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Database: PDB
Entry: 5FUQ
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HEADER    OXIDOREDUCTASE                          29-JAN-16   5FUQ              
TITLE     CRYSTAL STRUCTURE OF THE H80R VARIANT OF NQO1 BOUND TO DICOUMAROL     
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  NADPH, QUINONE OXIDOREDUCTASE 1, PHYLLOQUINONE REDUCTASE, QUINONE   
COMPND   6  REDUCTASE 1, QR1, NADPH DEHYDROGENASE QUINONE 1;                    
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_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET46 EK/LIC                              
KEYWDS    OXIDOREDUCTASE, NADPH-QUINONE OXIDOREDUCTASE 1, NQO1, FAD, DICOUMAROL 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.GAVIRA,E.MEDINA-CARMONA,A.L.PEY                                   
REVDAT   1   22-FEB-17 5FUQ    0                                                
JRNL        AUTH   E.MEDINA-CARMONA,J.E.FUCHS,J.A.GAVIRA,E.SALIDO,              
JRNL        AUTH 2 R.PALOMINO-MORALES,N.MESA-TORRES,D.J.TIMSON,A.L.PEY          
JRNL        TITL   IDENTIFICATION OF NOVEL STRUCTURAL HOT-SPOTS FOR THE         
JRNL        TITL 2 CORRECTION OF FUNCTIONAL AND STABILITY DEFECTS IN A          
JRNL        TITL 3 CANCER-ASSOCIATED POLYMORPHIC NADPH:QUINONE OXIDOREDUCTASE   
JRNL        TITL 4 1 FROM SEQUENCE-ALIGNMENT STATISTICS.                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 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) : 2.040                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.828                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.96                          
REMARK   3   NUMBER OF REFLECTIONS             : 72272                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1598                          
REMARK   3   R VALUE            (WORKING SET) : 0.1589                          
REMARK   3   FREE R VALUE                     : 0.1768                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3646                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWOR 
REMARK   3     1 49.8427 -  6.0401    1.00     2907   146  0.1561 0.1459   0.94 
REMARK   3     2  6.0401 -  4.7955    1.00     2746   133  0.1359 0.1519   0.95 
REMARK   3     3  4.7955 -  4.1896    1.00     2708   138  0.1114 0.1263   0.96 
REMARK   3     4  4.1896 -  3.8067    1.00     2696   147  0.1328 0.1281   0.95 
REMARK   3     5  3.8067 -  3.5340    1.00     2649   153  0.1431 0.1660   0.94 
REMARK   3     6  3.5340 -  3.3256    1.00     2656   149  0.1543 0.1958   0.93 
REMARK   3     7  3.3256 -  3.1591    1.00     2617   154  0.1668 0.1893   0.92 
REMARK   3     8  3.1591 -  3.0216    1.00     2662   131  0.1771 0.1883   0.90 
REMARK   3     9  3.0216 -  2.9053    1.00     2633   148  0.1703 0.1945   0.91 
REMARK   3    10  2.9053 -  2.8051    1.00     2624   148  0.1713 0.2009   0.91 
REMARK   3    11  2.8051 -  2.7174    1.00     2622   147  0.1680 0.2108   0.92 
REMARK   3    12  2.7174 -  2.6397    1.00     2626   123  0.1714 0.2106   0.91 
REMARK   3    13  2.6397 -  2.5702    1.00     2637   136  0.1777 0.1807   0.90 
REMARK   3    14  2.5702 -  2.5075    1.00     2593   145  0.1592 0.1934   0.92 
REMARK   3    15  2.5075 -  2.4505    1.00     2613   153  0.1712 0.2046   0.92 
REMARK   3    16  2.4505 -  2.3984    1.00     2590   141  0.1716 0.2108   0.91 
REMARK   3    17  2.3984 -  2.3504    1.00     2637   116  0.1819 0.1963   0.90 
REMARK   3    18  2.3504 -  2.3060    1.00     2638   125  0.1957 0.2279   0.89 
REMARK   3    19  2.3060 -  2.2648    1.00     2609   149  0.1969 0.2162   0.88 
REMARK   3    20  2.2648 -  2.2264    1.00     2574   138  0.2060 0.2436   0.87 
REMARK   3    21  2.2264 -  2.1905    1.00     2597   140  0.2178 0.2436   0.86 
REMARK   3    22  2.1905 -  2.1568    1.00     2612   145  0.2220 0.2457   0.84 
REMARK   3    23  2.1568 -  2.1251    1.00     2581   136  0.2367 0.2566   0.82 
REMARK   3    24  2.1251 -  2.0952    1.00     2603   138  0.2656 0.3026   0.78 
REMARK   3    25  2.0952 -  2.0669    1.00     2593   142  0.2869 0.3074   0.73 
REMARK   3    26  2.0669 -  2.0400    1.00     2603   125  0.3066 0.3209   0.70 
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)     : 0.21             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.29            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.87                          
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      :  0.007           4961                                  
REMARK   3   ANGLE     :  0.926           6753                                  
REMARK   3   CHIRALITY :  0.066            691                                  
REMARK   3   PLANARITY :  0.005            863                                  
REMARK   3   DIHEDRAL  : 14.660           2914                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID    1  THROUGH   17 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9028  34.1022 -43.6863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3079 T22:   0.4069                                     
