HEADER HUMAN PROGESTERONE RECEPTOR 19-JUN-00 1E3K
TITLE HUMAN PROGESTERON RECEPTOR LIGAND BINDING DOMAIN IN COMPLEX WITH THE
TITLE 2 LIGAND METRIBOLONE (R1881)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROGESTERONE RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HUMAN PROGESTERONE RECEPTOR, LIGAND BINDING DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.MATIAS,P.DONNER,R.COELHO,M.THOMAZ,C.PEIXOTO,S.MACEDO,N.OTTO,
AUTHOR 2 S.JOSCHKO,P.SCHOLZ,A.WEGG,S.BASLER,M.SCHAFER,U.EGNER,M.A.CARRONDO
REVDAT 6 13-DEC-23 1E3K 1 REMARK
REVDAT 5 08-MAY-19 1E3K 1 REMARK
REVDAT 4 28-FEB-18 1E3K 1 TITLE SOURCE JRNL
REVDAT 3 24-FEB-09 1E3K 1 VERSN
REVDAT 2 20-JAN-06 1E3K 1 COMPND
REVDAT 1 14-JUN-01 1E3K 0
JRNL AUTH P.M.MATIAS,P.DONNER,R.COELHO,M.THOMAZ,C.PEIXOTO,S.MACEDO,
JRNL AUTH 2 N.OTTO,S.JOSCHKO,P.SCHOLZ,A.WEGG,S.BASLER,M.SCHAFER,U.EGNER,
JRNL AUTH 3 M.A.CARRONDO
JRNL TITL STRUCTURAL EVIDENCE FOR LIGAND SPECIFICITY IN THE BINDING
JRNL TITL 2 DOMAIN OF THE HUMAN ANDROGEN RECEPTOR. IMPLICATIONS FOR
JRNL TITL 3 PATHOGENIC GENE MUTATIONS.
JRNL REF J. BIOL. CHEM. V. 275 26164 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10840043
JRNL DOI 10.1074/JBC.M004571200
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 67.0
REMARK 3 NUMBER OF REFLECTIONS : 8875
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.343
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4027
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.020 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.044 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: FINAL 2 C-TERMINAL RESIDUES NOT SEEN IN
REMARK 3 THE MAP
REMARK 4
REMARK 4 1E3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1290005073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI 111
REMARK 200 OPTICS : MIRRORS
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 : 8875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 12.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 67.0
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
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 1A28
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION: 10% ISO-PROPANOL,
REMARK 280 100MM SODIUM CITRATE 50MM HEPES PH 7.5. THE DROPS WERE SET UP
REMARK 280 USING THE HANGING DROP METHOD AND WERE COMPOSED OF A 2:1 RATIO
REMARK 280 OF PROTEIN AND RESERVOIR SOLUTIONS., PH 7.50, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.50550
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SER A 676
REMARK 465 PRO A 677
REMARK 465 GLY A 678
REMARK 465 GLN A 679
REMARK 465 ASP A 680
REMARK 465 ILE A 681
REMARK 465 LYS A 933
REMARK 465 SER B 676
REMARK 465 PRO B 677
REMARK 465 GLY B 678
REMARK 465 GLN B 679
REMARK 465 ASP B 680
REMARK 465 ILE B 681
REMARK 465 GLN B 682
REMARK 465 LYS B 932
REMARK 465 LYS B 933
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 GLN A 682 CG CD OE1 NE2
REMARK 470 ASP A 704 CG OD1 OD2
REMARK 470 ASN A 705 CG OD1 ND2
REMARK 470 THR A 706 OG1 CG2
REMARK 470 LYS A 707 CG CD CE NZ
REMARK 470 LYS A 790 CB CG CD CE NZ
REMARK 470 GLU A 791 CG CD OE1 OE2
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 GLU A 907 CD GLU A 907 OE2 -0.067
REMARK 500 SER B 735 CB SER B 735 OG -0.096
REMARK 500 GLU B 904 CD GLU B 904 OE2 0.066
REMARK 500 GLU B 907 CD GLU B 907 OE2 0.069
