HEADER RECEPTOR 20-JAN-09 2W8Y
TITLE RU486 BOUND TO THE PROGESTERONE RECEPTOR IN A DESTABILIZED AGONISTIC
TITLE 2 CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROGESTERONE RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PR LBD, RESIDUES 678-933;
COMPND 5 SYNONYM: PR, NUCLEAR RECEPTOR SUBFAMILY 3 GROUP C MEMBER 3;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RECEPTOR, PROGESTERONE RECEPTOR, RU-486, MIFEPRISTONE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.C.A.RAAIJMAKERS,J.VERSTEEG,J.C.M.UITDEHAAG
REVDAT 4 27-DEC-17 2W8Y 1 AUTHOR REMARK
REVDAT 3 13-JUL-11 2W8Y 1 VERSN
REVDAT 2 21-JUL-09 2W8Y 1 JRNL
REVDAT 1 28-APR-09 2W8Y 0
JRNL AUTH H.C.A.RAAIJMAKERS,J.VERSTEEGH,J.C.M.UITDEHAAG
JRNL TITL THE X-RAY STRUCTURE OF RU486 BOUND TO THE PROGESTERONE
JRNL TITL 2 RECEPTOR IN A DESTABILIZED AGONISTIC CONFORMATION.
JRNL REF J.BIOL.CHEM. V. 284 19572 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19372222
JRNL DOI 10.1074/JBC.M109.007872
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0078
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 43248
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2333
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2393
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.4180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4265 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2934 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5790 ; 1.082 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7210 ; 0.844 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 515 ; 4.817 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;34.596 ;24.407
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 803 ;13.045 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;10.728 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 664 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4568 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 820 ; 0.002 ; 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): 2540 ; 1.064 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4134 ; 1.747 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1725 ; 1.230 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1650 ; 1.926 ; 3.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 683 A 933
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4010 -0.0170 2.0110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1048 T22: 0.1354
REMARK 3 T33: 0.0350 T12: -0.0091
REMARK 3 T13: 0.0248 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.9737 L22: 1.8174
REMARK 3 L33: 1.5617 L12: 0.2356
REMARK 3 L13: -0.3644 L23: 0.6069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: -0.0706 S13: 0.0742
REMARK 3 S21: 0.0926 S22: 0.0147 S23: 0.0503
REMARK 3 S31: -0.0126 S32: 0.1387 S33: -0.0459
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 683 B 933
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0660 12.3560 -33.0040
REMARK 3 T TENSOR
REMARK 3 T11: 0.1501 T22: 0.0651
REMARK 3 T33: 0.0206 T12: 0.0063
REMARK 3 T13: 0.0537 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.2838 L22: 2.0964
REMARK 3 L33: 1.4236 L12: -0.3148
REMARK 3 L13: 0.1800 L23: -0.3394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0543 S12: -0.0672 S13: -0.0615
REMARK 3 S21: 0.1313 S22: 0.0174 S23: -0.0349
REMARK 3 S31: 0.0746 S32: -0.0264 S33: 0.0370
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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. U VALUES RESIDUAL ONLY. THE DIMETHYLAMINOREMARK A909.
REMARK 3 IN REALITY WE PROBABLY OBSERVE THE AVERAGE OF AN ENSEMBLE OF
REMARK 3 SUBTLY DIFFERENT DIMETHYLANILINE AND MET909 ORIENTATIONS, EACH
REMARK 3 STERICALLY ALLOWED. FOR THE FINAL REFINEMENT I SET THE OCCUPANCY
REMARK 3 OF M909 SIDECHAIN TO 0, TO IMPROVE THE FIT OF THE
REMARK 3 DIMETHYLANILINE TO THE ELECTRON DENSITY.