REMARK   3      T33:   0.5038 T12:  -0.0103                                     
REMARK   3      T13:  -0.0507 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6544 L22:   8.5538                                     
REMARK   3      L33:   6.5532 L12:   5.4712                                     
REMARK   3      L13:  -0.1803 L23:  -0.5265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3046 S12:   0.3648 S13:   0.6862                       
REMARK   3      S21:  -0.4297 S22:   0.3856 S23:   0.5652                       
REMARK   3      S31:  -0.6306 S32:  -0.1178 S33:  -0.1644                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   18  THROUGH   33 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.5704  37.1416 -42.5739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3453 T22:   0.4705                                     
REMARK   3      T33:   0.4514 T12:   0.0137                                     
REMARK   3      T13:  -0.0547 T23:  -0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0514 L22:   2.8101                                     
REMARK   3      L33:   2.8137 L12:   2.5120                                     
REMARK   3      L13:  -0.4011 L23:  -1.7408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0735 S12:   0.1594 S13:   0.1642                       
REMARK   3      S21:  -0.3236 S22:  -0.1143 S23:   0.4531                       
REMARK   3      S31:  -0.1753 S32:  -0.2452 S33:   0.0777                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   34  THROUGH   52 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7063  29.3073 -45.7382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3726 T22:   0.4094                                     
REMARK   3      T33:   0.4246 T12:  -0.0844                                     
REMARK   3      T13:  -0.0378 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7416 L22:   3.0753                                     
REMARK   3      L33:   1.2179 L12:  -2.6595                                     
REMARK   3      L13:  -0.7984 L23:   0.4399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.0477 S13:   0.2617                       
REMARK   3      S21:  -0.4951 S22:   0.0628 S23:  -0.0221                       
REMARK   3      S31:  -0.1161 S32:  -0.0460 S33:  -0.0365                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   53  THROUGH   67 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9709  21.0461 -44.7275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4345 T22:   0.6168                                     
REMARK   3      T33:   0.5251 T12:  -0.0078                                     
REMARK   3      T13:   0.0659 T23:  -0.1175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4004 L22:   8.7751                                     
REMARK   3      L33:   3.9241 L12:  -4.9307                                     
REMARK   3      L13:   0.0116 L23:  -4.8030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.3599 S13:  -0.3210                       
REMARK   3      S21:  -0.2758 S22:  -0.3743 S23:  -0.7798                       
REMARK   3      S31:   0.3497 S32:   0.6579 S33:   0.3335                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   68  THROUGH  187 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0517  31.6762 -33.7852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3223 T22:   0.4141                                     
REMARK   3      T33:   0.4084 T12:  -0.0434                                     
REMARK   3      T13:  -0.0222 T23:  -0.1092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8425 L22:   0.7938                                     
REMARK   3      L33:   1.0680 L12:   0.1010                                     
REMARK   3      L13:  -0.0870 L23:  -0.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0626 S12:  -0.2096 S13:   0.3423                       
REMARK   3      S21:  -0.0289 S22:   0.0831 S23:   0.0062                       
REMARK   3      S31:  -0.1671 S32:   0.0987 S33:  -0.0217                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  188  THROUGH  217 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -26.4820  36.1728 -33.1751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2904 T22:   0.4804                                     
REMARK   3      T33:   0.4558 T12:   0.0656                                     
REMARK   3      T13:  -0.0138 T23:  -0.1168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6277 L22:   4.8841                                     
REMARK   3      L33:   2.4721 L12:   2.5094                                     
REMARK   3      L13:  -1.1038 L23:  -1.1639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0929 S12:  -0.1815 S13:   0.4727                       
REMARK   3      S21:  -0.2998 S22:   0.0804 S23:   0.3416                       
REMARK   3      S31:  -0.2071 S32:  -0.3059 S33:   0.0426                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  218  THROUGH  240 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1565  39.7659 -19.7999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3974 T22:   0.5423                                     
