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Database: PDB
Entry: 4CF6
LinkDB: 4CF6
Original site: 4CF6 
HEADER    OXIDOREDUCTASE                          13-NOV-13   4CF6              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF THE P187S VARIANT OF HUMAN NAD(P) 
TITLE    2 H:QUINONE OXIDOREDUCTASE WITH CIBACRON BLUE AT 2.7 A RESOLUTION      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD(P)H DEHYDROGENASE [QUINONE] 1;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: AZOREDUCTASE, DT-DIAPHORASE, DTD, MENADIONE REDUCTASE,      
COMPND   5 NAD(P)H\:QUINONE OXIDOREDUCTASE 1, PHYLLOQUINONE REDUCTASE, QUINONE  
COMPND   6 REDUCTASE 1, QR1, NADPH QUINONE OXIDOREDUCTASE;                      
COMPND   7 EC: 1.6.5.2;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: 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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    FLAVOPROTEIN, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR COMPLEX,       
KEYWDS   2 SINGLE AMINO ACID EXCHANGE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.D.LIENHART,V.GUDIPATI,M.K.UHL,A.BINTER,S.PULIDO,R.SAF,K.ZANGGER,    
AUTHOR   2 K.GRUBER,P.MACHEROUX                                                 
REVDAT   4   27-SEP-17 4CF6    1       REMARK                                   
REVDAT   3   29-OCT-14 4CF6    1       JRNL                                     
REVDAT   2   03-SEP-14 4CF6    1       JRNL                                     
REVDAT   1   27-AUG-14 4CF6    0                                                
JRNL        AUTH   W.D.LIENHART,V.GUDIPATI,M.K.UHL,A.BINTER,S.PULIDO,R.SAF,     
JRNL        AUTH 2 K.ZANGGER,K.GRUBER,P.MACHEROUX                               
JRNL        TITL   COLLAPSE OF THE NATIVE STRUCTURE BY A SINGLE AMINO ACID      
JRNL        TITL 2 EXCHANGE IN HUMAN NAD(P)H:QUINONE OXIDOREDUCTASE (NQO1).     
JRNL        REF    FEBS J.                       V. 281  4691 2014              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   25143260                                                     
JRNL        DOI    10.1111/FEBS.12975                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18137                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 937                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 21.7369 -  5.1344    0.95     2602   127  0.1451 0.1485        
REMARK   3     2  5.1344 -  4.0842    0.95     2470   136  0.1440 0.1568        
REMARK   3     3  4.0842 -  3.5705    0.94     2447   139  0.1808 0.2161        
REMARK   3     4  3.5705 -  3.2452    0.95     2442   133  0.2066 0.2448        
REMARK   3     5  3.2452 -  3.0133    0.95     2448   131  0.2412 0.2567        
REMARK   3     6  3.0133 -  2.8360    0.95     2426   136  0.2889 0.3527        
REMARK   3     7  2.8360 -  2.6943    0.93     2332   126  0.3102 0.3448        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.3900                                                   
REMARK   3   OPERATOR: -K,-H,-L                                                 
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4658                                  
REMARK   3   ANGLE     :  0.719           6335                                  
REMARK   3   CHIRALITY :  0.027            647                                  
REMARK   3   PLANARITY :  0.003            776                                  
REMARK   3   DIHEDRAL  : 16.989           1676                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4CF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058949.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18149                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4CET                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 60%        
REMARK 280  TACSIMATE PH=7.0, PH 7.0                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       52.08350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.28150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.28300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.08350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.28150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       59.28300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.08350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.28150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       59.28300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.08350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.28150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       59.28300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     LYS A   274                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLY B     3                                                      
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   O    GLU B   247     NZ   LYS B   262              2.15            
REMARK 500   OG   SER B   154     O3D  CBD B  1276              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   251     OG   SER B   263     2555     2.04            
