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Database: PDB
Entry: 3BUV
LinkDB: 3BUV
Original site: 3BUV 
HEADER    OXIDOREDUCTASE                          03-JAN-08   3BUV              
TITLE     CRYSTAL STRUCTURE OF HUMAN DELTA(4)-3-KETOSTEROID 5-BETA-REDUCTASE IN 
TITLE    2 COMPLEX WITH NADP AND HEPES. RESOLUTION: 1.35 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, ALDO-KETO REDUCTASE
COMPND   5 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 ORGAN: LIVER;                                                        
SOURCE   6 GENE: AKR1D1, SRD5B1;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    5-BETA-REDUCTASE; CATALYTIC TETRAD; E120; HEPES; NADP, BILE ACID      
KEYWDS   2 CATABOLISM, DISEASE MUTATION, LIPID METABOLISM, OXIDOREDUCTASE,      
KEYWDS   3 STEROID METABOLISM                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DI COSTANZO,J.DRURY,T.M.PENNING,D.W.CHRISTIANSON                    
REVDAT   5   13-JUL-11 3BUV    1       VERSN                                    
REVDAT   4   24-FEB-09 3BUV    1       VERSN                                    
REVDAT   3   24-JUN-08 3BUV    1       JRNL                                     
REVDAT   2   22-APR-08 3BUV    1       ATOM                                     
REVDAT   1   01-APR-08 3BUV    0                                                
JRNL        AUTH   L.DI COSTANZO,J.E.DRURY,T.M.PENNING,D.W.CHRISTIANSON         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN LIVER {DELTA}4-3-KETOSTEROID      
JRNL        TITL 2 5{BETA}-REDUCTASE (AKR1D1) AND IMPLICATIONS FOR SUBSTRATE    
JRNL        TITL 3 BINDING AND CATALYSIS.                                       
JRNL        REF    J.BIOL.CHEM.                  V. 283 16830 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18407998                                                     
JRNL        DOI    10.1074/JBC.M801778200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 179622.190                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 140579                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7075                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.43                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 19491                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1035                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5254                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 123                                     
REMARK   3   SOLVENT ATOMS            : 556                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.28000                                             
REMARK   3    B22 (A**2) : -4.79000                                             
REMARK   3    B33 (A**2) : 8.06000                                              
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.030 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.590 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.760 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.590 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 49.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NAP.PAR                                        
REMARK   3  PARAMETER FILE  4  : EPE.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NAP.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : EPE.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3BUV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB045984.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
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 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 147700                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS 1.2                                               
REMARK 200 STARTING MODEL: 3BUR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% WT/VOL PEG 4000; 10%              
REMARK 280  ISOPROPANOL; 100MM HEPES PH 7.5; 2.0 MM NADP, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