REMARK   3      T33:   0.5790 T12:  -0.0306                                     
REMARK   3      T13:  -0.0213 T23:  -0.2112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1193 L22:   1.5817                                     
REMARK   3      L33:   1.9405 L12:  -1.2963                                     
REMARK   3      L13:   1.0628 L23:  -0.0803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1379 S12:  -0.3943 S13:   0.5130                       
REMARK   3      S21:  -0.0029 S22:   0.1310 S23:  -0.3749                       
REMARK   3      S31:  -0.1188 S32:   0.1572 S33:   0.0528                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  241  THROUGH  257 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2737  40.3728  -7.4428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6649 T22:   0.9153                                     
REMARK   3      T33:   0.5421 T12:   0.0122                                     
REMARK   3      T13:  -0.0871 T23:  -0.2501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3265 L22:   4.9397                                     
REMARK   3      L33:   4.6840 L12:   1.9333                                     
REMARK   3      L13:   4.5849 L23:   3.3856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3388 S12:  -1.3463 S13:   0.5766                       
REMARK   3      S21:   0.7267 S22:   0.3007 S23:  -0.2594                       
REMARK   3      S31:  -0.3770 S32:   0.0178 S33:   0.0961                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  258  THROUGH  273 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7437  36.8382 -14.7140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3707 T22:   0.6521                                     
REMARK   3      T33:   0.4750 T12:   0.0262                                     
REMARK   3      T13:  -0.0114 T23:  -0.2369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8719 L22:   2.3555                                     
REMARK   3      L33:   4.9852 L12:  -1.3479                                     
REMARK   3      L13:   1.4408 L23:  -0.4236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2420 S12:  -0.9206 S13:   0.5614                       
REMARK   3      S21:   0.2395 S22:   0.1699 S23:   0.0419                       
REMARK   3      S31:  -0.3534 S32:  -0.2028 S33:   0.0954                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID    1  THROUGH   17 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3804   3.3338 -29.1549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3488 T22:   0.4492                                     
REMARK   3      T33:   0.5882 T12:   0.0520                                     
REMARK   3      T13:  -0.0408 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6569 L22:   5.7564                                     
REMARK   3      L33:   8.2779 L12:   4.1918                                     
REMARK   3      L13:  -3.6926 L23:  -2.3879                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:  -0.2014 S13:  -1.0240                       
REMARK   3      S21:   0.0592 S22:  -0.2721 S23:  -0.7160                       
REMARK   3      S31:   0.8933 S32:   0.4009 S33:   0.2881                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   18  THROUGH   32 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8870   3.3938 -26.7656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3702 T22:   0.5352                                     
REMARK   3      T33:   0.6196 T12:   0.0467                                     
REMARK   3      T13:  -0.0375 T23:  -0.0883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5931 L22:   5.7405                                     
REMARK   3      L33:   3.4919 L12:   1.0983                                     
REMARK   3      L13:  -0.4817 L23:  -2.4121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0990 S12:  -0.2307 S13:  -0.4707                       
REMARK   3      S21:  -0.0892 S22:  -0.3154 S23:  -0.7665                       
REMARK   3      S31:   0.2903 S32:   0.4725 S33:   0.0736                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   33  THROUGH   55 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9292   6.6165 -37.1508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4343 T22:   0.3961                                     
REMARK   3      T33:   0.3912 T12:  -0.0302                                     
REMARK   3      T13:  -0.0127 T23:  -0.1027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8705 L22:   2.2631                                     
REMARK   3      L33:   2.5523 L12:  -0.1535                                     
REMARK   3      L13:   0.5027 L23:  -1.7004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0922 S12:   0.2654 S13:  -0.2422                       
REMARK   3      S21:  -0.1932 S22:   0.0312 S23:  -0.1878                       
REMARK   3      S31:   0.5336 S32:   0.0775 S33:  -0.2297                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   56  THROUGH   82 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4357   8.1620 -40.8583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4108 T22:   0.5206                                     
