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Database: PDB
Entry: 3G1R
LinkDB: 3G1R
Original site: 3G1R 
HEADER    OXIDOREDUCTASE                          30-JAN-09   3G1R              
TITLE     CRYSTAL STRUCTURE OF HUMAN LIVER 5BETA-REDUCTASE (AKR1D1) IN COMPLEX  
TITLE    2 WITH NADP AND FINASTERIDE. RESOLUTION 1.70 A                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-OXO-5-BETA-STEROID 4-DEHYDROGENASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DELTA(4)-3-KETOSTEROID 5-BETA-REDUCTASE, DELTA(4)-3-        
COMPND   5 OXOSTEROID 5-BETA-REDUCTASE, ALDO-KETO REDUCTASE FAMILY 1 MEMBER D1; 
COMPND   6 EC: 1.3.1.3;                                                         
COMPND   7 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: AKR1D1, SRD5B1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    FINASTERIDE COMPLEX, BILE ACID CATABOLISM, CYTOPLASM, DISEASE         
KEYWDS   2 MUTATION, INTRAHEPATIC CHOLESTASIS, LIPID METABOLISM, NADP,          
KEYWDS   3 OXIDOREDUCTASE, STEROID METABOLISM                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DI COSTANZO,J.E.DRURY,T.M.PENNING,D.W.CHRISTIANSON                  
REVDAT   3   24-JUL-19 3G1R    1       REMARK                                   
REVDAT   2   05-JAN-10 3G1R    1       JRNL                                     
REVDAT   1   09-JUN-09 3G1R    0                                                
JRNL        AUTH   J.E.DRURY,L.DI COSTANZO,T.M.PENNING,D.W.CHRISTIANSON         
JRNL        TITL   INHIBITION OF HUMAN STEROID 5BETA-REDUCTASE (AKR1D1) BY      
JRNL        TITL 2 FINASTERIDE AND STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX.   
JRNL        REF    J.BIOL.CHEM.                  V. 284 19786 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19515843                                                     
JRNL        DOI    10.1074/JBC.C109.016931                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.100                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 73560                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3717                            
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 24.3400 -  5.0880    0.99     2979   156  0.1500 0.1810        
REMARK   3     2  5.0880 -  4.0450    1.00     2844   145  0.1380 0.1420        
REMARK   3     3  4.0450 -  3.5350    1.00     2799   150  0.1530 0.1650        
REMARK   3     4  3.5350 -  3.2130    1.00     2826   140  0.1750 0.1880        
REMARK   3     5  3.2130 -  2.9830    0.99     2761   149  0.1790 0.2070        
REMARK   3     6  2.9830 -  2.8070    0.98     2685   179  0.1800 0.2010        
REMARK   3     7  2.8070 -  2.6670    0.98     2748   135  0.1840 0.1960        
REMARK   3     8  2.6670 -  2.5510    0.98     2687   163  0.1800 0.2250        
REMARK   3     9  2.5510 -  2.4530    0.98     2702   150  0.1760 0.2330        
REMARK   3    10  2.4530 -  2.3680    0.97     2670   146  0.1710 0.2030        
REMARK   3    11  2.3680 -  2.2940    0.97     2684   135  0.1800 0.2020        
REMARK   3    12  2.2940 -  2.2290    0.96     2652   153  0.1810 0.2390        
REMARK   3    13  2.2290 -  2.1700    0.97     2649   137  0.1720 0.1970        
REMARK   3    14  2.1700 -  2.1170    0.96     2657   160  0.1750 0.2290        
REMARK   3    15  2.1170 -  2.0690    0.96     2646   132  0.1760 0.2350        
REMARK   3    16  2.0690 -  2.0250    0.96     2670   128  0.1830 0.2200        
REMARK   3    17  2.0250 -  1.9850    0.94     2567   139  0.1810 0.1990        
REMARK   3    18  1.9850 -  1.9470    0.93     2527   142  0.1810 0.2150        
REMARK   3    19  1.9470 -  1.9120    0.91     2518   117  0.1790 0.1910        
REMARK   3    20  1.9120 -  1.8800    0.90     2468   142  0.1830 0.2430        
REMARK   3    21  1.8800 -  1.8500    0.87     2363   122  0.1920 0.2260        
REMARK   3    22  1.8500 -  1.8210    0.86     2370   115  0.1930 0.2440        
REMARK   3    23  1.8210 -  1.7940    0.86     2362   129  0.1880 0.2340        
REMARK   3    24  1.7940 -  1.7690    0.84     2273   116  0.1870 0.2210        
REMARK   3    25  1.7690 -  1.7450    0.84     2312   125  0.1900 0.2250        
REMARK   3    26  1.7450 -  1.7230    0.83     2251   102  0.1940 0.2420        
REMARK   3    27  1.7230 -  1.7010    0.78     2173   110  0.1900 0.2300        
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              : 0.33                                          