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  11       74.13   -107.84                                   
REMARK 500    SER A  40       65.85   -154.27                                   
REMARK 500    ALA A  64      -74.85    -73.84                                   
REMARK 500    GLU A 124      -35.12     71.06                                   
REMARK 500    ALA A 131       71.93   -156.25                                   
REMARK 500    TYR A 133     -101.15     59.02                                   
REMARK 500    PHE A 138       47.45   -101.76                                   
REMARK 500    SER A 140       43.57    -82.30                                   
REMARK 500    PRO A 171        5.30    -69.37                                   
REMARK 500    ASN A 214       48.19   -141.02                                   
REMARK 500    HIS A 258       53.04   -100.30                                   
REMARK 500    LYS A 262     -166.87   -127.31                                   
REMARK 500    ASP B  62       88.65   -155.68                                   
REMARK 500    GLU B 124      -29.21     70.82                                   
REMARK 500    PHE B 125      -66.18    -94.02                                   
REMARK 500    TYR B 133     -113.79     55.28                                   
REMARK 500    PHE B 138       43.54   -100.38                                   
REMARK 500    GLU B 247       37.08    -99.38                                   
REMARK 500    SER B 255     -159.65   -161.61                                   
REMARK 500    LYS B 262     -161.99   -110.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 1274                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1275                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBD A 1275                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBD B 1276                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CET   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF THE P187S VARIANT OF HUMAN       
REMARK 900 NAD(P)H:QUINONE OXIDOREDUCTASE WITH DICOUMAROL AT 2.2 A RESOLUTION   
DBREF  4CF6 A    1   274  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  4CF6 B    1   274  UNP    P15559   NQO1_HUMAN       1    274             
SEQADV 4CF6 MET A  -19  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY A  -18  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A  -17  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A  -16  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -15  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -14  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -13  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -12  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -11  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A  -10  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A   -9  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A   -8  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY A   -7  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 LEU A   -6  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 VAL A   -5  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 PRO A   -4  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 ARG A   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY A   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS A    0  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER A  187  UNP  P15559    PRO   187 ENGINEERED MUTATION            
SEQADV 4CF6 MET B  -19  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY B  -18  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B  -17  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B  -16  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -15  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -14  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -13  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -12  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -11  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B  -10  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B   -9  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B   -8  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY B   -7  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 LEU B   -6  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 VAL B   -5  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 PRO B   -4  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 ARG B   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 GLY B   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 HIS B    0  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CF6 SER B  187  UNP  P15559    PRO   187 ENGINEERED MUTATION            
SEQRES   1 A  294  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  294  LEU VAL PRO ARG GLY SER HIS MET VAL GLY ARG ARG ALA          