REMARK   3      T33:   0.4136 T12:  -0.1512                                     
REMARK   3      T13:  -0.0244 T23:  -0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7056 L22:   3.7797                                     
REMARK   3      L33:   3.5208 L12:  -1.0751                                     
REMARK   3      L13:   2.1536 L23:  -1.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2546 S12:  -0.2812 S13:  -0.1925                       
REMARK   3      S21:   0.0330 S22:  -0.1902 S23:   0.3621                       
REMARK   3      S31:   0.1642 S32:  -0.2733 S33:  -0.1220                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   83  THROUGH  187 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5995  13.4837 -24.7706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2767 T22:   0.4564                                     
REMARK   3      T33:   0.3198 T12:  -0.0163                                     
REMARK   3      T13:  -0.0205 T23:  -0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8701 L22:   1.7930                                     
REMARK   3      L33:   1.3139 L12:   0.1773                                     
REMARK   3      L13:  -0.1226 L23:   0.2733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:  -0.3433 S13:  -0.1158                       
REMARK   3      S21:   0.0853 S22:   0.0438 S23:   0.0024                       
REMARK   3      S31:   0.0743 S32:  -0.0850 S33:  -0.0191                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  188  THROUGH  217 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7373  10.3755 -19.6254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3259 T22:   0.5225                                     
REMARK   3      T33:   0.4002 T12:   0.0165                                     
REMARK   3      T13:  -0.0810 T23:  -0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8408 L22:   4.2778                                     
REMARK   3      L33:   2.0490 L12:   2.4597                                     
REMARK   3      L13:  -1.1421 L23:  -0.9961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0424 S12:  -0.5130 S13:  -0.4600                       
REMARK   3      S21:   0.2445 S22:  -0.0260 S23:  -0.5450                       
REMARK   3      S31:   0.1733 S32:   0.3558 S33:   0.0045                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  218  THROUGH  240 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7434  16.1347 -11.9929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3607 T22:   0.6969                                     
REMARK   3      T33:   0.3707 T12:  -0.0254                                     
REMARK   3      T13:   0.0105 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0628 L22:   1.2976                                     
REMARK   3      L33:   1.6601 L12:  -1.8961                                     
REMARK   3      L13:  -0.1882 L23:  -0.4631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0421 S12:  -0.7845 S13:  -0.1301                       
REMARK   3      S21:   0.1027 S22:   0.2325 S23:   0.1539                       
REMARK   3      S31:   0.0665 S32:  -0.2520 S33:  -0.1575                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  241  THROUGH  257 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -18.2101  23.2928  -2.1783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5810 T22:   0.9330                                     
REMARK   3      T33:   0.4623 T12:   0.0191                                     
REMARK   3      T13:   0.0236 T23:  -0.1225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7936 L22:   4.1002                                     
REMARK   3      L33:   9.1452 L12:  -0.4940                                     
REMARK   3      L13:  -4.1570 L23:   1.1271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1428 S12:  -1.2866 S13:   0.4453                       
REMARK   3      S21:   0.7859 S22:   0.0956 S23:   0.3846                       
REMARK   3      S31:   0.0992 S32:  -0.1626 S33:  -0.0059                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  258  THROUGH  273 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8427  21.5557  -8.8173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4255 T22:   0.7785                                     
REMARK   3      T33:   0.3420 T12:  -0.0324                                     
REMARK   3      T13:  -0.0039 T23:  -0.0914                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4384 L22:   3.6005                                     
REMARK   3      L33:   2.6104 L12:  -2.5664                                     
REMARK   3      L13:   1.1914 L23:   0.7388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0541 S12:  -0.7950 S13:   0.1880                       
REMARK   3      S21:   0.5037 S22:  -0.0203 S23:  -0.0853                       
REMARK   3      S31:   0.2041 S32:  -0.3192 S33:  -0.0047                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: H80R MUTANT                               
