HEADER HORMONE/GROWTH FACTOR RECEPTOR 16-SEP-05 2B1Z
TITLE HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH
TITLE 2 17METHYL-17ALPHA-DIHYDROEQUILENIN AND A GLUCOC INTERACTING PROTEIN 1
TITLE 3 NR BOX II PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: ER, ESTRADIOL RECEPTOR, ER-ALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: RESIDUES 686 - 698;
COMPND 12 SYNONYM: NCOA-2, TRANSCRIPTIONAL INTERMEDIARY FACTOR 2;
COMPND 13 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: ESR1, ESR, NR3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MCSG7 (PET12-DERIVATIVE);
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS ESTROGEN RECEPTOR, LBD, GRIP PEPTIDE, HORMONE-GROWTH FACTOR RECEPTOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.RAJAN,R.W.HSIEH,S.K.SHARMA,G.L.GREENE
REVDAT 7 23-AUG-23 2B1Z 1 REMARK
REVDAT 6 20-OCT-21 2B1Z 1 REMARK SEQADV
REVDAT 5 24-JUL-19 2B1Z 1 REMARK LINK
REVDAT 4 13-JUL-11 2B1Z 1 VERSN
REVDAT 3 24-FEB-09 2B1Z 1 VERSN
REVDAT 2 22-JUL-08 2B1Z 1 JRNL
REVDAT 1 19-SEP-06 2B1Z 0
JRNL AUTH R.W.HSIEH,S.S.RAJAN,S.K.SHARMA,G.L.GREENE
JRNL TITL MOLECULAR CHARACTERIZATION OF A B-RING UNSATURATED ESTROGEN:
JRNL TITL 2 IMPLICATIONS FOR CONJUGATED EQUINE ESTROGEN COMPONENTS OF
JRNL TITL 3 PREMARIN.
JRNL REF STEROIDS V. 73 59 2008
JRNL REFN ISSN 0039-128X
JRNL PMID 17949766
JRNL DOI 10.1016/J.STEROIDS.2007.08.014
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 45694
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2441
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) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3412
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3944
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.801
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4094 ; 0.005 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5527 ; 0.951 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 483 ; 4.249 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;34.915 ;23.977
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 768 ;14.681 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;21.439 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 647 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2897 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2096 ; 0.216 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2843 ; 0.318 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 313 ; 0.158 ; 0.500
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): 41 ; 0.236 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.168 ; 0.500
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): 2516 ; 1.549 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3944 ; 2.212 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1785 ; 3.773 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1583 ; 5.375 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 305 A 548 4
REMARK 3 1 B 305 B 547 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1871 ; 0.47 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1871 ; 1.83 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 688 C 695 4
REMARK 3 1 C 688 C 695 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 71 ; 0.00 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 71 ; 0.00 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 305 A 548
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6382 0.3518 -1.8583
REMARK 3 T TENSOR
REMARK 3 T11: -0.0630 T22: -0.0793
REMARK 3 T33: -0.0574 T12: 0.0050
REMARK 3 T13: 0.0143 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.0784 L22: 1.0544
REMARK 3 L33: 1.9787 L12: -0.0687
REMARK 3 L13: 0.3681 L23: -0.1697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.0368 S13: -0.0377
REMARK 3 S21: -0.1191 S22: 0.0027 S23: 0.0235
REMARK 3 S31: 0.0009 S32: -0.0069 S33: 0.0248
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 305 B 547
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4579 -0.5736 22.2392
REMARK 3 T TENSOR
REMARK 3 T11: -0.0548 T22: -0.0835
REMARK 3 T33: -0.0810 T12: -0.0052
REMARK 3 T13: -0.0044 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.7056 L22: 0.8682
REMARK 3 L33: 1.3301 L12: 0.2009
REMARK 3 L13: -0.8141 L23: -0.2218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: -0.1508 S13: 0.0588
REMARK 3 S21: 0.0720 S22: -0.0326 S23: 0.0530
REMARK 3 S31: -0.0586 S32: 0.1037 S33: -0.0293
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 688 C 695
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2234 -16.7487 -10.6555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1631 T22: -0.0305
REMARK 3 T33: 0.0003 T12: -0.0218
REMARK 3 T13: -0.0095 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 19.0064 L22: 9.7896