REMARK 4
REMARK 4 2W8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1290038546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45609
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG4000, 0.1M HEPES 6.5, 100 MM
REMARK 280 LI2SO4, PH 6.5
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 31.94850
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 GLY A 674
REMARK 465 SER A 675
REMARK 465 HIS A 676
REMARK 465 MET A 677
REMARK 465 GLY A 678
REMARK 465 GLN A 679
REMARK 465 ASP A 680
REMARK 465 ILE A 681
REMARK 465 GLN A 682
REMARK 465 GLY B 674
REMARK 465 SER B 675
REMARK 465 HIS B 676
REMARK 465 MET 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 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 932 CG CD CE NZ
REMARK 470 LYS A 933 CA C O CB CG CD CE
REMARK 470 LYS A 933 NZ
REMARK 470 LYS B 932 CG CD CE NZ
REMARK 470 LYS B 933 CA C O CB CG CD CE
REMARK 470 LYS B 933 NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 909 CB CG SD CE
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 SER A 793 -15.77 99.98
REMARK 500 PHE A 794 52.42 -142.55
REMARK 500 SER A 837 51.44 -102.11
REMARK 500 GLN A 916 -16.23 -150.00
REMARK 500 MET A 924 42.10 -93.77
REMARK 500 LYS A 932 -85.75 -77.47
REMARK 500 LEU B 782 78.37 -150.91
REMARK 500 MET B 789 68.78 -108.41
REMARK 500 SER B 837 49.98 -102.17
REMARK 500 GLN B 916 -15.78 -140.93
REMARK 500 MET B 924 41.96 -91.83
REMARK 500 LYS B 932 -165.57 -68.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 NORETHINDRONE (NDR): ALSO KNOWN AS NORETHISTERONE
REMARK 600 MIFEPRISTONE (486): RU486, 11BETA-4-N,
REMARK 600 N-DIMETHYLAMINOPHENYL-17ALPHA-PROP-1-YNYL-DELTA4,
REMARK 600 9-ESTRADIENE-17BETA-OL-3-ONE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 486 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDR B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1934
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1934
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C7A RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX
REMARK 900 RELATED ID: 1A28 RELATED DB: PDB
REMARK 900 HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN
REMARK 900 RELATED ID: 1ZUC RELATED DB: PDB
REMARK 900 PROGESTERONE RECEPTOR LIGAND BINDING DOMAIN IN COMPLEX WITHTHE
REMARK 900 NONSTEROIDAL AGONIST TANAPROGET
REMARK 900 RELATED ID: 1SQN RELATED DB: PDB
REMARK 900 PROGESTERONE RECEPTOR LIGAND BINDING DOMAIN WITH BOUNDNORETHINDRONE
REMARK 900 RELATED ID: 1SR7 RELATED DB: PDB
REMARK 900 PROGESTERONE RECEPTOR HORMONE BINDING DOMAIN WITH BOUNDMOMETASONE
REMARK 900 FUROATE
REMARK 900 RELATED ID: 1E3K RELATED DB: PDB
REMARK 900 HUMAN PROGESTERON RECEPTOR LIGAND BINDING DOMAIN IN COMPLEX WITH