REMARK   4                                                                      
REMARK   4 5FUQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JAN-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66131.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
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) : 0.977                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
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   : 72281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.04                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.83                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.9                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.38                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.49                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.45                               
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 1D4A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CAPILLARY COUNTERDIFFUSION               
REMARK 280  METHOD: 30% OF PEG 3350, 200 MM SODIUM-ACETATE, 100 MM              
REMARK 280  SODIUM-TRICINE AT PH 9.0                                            
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      100.95400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.41400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.41400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       50.47700            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.41400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.41400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      151.43100            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.41400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.41400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       50.47700            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.41400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.41400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      151.43100            
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      100.95400            
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: 11300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.9 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     LYS A   274                                                      
REMARK 465     LYS B   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   OD1  ASP A   230     O    HOH A  2188              1.94            
REMARK 500   OD2  ASP A   230     O    HOH A  2189              1.92            
REMARK 500   NH2B ARG A   273     O    HOH A  2198              2.19            
REMARK 500   OD1  ASP B   199     O    HOH B  2140              2.00            
REMARK 500   O    HOH A  2041     O    HOH A  2102              1.99            
REMARK 500   O    HOH A  2073     O    HOH A  2168              1.84            
REMARK 500   O    HOH A  2114     O    HOH A  2115              1.86            
REMARK 500   O    HOH A  2136     O    HOH A  2137              2.18            
REMARK 500   O    HOH B  2003     O    HOH B  2179              2.16            
REMARK 500   O    HOH B  2006     O    HOH B  2007              2.18            
REMARK 500   O    HOH B  2012     O    HOH A  2074              1.93            
REMARK 500   O    HOH B  2049     O    HOH B  2077              2.03            
REMARK 500   O    HOH B  2090     O    HOH B  2092              2.19            
REMARK 500   O    HOH B  2094     O    HOH B  2095              2.11            
REMARK 500   O    HOH B  2136     O    HOH B  2178              2.17            
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      -43.44     74.65                                   
REMARK 500    ALA A 131       60.67   -150.31                                   
REMARK 500    TYR A 133     -121.91     56.26                                   
REMARK 500    SER A 192       55.26     30.74                                   
REMARK 500    HIS A 258       50.97   -103.01                                   
REMARK 500    LYS A 262     -166.61   -109.32                                   
REMARK 500    GLU B 124      -47.18     76.49                                   
REMARK 500    TYR B 133     -125.16     57.92                                   
REMARK 500    HIS B 258       51.92   -102.34                                   
REMARK 500    LYS B 262     -166.62   -112.74                                   
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 B1274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTC B1275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTC A1275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTC A1276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1277                 
DBREF  5FUQ A    1   274  UNP    P15559   NQO1_HUMAN       1    274             
DBREF  5FUQ B    1   274  UNP    P15559   NQO1_HUMAN       1    274             
SEQADV 5FUQ ARG A   80  UNP  P15559    HIS    80 ENGINEERED MUTATION            
SEQADV 5FUQ ARG B   80  UNP  P15559    HIS    80 ENGINEERED MUTATION            
