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Database: PDB
Entry: 6F2U
LinkDB: 6F2U
Original site: 6F2U 
HEADER    OXIDOREDUCTASE                          27-NOV-17   6F2U              
TITLE     POTENT AND SELECTIVE ALDO-KETO REDUCTASE 1C3 (AKR1C3) INHIBITORS BASED
TITLE    2 ON THE BENZOISOXAZOLE MOIETY: APPLICATION OF A BIOISOSTERIC SCAFFOLD 
TITLE    3 HOPPING APPROACH TO FLUFENAMIC ACID                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER C3;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 17-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 5,17-BETA-HSD 5,3-
COMPND   5 ALPHA-HSD TYPE II,BRAIN,3-ALPHA-HYDROXYSTEROID DEHYDROGENASE TYPE 2, 
COMPND   6 3-ALPHA-HSD TYPE 2,CHLORDECONE REDUCTASE HOMOLOG HAKRB,DIHYDRODIOL   
COMPND   7 DEHYDROGENASE 3,DD3,DIHYDRODIOL DEHYDROGENASE TYPE I,HA1753,INDANOL  
COMPND   8 DEHYDROGENASE,PROSTAGLANDIN F SYNTHASE,PGFS,TESTOSTERONE 17-BETA-    
COMPND   9 DEHYDROGENASE 5,TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE;     
COMPND  10 EC: 1.-.-.-,1.1.1.357,1.1.1.112,1.1.1.188,1.1.1.239,1.1.1.64,        
COMPND  11 1.3.1.20;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AKR1C3, DDH1, HSD17B5, KIAA0119, PGFS;                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALDO-KETO REDUCTASE 1C3; AKR1C3; 17B-HSD5; PROSTATE CANCER (PCA);     
KEYWDS   2 CRPC; BIOISOSTERISM; SCAFFOLD HOPPING; INHIBITORS; X-RAY             
KEYWDS   3 CRYSTALLOGRAPHY, OXIDOREDUCTASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GOYAL,W.Y.WAHLGREN,R.FRIEMANN                                       
REVDAT   2   11-APR-18 6F2U    1       JRNL                                     
REVDAT   1   04-APR-18 6F2U    0                                                
JRNL        AUTH   A.C.PIPPIONE,I.M.CARNOVALE,D.BONANNI,M.SINI,P.GOYAL,         
JRNL        AUTH 2 E.MARINI,K.PORS,S.ADINOLFI,D.ZONARI,C.FESTUCCIA,             
JRNL        AUTH 3 W.Y.WAHLGREN,R.FRIEMANN,R.BAGNATI,D.BOSCHI,S.OLIARO-BOSSO,   
JRNL        AUTH 4 M.L.LOLLI                                                    
JRNL        TITL   POTENT AND SELECTIVE ALDO-KETO REDUCTASE 1C3 (AKR1C3)        
JRNL        TITL 2 INHIBITORS BASED ON THE BENZOISOXAZOLE MOIETY: APPLICATION   
JRNL        TITL 3 OF A BIOISOSTERIC SCAFFOLD HOPPING APPROACH TO FLUFENAMIC    
JRNL        TITL 4 ACID.                                                        
JRNL        REF    EUR J MED CHEM                V. 150   930 2018              
JRNL        REFN                   ISSN 1768-3254                               
JRNL        PMID   29602039                                                     
JRNL        DOI    10.1016/J.EJMECH.2018.03.040                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 46656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2309                            
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 39.8688 -  4.7349    0.99     2949   188  0.1722 0.2049        
REMARK   3     2  4.7349 -  3.7591    0.99     2986   144  0.1540 0.2129        
REMARK   3     3  3.7591 -  3.2842    0.99     2987   168  0.1802 0.2139        
REMARK   3     4  3.2842 -  2.9840    0.98     2953   148  0.2010 0.2708        
REMARK   3     5  2.9840 -  2.7702    0.75     2300   102  0.2046 0.2231        
REMARK   3     6  2.7702 -  2.6069    0.83     2503   127  0.2044 0.2543        
REMARK   3     7  2.6069 -  2.4764    0.88     2659   126  0.2125 0.2693        
REMARK   3     8  2.4764 -  2.3686    0.90     2743   129  0.2048 0.3072        