REMARK   3   B_SOL              : 31.45                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.77700                                              
REMARK   3    B22 (A**2) : -0.49300                                             
REMARK   3    B33 (A**2) : -0.28500                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.006           5527                                  
REMARK   3   ANGLE     :  0.992           7524                                  
REMARK   3   CHIRALITY :  0.067            796                                  
REMARK   3   PLANARITY :  0.006            955                                  
REMARK   3   DIHEDRAL  : 16.950           2212                                  
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: THE BINDING STEROID POCKET OF MONOMER A   
REMARK   3  SHOWED A DISCONTINUOUS PEAK THAT WAS NOT POSSIBLE TO FIT WITH       
REMARK   3  FINASTERIDE MOLECULE OR A DIFFERENT LIGAND.                         
REMARK   4                                                                      
REMARK   4 3G1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051313.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76941                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 3CMF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE TERNARY COMPLEXES OF AKR1D1-NADP+    
REMARK 280  -FINASTERIDE WAS CRYSTALLIZED BY THE HANGING DROP VAPOR             
REMARK 280  DIFFUSION METHOD AT 4 C. DROPS CONTAINING 3.0 L OF ENZYME           
REMARK 280  SOLUTION [5.0 MG/ML AKR1D1, 2.0 MM NADP+, 0.5 MM FINASTERIDE,       
REMARK 280  10.0 MM TRIS (PH 7.4)] AND 4.0 L OF PRECIPITANT BUFFER [0.1 M       
REMARK 280  TRIS-HCL (PH 7.0), 10-20% (WT/VOL) PEG 4000, 10% ISO-PROPANOL]      
REMARK 280  WERE EQUILIBRATED AGAINST A 1 ML RESERVOIR OF PRECIPITANT           
REMARK 280  BUFFER. CRYSTALS OF THE AKR1D1-NADP+-FINASTERIDE, COMPLEX WERE      
REMARK 280  SOAKED FOR 24 HOURS IN THE SAME MOTHER LIQUOR SOLUTION AUGMENTED    
REMARK 280  WITH 2.0 MM NADP+, 2.0 MM FINASTERIDE AND 30% ISO-PROPANOL,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       24.94600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.48050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.93850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.48050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.94600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.93850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 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    HIS A   8       34.21   -145.21                                   
REMARK 500    SER A 220       49.94     39.64                                   
REMARK 500    THR A 224      170.27     73.69                                   
REMARK 500    TRP A 230       -9.55   -140.69                                   
REMARK 500    HIS B   8       37.02   -144.54                                   
REMARK 500    ALA B  55      143.19   -170.12                                   
REMARK 500    THR B 224      168.72     78.74                                   
REMARK 500    TRP B 230      -16.57   -149.35                                   
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 944                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 943                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FIT B 327                 
DBREF  3G1R A    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
DBREF  3G1R B    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
SEQADV 3G1R MET A  -19  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY A  -18  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER A  -17  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER A  -16  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -15  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -14  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -13  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -12  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -11  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A  -10  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER A   -9  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER A   -8  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY A   -7  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R LEU A   -6  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R VAL A   -5  