SEQRES   1 A  274  MET VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER          
SEQRES   2 A  274  GLU ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA          
SEQRES   3 A  274  ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU          
SEQRES   4 A  274  SER ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER          
SEQRES   5 A  274  ARG LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN          
SEQRES   6 A  274  PHE GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU          
SEQRES   7 A  274  GLY ARG LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS          
SEQRES   8 A  274  LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU          
SEQRES   9 A  274  GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE          
SEQRES  10 A  274  GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA          
SEQRES  11 A  274  ALA MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA          
SEQRES  12 A  274  VAL LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR          
SEQRES  13 A  274  SER LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU          
SEQRES  14 A  274  TRP PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE          
SEQRES  15 A  274  GLN VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS          
SEQRES  16 A  274  THR PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP          
SEQRES  17 A  274  LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU          
SEQRES  18 A  274  TYR PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN          
SEQRES  19 A  274  ALA GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU          
SEQRES  20 A  274  LYS ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU          
SEQRES  21 A  274  GLY LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG          
SEQRES  22 A  274  LYS                                                          
SEQRES   1 B  274  MET VAL GLY ARG ARG ALA LEU ILE VAL LEU ALA HIS SER          
SEQRES   2 B  274  GLU ARG THR SER PHE ASN TYR ALA MET LYS GLU ALA ALA          
SEQRES   3 B  274  ALA ALA ALA LEU LYS LYS LYS GLY TRP GLU VAL VAL GLU          
SEQRES   4 B  274  SER ASP LEU TYR ALA MET ASN PHE ASN PRO ILE ILE SER          
SEQRES   5 B  274  ARG LYS ASP ILE THR GLY LYS LEU LYS ASP PRO ALA ASN          
SEQRES   6 B  274  PHE GLN TYR PRO ALA GLU SER VAL LEU ALA TYR LYS GLU          
SEQRES   7 B  274  GLY ARG LEU SER PRO ASP ILE VAL ALA GLU GLN LYS LYS          
SEQRES   8 B  274  LEU GLU ALA ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU          
SEQRES   9 B  274  GLN TRP PHE GLY VAL PRO ALA ILE LEU LYS GLY TRP PHE          
SEQRES  10 B  274  GLU ARG VAL PHE ILE GLY GLU PHE ALA TYR THR TYR ALA          
SEQRES  11 B  274  ALA MET TYR ASP LYS GLY PRO PHE ARG SER LYS LYS ALA          
SEQRES  12 B  274  VAL LEU SER ILE THR THR GLY GLY SER GLY SER MET TYR          
SEQRES  13 B  274  SER LEU GLN GLY ILE HIS GLY ASP MET ASN VAL ILE LEU          
SEQRES  14 B  274  TRP PRO ILE GLN SER GLY ILE LEU HIS PHE CYS GLY PHE          
SEQRES  15 B  274  GLN VAL LEU GLU PRO GLN LEU THR TYR SER ILE GLY HIS          
SEQRES  16 B  274  THR PRO ALA ASP ALA ARG ILE GLN ILE LEU GLU GLY TRP          
SEQRES  17 B  274  LYS LYS ARG LEU GLU ASN ILE TRP ASP GLU THR PRO LEU          
SEQRES  18 B  274  TYR PHE ALA PRO SER SER LEU PHE ASP LEU ASN PHE GLN          
SEQRES  19 B  274  ALA GLY PHE LEU MET LYS LYS GLU VAL GLN ASP GLU GLU          
SEQRES  20 B  274  LYS ASN LYS LYS PHE GLY LEU SER VAL GLY HIS HIS LEU          
SEQRES  21 B  274  GLY LYS SER ILE PRO THR ASP ASN GLN ILE LYS ALA ARG          
SEQRES  22 B  274  LYS                                                          
HET    FAD  B1274      53                                                       
HET    FAD  A1274      53                                                       
HET    DTC  B1275      25                                                       
HET    DTC  A1275      25                                                       
HET    DTC  A1276      25                                                       
HET    ACT  A1277       4                                                       
HET    ACT  B1276       4                                                       
HET    ACT  A1278       4                                                       
HET    ACT  B1277       4                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     DTC BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-                            
HETNAM   2 DTC  BENZOPYRONE]                                                    
HETNAM     ACT ACETATE ION                                                      
HETSYN     DTC DICOUMAROL                                                       
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  DTC    3(C19 H12 O6)                                                
FORMUL   5  ACT    4(C2 H3 O2 1-)                                               
FORMUL   6  HOH   *396(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 ASP A   62  PHE A   66  5                                   5    