REMARK   3     9  2.3686 -  2.2774    0.91     2707   147  0.2012 0.2936        
REMARK   3    10  2.2774 -  2.1988    0.92     2815   141  0.2150 0.3042        
REMARK   3    11  2.1988 -  2.1301    0.92     2748   172  0.2250 0.2747        
REMARK   3    12  2.1301 -  2.0692    0.92     2795   142  0.2258 0.2814        
REMARK   3    13  2.0692 -  2.0147    0.93     2800   142  0.2565 0.3561        
REMARK   3    14  2.0147 -  1.9656    0.93     2792   150  0.2963 0.3907        
REMARK   3    15  1.9656 -  1.9209    0.92     2782   146  0.3743 0.4036        
REMARK   3    16  1.9209 -  1.8800    0.93     2828   137  0.4113 0.3990        
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.510           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.008           5316                                  
REMARK   3   ANGLE     :  0.910           7218                                  
REMARK   3   CHIRALITY :  0.053            778                                  
REMARK   3   PLANARITY :  0.006            918                                  
REMARK   3   DIHEDRAL  :  7.659           3176                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6F2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007604.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1RY0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH 6.0, 25% PEG 8000, VAPOR    
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 2690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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    ASN A  57       10.74   -145.33                                   
REMARK 500    PHE A 197       72.82   -157.98                                   
REMARK 500    SER A 221      166.62     76.82                                   
REMARK 500    ARG A 250     -152.70   -118.62                                   
REMARK 500    GLN A 282        1.09    -65.94                                   
REMARK 500    ASN B  57       11.29   -144.90                                   
REMARK 500    ASP B 132     -160.84   -109.95                                   
REMARK 500    PHE B 197       71.70   -158.09                                   
REMARK 500    SER B 221      167.42     77.82                                   
REMARK 500    ARG B 250     -147.88   -123.03                                   
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 NAP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CJ2 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CJ2 B 402                 
DBREF  6F2U A    6   319  UNP    P42330   AK1C3_HUMAN      6    319             
DBREF  6F2U B    6   319  UNP    P42330   AK1C3_HUMAN      6    319             
SEQRES   1 A  314  GLN CYS VAL LYS LEU ASN ASP GLY HIS PHE MET PRO VAL          
SEQRES   2 A  314  LEU GLY PHE GLY THR TYR ALA PRO PRO GLU VAL PRO ARG          
SEQRES   3 A  314  SER LYS ALA LEU GLU VAL THR LYS LEU ALA ILE GLU ALA          
SEQRES   4 A  314  GLY PHE ARG HIS ILE ASP SER ALA HIS LEU TYR ASN ASN          
SEQRES   5 A  314  GLU GLU GLN VAL GLY LEU ALA ILE ARG SER LYS ILE ALA          
SEQRES   6 A  314  ASP GLY SER VAL LYS ARG GLU ASP ILE PHE TYR THR SER          
SEQRES   7 A  314  LYS LEU TRP SER THR PHE HIS ARG PRO GLU LEU VAL ARG          
SEQRES   8 A  314  PRO ALA LEU GLU ASN SER LEU LYS LYS ALA GLN LEU ASP          
SEQRES   9 A  314  TYR VAL ASP LEU TYR LEU ILE HIS SER PRO MET SER LEU          
SEQRES  10 A  314  LYS PRO GLY GLU GLU LEU SER PRO THR ASP GLU ASN GLY          
SEQRES  11 A  314  LYS VAL ILE PHE ASP ILE VAL ASP LEU CYS THR THR TRP          
