HEADER HORMONE/GROWTH FACTOR RECEPTOR 09-AUG-05 2AMB
TITLE CRYSTAL STRUCTURE OF HUMAN ANDROGEN RECEPTOR LIGAND BINDING DOMAIN IN
TITLE 2 COMPLEX WITH TETRAHYDROGESTRINONE
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
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)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS NUCLEAR RECEPTOR, ANDROGEN RECEPTOR, LIGAND BINDING DOMAIN, THG,
KEYWDS 2 AGONIST, DESIGNER ANDROGEN, HORMONE-GROWTH FACTOR RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.PEREIRA DE JESUS-TRAN,P.-L.COTE,L.CANTIN,J.BLANCHET,F.LABRIE,
AUTHOR 2 R.BRETON
REVDAT 4 23-AUG-23 2AMB 1 REMARK LINK
REVDAT 3 13-JUL-11 2AMB 1 VERSN
REVDAT 2 24-FEB-09 2AMB 1 VERSN
REVDAT 1 16-MAY-06 2AMB 0
JRNL AUTH K.PEREIRA DE JESUS-TRAN,P.-L.COTE,L.CANTIN,J.BLANCHET,
JRNL AUTH 2 F.LABRIE,R.BRETON
JRNL TITL COMPARISON OF CRYSTAL STRUCTURES OF HUMAN ANDROGEN RECEPTOR
JRNL TITL 2 LIGAND-BINDING DOMAIN COMPLEXED WITH VARIOUS AGONISTS
JRNL TITL 3 REVEALS MOLECULAR DETERMINANTS RESPONSIBLE FOR BINDING
JRNL TITL 4 AFFINITY.
JRNL REF PROTEIN SCI. V. 15 987 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16641486
JRNL DOI 10.1110/PS.051905906
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 25459
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) : 0.186
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1295
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 177
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1996
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.53500
REMARK 3 B22 (A**2) : 2.83000
REMARK 3 B33 (A**2) : 5.70500
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) : 0.20
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.029
REMARK 3 BOND ANGLES (DEGREES) : 2.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.490
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 57.69
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_CYS.PARAM
REMARK 3 PARAMETER FILE 2 : LIGLAST.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-04
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 II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25459
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 19.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
REMARK 200 R SYM FOR SHELL (I) : 0.28800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.010
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 2AMA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/K TARTRATE. MGSO4, HEPES, PH 6.5,
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 27.15500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.68500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.02000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.68500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.15500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.02000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 GLU A 654
REMARK 465 THR A 655
REMARK 465 THR A 656
REMARK 465 GLN A 657
REMARK 465 LYS A 658
REMARK 465 LEU A 659
REMARK 465 THR A 660
REMARK 465 VAL A 661
REMARK 465 SER A 662
REMARK 465 HIS A 663
REMARK 465 ILE A 664
REMARK 465 GLU A 665
REMARK 465 GLY A 666
REMARK 465 TYR A 667
REMARK 465 GLU A 668
REMARK 465 CYS A 669
REMARK 465 GLN A 670
REMARK 465 LYS A 847
REMARK 465 ASN A 848
REMARK 465 PRO A 849
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 822 CG CD CE NZ
REMARK 470 LYS A 845 CG CD CE NZ
REMARK 470 ARG A 854 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 893 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CA MET A 895 N ALA A 896 1.76
REMARK 500 CB CYS A 686 S1 DTT A 1003 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 843 C ALA A 843 O -0.188
REMARK 500 CYS A 852 C SER A 853 N -0.266
REMARK 500 MET A 894 C MET A 895 N -0.237
REMARK 500 MET A 895 C ALA A 896 N -0.360
REMARK 500 MET A 895 C ALA A 896 N -0.596
REMARK 500 ALA A 896 CA ALA A 896 CB -0.246
REMARK 500 HIS A 917 C THR A 918 N 0.303
REMARK 500 THR A 918 C THR A 918 O 0.152
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 686 CA - CB - SG ANGL. DEV. = 12.1 DEGREES