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R PRO A   -4  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R ARG A   -3  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY A   -2  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER A   -1  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS A    0  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R MET B  -19  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY B  -18  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER B  -17  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER B  -16  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -15  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -14  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -13  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -12  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -11  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B  -10  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER B   -9  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER B   -8  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY B   -7  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R LEU B   -6  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R VAL B   -5  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R PRO B   -4  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R ARG B   -3  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R GLY B   -2  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R SER B   -1  UNP  P51857              EXPRESSION TAG                 
SEQADV 3G1R HIS B    0  UNP  P51857              EXPRESSION TAG                 
SEQRES   1 A  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  346  LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA          
SEQRES   3 A  346  SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO          
SEQRES   4 A  346  ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR          
SEQRES   5 A  346  PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE          
SEQRES   6 A  346  ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR          
SEQRES   7 A  346  GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS          
SEQRES   8 A  346  ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR          
SEQRES   9 A  346  CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET          
SEQRES  10 A  346  VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN          
SEQRES  11 A  346  LEU ASP TYR VAL ASP LEU TYR ILE ILE GLU VAL PRO MET          
SEQRES  12 A  346  ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU          
SEQRES  13 A  346  ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA          
SEQRES  14 A  346  THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU          
SEQRES  15 A  346  VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN          
SEQRES  16 A  346  LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS          
SEQRES  17 A  346  PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR          
SEQRES  18 A  346  GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE          
SEQRES  19 A  346  VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN          
SEQRES  20 A  346  PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS          
SEQRES  21 A  346  ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS          
SEQRES  22 A  346  THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG          
SEQRES  23 A  346  GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG          
SEQRES  24 A  346  ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR          
SEQRES  25 A  346  GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN          
SEQRES  26 A  346  VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO          
SEQRES  27 A  346  GLU TYR PRO PHE HIS ASP GLU TYR                              
SEQRES   1 B  346  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  346  LEU VAL PRO ARG GLY SER HIS MET ASP LEU SER ALA ALA          
SEQRES   3 B  346  SER HIS ARG ILE PRO LEU SER ASP GLY ASN SER ILE PRO          
SEQRES   4 B  346  ILE ILE GLY LEU GLY THR TYR SER GLU PRO LYS SER THR          
SEQRES   5 B  346  PRO LYS GLY ALA CYS ALA THR SER VAL LYS VAL ALA ILE          
SEQRES   6 B  346  ASP THR GLY TYR ARG HIS ILE ASP GLY ALA TYR ILE TYR          
SEQRES   7 B  346  GLN ASN GLU HIS GLU VAL GLY GLU ALA ILE ARG GLU LYS          
