HEADER NUCLEAR RECEPTOR 28-JAN-05 2BJ4
TITLE ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED
TITLE 2 PEPTIDE ANTAGONIST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 305-533 (LIGAND-BINDING DOMAIN);
COMPND 5 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ESTROGEN RECEPTOR;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 305-533 (LIGAND-BINDING DOMAIN);
COMPND 11 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PEPTIDE ANTAGONIST;
COMPND 15 CHAIN: C, D;
COMPND 16 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;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 20 ORGANISM_TAXID: 32630
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, PEPTIDE ANTAGONIST, LIGAND-
KEYWDS 2 BINDING DOMAIN (LBD), DNA-BINDING, NUCLEAR PROTEIN STEROID-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR E.KONG,N.HELDRING,J.A.GUSTAFSSON,E.TREUTER,R.E.HUBBARD,A.C.W.PIKE
REVDAT 7 13-DEC-23 2BJ4 1 REMARK LINK
REVDAT 6 24-JAN-18 2BJ4 1 SOURCE
REVDAT 5 13-JUL-11 2BJ4 1 VERSN
REVDAT 4 02-FEB-10 2BJ4 1 VERSN
REVDAT 3 24-FEB-09 2BJ4 1 VERSN
REVDAT 2 16-MAR-05 2BJ4 1 JRNL
REVDAT 1 16-FEB-05 2BJ4 0
JRNL AUTH E.KONG,N.HELDRING,J.A.GUSTAFSSON,E.TREUTER,R.E.HUBBARD,
JRNL AUTH 2 A.C.W.PIKE
JRNL TITL DELINEATION OF A UNIQUE PROTEIN-PROTEIN INTERACTION SITE ON
JRNL TITL 2 THE SURFACE OF THE ESTROGEN RECEPTOR
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 3593 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15728727
JRNL DOI 10.1073/PNAS.0407189102
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0000
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 32933
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1725
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1905
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.2190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3649
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.01000
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): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3817 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3595 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5156 ; 1.378 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8256 ; 0.838 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 455 ; 5.366 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;36.003 ;24.037
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 691 ;15.759 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;17.796 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 597 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4108 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 722 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 918 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3493 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2194 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.146 ; 0.200
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): 14 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.209 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.194 ; 0.200
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): 2507 ; 0.965 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3699 ; 1.358 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1652 ; 2.162 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1457 ; 3.163 ; 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): 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 305 A 528
REMARK 3 RESIDUE RANGE : C 1 C 11
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6859 48.4862 28.9369
REMARK 3 T TENSOR
REMARK 3 T11: -0.1419 T22: -0.1259
REMARK 3 T33: -0.1471 T12: -0.0265
REMARK 3 T13: 0.0260 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.5623 L22: 2.5640
REMARK 3 L33: 2.4887 L12: -0.5386
REMARK 3 L13: 0.6203 L23: -0.8456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0358 S13: -0.0557
REMARK 3 S21: -0.0573 S22: -0.0426 S23: -0.0741
REMARK 3 S31: 0.0518 S32: 0.1245 S33: 0.0286
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 304 B 529
REMARK 3 RESIDUE RANGE : D 1 D 11
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5196 44.4142 6.8058
REMARK 3 T TENSOR
REMARK 3 T11: -0.1361 T22: -0.1205
REMARK 3 T33: -0.1346 T12: -0.0101
REMARK 3 T13: 0.0019 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.3179 L22: 2.9131
REMARK 3 L33: 2.7056 L12: 0.1634
REMARK 3 L13: 0.1558 L23: 0.3322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: 0.0779 S13: -0.0543
REMARK 3 S21: -0.0463 S22: -0.0191 S23: 0.1714
REMARK 3 S31: 0.1112 S32: 0.0147 S33: 0.0522
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 : 1.20
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 2BJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1290021502.
