HEADER HORMONE/GROWTH FACTOR RECEPTOR 16-SEP-05 2B23
TITLE HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN AND A
TITLE 2 GLUCOCORTICOID RECEPTOR-INTERACTING PROTEIN 1 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 9 23-AUG-23 2B23 1 REMARK
REVDAT 8 20-OCT-21 2B23 1 SEQADV
REVDAT 7 24-JUL-19 2B23 1 REMARK LINK
REVDAT 6 11-APR-18 2B23 1 REMARK
REVDAT 5 04-APR-18 2B23 1 REMARK
REVDAT 4 13-JUL-11 2B23 1 VERSN
REVDAT 3 01-APR-08 2B23 1 JRNL
REVDAT 2 18-MAR-08 2B23 1 JRNL VERSN
REVDAT 1 19-SEP-06 2B23 0
JRNL AUTH K.W.NETTLES,J.B.BRUNING,G.GIL,J.NOWAK,S.K.SHARMA,J.B.HAHM,
JRNL AUTH 2 K.KULP,R.B.HOCHBERG,H.ZHOU,J.A.KATZENELLENBOGEN,
JRNL AUTH 3 B.S.KATZENELLENBOGEN,Y.KIM,A.JOACHMIAK,G.L.GREENE
JRNL TITL NFKAPPAB SELECTIVITY OF ESTROGEN RECEPTOR LIGANDS REVEALED
JRNL TITL 2 BY COMPARATIVE CRYSTALLOGRAPHIC ANALYSES
JRNL REF NAT.CHEM.BIOL. V. 4 241 2008
JRNL REFN ISSN 1552-4450
JRNL PMID 18344977
JRNL DOI 10.1038/NCHEMBIO.76
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 24941
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1927
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 30
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) : 33.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.32000
REMARK 3 B22 (A**2) : 0.80000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.51000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.305
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.002
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3978 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5360 ; 1.157 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 474 ; 4.932 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;37.759 ;24.012
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 751 ;18.919 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.302 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 630 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2834 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1956 ; 0.235 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2737 ; 0.315 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 228 ; 0.168 ; 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): 45 ; 0.177 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.394 ; 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): 2481 ; 2.390 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3868 ; 3.460 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1668 ; 5.335 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1492 ; 7.185 ; 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 547 4
REMARK 3 1 B 305 B 547 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1810 ; 0.60 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1810 ; 2.62 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 688 C 696 4
REMARK 3 1 D 688 D 696 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 79 ; 0.82 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 79 ; 2.41 ; 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): -15.7282 -0.3154 4.1053
REMARK 3 T TENSOR
REMARK 3 T11: -0.0399 T22: -0.0375
REMARK 3 T33: -0.0346 T12: -0.0012
REMARK 3 T13: 0.0047 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.7548 L22: 0.5943
REMARK 3 L33: 0.4481 L12: 0.1864
REMARK 3 L13: -0.3588 L23: -0.0117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0798 S12: 0.1048 S13: -0.1293
REMARK 3 S21: -0.0100 S22: -0.0108 S23: -0.0564
REMARK 3 S31: 0.0226 S32: 0.0261 S33: 0.0906
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): -23.9209 0.8127 28.1731
REMARK 3 T TENSOR
REMARK 3 T11: -0.0273 T22: -0.0214
REMARK 3 T33: -0.0469 T12: -0.0119
REMARK 3 T13: 0.0109 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.3531 L22: 0.4379
REMARK 3 L33: 1.9513 L12: -0.1813
REMARK 3 L13: 0.3171 L23: -0.0980
REMARK 3 S TENSOR
REMARK 3 S11: -0.0526 S12: -0.1374 S13: 0.0007
REMARK 3 S21: 0.0783 S22: 0.0062 S23: 0.0099
REMARK 3 S31: -0.0244 S32: -0.0012 S33: 0.0463
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 687 C 696
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3977 13.2673 1.8484
REMARK 3 T TENSOR
REMARK 3 T11: -0.1131 T22: -0.0638
REMARK 3 T33: 0.1185 T12: -0.0020
REMARK 3 T13: 0.1045 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 7.6251 L22: 13.2772
REMARK 3 L33: 4.6686 L12: -0.3150
REMARK 3 L13: -0.5885 L23: -0.6684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: 0.1962 S13: 0.5660
REMARK 3 S21: -0.3436 S22: -0.2346 S23: -0.9456
REMARK 3 S31: -0.1591 S32: 0.3859 S33: 0.2733
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): -24.8942 -18.1058 35.7265
REMARK 3 T TENSOR
REMARK 3 T11: 0.0154 T22: -0.0091
REMARK 3 T33: -0.0126 T12: -0.0573
REMARK 3 T13: 0.0223 T23: 0.2063
REMARK 3 L TENSOR
REMARK 3 L11: 32.9204 L22: 6.8252
REMARK 3 L33: 8.4429 L12: 7.9326
REMARK 3 L13: 0.5744 L23: 5.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.2200 S12: -0.9499 S13: -1.5062
REMARK 3 S21: 0.5144 S22: 0.0874 S23: 0.0001
REMARK 3 S31: -0.0241 S32: -0.2457 S33: -0.3074
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 2B23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034579.