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       24.85550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.01150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.89900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.01150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.85550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.89900            
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 B     1                                                      
REMARK 465     MET A     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 B   8       37.96   -142.79                                   
REMARK 500    ASN B 146       77.96   -150.21                                   
REMARK 500    THR B 224      171.18     77.30                                   
REMARK 500    PRO B 236      153.69    -49.99                                   
REMARK 500    HIS A   8       36.18   -141.49                                   
REMARK 500    TYR A 132       71.19   -119.95                                   
REMARK 500    THR A 224      168.58     77.16                                   
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 B 3901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 3902                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 3999                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 330                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BUR   RELATED DB: PDB                                   
REMARK 900 SAME ENZYME IN COMPLEX WITH NADP AND TESTOSTERONE                    
DBREF  3BUV A    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
DBREF  3BUV B    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
SEQRES   1 A  326  MET ASP LEU SER ALA ALA SER HIS ARG ILE PRO LEU SER          
SEQRES   2 A  326  ASP GLY ASN SER ILE PRO ILE ILE GLY LEU GLY THR TYR          
SEQRES   3 A  326  SER GLU PRO LYS SER THR PRO LYS GLY ALA CYS ALA THR          
SEQRES   4 A  326  SER VAL LYS VAL ALA ILE ASP THR GLY TYR ARG HIS ILE          
SEQRES   5 A  326  ASP GLY ALA TYR ILE TYR GLN ASN GLU HIS GLU VAL GLY          
SEQRES   6 A  326  GLU ALA ILE ARG GLU LYS ILE ALA GLU GLY LYS VAL ARG          
SEQRES   7 A  326  ARG GLU ASP ILE PHE TYR CYS GLY LYS LEU TRP ALA THR          
SEQRES   8 A  326  ASN HIS VAL PRO GLU MET VAL ARG PRO THR LEU GLU ARG          
SEQRES   9 A  326  THR LEU ARG VAL LEU GLN LEU ASP TYR VAL ASP LEU TYR          
SEQRES  10 A  326  ILE ILE GLU VAL PRO MET ALA PHE LYS PRO GLY ASP GLU          
SEQRES  11 A  326  ILE TYR PRO ARG ASP GLU ASN GLY LYS TRP LEU TYR HIS          
SEQRES  12 A  326  LYS SER ASN LEU CYS ALA THR TRP GLU ALA MET GLU ALA          
SEQRES  13 A  326  CYS LYS ASP ALA GLY LEU VAL LYS SER LEU GLY VAL SER          
SEQRES  14 A  326  ASN PHE ASN ARG ARG GLN LEU GLU LEU ILE LEU ASN LYS          
SEQRES  15 A  326  PRO GLY LEU LYS HIS LYS PRO VAL SER ASN GLN VAL GLU          
SEQRES  16 A  326  CYS HIS PRO TYR PHE THR GLN PRO LYS LEU LEU LYS PHE          
SEQRES  17 A  326  CYS GLN GLN HIS ASP ILE VAL ILE THR ALA TYR SER PRO          
SEQRES  18 A  326  LEU GLY THR SER ARG ASN PRO ILE TRP VAL ASN VAL SER          
SEQRES  19 A  326  SER PRO PRO LEU LEU LYS ASP ALA LEU LEU ASN SER LEU          
SEQRES  20 A  326  GLY LYS ARG TYR ASN LYS THR ALA ALA GLN ILE VAL LEU          
SEQRES  21 A  326  ARG PHE ASN ILE GLN ARG GLY VAL VAL VAL ILE PRO LYS          
SEQRES  22 A  326  SER PHE ASN LEU GLU ARG ILE LYS GLU ASN PHE GLN ILE          
SEQRES  23 A  326  PHE ASP PHE SER LEU THR GLU GLU GLU MET LYS ASP ILE          
SEQRES  24 A  326  GLU ALA LEU ASN LYS ASN VAL ARG PHE VAL GLU LEU LEU          
SEQRES  25 A  326  MET TRP ARG ASP HIS PRO GLU TYR PRO PHE HIS ASP GLU          
SEQRES  26 A  326  TYR                                                          
SEQRES   1 B  326  MET ASP LEU SER ALA ALA SER HIS ARG ILE PRO LEU SER          
SEQRES   2 B  326  ASP GLY ASN SER ILE PRO ILE ILE GLY LEU GLY THR TYR          
SEQRES   3 B  326  SER GLU PRO LYS SER THR PRO LYS GLY ALA CYS ALA THR          
SEQRES   4 B  326  SER VAL LYS VAL ALA ILE ASP THR GLY TYR ARG HIS ILE          
SEQRES   5 B  326  ASP GLY ALA TYR ILE TYR GLN ASN GLU HIS GLU VAL GLY          
SEQRES   6 B  326  GLU ALA ILE ARG GLU LYS ILE ALA GLU GLY LYS VAL ARG          