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 LEU A 690 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 MET A 692 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 TYR A 700 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 THR A 716 CA - CB - OG1 ANGL. DEV. = -13.5 DEGREES
REMARK 500 THR A 716 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU A 718 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU A 721 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 LEU A 721 CA - CB - CG ANGL. DEV. = -16.3 DEGREES
REMARK 500 LEU A 721 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY A 722 C - N - CA ANGL. DEV. = 15.4 DEGREES
REMARK 500 GLU A 723 OE1 - CD - OE2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLU A 723 O - C - N ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 724 CG - CD - NE ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 724 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 724 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU A 726 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 TRP A 732 N - CA - CB ANGL. DEV. = 16.5 DEGREES
REMARK 500 TRP A 732 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 TRP A 732 CD1 - NE1 - CE2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 TRP A 732 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP A 732 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 LYS A 734 O - C - N ANGL. DEV. = -13.2 DEGREES
REMARK 500 LEU A 736 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 PRO A 737 O - C - N ANGL. DEV. = -11.7 DEGREES
REMARK 500 LEU A 742 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 746 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 GLN A 747 OE1 - CD - NE2 ANGL. DEV. = -15.3 DEGREES
REMARK 500 THR A 749 OG1 - CB - CG2 ANGL. DEV. = 19.3 DEGREES
REMARK 500 LEU A 750 CB - CG - CD1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ILE A 751 O - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 GLN A 752 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 GLN A 752 CG - CD - OE1 ANGL. DEV. = 16.7 DEGREES
REMARK 500 GLN A 752 CG - CD - NE2 ANGL. DEV. = -19.1 DEGREES
REMARK 500 TYR A 753 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 TYR A 753 CD1 - CG - CD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 TYR A 753 CG - CD1 - CE1 ANGL. DEV. = -11.9 DEGREES
REMARK 500 TYR A 753 CD1 - CE1 - CZ ANGL. DEV. = 8.3 DEGREES
REMARK 500 SER A 757 O - C - N ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU A 758 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 MET A 759 C - N - CA ANGL. DEV. = 22.7 DEGREES
REMARK 500 MET A 759 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 VAL A 760 CA - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 VAL A 760 O - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 GLY A 764 O - C - N ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG A 766 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG A 766 CD - NE - CZ ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 766 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TYR A 768 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 HIS A 770 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 HIS A 770 CE1 - NE2 - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 254 ANGLE DEVIATIONS.
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 ASN A 705 -51.48 55.61
REMARK 500 THR A 706 -90.36 -8.25
REMARK 500 ASP A 709 123.48 -31.33
REMARK 500 TRP A 765 -72.05 -49.11
