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Database: PDB
Entry: 1XQ3
LinkDB: 1XQ3
Original site: 1XQ3 
HEADER    TRANSCRIPTION                           11-OCT-04   1XQ3              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN ANDROGEN RECEPTOR LIGAND               
TITLE    2 BINDING DOMAIN BOUND WITH R1881                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANDROGEN RECEPTOR;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN;                                     
COMPND   5 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: INHIBITED BY R1881                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AR, NR3C4;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 OTHER_DETAILS: HUMAN AR LBD (663-919) WITH THROMBIN                  
SOURCE  12 CLEAVABLE NH2-TERMINAL HIS TAG                                       
KEYWDS    CRYSTAL STRUCTURE; HUMAN ANDROGEN RECEPTOR LIGAND BINDING             
KEYWDS   2 DOMAIN; R1881, TRANSCRIPTION                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.HE,R.T.GAMPE JR.,A.J.KOLE,A.T.HNAT,T.B.STANLEY,G.AN,                
AUTHOR   2 E.L.STEWART,R.I.KALMAN,J.T.MINGES,E.M.WILSON                         
REVDAT   2   24-FEB-09 1XQ3    1       VERSN                                    
REVDAT   1   16-NOV-04 1XQ3    0                                                
JRNL        AUTH   B.HE,R.T.GAMPE JR.,A.J.KOLE,A.T.HNAT,T.B.STANLEY,            
JRNL        AUTH 2 G.AN,E.L.STEWART,R.I.KALMAN,J.T.MINGES,E.M.WILSON            
JRNL        TITL   STRUCTURAL BASIS FOR ANDROGEN RECEPTOR INTERDOMAIN           
JRNL        TITL 2 AND COACTIVATOR INTERACTIONS SUGGESTS A TRANSITION           
JRNL        TITL 3 IN NUCLEAR RECEPTOR ACTIVATION FUNCTION DOMINANCE            
JRNL        REF    MOL.CELL                      V.  16   425 2004              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   15525515                                                     
JRNL        DOI    10.1016/J.MOLCEL.2004.09.036                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2000                                             
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  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 270372.200                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12871                          
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 + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1326                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 12871                
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1670                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 189                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1988                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 77                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
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) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81                            
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) : 0.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.510 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.210 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 38.55                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : R18_XPLOR_PAR.TXT                              
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XQ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030633.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 326.8000                           
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX 2000                                              
REMARK 200 STARTING MODEL: 1XOW.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BTP, 0.6-1.2M LISO4, PH 8.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       28.44200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.31500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.91800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.31500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.44200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.91800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     CYS A   844                                                      
REMARK 465     LYS A   845                                                      
REMARK 465     ARG A   846                                                      
REMARK 465     LYS A   847                                                      
REMARK 465     ASN A   848                                                      
REMARK 465     PRO A   849                                                      
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    LEU A 768       69.71   -155.37                                   
REMARK 500    PHE A 813       41.36   -103.86                                   
REMARK 500    GLU A 893      -71.88    -42.85                                   
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 R18 A 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1I37   RELATED DB: PDB                                   
REMARK 900 ANDROGEN RECEPTOR LBD BOUND WITH DHT                                 
REMARK 900 RELATED ID: 1E3G   RELATED DB: PDB                                   
REMARK 900 ANDROGEN RECEPTOR LBD BOUND WITH R1881                               
REMARK 900 RELATED ID: 1XOW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1XQ2   RELATED DB: PDB                                   
DBREF  1XQ3 A  671   919  UNP    P10275   ANDR_HUMAN     671    919             
SEQRES   1 A  249  PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU PRO GLY          
SEQRES   2 A  249  VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO ASP SER          
SEQRES   3 A  249  PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU GLY GLU          
SEQRES   4 A  249  ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS ALA LEU          
SEQRES   5 A  249  PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN MET ALA          
SEQRES   6 A  249  VAL ILE GLN TYR SER TRP MET GLY LEU MET VAL PHE ALA          
SEQRES   7 A  249  MET GLY TRP ARG SER PHE THR ASN VAL ASN SER ARG MET          
SEQRES   8 A  249  LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU TYR ARG          
SEQRES   9 A  249  MET HIS LYS SER ARG MET TYR SER GLN CYS VAL ARG MET          
SEQRES  10 A  249  ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN ILE THR          
SEQRES  11 A  249  PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU LEU PHE          
SEQRES  12 A  249  SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN LYS PHE          
SEQRES  13 A  249  PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU LEU ASP          
SEQRES  14 A  249  ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR SER CYS          
SEQRES  15 A  249  SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU ASP SER          
SEQRES  16 A  249  VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE THR PHE          
SEQRES  17 A  249  ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL ASP PHE          
SEQRES  18 A  249  PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN VAL PRO          
SEQRES  19 A  249  LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR PHE HIS          
SEQRES  20 A  249  THR GLN                                                      
HET    R18  A1001      21                                                       
HETNAM     R18 (17BETA)-17-HYDROXY-17-METHYLESTRA-4,9,11-TRIEN-3-ONE            
HETSYN     R18 METHYLTRIENOLONE; 17BETA-HYDROXY-17METHYL-                       
HETSYN   2 R18  19NORANDROSTA-4,9,11-TRIEN-3-ONE; R1881                         
FORMUL   2  R18    C19 H24 O2                                                   
FORMUL   3  HOH   *77(H2 O)                                                     
HELIX    1   1 PRO A  671  GLU A  681  1                                  11    
HELIX    2   2 SER A  696  ALA A  721  1                                  26    
HELIX    3   3 GLY A  724  LEU A  728  5                                   5    
HELIX    4   4 HIS A  729  ASN A  758  1                                  30    
HELIX    5   5 ASN A  771  SER A  778  1                                   8    
HELIX    6   6 MET A  780  LEU A  797  1                                  18    
HELIX    7   7 THR A  800  PHE A  813  1                                  14    
HELIX    8   8 ASN A  823  ALA A  843  1                                  21    
HELIX    9   9 THR A  850  LYS A  883  1                                  34    
HELIX   10  10 LYS A  883  SER A  888  1                                   6    
HELIX   11  11 PRO A  892  GLN A  902  1                                  11    
HELIX   12  12 GLN A  902  SER A  908  1                                   7    
SHEET    1   A 2 LEU A 762  ALA A 765  0                                        
SHEET    2   A 2 LEU A 768  PHE A 770 -1  O  PHE A 770   N  LEU A 762           
SHEET    1   B 2 ILE A 815  PRO A 817  0                                        
SHEET    2   B 2 VAL A 911  PRO A 913 -1  O  LYS A 912   N  ILE A 816           
SITE     1 AC1 10 HOH A   4  LEU A 701  LEU A 704  ASN A 705                    
SITE     2 AC1 10 GLN A 711  MET A 742  MET A 745  MET A 749                    
SITE     3 AC1 10 ARG A 752  THR A 877                                          
CRYST1   56.884   65.836   72.630  90.00  90.00  90.00 P 21 21 21    4          
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      0.017580  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013768        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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