102  LEU C 103  GLN C 104  TRP C 105                    
SITE     4 AC3 22 PHE C 106  THR C 147  THR C 148  GLY C 149                    
SITE     5 AC3 22 GLY C 150  TYR C 155  ILE C 192  ARG C 200                    
SITE     6 AC3 22 LEU C 204  DQN C 302                                          
SITE     1 AC4 22 GLN B  66  TYR B  67  PRO B  68  HIS D  11                    
SITE     2 AC4 22 THR D  15  SER D  16  PHE D  17  ASN D  18                    
SITE     3 AC4 22 ALA D  20  PRO D 102  LEU D 103  GLN D 104                    
SITE     4 AC4 22 TRP D 105  PHE D 106  THR D 147  THR D 148                    
SITE     5 AC4 22 GLY D 149  GLY D 150  TYR D 155  ILE D 192                    
SITE     6 AC4 22 ARG D 200  LEU D 204                                          
SITE     1 AC5  7 TRP A 105  GLY A 149  FAD A 301  TYR C 126                    
SITE     2 AC5  7 TYR C 128  PHE C 178  HOH C2017                               
SITE     1 AC6  8 FAD B 301  HOH B2020  GLY D 122  TYR D 126                    
SITE     2 AC6  8 PHE D 178  DQN D 302  HOH D2007  HOH D2011                    
SITE     1 AC7  7 TYR A 126  TYR A 128  PHE A 178  HOH A2014                    
SITE     2 AC7  7 TRP C 105  FAD C 301  HOH C2023                               
SITE     1 AC8  4 GLY B 149  HIS B 194  DQN B 302  PHE D 232                    
CRYST1   55.579   56.912   97.755  76.24  76.73  86.33 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017992 -0.001154 -0.004087        0.00000                         
SCALE2      0.000000  0.017607 -0.004156        0.00000                         
SCALE3      0.000000  0.000000  0.010799        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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