REMARK 500 GLN A 787 -95.75 -46.76
REMARK 500 ARG A 788 -30.69 -14.11
REMARK 500 LYS A 790 -71.27 -50.15
REMARK 500 GLU A 791 114.98 -36.02
REMARK 500 SER A 792 -95.55 -67.51
REMARK 500 SER A 793 -63.83 38.28
REMARK 500 GLN A 812 76.23 42.64
REMARK 500 SER A 837 51.18 -90.80
REMARK 500 GLN A 838 -70.91 -38.08
REMARK 500 ARG A 859 -52.75 -141.15
REMARK 500 VAL A 863 -29.17 -155.22
REMARK 500 HIS A 881 -73.10 -45.17
REMARK 500 PHE A 895 -83.09 -55.95
REMARK 500 ILE A 896 -54.79 -27.83
REMARK 500 LYS A 919 -57.93 -29.73
REMARK 500 MET A 924 52.07 -99.54
REMARK 500 ILE B 684 109.20 170.20
REMARK 500 PRO B 685 132.52 -36.13
REMARK 500 ASN B 705 -11.59 58.40
REMARK 500 ASP B 709 123.14 -33.68
REMARK 500 GLN B 720 -70.53 -27.90
REMARK 500 VAL B 771 19.63 -147.60
REMARK 500 SER B 772 3.28 85.63
REMARK 500 TYR B 777 66.88 -100.10
REMARK 500 GLN B 787 -88.73 -54.51
REMARK 500 ARG B 788 -55.08 -18.89
REMARK 500 MET B 789 -93.09 -39.81
REMARK 500 LYS B 790 -62.00 -5.13
REMARK 500 GLU B 791 46.52 -106.65
REMARK 500 SER B 793 5.88 98.09
REMARK 500 PHE B 794 27.10 -157.65
REMARK 500 GLN B 812 49.77 39.70
REMARK 500 CYS B 820 -36.86 -34.61
REMARK 500 SER B 837 36.57 -86.92
REMARK 500 GLN B 840 -60.80 -26.60
REMARK 500 ARG B 859 -66.15 -140.37
REMARK 500 GLN B 860 78.90 -63.95
REMARK 500 VAL B 863 -31.43 -156.00
REMARK 500 ASP B 882 -70.98 -30.08
REMARK 500 PHE B 895 -71.82 -64.11
REMARK 500 GLU B 907 -63.24 -5.64
REMARK 500 ALA B 922 7.49 -64.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 792 SER A 793 -132.99
REMARK 500 LYS A 861 GLY A 862 147.16
REMARK 500 LEU A 929 PHE A 930 148.47
REMARK 500 LYS B 861 GLY B 862 149.63
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 LEU A 687 -10.70
REMARK 500 PHE B 739 -12.03
REMARK 500 ALA B 915 11.73
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 A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R18 B1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A28 RELATED DB: PDB
REMARK 900 HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN
DBREF 1E3K A 676 933 UNP P06401 PRGR_HUMAN 676 933
DBREF 1E3K B 676 933 UNP P06401 PRGR_HUMAN 676 933
SEQRES 1 A 258 SER PRO GLY GLN ASP ILE GLN LEU ILE PRO PRO LEU ILE
SEQRES 2 A 258 ASN LEU LEU MET SER ILE GLU PRO ASP VAL ILE TYR ALA
SEQRES 3 A 258 GLY HIS ASP ASN THR LYS PRO ASP THR SER SER SER LEU
SEQRES 4 A 258 LEU THR SER LEU ASN GLN LEU GLY GLU ARG GLN LEU LEU
SEQRES 5 A 258 SER VAL VAL LYS TRP SER LYS SER LEU PRO GLY PHE ARG
SEQRES 6 A 258 ASN LEU HIS ILE ASP ASP GLN ILE THR LEU ILE GLN TYR
SEQRES 7 A 258 SER TRP MET SER LEU MET VAL PHE GLY LEU GLY TRP ARG
SEQRES 8 A 258 SER TYR LYS HIS VAL SER GLY GLN MET LEU TYR PHE ALA
SEQRES 9 A 258 PRO ASP LEU ILE LEU ASN GLU GLN ARG MET LYS GLU SER
SEQRES 10 A 258 SER PHE TYR SER LEU CYS LEU THR MET TRP GLN ILE PRO
SEQRES 11 A 258 GLN GLU PHE VAL LYS LEU GLN VAL SER GLN GLU GLU PHE
SEQRES 12 A 258 LEU CYS MET LYS VAL LEU LEU LEU LEU ASN THR ILE PRO
SEQRES 13 A 258 LEU GLU GLY LEU ARG SER GLN THR GLN PHE GLU GLU MET
SEQRES 14 A 258 ARG SER SER TYR ILE ARG GLU LEU ILE LYS ALA ILE GLY
SEQRES 15 A 258 LEU ARG GLN LYS GLY VAL VAL SER SER SER GLN ARG PHE
SEQRES 16 A 258 TYR GLN LEU THR LYS LEU LEU ASP ASN LEU HIS ASP LEU
SEQRES 17 A 258 VAL LYS GLN LEU HIS LEU TYR CYS LEU ASN THR PHE ILE
SEQRES 18 A 258 GLN SER ARG ALA LEU SER VAL GLU PHE PRO GLU MET MET
SEQRES 19 A 258 SER GLU VAL ILE ALA ALA GLN LEU PRO LYS ILE LEU ALA
