HEADER HORMONE RECEPTOR/PEPTIDE 15-JAN-14 4OFR
TITLE CRYSTAL STRUCTURE OF AR-LBD BOUND WITH CO-REGULATOR PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANDROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR, NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 6 GROUP C MEMBER 4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CO-REGULATOR PEPTIDE;
COMPND 11 CHAIN: B;
COMPND 12 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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630
KEYWDS ALPHA-HELIX, HORMONE/GROWTH FACTOR RECEPTOR, PHOSPHORYLATION, HORMONE
KEYWDS 2 RECEPTOR-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.LIU,C.L.HSU,W.G.WU
REVDAT 3 20-SEP-23 4OFR 1 REMARK SEQADV
REVDAT 2 24-DEC-14 4OFR 1 JRNL
REVDAT 1 20-AUG-14 4OFR 0
JRNL AUTH C.L.HSU,J.S.LIU,P.L.WU,H.H.GUAN,Y.L.CHEN,A.C.LIN,H.J.TING,
JRNL AUTH 2 S.T.PANG,S.D.YEH,W.L.MA,C.J.CHEN,W.G.WU,C.CHANG
JRNL TITL IDENTIFICATION OF A NEW ANDROGEN RECEPTOR (AR) CO-REGULATOR
JRNL TITL 2 BUD31 AND RELATED PEPTIDES TO SUPPRESS WILD-TYPE AND MUTATED
JRNL TITL 3 AR-MEDIATED PROSTATE CANCER GROWTH VIA PEPTIDE SCREENING AND
JRNL TITL 4 X-RAY STRUCTURE ANALYSIS.
JRNL REF MOL ONCOL V. 8 1575 2014
JRNL REFN
JRNL PMID 25091737
JRNL DOI 10.1016/J.MOLONC.2014.06.009
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 11327
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 576
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) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 545
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.85000
REMARK 3 B22 (A**2) : -4.18000
REMARK 3 B33 (A**2) : -3.67000
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): 0.415
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.260
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.247
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.755
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2195 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2128 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2969 ; 1.519 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4884 ; 0.827 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 255 ; 7.358 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;33.112 ;23.301
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 390 ;16.646 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.282 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 324 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2410 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 537 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4OFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 150
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : 1.0
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 : 11769
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 25.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07000
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 4OEA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M MAGNESIUM SULPHATE, 0.1M MES, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 27.87550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.55050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.55050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.87550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.11500
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: 1710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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 GLN A 670
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 GLN A 919
REMARK 465 ALA B -1
REMARK 465 ASN B 0
REMARK 465 SER B 9
REMARK 465 SER B 10
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 VAL A 757 22.75 -140.73
REMARK 500 ASN A 758 44.32 23.20
REMARK 500 LEU A 768 72.47 -155.48
REMARK 500 CYS A 852 1.06 -56.56
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 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OEA RELATED DB: PDB
REMARK 900 RELATED ID: 4OED RELATED DB: PDB
REMARK 900 RELATED ID: 4OEY RELATED DB: PDB
REMARK 900 RELATED ID: 4OEZ RELATED DB: PDB
REMARK 900 RELATED ID: 4OFU RELATED DB: PDB
REMARK 900 RELATED ID: 4OGH RELATED DB: PDB
REMARK 900 RELATED ID: 4OH5 RELATED DB: PDB
REMARK 900 RELATED ID: 4OH6 RELATED DB: PDB
REMARK 900 RELATED ID: 4OHA RELATED DB: PDB
REMARK 900 RELATED ID: 4OIL RELATED DB: PDB
REMARK 900 RELATED ID: 4OIU RELATED DB: PDB
REMARK 900 RELATED ID: 4OJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 4OJB RELATED DB: PDB
REMARK 900 RELATED ID: 4OK1 RELATED DB: PDB
REMARK 900 RELATED ID: 4OKB RELATED DB: PDB
REMARK 900 RELATED ID: 4OKT RELATED DB: PDB
REMARK 900 RELATED ID: 4OKW RELATED DB: PDB
REMARK 900 RELATED ID: 4OKX RELATED DB: PDB
REMARK 900 RELATED ID: 4OLM RELATED DB: PDB
DBREF 4OFR A 670 919 UNP P10275 ANDR_HUMAN 670 919
DBREF 4OFR B -1 10 PDB 4OFR 4OFR -1 10
SEQADV 4OFR ALA A 760 UNP P10275 ARG 760 ENGINEERED MUTATION
SEQRES 1 A 250 GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU PRO
SEQRES 2 A 250 GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO ASP
SEQRES 3 A 250 SER PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU GLY
SEQRES 4 A 250 GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS ALA
SEQRES 5 A 250 LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN MET
SEQRES 6 A 250 ALA VAL ILE GLN TYR SER TRP MET GLY LEU MET VAL PHE
SEQRES 7 A 250 ALA MET GLY TRP ARG SER PHE THR ASN VAL ASN SER ALA
SEQRES 8 A 250 MET LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU TYR
SEQRES 9 A 250 ARG MET HIS LYS SER ARG MET TYR SER GLN CYS VAL ARG
SEQRES 10 A 250 MET ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN ILE
SEQRES 11 A 250 THR PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU LEU
SEQRES 12 A 250 PHE SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN LYS
SEQRES 13 A 250 PHE PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU LEU
SEQRES 14 A 250 ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR SER
SEQRES 15 A 250 CYS SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU ASP
SEQRES 16 A 250 SER VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE THR
SEQRES 17 A 250 PHE ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL ASP
SEQRES 18 A 250 PHE PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN VAL
SEQRES 19 A 250 PRO LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR PHE
SEQRES 20 A 250 HIS THR GLN
SEQRES 1 B 12 ALA ASN SER SER PHE ARG ASP TRP TYR THR SER SER
HET DHT A1001 21
HETNAM DHT 5-ALPHA-DIHYDROTESTOSTERONE
FORMUL 3 DHT C19 H30 O2
FORMUL 4 HOH *50(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
HELIX 13 13 SER B 2 THR B 8 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 7 LEU A 704 ASN A 705 GLN A 711 ARG A 752
SITE 2 AC1 7 PHE A 764 THR A 877 HOH A1104
CRYST1 55.751 66.230 71.101 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 0.017937 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015099 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