HELIX    4   4 GLN A   67  GLY A   79  1                                  13    
HELIX    5   5 SER A   82  ALA A   95  1                                  14    
HELIX    6   6 PRO A  110  PHE A  121  1                                  12    
HELIX    7   7 THR A  128  MET A  132  5                                   5    
HELIX    8   8 MET A  132  GLY A  136  5                                   5    
HELIX    9   9 SER A  152  SER A  157  5                                   6    
HELIX   10  10 ASP A  164  SER A  174  1                                  11    
HELIX   11  11 LEU A  177  GLY A  181  5                                   5    
HELIX   12  12 SER A  192  THR A  196  5                                   5    
HELIX   13  13 PRO A  197  GLU A  213  1                                  17    
HELIX   14  14 ASN A  214  GLU A  218  5                                   5    
HELIX   15  15 PRO A  225  LEU A  228  5                                   4    
HELIX   16  16 LYS A  240  LYS A  248  1                                   9    
HELIX   17  17 SER B   17  LYS B   33  1                                  17    
HELIX   18  18 SER B   52  ASP B   55  5                                   4    
HELIX   19  19 GLN B   67  GLY B   79  1                                  13    
HELIX   20  20 SER B   82  ALA B   95  1                                  14    
HELIX   21  21 PRO B  110  PHE B  121  1                                  12    
HELIX   22  22 THR B  128  MET B  132  5                                   5    
HELIX   23  23 MET B  132  GLY B  136  5                                   5    
HELIX   24  24 SER B  152  SER B  157  5                                   6    
HELIX   25  25 ASP B  164  SER B  174  1                                  11    
HELIX   26  26 LEU B  177  GLY B  181  5                                   5    
HELIX   27  27 SER B  192  THR B  196  5                                   5    
HELIX   28  28 PRO B  197  GLU B  213  1                                  17    
HELIX   29  29 ASN B  214  GLU B  218  5                                   5    
HELIX   30  30 PRO B  225  LEU B  228  5                                   4    
HELIX   31  31 LYS B  240  LYS B  248  1                                   9    
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  ASP B  41  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  ASP B  41  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 33 GLN A  67  TYR A  68  HOH A2072  HOH A2075                    
SITE     2 AC1 33 HOH A2117  HIS B  12  THR B  16  SER B  17                    
SITE     3 AC1 33 PHE B  18  ASN B  19  ALA B  21  PRO B 103                    
SITE     4 AC1 33 LEU B 104  GLN B 105  TRP B 106  PHE B 107                    
SITE     5 AC1 33 THR B 148  THR B 149  GLY B 150  GLY B 151                    
SITE     6 AC1 33 TYR B 156  ILE B 193  ARG B 201  LEU B 205                    
SITE     7 AC1 33 DTC B1275  HOH B2012  HOH B2174  HOH B2175                    
SITE     8 AC1 33 HOH B2176  HOH B2177  HOH B2178  HOH B2179                    
SITE     9 AC1 33 HOH B2180                                                     
SITE     1 AC2 25 HIS A  12  THR A  16  SER A  17  PHE A  18                    
SITE     2 AC2 25 ASN A  19  ALA A  21  PRO A 103  LEU A 104                    
SITE     3 AC2 25 GLN A 105  TRP A 106  PHE A 107  THR A 148                    
SITE     4 AC2 25 THR A 149  GLY A 150  GLY A 151  TYR A 156                    
SITE     5 AC2 25 ILE A 193  ARG A 201  LEU A 205  DTC A1275                    
SITE     6 AC2 25 HOH A2209  HOH A2210  HOH A2212  GLN B  67                    
SITE     7 AC2 25 PRO B  69                                                     
SITE     1 AC3 14 TYR A 127  TYR A 129  MET A 132  PHE A 179                    
SITE     2 AC3 14 PHE A 237  DTC A1276  HOH A2122  TRP B 106                    
SITE     3 AC3 14 GLY B 150  GLY B 151  MET B 155  HIS B 162                    
SITE     4 AC3 14 FAD B1274  HOH B2181                                          
SITE     1 AC4 12 GLY A 150  GLY A 151  MET A 155  HIS A 162                    
SITE     2 AC4 12 FAD A1274  DTC A1276  HOH A2211  TYR B 127                    
SITE     3 AC4 12 TYR B 129  PHE B 179  PHE B 233  PHE B 237                    
SITE     1 AC5  9 TYR A 129  GLY A 150  HIS A 195  DTC A1275                    
SITE     2 AC5  9 HOH A2214  HIS B 195  PHE B 233  GLN B 234                    
SITE     3 AC5  9 DTC B1275                                                     
SITE     1 AC6  3 THR A 128  TYR A 129  GLN B 234                               
SITE     1 AC7  3 SER B  13  HOH B2005  HOH B2088                               
SITE     1 AC8  3 SER A  13  HOH A2004  HOH A2107                               
SITE     1 AC9  4 GLU B 124  TYR B 127  THR B 128  TYR B 129                    
CRYST1  104.828  104.828  201.908  90.00  90.00  90.00 P 41 21 2     2          
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      0.009539  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009539  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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