SEQRES 20 A 258 GLY MET VAL LYS PRO LEU LEU PHE HIS LYS LYS
SEQRES 1 B 258 SER PRO GLY GLN ASP ILE GLN LEU ILE PRO PRO LEU ILE
SEQRES 2 B 258 ASN LEU LEU MET SER ILE GLU PRO ASP VAL ILE TYR ALA
SEQRES 3 B 258 GLY HIS ASP ASN THR LYS PRO ASP THR SER SER SER LEU
SEQRES 4 B 258 LEU THR SER LEU ASN GLN LEU GLY GLU ARG GLN LEU LEU
SEQRES 5 B 258 SER VAL VAL LYS TRP SER LYS SER LEU PRO GLY PHE ARG
SEQRES 6 B 258 ASN LEU HIS ILE ASP ASP GLN ILE THR LEU ILE GLN TYR
SEQRES 7 B 258 SER TRP MET SER LEU MET VAL PHE GLY LEU GLY TRP ARG
SEQRES 8 B 258 SER TYR LYS HIS VAL SER GLY GLN MET LEU TYR PHE ALA
SEQRES 9 B 258 PRO ASP LEU ILE LEU ASN GLU GLN ARG MET LYS GLU SER
SEQRES 10 B 258 SER PHE TYR SER LEU CYS LEU THR MET TRP GLN ILE PRO
SEQRES 11 B 258 GLN GLU PHE VAL LYS LEU GLN VAL SER GLN GLU GLU PHE
SEQRES 12 B 258 LEU CYS MET LYS VAL LEU LEU LEU LEU ASN THR ILE PRO
SEQRES 13 B 258 LEU GLU GLY LEU ARG SER GLN THR GLN PHE GLU GLU MET
SEQRES 14 B 258 ARG SER SER TYR ILE ARG GLU LEU ILE LYS ALA ILE GLY
SEQRES 15 B 258 LEU ARG GLN LYS GLY VAL VAL SER SER SER GLN ARG PHE
SEQRES 16 B 258 TYR GLN LEU THR LYS LEU LEU ASP ASN LEU HIS ASP LEU
SEQRES 17 B 258 VAL LYS GLN LEU HIS LEU TYR CYS LEU ASN THR PHE ILE
SEQRES 18 B 258 GLN SER ARG ALA LEU SER VAL GLU PHE PRO GLU MET MET
SEQRES 19 B 258 SER GLU VAL ILE ALA ALA GLN LEU PRO LYS ILE LEU ALA
SEQRES 20 B 258 GLY MET VAL LYS PRO LEU LEU PHE HIS LYS LYS
HET R18 A1000 21
HET R18 B1000 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 3 R18 2(C19 H24 O2)
FORMUL 5 HOH *(H2 O)
HELIX 1 1 PRO A 685 GLU A 695 1 11
HELIX 2 2 THR A 710 SER A 735 1 26
HELIX 3 3 GLY A 738 LEU A 742 5 5
HELIX 4 4 HIS A 743 VAL A 771 1 29
HELIX 5 5 PHE A 794 TRP A 802 1 9
HELIX 6 6 TRP A 802 GLN A 812 1 11
HELIX 7 7 SER A 814 LEU A 827 1 14
HELIX 8 8 SER A 837 GLY A 857 1 21
HELIX 9 9 VAL A 864 GLN A 897 1 34
HELIX 10 10 GLN A 897 SER A 902 1 6
HELIX 11 11 PRO A 906 ALA A 922 1 17
HELIX 12 12 PRO B 685 GLU B 695 1 11
HELIX 13 13 THR B 710 LEU B 736 1 27
HELIX 14 14 GLY B 738 LEU B 742 5 5
HELIX 15 15 HIS B 743 VAL B 771 1 29
HELIX 16 16 ASN B 785 GLU B 791 1 7
HELIX 17 17 PHE B 794 TRP B 802 1 9
HELIX 18 18 TRP B 802 GLN B 812 1 11
HELIX 19 19 SER B 814 LEU B 827 1 14
HELIX 20 20 SER B 837 GLY B 857 1 21
HELIX 21 21 VAL B 864 GLN B 897 1 34
HELIX 22 22 GLN B 897 SER B 902 1 6
HELIX 23 23 PRO B 906 ALA B 922 1 17
SHEET 1 A 2 LEU A 776 ALA A 779 0
SHEET 2 A 2 LEU A 782 LEU A 784 -1 O LEU A 782 N ALA A 779
SHEET 1 B 2 THR A 829 ILE A 830 0
SHEET 2 B 2 LYS A 926 PRO A 927 -1 O LYS A 926 N ILE A 830
SHEET 1 C 2 LEU B 776 ALA B 779 0
SHEET 2 C 2 LEU B 782 LEU B 784 -1 O LEU B 782 N ALA B 779
SHEET 1 D 2 THR B 829 ILE B 830 0
SHEET 2 D 2 LYS B 926 PRO B 927 -1 O LYS B 926 N ILE B 830
SITE 1 AC1 11 LEU A 718 ASN A 719 LEU A 721 GLN A 725
SITE 2 AC1 11 MET A 759 ARG A 766 PHE A 778 MET A 801
SITE 3 AC1 11 CYS A 891 MET A 909 HOH A2001
SITE 1 AC2 8 LEU B 718 ASN B 719 GLN B 725 MET B 759
SITE 2 AC2 8 ARG B 766 PHE B 778 TYR B 890 CYS B 891
CRYST1 58.402 65.011 71.181 90.00 95.65 90.00 P 1 21 1 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 0.017120 0.000000 0.001690 0.00000
SCALE2 0.000000 0.015380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014120 0.00000
MTRIX1 1 0.529830 0.829730 0.175610 3.26396 1
MTRIX2 1 0.836110 -0.545710 0.055790 -13.18369 1
MTRIX3 1 0.142120 0.117260 -0.982880 32.57034 1
(ATOM LINES ARE NOT SHOWN.)
END