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 : 4.50
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 : 30529
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9650
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 (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.318
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 (%): 39.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.50
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 40.45250
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 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 PRO A 333
REMARK 465 THR A 334
REMARK 465 ARG A 335
REMARK 465 PRO A 336
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 GLU A 471
REMARK 465 LYS A 472
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 LEU B 462
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 THR B 465
REMARK 465 LEU B 466
REMARK 465 LYS B 467
REMARK 465 SER B 468
REMARK 465 LEU B 469
REMARK 465 GLU B 470
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 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 -36.35 -163.41
REMARK 500 GLU A 330 33.65 -73.39
REMARK 500 THR A 460 29.19 -68.27
REMARK 500 LYS A 531 -1.18 -59.46
REMARK 500 ASN A 532 47.17 32.75
REMARK 500 MET B 421 -13.26 170.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B1V RELATED DB: PDB
REMARK 900 RELATED ID: 2B1Z RELATED DB: PDB
DBREF 2B23 A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2B23 B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 2B23 C 686 698 UNP Q15596 NCOA2_HUMAN 686 698
DBREF 2B23 D 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 2B23 CME A 381 UNP P03372 CYS 381 MODIFIED RESIDUE
SEQADV 2B23 CME A 417 UNP P03372 CYS 417 MODIFIED RESIDUE
SEQADV 2B23 CME A 530 UNP P03372 CYS 530 MODIFIED RESIDUE
SEQADV 2B23 SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 2B23 CME B 381 UNP P03372 CYS 381 MODIFIED RESIDUE
SEQADV 2B23 CME B 417 UNP P03372 CYS 417 MODIFIED RESIDUE
SEQADV 2B23 CME B 530 UNP P03372 CYS 530 MODIFIED RESIDUE
SEQADV 2B23 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 2B23 CME A 381 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B23 CME A 417 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B23 CME A 530 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B23 CME B 381 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B23 CME B 417 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2B23 CME B 530 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 381 10
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
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
FORMUL 1 CME 6(C5 H11 N O3 S2)
FORMUL 5 HOH *30(H2 O)
HELIX 1 1 LEU A 306 LEU A 310 5 5
HELIX 2 2 THR A 311 GLU A 323 1 13
HELIX 3 3 SER A 338 LYS A 362 1 25
HELIX 4 4 THR A 371 SER A 395 1 25
HELIX 5 5 ASP A 411 VAL A 418 1 8
HELIX 6 6 MET A 421 MET A 438 1 18
HELIX 7 7 GLN A 441 GLY A 457 1 17
HELIX 8 8 ASP A 473 ALA A 493 1 21
HELIX 9 9 THR A 496 LYS A 531 1 36
HELIX 10 10 SER A 537 ALA A 546 1 10
HELIX 11 11 THR B 311 GLU B 323 1 13
HELIX 12 12 SER B 338 LYS B 362 1 25
HELIX 13 13 THR B 371 MET B 396 1 26
HELIX 14 14 MET B 421 MET B 438 1 18
HELIX 15 15 GLN B 441 SER B 456 1 16
HELIX 16 16 GLY B 457 PHE B 461 5 5
HELIX 17 17 LYS B 472 ALA B 493 1 22
HELIX 18 18 THR B 496 ASN B 532 1 37
HELIX 19 19 SER B 537 ALA B 546 1 10
HELIX 20 20 LYS C 688 LEU C 694 1 7
HELIX 21 21 LYS D 688 ASP D 696 1 9
SHEET 1 A 2 LEU A 402 ALA A 405 0
SHEET 2 A 2 LEU A 408 LEU A 410 -1 O LEU A 408 N ALA A 405
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 1.34
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
CRYST1 54.372 80.905 58.241 90.00 109.68 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 0.018392 0.000000 0.006577 0.00000
SCALE2 0.000000 0.012360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018235 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