SEQRES   7 B  326  ARG GLU ASP ILE PHE TYR CYS GLY LYS LEU TRP ALA THR          
SEQRES   8 B  326  ASN HIS VAL PRO GLU MET VAL ARG PRO THR LEU GLU ARG          
SEQRES   9 B  326  THR LEU ARG VAL LEU GLN LEU ASP TYR VAL ASP LEU TYR          
SEQRES  10 B  326  ILE ILE GLU VAL PRO MET ALA PHE LYS PRO GLY ASP GLU          
SEQRES  11 B  326  ILE TYR PRO ARG ASP GLU ASN GLY LYS TRP LEU TYR HIS          
SEQRES  12 B  326  LYS SER ASN LEU CYS ALA THR TRP GLU ALA MET GLU ALA          
SEQRES  13 B  326  CYS LYS ASP ALA GLY LEU VAL LYS SER LEU GLY VAL SER          
SEQRES  14 B  326  ASN PHE ASN ARG ARG GLN LEU GLU LEU ILE LEU ASN LYS          
SEQRES  15 B  326  PRO GLY LEU LYS HIS LYS PRO VAL SER ASN GLN VAL GLU          
SEQRES  16 B  326  CYS HIS PRO TYR PHE THR GLN PRO LYS LEU LEU LYS PHE          
SEQRES  17 B  326  CYS GLN GLN HIS ASP ILE VAL ILE THR ALA TYR SER PRO          
SEQRES  18 B  326  LEU GLY THR SER ARG ASN PRO ILE TRP VAL ASN VAL SER          
SEQRES  19 B  326  SER PRO PRO LEU LEU LYS ASP ALA LEU LEU ASN SER LEU          
SEQRES  20 B  326  GLY LYS ARG TYR ASN LYS THR ALA ALA GLN ILE VAL LEU          
SEQRES  21 B  326  ARG PHE ASN ILE GLN ARG GLY VAL VAL VAL ILE PRO LYS          
SEQRES  22 B  326  SER PHE ASN LEU GLU ARG ILE LYS GLU ASN PHE GLN ILE          
SEQRES  23 B  326  PHE ASP PHE SER LEU THR GLU GLU GLU MET LYS ASP ILE          
SEQRES  24 B  326  GLU ALA LEU ASN LYS ASN VAL ARG PHE VAL GLU LEU LEU          
SEQRES  25 B  326  MET TRP ARG ASP HIS PRO GLU TYR PRO PHE HIS ASP GLU          
SEQRES  26 B  326  TYR                                                          
HET    NAP  B3901      48                                                       
HET    NAP  A3902      48                                                       
HET    EPE  A3999      15                                                       
HET    GOL  B 329       6                                                       
HET    GOL  B 330       6                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     GOL GLYCEROL                                                         
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     EPE HEPES                                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  EPE    C8 H18 N2 O4 S                                               
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  HOH   *556(H2 O)                                                    
HELIX    1  17 GLU B   28  THR B   32  5                                   5    
HELIX    2  18 GLY B   35  GLY B   48  1                                  14    
HELIX    3  19 ALA B   55  GLN B   59  5                                   5    
HELIX    4  20 ASN B   60  GLU B   74  1                                  15    
HELIX    5  21 ARG B   78  ILE B   82  5                                   5    
HELIX    6  22 TRP B   89  HIS B   93  5                                   5    
HELIX    7  23 VAL B   94  GLU B   96  5                                   3    
HELIX    8  24 MET B   97  GLN B  110  1                                  14    
HELIX    9  25 ASN B  146  ALA B  160  1                                  15    
HELIX   10  26 ASN B  172  ASN B  181  1                                  10    
HELIX   11  27 GLN B  202  HIS B  212  1                                  11    
HELIX   12  28 PRO B  237  LYS B  240  5                                   4    
HELIX   13  29 ASP B  241  ASN B  252  1                                  12    
HELIX   14  30 THR B  254  ARG B  266  1                                  13    
HELIX   15  31 ASN B  276  GLN B  285  1                                  10    
HELIX   16  32 THR B  292  ALA B  301  1                                  10    
HELIX   17  33 LEU B  311  ARG B  315  5                                   5    
HELIX   18   1 GLY A   35  GLY A   48  1                                  14    
HELIX   19   2 ALA A   55  GLN A   59  5                                   5    
HELIX   20   3 ASN A   60  GLU A   74  1                                  15    
HELIX   21   4 ARG A   78  ILE A   82  5                                   5    