SEQRES   8 B  346  ILE ALA GLU GLY LYS VAL ARG ARG GLU ASP ILE PHE TYR          
SEQRES   9 B  346  CYS GLY LYS LEU TRP ALA THR ASN HIS VAL PRO GLU MET          
SEQRES  10 B  346  VAL ARG PRO THR LEU GLU ARG THR LEU ARG VAL LEU GLN          
SEQRES  11 B  346  LEU ASP TYR VAL ASP LEU TYR ILE ILE GLU VAL PRO MET          
SEQRES  12 B  346  ALA PHE LYS PRO GLY ASP GLU ILE TYR PRO ARG ASP GLU          
SEQRES  13 B  346  ASN GLY LYS TRP LEU TYR HIS LYS SER ASN LEU CYS ALA          
SEQRES  14 B  346  THR TRP GLU ALA MET GLU ALA CYS LYS ASP ALA GLY LEU          
SEQRES  15 B  346  VAL LYS SER LEU GLY VAL SER ASN PHE ASN ARG ARG GLN          
SEQRES  16 B  346  LEU GLU LEU ILE LEU ASN LYS PRO GLY LEU LYS HIS LYS          
SEQRES  17 B  346  PRO VAL SER ASN GLN VAL GLU CYS HIS PRO TYR PHE THR          
SEQRES  18 B  346  GLN PRO LYS LEU LEU LYS PHE CYS GLN GLN HIS ASP ILE          
SEQRES  19 B  346  VAL ILE THR ALA TYR SER PRO LEU GLY THR SER ARG ASN          
SEQRES  20 B  346  PRO ILE TRP VAL ASN VAL SER SER PRO PRO LEU LEU LYS          
SEQRES  21 B  346  ASP ALA LEU LEU ASN SER LEU GLY LYS ARG TYR ASN LYS          
SEQRES  22 B  346  THR ALA ALA GLN ILE VAL LEU ARG PHE ASN ILE GLN ARG          
SEQRES  23 B  346  GLY VAL VAL VAL ILE PRO LYS SER PHE ASN LEU GLU ARG          
SEQRES  24 B  346  ILE LYS GLU ASN PHE GLN ILE PHE ASP PHE SER LEU THR          
SEQRES  25 B  346  GLU GLU GLU MET LYS ASP ILE GLU ALA LEU ASN LYS ASN          
SEQRES  26 B  346  VAL ARG PHE VAL GLU LEU LEU MET TRP ARG ASP HIS PRO          
SEQRES  27 B  346  GLU TYR PRO PHE HIS ASP GLU TYR                              
HET    NAP  A 944      48                                                       
HET    NAP  B 943      48                                                       
HET    FIT  B 327      27                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     FIT (4AR,4BS,6AS,7S,9AS,9BS,11AR)-N-TERT-BUTYL-4A,6A-                
HETNAM   2 FIT  DIMETHYL-2-OXO-2,4A,4B,5,6,6A,7,8,9,9A,9B,10,11,11A-            
HETNAM   3 FIT  TETRADECAHYDRO-1H-INDENO[5,4-F]QUINOLINE-7-CARBOXAMIDE          
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     FIT FINASTERIDE                                                      
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  FIT    C23 H36 N2 O2                                                
FORMUL   6  HOH   *754(H2 O)                                                    
HELIX    1   1 GLU A   28  THR A   32  5                                   5    
HELIX    2   2 GLY A   35  GLY A   48  1                                  14    
HELIX    3   3 ALA A   55  GLN A   59  5                                   5    
HELIX    4   4 ASN A   60  GLU A   74  1                                  15    
HELIX    5   5 ARG A   78  ILE A   82  5                                   5    
HELIX    6   6 TRP A   89  HIS A   93  5                                   5    
HELIX    7   7 VAL A   94  GLN A  110  1                                  17    
HELIX    8   8 ASN A  146  ALA A  160  1                                  15    
HELIX    9   9 ASN A  172  ASN A  181  1                                  10    
HELIX   10  10 GLN A  202  HIS A  212  1                                  11    
HELIX   11  11 PRO A  237  LYS A  240  5                                   4    
HELIX   12  12 ASP A  241  ASN A  252  1                                  12    
HELIX   13  13 THR A  254  ARG A  266  1                                  13    
HELIX   14  14 ASN A  276  GLN A  285  1                                  10    
HELIX   15  15 THR A  292  ALA A  301  1                                  10    
HELIX   16  16 LEU A  311  ARG A  315  5                                   5    
HELIX   17  17 GLU B   28  THR B   32  5                                   5    
HELIX   18  18 GLY B   35  GLY B   48  1                                  14    
HELIX   19  19 ALA B   55  GLN B   59  5                                   5    
HELIX   20  20 ASN B   60  GLU B   74  1                                  15    
HELIX   21  21 ARG B   78  ILE B   82  5                                   5    
HELIX   22  22 TRP B   89  HIS B   93  5                                   5    
HELIX   23  23 VAL B   94  GLU B   96  5                                   3    
HELIX   24  24 MET B   97  GLN B  110  1                                  14    
HELIX   25  25 ASN B  146  ALA B  160  1                                  15    