SEQRES   3 A  294  LEU ILE VAL LEU ALA HIS SER GLU ARG THR SER PHE ASN          
SEQRES   4 A  294  TYR ALA MET LYS GLU ALA ALA ALA ALA ALA LEU LYS LYS          
SEQRES   5 A  294  LYS GLY TRP GLU VAL VAL GLU SER ASP LEU TYR ALA MET          
SEQRES   6 A  294  ASN PHE ASN PRO ILE ILE SER ARG LYS ASP ILE THR GLY          
SEQRES   7 A  294  LYS LEU LYS ASP PRO ALA ASN PHE GLN TYR PRO ALA GLU          
SEQRES   8 A  294  SER VAL LEU ALA TYR LYS GLU GLY HIS LEU SER PRO ASP          
SEQRES   9 A  294  ILE VAL ALA GLU GLN LYS LYS LEU GLU ALA ALA ASP LEU          
SEQRES  10 A  294  VAL ILE PHE GLN PHE PRO LEU GLN TRP PHE GLY VAL PRO          
SEQRES  11 A  294  ALA ILE LEU LYS GLY TRP PHE GLU ARG VAL PHE ILE GLY          
SEQRES  12 A  294  GLU PHE ALA TYR THR TYR ALA ALA MET TYR ASP LYS GLY          
SEQRES  13 A  294  PRO PHE ARG SER LYS LYS ALA VAL LEU SER ILE THR THR          
SEQRES  14 A  294  GLY GLY SER GLY SER MET TYR SER LEU GLN GLY ILE HIS          
SEQRES  15 A  294  GLY ASP MET ASN VAL ILE LEU TRP PRO ILE GLN SER GLY          
SEQRES  16 A  294  ILE LEU HIS PHE CYS GLY PHE GLN VAL LEU GLU SER GLN          
SEQRES  17 A  294  LEU THR TYR SER ILE GLY HIS THR PRO ALA ASP ALA ARG          
SEQRES  18 A  294  ILE GLN ILE LEU GLU GLY TRP LYS LYS ARG LEU GLU ASN          
SEQRES  19 A  294  ILE TRP ASP GLU THR PRO LEU TYR PHE ALA PRO SER SER          
SEQRES  20 A  294  LEU PHE ASP LEU ASN PHE GLN ALA GLY PHE LEU MET LYS          
SEQRES  21 A  294  LYS GLU VAL GLN ASP GLU GLU LYS ASN LYS LYS PHE GLY          
SEQRES  22 A  294  LEU SER VAL GLY HIS HIS LEU GLY LYS SER ILE PRO THR          
SEQRES  23 A  294  ASP ASN GLN ILE LYS ALA ARG LYS                              
SEQRES   1 B  294  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  294  LEU VAL PRO ARG GLY SER HIS MET VAL GLY ARG ARG ALA          
SEQRES   3 B  294  LEU ILE VAL LEU ALA HIS SER GLU ARG THR SER PHE ASN          
SEQRES   4 B  294  TYR ALA MET LYS GLU ALA ALA ALA ALA ALA LEU LYS LYS          
SEQRES   5 B  294  LYS GLY TRP GLU VAL VAL GLU SER ASP LEU TYR ALA MET          
SEQRES   6 B  294  ASN PHE ASN PRO ILE ILE SER ARG LYS ASP ILE THR GLY          
SEQRES   7 B  294  LYS LEU LYS ASP PRO ALA ASN PHE GLN TYR PRO ALA GLU          
SEQRES   8 B  294  SER VAL LEU ALA TYR LYS GLU GLY HIS LEU SER PRO ASP          
SEQRES   9 B  294  ILE VAL ALA GLU GLN LYS LYS LEU GLU ALA ALA ASP LEU          
SEQRES  10 B  294  VAL ILE PHE GLN PHE PRO LEU GLN TRP PHE GLY VAL PRO          
SEQRES  11 B  294  ALA ILE LEU LYS GLY TRP PHE GLU ARG VAL PHE ILE GLY          
SEQRES  12 B  294  GLU PHE ALA TYR THR TYR ALA ALA MET TYR ASP LYS GLY          
SEQRES  13 B  294  PRO PHE ARG SER LYS LYS ALA VAL LEU SER ILE THR THR          
SEQRES  14 B  294  GLY GLY SER GLY SER MET TYR SER LEU GLN GLY ILE HIS          
SEQRES  15 B  294  GLY ASP MET ASN VAL ILE LEU TRP PRO ILE GLN SER GLY          
SEQRES  16 B  294  ILE LEU HIS PHE CYS GLY PHE GLN VAL LEU GLU SER GLN          
SEQRES  17 B  294  LEU THR TYR SER ILE GLY HIS THR PRO ALA ASP ALA ARG          
SEQRES  18 B  294  ILE GLN ILE LEU GLU GLY TRP LYS LYS ARG LEU GLU ASN          
SEQRES  19 B  294  ILE TRP ASP GLU THR PRO LEU TYR PHE ALA PRO SER SER          
SEQRES  20 B  294  LEU PHE ASP LEU ASN PHE GLN ALA GLY PHE LEU MET LYS          
SEQRES  21 B  294  LYS GLU VAL GLN ASP GLU GLU LYS ASN LYS LYS PHE GLY          
SEQRES  22 B  294  LEU SER VAL GLY HIS HIS LEU GLY LYS SER ILE PRO THR          
SEQRES  23 B  294  ASP ASN GLN ILE LYS ALA ARG LYS                              
HET    FAD  A1274      53                                                       
HET    CBD  A1275      51                                                       
HET    FAD  B1275      53                                                       
HET    CBD  B1276      51                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     CBD CIBACRON BLUE                                                    
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  CBD    2(C29 H20 CL N7 O11 S3)                                      
FORMUL   7  HOH   *7(H2 O)                                                      
HELIX    1   1 SER A   17  LYS A   32  1                                  16    
HELIX    2   2 SER A   52  ASP A   55  5                                   4    
HELIX    3   3 GLN A   67  GLY A   79  1                                  13    
HELIX    4   4 SER A   82  ALA A   95  1                                  14    
HELIX    5   5 PRO A  110  PHE A  121  1                                  12    
HELIX    6   6 MET A  132  GLY A  136  5                                   5    
HELIX    7   7 ASP A  164  SER A  174  1                                  11    
HELIX    8   8 LEU A  177  GLY A  181  5                                   5    
HELIX    9   9 SER A  192  THR A  196  5                                   5    
HELIX   10  10 PRO A  197  LEU A  212  1                                  16    
HELIX   11  11 PRO A  225  LEU A  228  5                                   4    