REMARK 900 THE LIGAND METRIBOLONE (R1881)
DBREF 2W8Y A 674 677 PDB 2W8Y 2W8Y 674 677
DBREF 2W8Y A 678 933 UNP P06401 PRGR_HUMAN 678 933
DBREF 2W8Y B 674 677 PDB 2W8Y 2W8Y 674 677
DBREF 2W8Y B 678 933 UNP P06401 PRGR_HUMAN 678 933
SEQRES 1 A 260 GLY SER HIS MET GLY GLN ASP ILE GLN LEU ILE PRO PRO
SEQRES 2 A 260 LEU ILE ASN LEU LEU MET SER ILE GLU PRO ASP VAL ILE
SEQRES 3 A 260 TYR ALA GLY HIS ASP ASN THR LYS PRO ASP THR SER SER
SEQRES 4 A 260 SER LEU LEU THR SER LEU ASN GLN LEU GLY GLU ARG GLN
SEQRES 5 A 260 LEU LEU SER VAL VAL LYS TRP SER LYS SER LEU PRO GLY
SEQRES 6 A 260 PHE ARG ASN LEU HIS ILE ASP ASP GLN ILE THR LEU ILE
SEQRES 7 A 260 GLN TYR SER TRP MET SER LEU MET VAL PHE GLY LEU GLY
SEQRES 8 A 260 TRP ARG SER TYR LYS HIS VAL SER GLY GLN MET LEU TYR
SEQRES 9 A 260 PHE ALA PRO ASP LEU ILE LEU ASN GLU GLN ARG MET LYS
SEQRES 10 A 260 GLU SER SER PHE TYR SER LEU CYS LEU THR MET TRP GLN
SEQRES 11 A 260 ILE PRO GLN GLU PHE VAL LYS LEU GLN VAL SER GLN GLU
SEQRES 12 A 260 GLU PHE LEU CYS MET LYS VAL LEU LEU LEU LEU ASN THR
SEQRES 13 A 260 ILE PRO LEU GLU GLY LEU ARG SER GLN THR GLN PHE GLU
SEQRES 14 A 260 GLU MET ARG SER SER TYR ILE ARG GLU LEU ILE LYS ALA
SEQRES 15 A 260 ILE GLY LEU ARG GLN LYS GLY VAL VAL SER SER SER GLN
SEQRES 16 A 260 ARG PHE TYR GLN LEU THR LYS LEU LEU ASP ASN LEU HIS
SEQRES 17 A 260 ASP LEU VAL LYS GLN LEU HIS LEU TYR CYS LEU ASN THR
SEQRES 18 A 260 PHE ILE GLN SER ARG ALA LEU SER VAL GLU PHE PRO GLU
SEQRES 19 A 260 MET MET SER GLU VAL ILE ALA ALA GLN LEU PRO LYS ILE
SEQRES 20 A 260 LEU ALA GLY MET VAL LYS PRO LEU LEU PHE HIS LYS LYS
SEQRES 1 B 260 GLY SER HIS MET GLY GLN ASP ILE GLN LEU ILE PRO PRO
SEQRES 2 B 260 LEU ILE ASN LEU LEU MET SER ILE GLU PRO ASP VAL ILE
SEQRES 3 B 260 TYR ALA GLY HIS ASP ASN THR LYS PRO ASP THR SER SER
SEQRES 4 B 260 SER LEU LEU THR SER LEU ASN GLN LEU GLY GLU ARG GLN
SEQRES 5 B 260 LEU LEU SER VAL VAL LYS TRP SER LYS SER LEU PRO GLY
SEQRES 6 B 260 PHE ARG ASN LEU HIS ILE ASP ASP GLN ILE THR LEU ILE
SEQRES 7 B 260 GLN TYR SER TRP MET SER LEU MET VAL PHE GLY LEU GLY
SEQRES 8 B 260 TRP ARG SER TYR LYS HIS VAL SER GLY GLN MET LEU TYR
SEQRES 9 B 260 PHE ALA PRO ASP LEU ILE LEU ASN GLU GLN ARG MET LYS
SEQRES 10 B 260 GLU SER SER PHE TYR SER LEU CYS LEU THR MET TRP GLN
SEQRES 11 B 260 ILE PRO GLN GLU PHE VAL LYS LEU GLN VAL SER GLN GLU
SEQRES 12 B 260 GLU PHE LEU CYS MET LYS VAL LEU LEU LEU LEU ASN THR
SEQRES 13 B 260 ILE PRO LEU GLU GLY LEU ARG SER GLN THR GLN PHE GLU
SEQRES 14 B 260 GLU MET ARG SER SER TYR ILE ARG GLU LEU ILE LYS ALA
SEQRES 15 B 260 ILE GLY LEU ARG GLN LYS GLY VAL VAL SER SER SER GLN
SEQRES 16 B 260 ARG PHE TYR GLN LEU THR LYS LEU LEU ASP ASN LEU HIS