HELIX   26  26 ASN B  172  ASN B  181  1                                  10    
HELIX   27  27 GLN B  202  HIS B  212  1                                  11    
HELIX   28  28 PRO B  237  LYS B  240  5                                   4    
HELIX   29  29 ASP B  241  TYR B  251  1                                  11    
HELIX   30  30 THR B  254  ARG B  266  1                                  13    
HELIX   31  31 ASN B  276  GLN B  285  1                                  10    
HELIX   32  32 THR B  292  ALA B  301  1                                  10    
HELIX   33  33 LEU B  311  ARG B  315  5                                   5    
SHEET    1   A 2 ARG A   9  PRO A  11  0                                        
SHEET    2   A 2 SER A  17  PRO A  19 -1  O  ILE A  18   N  ILE A  10           
SHEET    1   B 8 LEU A  23  GLY A  24  0                                        
SHEET    2   B 8 HIS A  51  ASP A  53  1  O  ASP A  53   N  LEU A  23           
SHEET    3   B 8 PHE A  83  LEU A  88  1  O  PHE A  83   N  ILE A  52           
SHEET    4   B 8 VAL A 114  ILE A 119  1  O  ILE A 118   N  LEU A  88           
SHEET    5   B 8 VAL A 163  SER A 169  1  O  GLY A 167   N  TYR A 117           
SHEET    6   B 8 SER A 191  GLU A 195  1  O  SER A 191   N  VAL A 168           
SHEET    7   B 8 VAL A 215  TYR A 219  1  O  TYR A 219   N  VAL A 194           
SHEET    8   B 8 VAL A 269  VAL A 270  1  O  VAL A 269   N  ALA A 218           
SHEET    1   C 2 ALA A 124  PHE A 125  0                                        
SHEET    2   C 2 TYR A 142  HIS A 143 -1  O  HIS A 143   N  ALA A 124           
SHEET    1   D 2 ARG B   9  PRO B  11  0                                        
SHEET    2   D 2 SER B  17  PRO B  19 -1  O  ILE B  18   N  ILE B  10           
SHEET    1   E 8 LEU B  23  GLY B  24  0                                        
SHEET    2   E 8 HIS B  51  ASP B  53  1  O  ASP B  53   N  LEU B  23           
SHEET    3   E 8 PHE B  83  LEU B  88  1  O  PHE B  83   N  ILE B  52           
SHEET    4   E 8 VAL B 114  ILE B 119  1  O  ILE B 118   N  LEU B  88           
SHEET    5   E 8 VAL B 163  SER B 169  1  O  LYS B 164   N  VAL B 114           
SHEET    6   E 8 SER B 191  GLU B 195  1  O  SER B 191   N  VAL B 168           
SHEET    7   E 8 VAL B 215  TYR B 219  1  O  TYR B 219   N  VAL B 194           
SHEET    8   E 8 VAL B 269  VAL B 270  1  O  VAL B 269   N  ALA B 218           
SITE     1 AC1 33 GLY A  24  THR A  25  TYR A  26  ASP A  53                    
SITE     2 AC1 33 TYR A  58  SER A 169  ASN A 170  GLN A 193                    
SITE     3 AC1 33 TYR A 219  SER A 220  PRO A 221  LEU A 222                    
SITE     4 AC1 33 GLY A 223  THR A 224  SER A 225  LEU A 239                    
SITE     5 AC1 33 ALA A 256  ILE A 271  PRO A 272  LYS A 273                    
SITE     6 AC1 33 SER A 274  PHE A 275  ARG A 279  GLU A 282                    
SITE     7 AC1 33 ASN A 283  HOH A 338  HOH A 394  HOH A 395                    
SITE     8 AC1 33 HOH A 456  HOH A 519  HOH A 541  HOH A 580                    
SITE     9 AC1 33 HOH A 738                                                     
SITE     1 AC2 37 GLY B  24  THR B  25  TYR B  26  ASP B  53                    
SITE     2 AC2 37 TYR B  58  SER B 169  ASN B 170  GLN B 193                    
SITE     3 AC2 37 TYR B 219  SER B 220  PRO B 221  LEU B 222                    
SITE     4 AC2 37 GLY B 223  THR B 224  SER B 225  LEU B 239                    
SITE     5 AC2 37 ALA B 256  ILE B 271  PRO B 272  LYS B 273                    
SITE     6 AC2 37 SER B 274  PHE B 275  ARG B 279  GLU B 282                    
SITE     7 AC2 37 ASN B 283  FIT B 327  HOH B 387  HOH B 418                    
SITE     8 AC2 37 HOH B 422  HOH B 426  HOH B 459  HOH B 460                    
SITE     9 AC2 37 HOH B 529  HOH B 534  HOH B 558  HOH B 598                    
SITE    10 AC2 37 HOH B 623                                                     
SITE     1 AC3 10 TYR B  26  TYR B  58  TRP B  89  GLU B 120                    
SITE     2 AC3 10 TYR B 132  TRP B 140  TRP B 230  HOH B 460                    
SITE     3 AC3 10 HOH B 463  NAP B 943                                          
CRYST1   49.892  109.877  128.961  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020043  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007754        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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