SEQRES  12 A  314  GLU ALA MET GLU LYS CYS LYS ASP ALA GLY LEU ALA LYS          
SEQRES  13 A  314  SER ILE GLY VAL SER ASN PHE ASN ARG ARG GLN LEU GLU          
SEQRES  14 A  314  MET ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO VAL          
SEQRES  15 A  314  CYS ASN GLN VAL GLU CYS HIS PRO TYR PHE ASN ARG SER          
SEQRES  16 A  314  LYS LEU LEU ASP PHE CYS LYS SER LYS ASP ILE VAL LEU          
SEQRES  17 A  314  VAL ALA TYR SER ALA LEU GLY SER GLN ARG ASP LYS ARG          
SEQRES  18 A  314  TRP VAL ASP PRO ASN SER PRO VAL LEU LEU GLU ASP PRO          
SEQRES  19 A  314  VAL LEU CYS ALA LEU ALA LYS LYS HIS LYS ARG THR PRO          
SEQRES  20 A  314  ALA LEU ILE ALA LEU ARG TYR GLN LEU GLN ARG GLY VAL          
SEQRES  21 A  314  VAL VAL LEU ALA LYS SER TYR ASN GLU GLN ARG ILE ARG          
SEQRES  22 A  314  GLN ASN VAL GLN VAL PHE GLU PHE GLN LEU THR ALA GLU          
SEQRES  23 A  314  ASP MET LYS ALA ILE ASP GLY LEU ASP ARG ASN LEU HIS          
SEQRES  24 A  314  TYR PHE ASN SER ASP SER PHE ALA SER HIS PRO ASN TYR          
SEQRES  25 A  314  PRO TYR                                                      
SEQRES   1 B  314  GLN CYS VAL LYS LEU ASN ASP GLY HIS PHE MET PRO VAL          
SEQRES   2 B  314  LEU GLY PHE GLY THR TYR ALA PRO PRO GLU VAL PRO ARG          
SEQRES   3 B  314  SER LYS ALA LEU GLU VAL THR LYS LEU ALA ILE GLU ALA          
SEQRES   4 B  314  GLY PHE ARG HIS ILE ASP SER ALA HIS LEU TYR ASN ASN          
SEQRES   5 B  314  GLU GLU GLN VAL GLY LEU ALA ILE ARG SER LYS ILE ALA          
SEQRES   6 B  314  ASP GLY SER VAL LYS ARG GLU ASP ILE PHE TYR THR SER          
SEQRES   7 B  314  LYS LEU TRP SER THR PHE HIS ARG PRO GLU LEU VAL ARG          
SEQRES   8 B  314  PRO ALA LEU GLU ASN SER LEU LYS LYS ALA GLN LEU ASP          
SEQRES   9 B  314  TYR VAL ASP LEU TYR LEU ILE HIS SER PRO MET SER LEU          
SEQRES  10 B  314  LYS PRO GLY GLU GLU LEU SER PRO THR ASP GLU ASN GLY          
SEQRES  11 B  314  LYS VAL ILE PHE ASP ILE VAL ASP LEU CYS THR THR TRP          
SEQRES  12 B  314  GLU ALA MET GLU LYS CYS LYS ASP ALA GLY LEU ALA LYS          
SEQRES  13 B  314  SER ILE GLY VAL SER ASN PHE ASN ARG ARG GLN LEU GLU          
SEQRES  14 B  314  MET ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO VAL          
SEQRES  15 B  314  CYS ASN GLN VAL GLU CYS HIS PRO TYR PHE ASN ARG SER          
SEQRES  16 B  314  LYS LEU LEU ASP PHE CYS LYS SER LYS ASP ILE VAL LEU          
SEQRES  17 B  314  VAL ALA TYR SER ALA LEU GLY SER GLN ARG ASP LYS ARG          
SEQRES  18 B  314  TRP VAL ASP PRO ASN SER PRO VAL LEU LEU GLU ASP PRO          
SEQRES  19 B  314  VAL LEU CYS ALA LEU ALA LYS LYS HIS LYS ARG THR PRO          
SEQRES  20 B  314  ALA LEU ILE ALA LEU ARG TYR GLN LEU GLN ARG GLY VAL          
SEQRES  21 B  314  VAL VAL LEU ALA LYS SER TYR ASN GLU GLN ARG ILE ARG          
SEQRES  22 B  314  GLN ASN VAL GLN VAL PHE GLU PHE GLN LEU THR ALA GLU          
SEQRES  23 B  314  ASP MET LYS ALA ILE ASP GLY LEU ASP ARG ASN LEU HIS          
SEQRES  24 B  314  TYR PHE ASN SER ASP SER PHE ALA SER HIS PRO ASN TYR          
SEQRES  25 B  314  PRO TYR                                                      
HET    NAP  A 401      48                                                       
HET    CJ2  A 402      28                                                       
HET    NAP  B 401      48                                                       
HET    CJ2  B 402      28                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     CJ2 3-[(4-METHOXYPHENYL)METHYL]-5-OXIDANYL-~{N}-[3-                  
