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Database: PDB
Entry: 3CAV
LinkDB: 3CAV
Original site: 3CAV 
HEADER    OXIDOREDUCTASE                          20-FEB-08   3CAV              
TITLE     CRYSTAL STRUCTURE OF 5BETA-REDUCTASE (AKR1D1) IN COMPLEX              
TITLE    2 WITH NADP+ AND 5BETA-PREGNAN-3,20-DIONE                              
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-              
COMPND   5 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 GENE: AKR1D1, SRD5B1;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;                             
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX6P1                                   
KEYWDS    5B-REDUCTASE, 5BETA-REDUCTASE, 5B-RED, AKR1D1, AKR, ALDO-             
KEYWDS   2 KETO REDUCTASE, NADP, ANDROSTENEDIONE. NADPH, MECHANISM,             
KEYWDS   3 BILE ACID CATABOLISM, CYTOPLASM, DISEASE MUTATION, LIPID             
KEYWDS   4 METABOLISM, OXIDOREDUCTASE, STEROID METABOLISM                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FAUCHER,L.CANTIN,R.BRETON                                           
REVDAT   3   24-FEB-09 3CAV    1       VERSN                                    
REVDAT   2   19-AUG-08 3CAV    1       JRNL                                     
REVDAT   1   29-JUL-08 3CAV    0                                                
JRNL        AUTH   F.FAUCHER,L.CANTIN,V.LUU-THE,F.LABRIE,R.BRETON               
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN                               
JRNL        TITL 2 DELTA4-3-KETOSTEROID 5BETA-REDUCTASE DEFINES THE             
JRNL        TITL 3 FUNCTIONAL ROLE OF THE RESIDUES OF THE CATALYTIC             
JRNL        TITL 4 TETRAD IN THE STEROID DOUBLE BOND REDUCTION                  
JRNL        TITL 5 MECHANISM.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  47  8261 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18624455                                                     
JRNL        DOI    10.1021/BI800572S                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2706142.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 55806                          
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) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2831                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9197                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3720                       
REMARK   3   BIN FREE R VALUE                    : 0.3950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 500                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5322                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 170                                     
REMARK   3   SOLVENT ATOMS            : 614                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.17000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 1.25000                                              
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) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
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) : 1.060 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.520 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.340 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 50.27                                                
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  : LIGANDS_.PARAM                                 
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : LIGANDS_.TOP                                   
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3CAV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046553.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55806                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.2400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.34                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.28300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-4000 20%, 0.1M NACACO, 0.2M          
REMARK 280  NACITRATE, 0.5M (NH4)2SO4, PH 6.5, VAPOR DIFFUSION, SITTING         
REMARK 280  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       25.32500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.44500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.63500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.44500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.32500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.63500            
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     1                                                      
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       32.03   -142.43                                   
REMARK 500    GLU A  28      107.19    -46.87                                   
REMARK 500    GLN A  59       -1.88     71.53                                   
REMARK 500    THR A 224      171.09     77.69                                   
REMARK 500    ASP B 135     -153.72    -74.23                                   
REMARK 500    ASN B 146       75.88   -153.61                                   
REMARK 500    THR B 224      172.70     76.25                                   
REMARK 500    TRP B 230       -3.65   -151.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 219         0.07    SIDE_CHAIN                              
REMARK 500    TYR B 219         0.08    SIDE_CHAIN                              
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 327                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 327                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CI2 A 328                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CI2 B 328                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 329                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 329                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 330                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 331                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 330                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 332                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 331                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CAQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CAS   RELATED DB: PDB                                   
