HEADER TRANSCRIPTION 07-JUN-16 5KCT
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN (Y537S) IN
TITLE 2 COMPLEX WITH AN N-ETHYL, 4-CHLOROBENZYL OBHS-N DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN;
COMPND 5 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 6 GROUP A MEMBER 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NCOA2;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: NUCLEAR RECEPTOR-INTERACTING PEPTIDE;
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, LIGAND BINDING, PROTEIN-
KEYWDS 2 LIGAND COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.NWACHUKWU,S.SRINIVASAN,N.E.BRUNO,V.DHARMARAJAN,D.GOSWAMI,
AUTHOR 2 I.KASTRATI,S.NOVICK,J.NOWAK,H.B.ZHOU,N.BOONMUEN,Y.ZHAO,J.MIN,
AUTHOR 3 J.FRASOR,B.S.KATZENELLENBOGEN,P.R.GRIFFIN,J.A.KATZENELLENBOGEN,
AUTHOR 4 K.W.NETTLES
REVDAT 5 06-MAR-24 5KCT 1 REMARK
REVDAT 4 26-FEB-20 5KCT 1 REMARK
REVDAT 3 28-DEC-16 5KCT 1 JRNL
REVDAT 2 21-DEC-16 5KCT 1 JRNL
REVDAT 1 16-NOV-16 5KCT 0
SPRSDE 16-NOV-16 5KCT 5BNU
JRNL AUTH S.SRINIVASAN,J.C.NWACHUKWU,N.E.BRUNO,V.DHARMARAJAN,
JRNL AUTH 2 D.GOSWAMI,I.KASTRATI,S.NOVICK,J.NOWAK,V.CAVETT,H.B.ZHOU,
JRNL AUTH 3 N.BOONMUEN,Y.ZHAO,J.MIN,J.FRASOR,B.S.KATZENELLENBOGEN,
JRNL AUTH 4 P.R.GRIFFIN,J.A.KATZENELLENBOGEN,K.W.NETTLES
JRNL TITL FULL ANTAGONISM OF THE ESTROGEN RECEPTOR WITHOUT A
JRNL TITL 2 PROTOTYPICAL LIGAND SIDE CHAIN.
JRNL REF NAT. CHEM. BIOL. V. 13 111 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 27870835
JRNL DOI 10.1038/NCHEMBIO.2236
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1690
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 59373
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1929
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.5558 - 3.8500 0.94 4290 141 0.1597 0.1876
REMARK 3 2 3.8500 - 3.0560 0.94 4231 141 0.1739 0.1989
REMARK 3 3 3.0560 - 2.6698 0.98 4370 142 0.1825 0.1963
REMARK 3 4 2.6698 - 2.4257 0.99 4403 150 0.1831 0.1897
REMARK 3 5 2.4257 - 2.2518 0.95 4228 138 0.1831 0.2351
REMARK 3 6 2.2518 - 2.1191 0.90 3998 137 0.1958 0.2264
REMARK 3 7 2.1191 - 2.0129 0.95 4216 148 0.2003 0.2360
REMARK 3 8 2.0129 - 1.9253 0.93 4151 130 0.2160 0.2587
REMARK 3 9 1.9253 - 1.8512 0.86 3816 128 0.2593 0.3192
REMARK 3 10 1.8512 - 1.7873 0.93 4110 146 0.2138 0.2552
REMARK 3 11 1.7873 - 1.7314 0.91 4026 142 0.2141 0.2255
REMARK 3 12 1.7314 - 1.6819 0.91 4045 137 0.2204 0.2742
REMARK 3 13 1.6819 - 1.6376 0.89 3917 125 0.2231 0.2684
REMARK 3 14 1.6376 - 1.5977 0.82 3643 124 0.2346 0.2675
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4047
REMARK 3 ANGLE : 1.050 5504
REMARK 3 CHIRALITY : 0.043 645
REMARK 3 PLANARITY : 0.005 683
REMARK 3 DIHEDRAL : 15.063 1522
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 303:333)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5577 -13.3215 6.0311
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.2643
REMARK 3 T33: 0.1752 T12: -0.0134
REMARK 3 T13: -0.0188 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 4.1557 L22: 4.6063
REMARK 3 L33: 2.9716 L12: 1.6851
REMARK 3 L13: -0.6881 L23: -0.5604
REMARK 3 S TENSOR
REMARK 3 S11: 0.1799 S12: -0.4497 S13: 0.3378
REMARK 3 S21: 0.2337 S22: -0.3551 S23: 0.1618
REMARK 3 S31: -0.1925 S32: 0.1664 S33: 0.2296
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 334:486)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3067 -20.7477 -3.5689
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.1437
REMARK 3 T33: 0.1403 T12: -0.0050
REMARK 3 T13: -0.0134 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.5541 L22: 1.6123
REMARK 3 L33: 2.2131 L12: 0.5737
REMARK 3 L13: -0.8019 L23: -0.8370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0694 S12: -0.0187 S13: -0.1141
REMARK 3 S21: -0.0892 S22: -0.0099 S23: -0.0221
REMARK 3 S31: 0.1963 S32: -0.0201 S33: 0.0274
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 487:548)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1785 -20.6581 -9.2787
REMARK 3 T TENSOR
REMARK 3 T11: 0.1874 T22: 0.1232
REMARK 3 T33: 0.1404 T12: -0.0080
REMARK 3 T13: 0.0107 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 2.8255 L22: 1.5017
REMARK 3 L33: 1.7815 L12: -0.0960
REMARK 3 L13: -0.4161 L23: 0.0149
REMARK 3 S TENSOR
REMARK 3 S11: -0.0372 S12: 0.1335 S13: -0.1451
REMARK 3 S21: -0.0552 S22: -0.0527 S23: 0.1131
REMARK 3 S31: 0.1078 S32: -0.1615 S33: 0.0598
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 306:410)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8991 -19.9810 -34.2233
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: 0.1996
REMARK 3 T33: 0.1674 T12: 0.0094
REMARK 3 T13: 0.0289 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.4240 L22: 1.4171
REMARK 3 L33: 3.8490 L12: 0.6425
REMARK 3 L13: -0.0061 L23: -0.2265
REMARK 3 S TENSOR
REMARK 3 S11: -0.1345 S12: 0.1337 S13: -0.0829
REMARK 3 S21: -0.1151 S22: 0.0638 S23: -0.0862