HETNAM   2 CJ2  (TRIFLUOROMETHYL)PHENYL]-1,2,3-TRIAZOLE-4-CARBOXAMIDE           
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  CJ2    2(C18 H15 F3 N4 O3)                                          
FORMUL   7  HOH   *217(H2 O)                                                    
HELIX    1 AA1 ARG A   31  GLY A   45  1                                  15    
HELIX    2 AA2 ALA A   52  ASN A   56  5                                   5    
HELIX    3 AA3 ASN A   57  ASP A   71  1                                  15    
HELIX    4 AA4 LYS A   75  ILE A   79  5                                   5    
HELIX    5 AA5 TRP A   86  HIS A   90  5                                   5    
HELIX    6 AA6 ARG A   91  GLU A   93  5                                   3    
HELIX    7 AA7 LEU A   94  GLN A  107  1                                  14    
HELIX    8 AA8 ASP A  143  ALA A  157  1                                  15    
HELIX    9 AA9 ASN A  169  ASN A  178  1                                  10    
HELIX   10 AB1 ARG A  199  LYS A  209  1                                  11    
HELIX   11 AB2 VAL A  234  GLU A  237  5                                   4    
HELIX   12 AB3 ASP A  238  LYS A  249  1                                  12    
HELIX   13 AB4 THR A  251  ARG A  263  1                                  13    
HELIX   14 AB5 ASN A  273  VAL A  281  1                                   9    
HELIX   15 AB6 GLN A  282  PHE A  286  5                                   5    
HELIX   16 AB7 THR A  289  GLY A  298  1                                  10    
HELIX   17 AB8 ASN A  307  ALA A  312  5                                   6    
HELIX   18 AB9 ARG B   31  GLY B   45  1                                  15    
HELIX   19 AC1 ALA B   52  ASN B   56  5                                   5    
HELIX   20 AC2 ASN B   57  ASP B   71  1                                  15    
HELIX   21 AC3 LYS B   75  ILE B   79  5                                   5    
HELIX   22 AC4 TRP B   86  HIS B   90  5                                   5    
HELIX   23 AC5 ARG B   91  GLU B   93  5                                   3    
HELIX   24 AC6 LEU B   94  GLN B  107  1                                  14    
HELIX   25 AC7 ASP B  143  ALA B  157  1                                  15    
HELIX   26 AC8 ASN B  169  ASN B  178  1                                  10    
HELIX   27 AC9 ARG B  199  LYS B  209  1                                  11    
HELIX   28 AD1 VAL B  234  GLU B  237  5                                   4    
HELIX   29 AD2 ASP B  238  LYS B  249  1                                  12    
HELIX   30 AD3 THR B  251  ARG B  263  1                                  13    
HELIX   31 AD4 ASN B  273  VAL B  281  1                                   9    
HELIX   32 AD5 GLN B  282  PHE B  286  5                                   5    
HELIX   33 AD6 THR B  289  GLY B  298  1                                  10    
HELIX   34 AD7 SER B  308  ALA B  312  5                                   5    
SHEET    1 AA1 2 CYS A   7  LYS A   9  0                                        
SHEET    2 AA1 2 PHE A  15  PRO A  17 -1  O  MET A  16   N  VAL A   8           
SHEET    1 AA2 9 LEU A  19  GLY A  22  0                                        
SHEET    2 AA2 9 HIS A  48  ASP A  50  1  O  HIS A  48   N  PHE A  21           
SHEET    3 AA2 9 PHE A  80  LEU A  85  1  O  PHE A  80   N  ILE A  49           