DBREF  3CAV A    1   326  UNP    P51857   AK1D1_HUMAN      1    326             
DBREF  3CAV 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  A 327      48                                                       
HET    CI2  A 328      23                                                       
HET    BME  A 329       4                                                       
HET    EDO  A 330       4                                                       
HET    EDO  A 331       4                                                       
HET    EDO  A 332       4                                                       
HET    NAP  B 327      48                                                       
HET    CI2  B 328      23                                                       
HET    BME  B 329       4                                                       
HET    EDO  B 330       4                                                       
HET    EDO  B 331       4                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     CI2 (5BETA)-PREGNANE-3,20-DIONE                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  CI2    2(C21 H32 O2)                                                
FORMUL   5  BME    2(C2 H6 O S)                                                 
FORMUL   6  EDO    5(C2 H6 O2)                                                  
FORMUL  14  HOH   *614(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  GLU A   96  5                                   3    
HELIX    8   8 MET A   97  GLN A  110  1                                  14    
HELIX    9   9 ASN A  146  ALA A  160  1                                  15    
HELIX   10  10 ASN A  172  ASN A  181  1                                  10    
HELIX   11  11 GLN A  202  HIS A  212  1                                  11    
HELIX   12  12 PRO A  237  LYS A  240  5                                   4    
HELIX   13  13 ASP A  241  TYR A  251  1                                  11    
HELIX   14  14 THR A  254  ARG A  266  1                                  13    
HELIX   15  15 ASN A  276  GLN A  285  1                                  10    
HELIX   16  16 THR A  292  ALA A  301  1                                  10    
HELIX   17  17 LEU A  311  ARG A  315  5                                   5    
HELIX   18  18 GLU B   28  THR B   32  5                                   5    
HELIX   19  19 GLY B   35  GLY B   48  1                                  14    
HELIX   20  20 ALA B   55  GLN B   59  5                                   5    
HELIX   21  21 ASN B   60  GLU B   74  1                                  15    
HELIX   22  22 ARG B   78  ILE B   82  5                                   5    
HELIX   23  23 TRP B   89  HIS B   93  5                                   5    
HELIX   24  24 VAL B   94  GLU B   96  5                                   3    
HELIX   25  25 MET B   97  GLN B  110  1                                  14    
HELIX   26  26 ASN B  146  ALA B  160  1                                  15    
HELIX   27  27 ASN B  172  ASN B  181  1                                  10    
HELIX   28  28 GLN B  202  HIS B  212  1                                  11    
HELIX   29  29 PRO B  237  LYS B  240  5                                   4    
HELIX   30  30 ASP B  241  ASN B  252  1                                  12    
HELIX   31  31 THR B  254  ARG B  266  1                                  13    
HELIX   32  32 ASN B  276  ASN B  283  1                                   8    
HELIX   33  33 THR B  292  ALA B  301  1                                  10    
HELIX   34  34 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 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  LEU B 116   N  GLY B  86           
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           
SHEET    1   E 2 ALA B 124  PHE B 125  0                                        
SHEET    2   E 2 TYR B 142  HIS B 143 -1  O  HIS B 143   N  ALA B 124           
LINK         SG  CYS A 148                 S2  BME A 329     1555   1555  1.61  
SITE     1 AC1 25 GLY A  24  THR A  25  TYR A  26  ASP A  53                    
SITE     2 AC1 25 TYR A  58  SER A 169  ASN A 170  GLN A 193                    
SITE     3 AC1 25 TYR A 219  SER A 220  PRO A 221  LEU A 222                    
SITE     4 AC1 25 GLY A 223  THR A 224  SER A 225  LEU A 239                    
SITE     5 AC1 25 ALA A 256  ILE A 271  PRO A 272  LYS A 273                    
SITE     6 AC1 25 SER A 274  PHE A 275  ARG A 279  GLU A 282                    
SITE     7 AC1 25 ASN A 283                                                     
SITE     1 AC2 25 GLY B  24  THR B  25  TYR B  26  ASP B  53                    
SITE     2 AC2 25 TYR B  58  SER B 169  ASN B 170  GLN B 193                    
SITE     3 AC2 25 TYR B 219  SER B 220  PRO B 221  LEU B 222                    
SITE     4 AC2 25 GLY B 223  THR B 224  SER B 225  LEU B 239                    
SITE     5 AC2 25 ALA B 256  ILE B 271  PRO B 272  LYS B 273                    
SITE     6 AC2 25 SER B 274  PHE B 275  ARG B 279  GLU B 282                    
SITE     7 AC2 25 ASN B 283                                                     
SITE     1 AC3  7 TYR A  26  TYR A  58  GLU A 120  TRP A 230                    
SITE     2 AC3  7 LEU A 311  MET A 313  TRP A 314                               
SITE     1 AC4  3 TYR B  58  TYR B 132  TRP B 230                               
SITE     1 AC5  3 CYS B 148  LEU B 178  LYS B 182                               
SITE     1 AC6  2 ASN A 146  CYS A 148                                          
SITE     1 AC7  6 PRO A  95  GLU A  96  ARG A  99  PRO A 100                    
SITE     2 AC7  6 ALA A 153  ALA A 156                                          
SITE     1 AC8  5 ALA A   6  SER A   7  HIS A   8  ARG A   9                    
SITE     2 AC8  5 ARG A  50                                                     
SITE     1 AC9  4 ALA B   6  SER B   7  HIS B   8  ARG B   9                    
SITE     1 BC1  1 THR A 224                                                     
SITE     1 BC2  4 GLU B 152  GLU B 155  ALA B 156  LYS B 186                    
CRYST1   50.650  111.270  130.890  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      0.019743  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008987  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007640        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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