HEADER PROTEIN BINDING 18-DEC-09 3L3X
TITLE CRYSTAL STRUCTURE OF DHT-BOUND ANDROGEN RECEPTOR IN COMPLEX WITH THE
TITLE 2 FIRST MOTIF OF STEROID RECEPTOR COACTIVATOR 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANDROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR, NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 5 GROUP C MEMBER 4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 3;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AR, DHTR, NR3C4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS ANDROGEN RECEPTOR, LIGAND BINDING DOMAIN, STEROID RECEPTOR
KEYWDS 2 COACTIVATOR 3, 5-ALPHA-DIHYDROTESTOSTERONE (DHT), PROSTATE CANCER,
KEYWDS 3 PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,K.M.SUINO-POWELL,J.LI,A.HE,J.P.MACKEIGAN,K.MELCHER,E.-
AUTHOR 2 L.YONG,H.E.XU
REVDAT 4 01-NOV-17 3L3X 1 REMARK
REVDAT 3 31-MAR-10 3L3X 1 JRNL
REVDAT 2 02-FEB-10 3L3X 1 JRNL
REVDAT 1 12-JAN-10 3L3X 0
JRNL AUTH X.E.ZHOU,K.M.SUINO-POWELL,J.LI,Y.HE,J.P.MACKEIGAN,K.MELCHER,
JRNL AUTH 2 E.L.YONG,H.E.XU
JRNL TITL IDENTIFICATION OF SRC3/AIB1 AS A PREFERRED COACTIVATOR FOR
JRNL TITL 2 HORMONE-ACTIVATED ANDROGEN RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 285 9161 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20086010
JRNL DOI 10.1074/JBC.M109.085779
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 37974
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2927
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2601
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.32000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -1.43000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.121
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2213 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1548 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2993 ; 1.253 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3771 ; 0.888 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 260 ; 3.886 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;30.852 ;23.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 404 ;12.548 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;10.547 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2371 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 455 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1311 ; 1.407 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 519 ; 0.421 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2127 ; 2.466 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 902 ; 3.295 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 866 ; 4.989 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3761 ; 1.635 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 211 ; 9.433 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3706 ; 3.556 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3L3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-06
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 : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38124
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.42800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, PH 7.5, VAPOR DIFFUSION,
REMARK 280 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 28.65700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.56850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.35200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.56850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.65700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.35200
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 671 -158.19 -82.70
REMARK 500 ILE A 672 -45.65 -151.45
REMARK 500 LEU A 768 76.79 -150.51
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 DHT A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L3Z RELATED DB: PDB
DBREF 3L3X A 670 918 UNP P10275 ANDR_HUMAN 670 918
DBREF 3L3X B 618 629 UNP Q9Y6Q9 NCOA3_HUMAN 618 629
SEQADV 3L3X SER A 669 UNP P10275 EXPRESSION TAG
SEQRES 1 A 250 SER GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU
SEQRES 2 A 250 PRO GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO
SEQRES 3 A 250 ASP SER PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU
SEQRES 4 A 250 GLY GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS
SEQRES 5 A 250 ALA LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN
SEQRES 6 A 250 MET ALA VAL ILE GLN TYR SER TRP MET GLY LEU MET VAL
SEQRES 7 A 250 PHE ALA MET GLY TRP ARG SER PHE THR ASN VAL ASN SER
SEQRES 8 A 250 ARG MET LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU
SEQRES 9 A 250 TYR ARG MET HIS LYS SER ARG MET TYR SER GLN CYS VAL
SEQRES 10 A 250 ARG MET ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN
SEQRES 11 A 250 ILE THR PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU
SEQRES 12 A 250 LEU PHE SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN
SEQRES 13 A 250 LYS PHE PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU
SEQRES 14 A 250 LEU ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR
SEQRES 15 A 250 SER CYS SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU
SEQRES 16 A 250 ASP SER VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE
SEQRES 17 A 250 THR PHE ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL
SEQRES 18 A 250 ASP PHE PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN
SEQRES 19 A 250 VAL PRO LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR
SEQRES 20 A 250 PHE HIS THR
SEQRES 1 B 12 HIS LYS LYS LEU LEU GLN LEU LEU THR CYS SER SER
HET DHT A 1 21
HETNAM DHT 5-ALPHA-DIHYDROTESTOSTERONE
FORMUL 3 DHT C19 H30 O2
FORMUL 4 HOH *211(H2 O)
HELIX 1 1 ILE A 672 GLU A 681 1 10
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 LEU A 812 1 13
HELIX 8 8 ASN A 823 ILE A 842 1 20
HELIX 9 9 ASN A 848 LYS A 883 1 36
HELIX 10 10 PRO A 892 GLN A 902 1 11
HELIX 11 11 GLN A 902 SER A 908 1 7
HELIX 12 12 HIS B 618 CYS B 627 1 10
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
SSBOND 1 CYS A 844 CYS A 852 1555 1555 2.05
SITE 1 AC1 7 LEU A 704 ASN A 705 GLN A 711 MET A 745
SITE 2 AC1 7 MET A 749 ARG A 752 THR A 877
CRYST1 57.314 66.704 73.137 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 0.017448 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013673 0.00000
(ATOM LINES ARE NOT SHOWN.)
END