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 : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34714
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 1ERE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG2000MME 0.6M SODIUM FORMATE
REMARK 280 0.1M TRIS PH8, PH 8.00
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 25.38000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.38000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.38000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.38000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 FUNCTION: NUCLEAR HORMONE RECEPTOR
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 MET A 282
REMARK 465 GLY A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 SER A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
REMARK 465 LEU A 295
REMARK 465 VAL A 296
REMARK 465 PRO A 297
REMARK 465 ARG A 298
REMARK 465 GLY A 299
REMARK 465 SER A 300
REMARK 465 HIS A 301
REMARK 465 MET A 302
REMARK 465 GLU A 303
REMARK 465 ASN A 304
REMARK 465 TYR A 331
REMARK 465 ASP A 332
REMARK 465 PRO A 333
REMARK 465 THR A 334
REMARK 465 ARG A 335
REMARK 465 SER A 463
REMARK 465 LYS A 529
REMARK 465 CYS A 530
REMARK 465 LYS A 531
REMARK 465 ASN A 532
REMARK 465 VAL A 533
REMARK 465 MET B 282
REMARK 465 GLY B 283
REMARK 465 SER B 284
REMARK 465 SER B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 SER B 292
REMARK 465 SER B 293
REMARK 465 GLY B 294
REMARK 465 LEU B 295
REMARK 465 VAL B 296
REMARK 465 PRO B 297
REMARK 465 ARG B 298
REMARK 465 GLY B 299
REMARK 465 SER B 300
REMARK 465 HIS B 301
REMARK 465 MET B 302
REMARK 465 GLU B 303
REMARK 465 PHE B 461
REMARK 465 LEU B 462
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 CYS B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 VAL B 533
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 416 CB CG CD CE NZ
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 LEU A 462 CG CD1 CD2
REMARK 470 SER A 464 CB OG
REMARK 470 LYS A 492 CD CE NZ
REMARK 470 ASN B 304 CG OD1 ND2
REMARK 470 ARG B 335 NE CZ NH1 NH2
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 GLU B 419 CD OE1 OE2
REMARK 470 THR B 465 OG1 CG2
REMARK 470 LEU B 466 CG CD1 CD2
REMARK 470 LYS B 467 CG CD CE NZ
REMARK 470 LYS B 472 CG CD CE NZ
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 THR B 334 CB THR B 334 OG1 0.145
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 ARG A 515 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 515 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP D 5 CB - CG - OD2 ANGL. DEV. = 6.1 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 PHE A 461 -86.95 -50.04
REMARK 500 LEU B 408 79.87 -153.76
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 OHT A 1529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OHT B 1530
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A52 RELATED DB: PDB
REMARK 900 ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL
REMARK 900 RELATED ID: 1AKF RELATED DB: PDB
REMARK 900 HOMOLOGOUS-EXTENSION-BASED MODEL OF HUMAN ESTROGEN RECEPTOR WITH
REMARK 900 BOUND ESTRADIOL, THEORETICAL MODEL
REMARK 900 RELATED ID: 1ERE RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 17BETA-ESTRADIOL
REMARK 900 RELATED ID: 1ERR RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 RALOXIFENE
REMARK 900 RELATED ID: 1G50 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1GWQ RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH RALOXIFENE CORE AND TIF2 NRBOX2 PEPTIDE
REMARK 900 RELATED ID: 1GWR RELATED DB: PDB
REMARK 900 HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
REMARK 900 WITH 17BETA-OESTRADIOL AND TIF2 NRBOX3 PEPTIDE
REMARK 900 RELATED ID: 1HCP RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: HUMAN/CHICKEN ESTROGEN RECEPTOR; CHAIN: NULL;
REMARK 900 DOMAIN: DEOXYRIBONUCLEIC ACID-BINDING DOMAIN (ERDBD); ENGINEERED:
REMARK 900 YES
REMARK 900 RELATED ID: 1HCQ RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: HUMAN/CHICKEN ESTROGEN RECEPTOR; CHAIN: A, B,
REMARK 900 E, F; DOMAIN: DEOXYRIBONUCLEIC ACID-BINDING DOMAIN (ERDBD);
REMARK 900 ENGINEERED: YES; MOL_ID: 2; MOLECULE: DEOXYRIBONUCLEIC ACID (5'-D(
REMARK 900 CPCPAPGPGPTPCPAPCPAPGPTPGP APCPCPTPG)-3') (DOT) DEOXYRIBONUCLEIC
REMARK 900 ACID (5'- D(CPCPAPGPGPTPCPA PCPTPGPTPGPAPCPCPTPG)-3'); CHAIN: C, D,
REMARK 900 G, H
REMARK 900 RELATED ID: 1L2I RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 (R,R)-5,11-CIS- DIETHYL-5,6,11,12- TETRAHYDROCHRYSENE-2,8- DIOL AND
REMARK 900 A GLUCOCORTICOID RECEPTORINTERACTING PROTEIN 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 1PCG RELATED DB: PDB
REMARK 900 HELIX-STABILIZED CYCLIC PEPTIDES AS SELECTIVE INHIBITORS OFSTEROID
REMARK 900 RECEPTOR-COACTIVATOR INTERACTIONS
REMARK 900 RELATED ID: 1QKT RELATED DB: PDB
REMARK 900 RELATED ID: 1QKU RELATED DB: PDB
REMARK 900 RELATED ID: 1R5K RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 GW5638
REMARK 900 RELATED ID: 1SJ0 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 THE ANTAGONIST LIGAND 4-D
REMARK 900 RELATED ID: 1UOM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF ESTROGEN RECEPTOR IN COMPLEX WITH A SELECTIVE AND
REMARK 900 POTENT TETRAHYDROISOCHIOLIN LIGAND.