REMARK 3 L33: 1.2667 L12: 0.9885
REMARK 3 L13: 4.2556 L23: 1.9695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0864 S12: 0.0286 S13: -0.8820
REMARK 3 S21: -0.2719 S22: 0.0249 S23: 0.0660
REMARK 3 S31: 0.9651 S32: 0.1139 S33: -0.1114
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 688 D 696
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5938 16.2190 27.2495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: -0.0404
REMARK 3 T33: 0.1310 T12: -0.0237
REMARK 3 T13: 0.1003 T23: -0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 8.6043 L22: 5.7422
REMARK 3 L33: 3.7283 L12: -4.8675
REMARK 3 L13: 0.2591 L23: -2.7583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0556 S12: -0.1975 S13: 0.6396
REMARK 3 S21: 0.1759 S22: -0.3193 S23: 0.2504
REMARK 3 S31: -0.2457 S32: -0.6391 S33: 0.2637
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2B1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 77.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
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 : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48202
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5140
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.139
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XTALVIEW
REMARK 200 STARTING MODEL: PDB ENTRY 1ZKY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.50
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 41.89950
REMARK 290 SMTRY3 2 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: 6870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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 ILE A 298
REMARK 465 LYS A 299
REMARK 465 ARG A 300
REMARK 465 SER A 301
REMARK 465 LYS A 302
REMARK 465 LYS A 303
REMARK 465 ASN A 304
REMARK 465 LEU A 462
REMARK 465 SER A 463
REMARK 465 SER A 464
REMARK 465 THR A 465
REMARK 465 LEU A 466
REMARK 465 LYS A 467
REMARK 465 SER A 468
REMARK 465 LEU A 469
REMARK 465 GLU A 470
REMARK 465 LEU A 549
REMARK 465 HIS A 550
REMARK 465 ALA A 551
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
REMARK 465 ILE B 298
REMARK 465 LYS B 299
REMARK 465 ARG B 300
REMARK 465 SER B 301
REMARK 465 LYS B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 THR B 465
REMARK 465 LEU B 466
REMARK 465 GLU B 471
REMARK 465 ARG B 548
REMARK 465 LEU B 549
REMARK 465 HIS B 550
REMARK 465 ALA B 551
REMARK 465 PRO B 552
REMARK 465 THR B 553
REMARK 465 SER B 554
REMARK 465 LYS C 686
REMARK 465 HIS C 687
REMARK 465 ASP C 696
REMARK 465 SER C 697
REMARK 465 SER C 698
REMARK 465 LYS D 686
REMARK 465 HIS D 687
REMARK 465 SER D 697
REMARK 465 SER D 698
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 306 -37.35 -153.01
REMARK 500 GLU B 330 30.64 -98.92
REMARK 500 PRO B 333 3.25 -69.65
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 17M A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 17M B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B1V RELATED DB: PDB
REMARK 900 RELATED ID: 2B23 RELATED DB: PDB
DBREF 2B1Z A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2B1Z B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2B1Z C 686 698 UNP Q15596 NCOA2_HUMAN 686 698
DBREF 2B1Z D 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 2B1Z CME A 381 UNP P03372 CYS 381 MODIFIED RESIDUE
SEQADV 2B1Z CME A 417 UNP P03372 CYS 417 MODIFIED RESIDUE
SEQADV 2B1Z CME A 530 UNP P03372 CYS 530 MODIFIED RESIDUE
SEQADV 2B1Z SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 2B1Z CME B 381 UNP P03372 CYS 381 MODIFIED RESIDUE
SEQADV 2B1Z CME B 417 UNP P03372 CYS 417 MODIFIED RESIDUE
SEQADV 2B1Z CME B 530 UNP P03372 CYS 530 MODIFIED RESIDUE
SEQADV 2B1Z SER B 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQRES 1 A 257 ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER LEU
SEQRES 2 A 257 THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA GLU
SEQRES 3 A 257 PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG PRO
SEQRES 4 A 257 PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN LEU
SEQRES 5 A 257 ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA LYS
SEQRES 6 A 257 ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP GLN
SEQRES 7 A 257 VAL HIS LEU LEU GLU CME ALA TRP LEU GLU ILE LEU MET
SEQRES 8 A 257 ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY LYS
SEQRES 9 A 257 LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN
SEQRES 10 A 257 GLY LYS CME VAL GLU GLY MET VAL GLU ILE PHE ASP MET
SEQRES 11 A 257 LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN LEU
SEQRES 12 A 257 GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE LEU
SEQRES 13 A 257 LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR LEU
SEQRES 14 A 257 LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU
SEQRES 15 A 257 ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA LYS
SEQRES 16 A 257 ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU ALA
SEQRES 17 A 257 GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET SER
SEQRES 18 A 257 ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CME LYS
SEQRES 19 A 257 ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET LEU
SEQRES 20 A 257 ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 B 257 ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER LEU
SEQRES 2 B 257 THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA GLU
SEQRES 3 B 257 PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG PRO
SEQRES 4 B 257 PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN LEU
SEQRES 5 B 257 ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA LYS
SEQRES 6 B 257 ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP GLN
SEQRES 7 B 257 VAL HIS LEU LEU GLU CME ALA TRP LEU GLU ILE LEU MET
SEQRES 8 B 257 ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY LYS
SEQRES 9 B 257 LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN
SEQRES 10 B 257 GLY LYS CME VAL GLU GLY MET VAL GLU ILE PHE ASP MET
SEQRES 11 B 257 LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN LEU
SEQRES 12 B 257 GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE LEU
SEQRES 13 B 257 LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR LEU
SEQRES 14 B 257 LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU
SEQRES 15 B 257 ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA LYS
SEQRES 16 B 257 ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU ALA
SEQRES 17 B 257 GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET SER
SEQRES 18 B 257 ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CME LYS
SEQRES 19 B 257 ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET LEU
SEQRES 20 B 257 ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 C 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 1 D 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
MODRES 2B1Z CME A 381 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B1Z CME A 417 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B1Z CME A 530 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B1Z CME B 381 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B1Z CME B 417 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B1Z CME B 530 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 381 16
HET CME A 417 10
HET CME A 530 10
HET CME B 381 16
HET CME B 417 10
HET CME B 530 10
HET 17M A 201 21
HET 17M B 202 21
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM 17M 17-METHYL-17-ALPHA-DIHYDROEQUILENIN
FORMUL 1 CME 6(C5 H11 N O3 S2)
FORMUL 5 17M 2(C19 H22 O2)
FORMUL 7 HOH *110(H2 O)
HELIX 1 1 LEU A 306 LEU A 310 5 5
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 SER A 395 1 25
HELIX 6 6 ASN A 413 VAL A 418 5 6
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 GLU A 471 ALA A 493 1 23
HELIX 10 10 THR A 496 ASN A 532 1 37
HELIX 11 11 SER A 537 ALA A 546 1 10
HELIX 12 12 HIS A 547 ARG A 548 5 2
HELIX 13 13 SER B 305 LEU B 310 5 6
HELIX 14 14 THR B 311 ALA B 322 1 12
HELIX 15 15 SER B 338 LYS B 362 1 25
HELIX 16 16 THR B 371 SER B 395 1 25
HELIX 17 17 ARG B 412 LYS B 416 1 5
HELIX 18 18 GLY B 420 ASN B 439 1 20
HELIX 19 19 GLN B 441 SER B 456 1 16
HELIX 20 20 GLY B 457 PHE B 461 5 5
HELIX 21 21 LYS B 472 ALA B 493 1 22
HELIX 22 22 THR B 496 LYS B 531 1 36
HELIX 23 23 SER B 537 ALA B 546 1 10
HELIX 24 24 LYS C 688 GLN C 695 1 8
HELIX 25 25 LYS D 688 ASP D 696 1 9
SHEET 1 A 2 LYS A 401 ALA A 405 0
SHEET 2 A 2 LEU A 408 ASP A 411 -1 O LEU A 410 N LEU A 402
SHEET 1 B 2 LYS B 401 ALA B 405 0
SHEET 2 B 2 LEU B 408 ASP B 411 -1 O LEU B 410 N LEU B 402
LINK C GLU A 380 N CME A 381 1555 1555 1.33
LINK C CME A 381 N ALA A 382 1555 1555 1.33
LINK C LYS A 416 N CME A 417 1555 1555 1.33
LINK C CME A 417 N VAL A 418 1555 1555 1.33
LINK C LYS A 529 N CME A 530 1555 1555 1.33
LINK C CME A 530 N LYS A 531 1555 1555 1.33
LINK C GLU B 380 N CME B 381 1555 1555 1.33
LINK C CME B 381 N ALA B 382 1555 1555 1.33
LINK C LYS B 416 N CME B 417 1555 1555 1.33
LINK C CME B 417 N VAL B 418 1555 1555 1.33
LINK C LYS B 529 N CME B 530 1555 1555 1.33
LINK C CME B 530 N LYS B 531 1555 1555 1.33
SITE 1 AC1 8 HOH A 8 GLU A 353 LEU A 387 ARG A 394
SITE 2 AC1 8 PHE A 404 MET A 421 HIS A 524 LEU A 525
SITE 1 AC2 7 HOH B 42 GLU B 353 LEU B 387 ARG B 394
SITE 2 AC2 7 MET B 421 HIS B 524 LEU B 525
CRYST1 55.923 83.799 58.523 90.00 108.94 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 0.017882 0.000000 0.006137 0.00000
SCALE2 0.000000 0.011933 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