SHEET    4 AA2 9 VAL A 111  ILE A 116  1  O  LEU A 115   N  LEU A  85           
SHEET    5 AA2 9 ALA A 160  SER A 166  1  O  LYS A 161   N  VAL A 111           
SHEET    6 AA2 9 CYS A 188  GLU A 192  1  O  CYS A 188   N  VAL A 165           
SHEET    7 AA2 9 VAL A 212  TYR A 216  1  O  VAL A 212   N  ASN A 189           
SHEET    8 AA2 9 VAL A 266  LYS A 270  1  O  VAL A 266   N  ALA A 215           
SHEET    9 AA2 9 LEU A  19  GLY A  22  1  N  GLY A  20   O  VAL A 267           
SHEET    1 AA3 2 CYS B   7  LYS B   9  0                                        
SHEET    2 AA3 2 PHE B  15  PRO B  17 -1  O  MET B  16   N  VAL B   8           
SHEET    1 AA4 9 LEU B  19  GLY B  22  0                                        
SHEET    2 AA4 9 HIS B  48  ASP B  50  1  O  HIS B  48   N  PHE B  21           
SHEET    3 AA4 9 PHE B  80  LEU B  85  1  O  PHE B  80   N  ILE B  49           
SHEET    4 AA4 9 VAL B 111  ILE B 116  1  O  LEU B 115   N  LEU B  85           
SHEET    5 AA4 9 ALA B 160  SER B 166  1  O  LYS B 161   N  VAL B 111           
SHEET    6 AA4 9 CYS B 188  GLU B 192  1  O  CYS B 188   N  VAL B 165           
SHEET    7 AA4 9 VAL B 212  TYR B 216  1  O  TYR B 216   N  VAL B 191           
SHEET    8 AA4 9 VAL B 266  LYS B 270  1  O  VAL B 266   N  ALA B 215           
SHEET    9 AA4 9 LEU B  19  GLY B  22  1  N  GLY B  20   O  VAL B 267           
SITE     1 AC1 31 GLY A  22  THR A  23  TYR A  24  ASP A  50                    
SITE     2 AC1 31 TYR A  55  HIS A 117  SER A 166  ASN A 167                    
SITE     3 AC1 31 GLN A 190  TYR A 216  SER A 217  ALA A 218                    
SITE     4 AC1 31 LEU A 219  GLY A 220  SER A 221  GLN A 222                    
SITE     5 AC1 31 LEU A 236  ALA A 253  LEU A 268  LYS A 270                    
SITE     6 AC1 31 SER A 271  TYR A 272  ARG A 276  GLN A 279                    
SITE     7 AC1 31 ASN A 280  CJ2 A 402  HOH A 511  HOH A 519                    
SITE     8 AC1 31 HOH A 523  HOH A 532  HOH A 541                               
SITE     1 AC2 10 LEU A  54  TYR A  55  TRP A  86  HIS A 117                    
SITE     2 AC2 10 ASN A 167  TYR A 216  SER A 217  PHE A 306                    
SITE     3 AC2 10 NAP A 401  HOH A 541                                          
SITE     1 AC3 29 GLY B  22  THR B  23  TYR B  24  ASP B  50                    
SITE     2 AC3 29 TYR B  55  HIS B 117  SER B 166  ASN B 167                    
SITE     3 AC3 29 GLN B 190  TYR B 216  SER B 217  ALA B 218                    
SITE     4 AC3 29 LEU B 219  GLY B 220  SER B 221  GLN B 222                    
SITE     5 AC3 29 LEU B 236  ALA B 253  LEU B 268  LYS B 270                    
SITE     6 AC3 29 SER B 271  TYR B 272  ARG B 276  GLN B 279                    
SITE     7 AC3 29 ASN B 280  CJ2 B 402  HOH B 541  HOH B 552                    
SITE     8 AC3 29 HOH B 570                                                     
SITE     1 AC4 11 LEU B  54  TYR B  55  HIS B 117  MET B 120                    
SITE     2 AC4 11 ASN B 167  GLU B 192  TYR B 216  SER B 217                    
SITE     3 AC4 11 PHE B 306  NAP B 401  HOH B 570                               
CRYST1   41.046   53.936   76.714 102.12  85.42 103.69 P 1           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      0.024363  0.005935 -0.000796        0.00000                         
SCALE2      0.000000  0.019083  0.003840        0.00000                         
SCALE3      0.000000  0.000000  0.013339        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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