HELIX   22   5 TRP A   89  HIS A   93  5                                   5    
HELIX   23   6 VAL A   94  GLU A   96  5                                   3    
HELIX   24   7 MET A   97  GLN A  110  1                                  14    
HELIX   25   8 ASN A  146  ALA A  160  1                                  15    
HELIX   26   9 ASN A  172  ASN A  181  1                                  10    
HELIX   27  10 GLN A  202  HIS A  212  1                                  11    
HELIX   28  11 PRO A  237  LYS A  240  5                                   4    
HELIX   29  12 ASP A  241  TYR A  251  1                                  11    
HELIX   30  13 THR A  254  ARG A  266  1                                  13    
HELIX   31  14 ASN A  276  GLN A  285  1                                  10    
HELIX   32  15 THR A  292  ALA A  301  1                                  10    
HELIX   33  16 LEU A  311  ARG A  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 ARG B   9  PRO B  11  0                                        
SHEET    2   C 2 SER B  17  PRO B  19 -1  O  ILE B  18   N  ILE B  10           
SHEET    1   D 8 LEU B  23  GLY B  24  0                                        
SHEET    2   D 8 HIS B  51  ASP B  53  1  O  ASP B  53   N  LEU B  23           
SHEET    3   D 8 PHE B  83  LEU B  88  1  O  PHE B  83   N  ILE B  52           
SHEET    4   D 8 VAL B 114  ILE B 119  1  O  ILE B 118   N  LEU B  88           
SHEET    5   D 8 VAL B 163  SER B 169  1  O  GLY B 167   N  TYR B 117           
SHEET    6   D 8 SER B 191  GLU B 195  1  O  SER B 191   N  VAL B 168           
SHEET    7   D 8 VAL B 215  TYR B 219  1  O  TYR B 219   N  VAL B 194           
SHEET    8   D 8 VAL B 269  VAL B 270  1  O  VAL B 269   N  ALA B 218           
SITE     1 AC1 34 GLY B  24  THR B  25  TYR B  26  ASP B  53                    
SITE     2 AC1 34 TYR B  58  LYS B  87  SER B 169  ASN B 170                    
SITE     3 AC1 34 GLN B 193  TYR B 219  SER B 220  PRO B 221                    
SITE     4 AC1 34 LEU B 222  GLY B 223  THR B 224  SER B 225                    
SITE     5 AC1 34 LEU B 239  ALA B 256  ILE B 271  PRO B 272                    
SITE     6 AC1 34 LYS B 273  SER B 274  PHE B 275  ARG B 279                    
SITE     7 AC1 34 GLU B 282  ASN B 283  HOH B3941  HOH B3944                    
SITE     8 AC1 34 HOH B4019  HOH B4041  HOH B4074  HOH B4107                    
SITE     9 AC1 34 HOH B4125  HOH B4135                                          
SITE     1 AC2 37 GLY A  24  THR A  25  TYR A  26  ASP A  53                    
SITE     2 AC2 37 TYR A  58  SER A 169  ASN A 170  GLN A 193                    
SITE     3 AC2 37 TYR A 219  SER A 220  PRO A 221  LEU A 222                    
SITE     4 AC2 37 GLY A 223  THR A 224  SER A 225  LEU A 239                    
SITE     5 AC2 37 ALA A 256  ILE A 271  PRO A 272  LYS A 273                    
SITE     6 AC2 37 SER A 274  PHE A 275  ARG A 279  GLU A 282                    
SITE     7 AC2 37 ASN A 283  EPE A3999  HOH A4006  HOH A4038                    
SITE     8 AC2 37 HOH A4072  HOH A4095  HOH A4121  HOH A4148                    
SITE     9 AC2 37 HOH A4160  HOH A4174  HOH A4206  HOH A4230                    
SITE    10 AC2 37 HOH A4246                                                     
SITE     1 AC3 12 TYR A  26  ILE A  57  ILE A 131  TYR A 132                    
SITE     2 AC3 12 TRP A 230  VAL A 309  LEU A 311  NAP A3902                    
SITE     3 AC3 12 HOH A4158  HOH A4160  HOH A4174  HOH A4240                    
SITE     1 AC4  5 GLU A 103  ASP B 129  HOH B3923  HOH B4101                    
SITE     2 AC4  5 HOH B4137                                                     
SITE     1 AC5  6 ASP A 112  HOH A4053  MET B  97  PRO B 100                    
SITE     2 AC5  6 THR B 101  ARG B 104                                          
CRYST1   49.711  109.798  128.023  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      0.020116  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009108  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007811        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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