HELIX   12  12 LYS A  240  ASP A  245  1                                   6    
HELIX   13  13 SER B   17  LYS B   33  1                                  17    
HELIX   14  14 SER B   52  ASP B   55  5                                   4    
HELIX   15  15 GLN B   67  GLY B   79  1                                  13    
HELIX   16  16 SER B   82  ALA B   95  1                                  14    
HELIX   17  17 PRO B  110  PHE B  121  1                                  12    
HELIX   18  18 MET B  132  GLY B  136  5                                   5    
HELIX   19  19 ASP B  164  SER B  174  1                                  11    
HELIX   20  20 LEU B  177  GLY B  181  5                                   5    
HELIX   21  21 PRO B  197  LEU B  212  1                                  16    
HELIX   22  22 GLU B  213  ILE B  215  5                                   3    
HELIX   23  23 PRO B  225  LEU B  228  5                                   4    
HELIX   24  24 LYS B  240  ASP B  245  1                                   6    
SHEET    1  AA 5 GLU A  36  ASP A  41  0                                        
SHEET    2  AA 5 ARG A   5  LEU A  10  1  O  ALA A   6   N  VAL A  38           
SHEET    3  AA 5 LEU A  97  PRO A 103  1  O  LEU A  97   N  LEU A   7           
SHEET    4  AA 5 LYS A 142  THR A 148  1  O  LYS A 142   N  VAL A  98           
SHEET    5  AA 5 GLN A 188  THR A 190 -1  O  GLN A 188   N  ILE A 147           
SHEET    1  AB 5 GLU A  36  ASP A  41  0                                        
SHEET    2  AB 5 ARG A   5  LEU A  10  1  O  ALA A   6   N  VAL A  38           
SHEET    3  AB 5 LEU A  97  PRO A 103  1  O  LEU A  97   N  LEU A   7           
SHEET    4  AB 5 LYS A 142  THR A 148  1  O  LYS A 142   N  VAL A  98           
SHEET    5  AB 5 GLN A 183  VAL A 184  1  O  GLN A 183   N  ALA A 143           
SHEET    1  AC 2 GLN A 188  THR A 190  0                                        
SHEET    2  AC 2 LYS A 142  THR A 148 -1  O  LEU A 145   N  GLN A 188           
SHEET    1  BA 5 GLU B  36  GLU B  39  0                                        
SHEET    2  BA 5 ARG B   5  LEU B  10  1  O  ALA B   6   N  VAL B  38           
SHEET    3  BA 5 LEU B  97  PRO B 103  1  O  LEU B  97   N  LEU B   7           
SHEET    4  BA 5 LYS B 142  THR B 148  1  O  LYS B 142   N  VAL B  98           
SHEET    5  BA 5 GLN B 188  THR B 190 -1  O  GLN B 188   N  ILE B 147           
SHEET    1  BB 5 GLU B  36  GLU B  39  0                                        
SHEET    2  BB 5 ARG B   5  LEU B  10  1  O  ALA B   6   N  VAL B  38           
SHEET    3  BB 5 LEU B  97  PRO B 103  1  O  LEU B  97   N  LEU B   7           
SHEET    4  BB 5 LYS B 142  THR B 148  1  O  LYS B 142   N  VAL B  98           
SHEET    5  BB 5 GLN B 183  VAL B 184  1  O  GLN B 183   N  ALA B 143           
SHEET    1  BC 2 GLN B 188  THR B 190  0                                        
SHEET    2  BC 2 LYS B 142  THR B 148 -1  O  LEU B 145   N  GLN B 188           
SITE     1 AC1 23 HIS A  12  THR A  16  SER A  17  PHE A  18                    
SITE     2 AC1 23 ASN A  19  ALA A  21  PRO A 103  LEU A 104                    
SITE     3 AC1 23 GLN A 105  TRP A 106  PHE A 107  THR A 148                    
SITE     4 AC1 23 THR A 149  GLY A 150  GLY A 151  TYR A 156                    
SITE     5 AC1 23 ILE A 193  ARG A 201  CBD A1275  GLN B  67                    
SITE     6 AC1 23 TYR B  68  PRO B  69  GLU B 118                               
SITE     1 AC2 22 GLN A  67  TYR A  68  PRO A  69  HOH A2002                    
SITE     2 AC2 22 HIS B  12  SER B  17  PHE B  18  ASN B  19                    
SITE     3 AC2 22 ALA B  21  PRO B 103  LEU B 104  GLN B 105                    
SITE     4 AC2 22 TRP B 106  PHE B 107  THR B 148  THR B 149                    
SITE     5 AC2 22 GLY B 150  GLY B 151  TYR B 156  ILE B 193                    
SITE     6 AC2 22 ARG B 201  CBD B1276                                          
SITE     1 AC3 16 GLY A 150  GLY A 151  MET A 155  SER A 192                    
SITE     2 AC3 16 GLY A 194  HIS A 195  PHE A 233  GLN A 234                    
SITE     3 AC3 16 FAD A1274  PRO B  69  TYR B 127  TYR B 129                    
SITE     4 AC3 16 PHE B 179  HIS B 195  PHE B 233  CBD B1276                    
SITE     1 AC4 19 PRO A  69  TYR A 129  PHE A 179  HIS A 195                    
SITE     2 AC4 19 THR A 196  PRO A 197  PHE A 233  GLY A 236                    
SITE     3 AC4 19 PHE A 237  CBD A1275  GLY B 150  SER B 152                    
SITE     4 AC4 19 SER B 154  MET B 155  HIS B 162  SER B 192                    
SITE     5 AC4 19 HIS B 195  GLN B 234  FAD B1275                               
CRYST1  104.167  104.563  118.566  90.00  90.00  90.00 I 2 2 2      16          
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      0.009600  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009564  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008434        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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