REMARK 900 RELATED ID: 1XP1 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 15
REMARK 900 RELATED ID: 1XP6 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 16
REMARK 900 RELATED ID: 1XP9 RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 18
REMARK 900 RELATED ID: 1XPC RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 COMPOUND 19
REMARK 900 RELATED ID: 3ERD RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN INCOMPLEX WITH
REMARK 900 DIETHYLSTILBESTROL AND A GLUCOCORTICOIDRECEPTOR INTERACTING PROTEIN
REMARK 900 1 NR BOX II PEPTIDE
REMARK 900 RELATED ID: 3ERT RELATED DB: PDB
REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH
REMARK 900 4-HYDROXYTAMOXIFEN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL HIS-TAG LBD TRUNCATED AT END OF H11
DBREF 2BJ4 A 282 304 PDB 2BJ4 2BJ4 282 304
DBREF 2BJ4 A 305 533 UNP P03372 ESR1_HUMAN 305 533
DBREF 2BJ4 B 282 304 PDB 2BJ4 2BJ4 282 304
DBREF 2BJ4 B 305 533 UNP P03372 ESR1_HUMAN 305 533
DBREF 2BJ4 C 1 11 PDB 2BJ4 2BJ4 1 11
DBREF 2BJ4 D 1 11 PDB 2BJ4 2BJ4 1 11
SEQRES 1 A 252 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 252 LEU VAL PRO ARG GLY SER HIS MET GLU ASN SER LEU ALA
SEQRES 3 A 252 LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU
SEQRES 4 A 252 ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO
SEQRES 5 A 252 THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU LEU
SEQRES 6 A 252 THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN
SEQRES 7 A 252 TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU
SEQRES 8 A 252 HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU
SEQRES 9 A 252 ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS
SEQRES 10 A 252 PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP
SEQRES 11 A 252 ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU ILE
SEQRES 12 A 252 PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG MET
SEQRES 13 A 252 MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER
SEQRES 14 A 252 ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER
SEQRES 15 A 252 SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS
SEQRES 16 A 252 ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU
SEQRES 17 A 252 MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN
SEQRES 18 A 252 ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG
SEQRES 19 A 252 HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER MET
SEQRES 20 A 252 LYS CYS LYS ASN VAL
SEQRES 1 B 252 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 252 LEU VAL PRO ARG GLY SER HIS MET GLU ASN SER LEU ALA
SEQRES 3 B 252 LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU LEU
SEQRES 4 B 252 ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP PRO
SEQRES 5 B 252 THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU LEU
SEQRES 6 B 252 THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE ASN
SEQRES 7 B 252 TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR LEU
SEQRES 8 B 252 HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU
SEQRES 9 B 252 ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU HIS
SEQRES 10 B 252 PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP
SEQRES 11 B 252 ARG ASN GLN GLY LYS CCS VAL GLU GLY MET VAL GLU ILE
SEQRES 12 B 252 PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG MET
SEQRES 13 B 252 MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SER
SEQRES 14 B 252 ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SER
SEQRES 15 B 252 SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE HIS
SEQRES 16 B 252 ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS LEU
SEQRES 17 B 252 MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS GLN
SEQRES 18 B 252 ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE ARG
SEQRES 19 B 252 HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER MET
SEQRES 20 B 252 LYS CYS LYS ASN VAL
SEQRES 1 C 11 LEU THR SER ARG ASP PHE GLY SER TRP TYR ALA
SEQRES 1 D 11 LEU THR SER ARG ASP PHE GLY SER TRP TYR ALA
MODRES 2BJ4 CCS B 417 CYS CARBOXYMETHYLATED CYSTEINE
HET CCS B 417 10
HET OHT A1529 29
HET OHT B1530 29
HETNAM CCS CARBOXYMETHYLATED CYSTEINE
HETNAM OHT 4-HYDROXYTAMOXIFEN
FORMUL 2 CCS C5 H9 N O4 S
FORMUL 5 OHT 2(C26 H29 N O2)
FORMUL 7 HOH *179(H2 O)
HELIX 1 1 SER A 305 LEU A 310 5 6
HELIX 2 2 THR A 311 ALA A 322 1 12
HELIX 3 3 SER A 338 ARG A 363 1 26
HELIX 4 4 GLY A 366 LEU A 370 5 5
HELIX 5 5 THR A 371 MET A 396 1 26
HELIX 6 6 ARG A 412 LYS A 416 1 5
HELIX 7 7 GLY A 420 ASN A 439 1 20
HELIX 8 8 GLN A 441 SER A 456 1 16
HELIX 9 9 GLY A 457 PHE A 461 5 5
HELIX 10 10 THR A 465 ALA A 493 1 29
HELIX 11 11 THR A 496 MET A 528 1 33
HELIX 12 12 LEU B 306 LEU B 310 5 5
HELIX 13 13 THR B 311 ALA B 322 1 12
HELIX 14 14 ARG B 335 GLU B 339 5 5
HELIX 15 15 SER B 341 LYS B 362 1 22
HELIX 16 16 GLY B 366 LEU B 370 5 5
HELIX 17 17 THR B 371 MET B 396 1 26
HELIX 18 18 ASN B 413 VAL B 418 5 6
HELIX 19 19 GLY B 420 MET B 438 1 19
HELIX 20 20 GLN B 441 SER B 456 1 16
HELIX 21 21 THR B 465 ALA B 493 1 29
HELIX 22 22 THR B 496 MET B 528 1 33
HELIX 23 23 THR C 2 PHE C 6 5 5
HELIX 24 24 SER D 3 PHE D 6 5 4
SHEET 1 AA 2 LYS A 401 ALA A 405 0
SHEET 2 AA 2 LEU A 408 ASP A 411 -1 O LEU A 408 N PHE A 404
SHEET 1 BA 2 LYS B 401 ALA B 405 0
SHEET 2 BA 2 LEU B 408 ASP B 411 -1 O LEU B 408 N ALA B 405
LINK C LYS B 416 N CCS B 417 1555 1555 1.32
LINK C CCS B 417 N VAL B 418 1555 1555 1.32
SITE 1 AC1 11 LEU A 346 THR A 347 ALA A 350 ASP A 351
SITE 2 AC1 11 GLU A 353 LEU A 354 ARG A 394 PHE A 404
SITE 3 AC1 11 MET A 421 LEU A 428 GLY A 521
SITE 1 AC2 16 TYR B 331 PRO B 333 MET B 343 LEU B 346
SITE 2 AC2 16 THR B 347 ALA B 350 ASP B 351 GLU B 353
SITE 3 AC2 16 LEU B 354 TRP B 383 ARG B 394 PHE B 404
SITE 4 AC2 16 MET B 421 ILE B 424 GLY B 521 HIS B 524
CRYST1 50.760 98.760 105.640 90.00 90.00 90.00 P 21 21 21 8
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 0.019701 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009466 0.00000
MTRIX1 1 -0.976510 -0.201800 0.075520 26.17764 1
MTRIX2 1 -0.212370 0.960610 -0.179260 6.96425 1
MTRIX3 1 -0.036370 -0.191090 -0.980900 45.18856 1
MTRIX1 2 -0.975130 -0.208060 0.076330 26.42859 1
MTRIX2 2 -0.219010 0.957370 -0.188370 7.67486 1
MTRIX3 2 -0.033880 -0.200400 -0.979130 45.78958 1
(ATOM LINES ARE NOT SHOWN.)
END