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Database: PDB
Entry: 4CET
LinkDB: 4CET
Original site: 4CET 
HEADER    OXIDOREDUCTASE                          12-NOV-13   4CET              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF THE P187S VARIANT OF              
TITLE    2 HUMAN NAD(P)H:QUINONE OXIDOREDUCTASE WITH DICOUMAROL AT 2.           
TITLE    3 2 A RESOLUTION                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD(P)H DEHYDROGENASE [QUINONE] 1;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AZOREDUCTASE, DT-DIAPHORASE, DTD, MENADIONE REDUCTASE,      
COMPND   5  NAD(P)H\:QUINONE OXIDOREDUCTASE 1, PHYLLOQUINONE REDUCTASE,         
COMPND   6  QUINONE 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: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    COUMARIN-BASED INHIBITORS, NQ01, FAD, FLAVOPROTEIN, NAD, NADP,        
KEYWDS   2 NADPH, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR COMPLEX, SINGLE      
KEYWDS   3 AMINO ACID EXCHANGE, P187S                                           
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   3   29-OCT-14 4CET    1       JRNL                                     
REVDAT   2   17-SEP-14 4CET    1       JRNL                                     
REVDAT   1   27-AUG-14 4CET    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.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.200                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.197                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.77                          
REMARK   3   NUMBER OF REFLECTIONS             : 12065                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1780                          
REMARK   3   R VALUE            (WORKING SET) : 0.1755                          
REMARK   3   FREE R VALUE                     : 0.2239                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.8                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 576                             
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 33.2006 -  3.4917    1.00     3056   149  0.1445 0.1785        
REMARK   3     2  3.4917 -  2.7719    1.00     2853   149  0.1856 0.2434        
REMARK   3     3  2.7719 -  2.4216    1.00     2805   134  0.2070 0.2597        
REMARK   3     4  2.4216 -  2.2003    0.99     2775   144  0.2292 0.2955        
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)     : 0.13             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.24            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.2                           
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: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           1926                                  
REMARK   3   ANGLE     :  0.895           2626                                  
REMARK   3   CHIRALITY :  0.060            273                                  
REMARK   3   PLANARITY :  0.004            326                                  
REMARK   3   DIHEDRAL  : 15.626            699                                  
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: NO ELECTRON DENSITY WAS OBSERVED FOR      
REMARK   3  THE FIRST 2 AND THE LAST 51 RESIDUES (MISSING C-TERMINAL REGION).   
REMARK   4                                                                      
REMARK   4 4CET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58923.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1354                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12127                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.2                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.9                               
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.66                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.20                               
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 1QBG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 26.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  0.005 M CO(II)CL-HEXAHYDRATE, 0.005 M NI(II)CL-HEXAHYDRATE,         
REMARK 280   0.005 M CDCL-HYDRATE, 0.005 M MGCL-HEAXHYDRATE, 0.1 M              
REMARK 280  HEPES PH 7.5, 12 % PEG-3350 (W/V)                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       84.52000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       25.52500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       25.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       42.26000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       25.52500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       25.52500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      126.78000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       25.52500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       25.52500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       42.26000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       25.52500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       25.52500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      126.78000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       84.52000            
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: 7400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     PRO A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     LEU A   228                                                      
REMARK 465     PHE A   229                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     ASN A   232                                                      
REMARK 465     PHE A   233                                                      
REMARK 465     GLN A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     PHE A   237                                                      
REMARK 465     LEU A   238                                                      
REMARK 465     MET A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     LYS A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     VAL A   243                                                      
REMARK 465     GLN A   244                                                      
REMARK 465     ASP A   245                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     ASN A   249                                                      
REMARK 465     LYS A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     PHE A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     VAL A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     LEU A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     ILE A   264                                                      
REMARK 465     PRO A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     ASN A   268                                                      
REMARK 465     GLN A   269                                                      
REMARK 465     ILE A   270                                                      
REMARK 465     LYS A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     ARG A   273                                                      
REMARK 465     LYS A   274                                                      
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   OE1  GLU A    78     O    HOH A  2049              2.18            
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    GLU A 124      -43.23     67.50                                   
REMARK 500    TYR A 133     -124.87     53.94                                   
REMARK 500    TYR A 156       52.76    -95.71                                   
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 A1225                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTC A1226                 
DBREF  4CET A    1   274  UNP    P15559   NQO1_HUMAN       1    274             
SEQADV 4CET MET A  -19  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET GLY A  -18  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A  -17  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A  -16  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -15  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -14  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -13  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -12  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -11  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A  -10  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A   -9  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A   -8  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET GLY A   -7  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET LEU A   -6  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET VAL A   -5  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET PRO A   -4  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET ARG A   -3  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET GLY A   -2  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A   -1  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET HIS A    0  UNP  P15559              EXPRESSION TAG                 
SEQADV 4CET SER A  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                              
HET    FAD  A1225      53                                                       
HET    DTC  A1226      25                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     DTC BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-                            
HETNAM   2 DTC  BENZOPYRONE]                                                    
HETSYN     DTC DICOUMAROL                                                       
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  DTC    C19 H12 O6                                                   
FORMUL   4  HOH   *139(H2 O)                                                    
HELIX    1   1 SER A   17  LYS A   33  1                                  17    
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  LEU A  169  1                                   6    
HELIX    8   8 LEU A  169  SER A  174  1                                   6    
HELIX    9   9 GLY A  175  PHE A  179  1                                   5    
HELIX   10  10 SER A  192  THR A  196  5                                   5    
HELIX   11  11 PRO A  197  GLU A  213  1                                  17    
HELIX   12  12 ASN A  214  GLU A  218  5                                   5    
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           
SITE     1 AC1 31 HIS A  12  THR A  16  SER A  17  PHE A  18                    
SITE     2 AC1 31 ASN A  19  ALA A  21  GLN A  67  PRO A 103                    
SITE     3 AC1 31 LEU A 104  GLN A 105  TRP A 106  PHE A 107                    
SITE     4 AC1 31 THR A 148  THR A 149  GLY A 150  GLY A 151                    
SITE     5 AC1 31 TYR A 156  ILE A 193  ARG A 201  LEU A 205                    
SITE     6 AC1 31 DTC A1226  HOH A2008  HOH A2013  HOH A2014                    
SITE     7 AC1 31 HOH A2131  HOH A2132  HOH A2133  HOH A2135                    
SITE     8 AC1 31 HOH A2136  HOH A2137  HOH A2138                               
SITE     1 AC2 14 LYS A  90  TRP A 106  TYR A 127  TYR A 129                    
SITE     2 AC2 14 GLY A 150  GLY A 151  MET A 155  TYR A 156                    
SITE     3 AC2 14 ILE A 161  HIS A 162  PHE A 179  FAD A1225                    
SITE     4 AC2 14 HOH A2118  HOH A2139                                          
CRYST1   51.050   51.050  169.040  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019589  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019589  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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