SEQRES 17 B 260 ASP LEU VAL LYS GLN LEU HIS LEU TYR CYS LEU ASN THR
SEQRES 18 B 260 PHE ILE GLN SER ARG ALA LEU SER VAL GLU PHE PRO GLU
SEQRES 19 B 260 MET MET SER GLU VAL ILE ALA ALA GLN LEU PRO LYS ILE
SEQRES 20 B 260 LEU ALA GLY MET VAL LYS PRO LEU LEU PHE HIS LYS LYS
HET 486 A1000 32
HET SO4 A1934 5
HET NDR B1000 22
HET EDO B1934 4
HETNAM 486 11-(4-DIMETHYLAMINO-PHENYL)-17-HYDROXY-13-METHYL-17-
HETNAM 2 486 PROP-1-YNYL-1,2,6,7,8,11,12,13,14,15,16,17-DODEC
HETNAM 3 486 AHYDRO-CYCLOPENTA[A]PHENANTHREN-3-ONE
HETNAM SO4 SULFATE ION
HETNAM NDR (14BETA,17ALPHA)-17-ETHYNYL-17-HYDROXYESTR-4-EN-3-ONE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN 486 RU-486, MIFEPRISTONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 486 C29 H35 N O2
FORMUL 4 SO4 O4 S 2-
FORMUL 5 NDR C20 H26 O2
FORMUL 6 EDO C2 H6 O2
FORMUL 7 HOH *200(H2 O)
HELIX 1 1 PRO A 685 ILE A 694 1 10
HELIX 2 2 THR A 710 LEU A 736 1 27
HELIX 3 3 GLY A 738 LEU A 742 5 5
HELIX 4 4 HIS A 743 SER A 772 1 30
HELIX 5 5 ASN A 785 GLU A 791 1 7
HELIX 6 6 PHE A 794 GLN A 812 1 19
HELIX 7 7 SER A 814 LEU A 827 1 14
HELIX 8 8 SER A 837 LEU A 858 1 22
HELIX 9 9 GLY A 862 GLN A 897 1 36
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 ILE B 694 1 10
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 SER B 772 1 30
HELIX 16 16 ASN B 785 MET B 789 5 5
HELIX 17 17 GLU B 791 GLN B 812 1 22
HELIX 18 18 SER B 814 LEU B 827 1 14
HELIX 19 19 SER B 837 LEU B 858 1 22
HELIX 20 20 GLY B 862 GLN B 897 1 36
HELIX 21 21 GLN B 897 SER B 902 1 6
HELIX 22 22 PRO B 906 ALA B 922 1 17
SHEET 1 AA 2 LEU A 776 ALA A 779 0
SHEET 2 AA 2 LEU A 782 LEU A 784 -1 O LEU A 782 N ALA A 779
SHEET 1 AB 2 THR A 829 ILE A 830 0
SHEET 2 AB 2 LYS A 926 PRO A 927 -1 O LYS A 926 N ILE A 830
SHEET 1 BA 2 LEU B 776 ALA B 779 0
SHEET 2 BA 2 LEU B 782 LEU B 784 -1 O LEU B 782 N ALA B 779
SHEET 1 BB 2 THR B 829 PRO B 831 0
SHEET 2 BB 2 VAL B 925 PRO B 927 -1 O LYS B 926 N ILE B 830
SITE 1 AC1 18 LEU A 715 LEU A 718 ASN A 719 LEU A 721
SITE 2 AC1 18 GLY A 722 GLU A 723 GLN A 725 TRP A 755
SITE 3 AC1 18 MET A 756 MET A 759 ARG A 766 PHE A 794
SITE 4 AC1 18 LEU A 797 MET A 801 TYR A 890 CYS A 891
SITE 5 AC1 18 MET A 909 HOH A2016
SITE 1 AC2 10 LEU B 715 LEU B 718 ASN B 719 GLN B 725
SITE 2 AC2 10 MET B 756 MET B 759 ARG B 766 MET B 801
SITE 3 AC2 10 TYR B 890 CYS B 891
SITE 1 AC3 3 TRP B 765 HIS B 770 GLN B 815
SITE 1 AC4 5 PRO A 737 GLY A 738 ARG A 740 ASN A 741
SITE 2 AC4 5 HOH A2106
CRYST1 58.164 63.897 70.051 90.00 95.57 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 0.017193 0.000000 0.001677 0.00000
SCALE2 0.000000 0.015650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014343 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