REMARK 500 ALA A 843 CA - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 ALA A 843 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 CYS A 844 N - CA - C ANGL. DEV. = 28.1 DEGREES
REMARK 500 THR A 850 CA - C - N ANGL. DEV. = -13.6 DEGREES
REMARK 500 MET A 895 CA - C - N ANGL. DEV. = -29.1 DEGREES
REMARK 500 MET A 895 O - C - N ANGL. DEV. = 12.9 DEGREES
REMARK 500 ALA A 896 C - N - CA ANGL. DEV. = -27.2 DEGREES
REMARK 500 THR A 918 CA - C - N ANGL. DEV. = -20.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 79.43 -150.73
REMARK 500 PHE A 813 40.92 -101.01
REMARK 500 CYS A 844 48.29 -46.51
REMARK 500 LYS A 845 -9.81 173.95
REMARK 500 SER A 888 18.24 59.36
REMARK 500 MET A 894 9.04 -56.88
REMARK 500 MET A 895 -13.20 -150.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET A 894 -10.62
REMARK 500 MET A 894 11.73
REMARK 500 MET A 895 -12.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EPE A 1004
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 17H A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AM9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANDROGEN RECEPTOR LIGAND BINDING DOMAIN
REMARK 900 IN COMPLEX WITH TESTOSTERONE
REMARK 900 RELATED ID: 2AMA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANDROGEN RECEPTOR LIGAND BINDING DOMAIN
REMARK 900 IN COMPLEX WITH DIHYDROTESTOSTERONE
DBREF 2AMB A 654 919 UNP P10275 ANDR_HUMAN 654 919
SEQRES 1 A 266 GLU THR THR GLN LYS LEU THR VAL SER HIS ILE GLU GLY
SEQRES 2 A 266 TYR GLU CYS GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA
SEQRES 3 A 266 ILE GLU PRO GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN
SEQRES 4 A 266 GLN PRO ASP SER PHE ALA ALA LEU LEU SER SER LEU ASN
SEQRES 5 A 266 GLU LEU GLY GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP
SEQRES 6 A 266 ALA LYS ALA LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP
SEQRES 7 A 266 ASP GLN MET ALA VAL ILE GLN TYR SER TRP MET GLY LEU
SEQRES 8 A 266 MET VAL PHE ALA MET GLY TRP ARG SER PHE THR ASN VAL
SEQRES 9 A 266 ASN SER ARG MET LEU TYR PHE ALA PRO ASP LEU VAL PHE
SEQRES 10 A 266 ASN GLU TYR ARG MET HIS LYS SER ARG MET TYR SER GLN
SEQRES 11 A 266 CYS VAL ARG MET ARG HIS LEU SER GLN GLU PHE GLY TRP
SEQRES 12 A 266 LEU GLN ILE THR PRO GLN GLU PHE LEU CYS MET LYS ALA
SEQRES 13 A 266 LEU LEU LEU PHE SER ILE ILE PRO VAL ASP GLY LEU LYS
SEQRES 14 A 266 ASN GLN LYS PHE PHE ASP GLU LEU ARG MET ASN TYR ILE
SEQRES 15 A 266 LYS GLU LEU ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN
SEQRES 16 A 266 PRO THR SER CYS SER ARG ARG PHE TYR GLN LEU THR LYS
SEQRES 17 A 266 LEU LEU ASP SER VAL GLN PRO ILE ALA ARG GLU LEU HIS
SEQRES 18 A 266 GLN PHE THR PHE ASP LEU LEU ILE LYS SER HIS MET VAL
SEQRES 19 A 266 SER VAL ASP PHE PRO GLU MET MET ALA GLU ILE ILE SER
SEQRES 20 A 266 VAL GLN VAL PRO LYS ILE LEU SER GLY LYS VAL LYS PRO
SEQRES 21 A 266 ILE TYR PHE HIS THR GLN
HET SO4 A1002 5
HET 17H A1001 23
HET DTT A1003 8
HET EPE A1004 12
HET GOL A1005 6
HETNAM SO4 SULFATE ION
HETNAM 17H 17-HYDROXY-18A-HOMO-19-NOR-17ALPHA-PREGNA-4,9,11-TRIEN-
HETNAM 2 17H 3-ONE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN DTT 1,4-DITHIOTHREITOL
HETSYN EPE HEPES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 17H C21 H28 O2
FORMUL 4 DTT C4 H10 O2 S2
FORMUL 5 EPE C8 H18 N2 O4 S
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *192(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 CYS A 844 1 22
HELIX 9 9 THR A 850 SER A 888 1 39
HELIX 10 10 PRO A 892 GLN A 902 1 11
HELIX 11 11 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
LINK SG CYS A 686 S1 DTT A1003 1555 1555 1.94
SITE 1 AC1 6 HOH A 65 SER A 696 PHE A 697 LYS A 777
SITE 2 AC1 6 ARG A 779 SER A 853
SITE 1 AC2 11 HOH A 4 LEU A 704 ASN A 705 LEU A 707
SITE 2 AC2 11 GLN A 711 TRP A 741 MET A 745 MET A 749
SITE 3 AC2 11 ARG A 752 THR A 877 LEU A 880
SITE 1 AC3 5 CYS A 686 PRO A 766 GLN A 798 ILE A 799
SITE 2 AC3 5 THR A 800
SITE 1 AC4 7 HOH A 130 HIS A 789 TRP A 796 LEU A 821
SITE 2 AC4 7 LYS A 822 ASN A 823 GLN A 824
SITE 1 AC5 9 HOH A 4 HOH A 9 HOH A 74 HOH A 129
SITE 2 AC5 9 HOH A 134 PRO A 682 GLN A 711 MET A 745
SITE 3 AC5 9 ARG A 752
CRYST1 54.310 66.040 71.370 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 0.018413 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