REMARK 3 S31: 0.0303 S32: 0.0810 S33: 0.0399
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 411:486)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0937 -17.3529 -22.7499
REMARK 3 T TENSOR
REMARK 3 T11: 0.1971 T22: 0.2262
REMARK 3 T33: 0.1325 T12: 0.0161
REMARK 3 T13: 0.0292 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 3.3747 L22: 2.3168
REMARK 3 L33: 4.3342 L12: 0.0352
REMARK 3 L13: -0.0661 L23: -0.2586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0512 S12: 0.0513 S13: 0.0319
REMARK 3 S21: 0.0151 S22: -0.0006 S23: 0.0356
REMARK 3 S31: -0.1315 S32: -0.0754 S33: 0.0321
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 487:548)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0090 -17.7386 -21.9375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1983 T22: 0.1714
REMARK 3 T33: 0.1905 T12: 0.0033
REMARK 3 T13: 0.0171 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 0.9078 L22: 1.0459
REMARK 3 L33: 4.1546 L12: -0.7538
REMARK 3 L13: -0.0191 L23: 0.6995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: 0.0177 S13: -0.0666
REMARK 3 S21: -0.1296 S22: -0.1078 S23: 0.0871
REMARK 3 S31: -0.0048 S32: -0.2733 S33: 0.1596
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222038.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE I-BEAM
REMARK 200 SINGLE CRYSTAL ASYMMETRIC CUT
REMARK 200 4.965 DEGS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62319
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.72800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.05M MGCL2, 0.067M
REMARK 280 NACL, 0.1M TRIS, PH 8.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
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 40.78000
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: 5140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 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 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 305
REMARK 465 CYS B 417
REMARK 465 VAL B 418
REMARK 465 GLU B 419
REMARK 465 GLY B 420
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 527
REMARK 465 MET B 528
REMARK 465 LYS B 529
REMARK 465 CYS B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 VAL B 533
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 SER C 699
REMARK 465 LYS D 686
REMARK 465 HIS D 687
REMARK 465 SER D 697
REMARK 465 SER D 698
REMARK 465 SER D 699
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 303 CG CD CE NZ
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 LYS A 472 CG CD CE NZ
REMARK 470 LYS A 531 CG CD CE NZ
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 LYS B 416 CG CD CE NZ
REMARK 470 GLU B 470 CG CD OE1 OE2
REMARK 470 GLU B 471 CG CD OE1 OE2
REMARK 470 ARG B 477 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 534 CG1 CG2
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 696 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 794 O HOH B 841 1.91
REMARK 500 O HOH D 704 O HOH D 706 1.92
REMARK 500 O HOH B 840 O HOH B 841 1.97
REMARK 500 O HOH A 862 O HOH A 866 1.97
REMARK 500 O HOH B 701 O HOH B 815 2.04
REMARK 500 O HOH B 804 O HOH B 835 2.07
REMARK 500 O HOH A 834 O HOH B 845 2.11
REMARK 500 O HOH A 822 O HOH A 863 2.12
REMARK 500 SG CYS A 381 O HOH A 873 2.13
REMARK 500 O HOH A 802 O HOH A 870 2.18
REMARK 500 NZ LYS B 492 O HOH B 701 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 883 O HOH B 774 2555 1.89
REMARK 500 O TYR A 331 NH2 ARG D 692 1556 2.15
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 OB7 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OB6 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KCC RELATED DB: PDB
REMARK 900 RELATED ID: 5KCD RELATED DB: PDB
REMARK 900 RELATED ID: 5KCF RELATED DB: PDB
REMARK 900 RELATED ID: 5KCU RELATED DB: PDB
REMARK 900 RELATED ID: 5KCW RELATED DB: PDB
REMARK 900 RELATED ID: 5KD9 RELATED DB: PDB
DBREF 5KCT A 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KCT B 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KCT C 686 699 PDB 5KCT 5KCT 686 699
DBREF 5KCT D 686 699 PDB 5KCT 5KCT 686 699
SEQADV 5KCT SER A 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQADV 5KCT SER B 537 UNP P03372 TYR 364 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 CYS 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 14 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 2 C 14 SER
SEQRES 1 D 14 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 2 D 14 SER
HET OB7 A 601 34
HET OB6 B 601 34
HETNAM OB7 (1R,2S,4R)-N-(4-CHLOROPHENYL)-N-ETHYL-5,6-BIS(4-
HETNAM 2 OB7 HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-
HETNAM 3 OB7 SULFONAMIDE
HETNAM OB6 (1S,2R,4S)-N-(4-CHLOROPHENYL)-N-ETHYL-5,6-BIS(4-
HETNAM 2 OB6 HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-
HETNAM 3 OB6 SULFONAMIDE
FORMUL 5 OB7 C26 H24 CL N O5 S
FORMUL 6 OB6 C26 H24 CL N O5 S
FORMUL 7 HOH *361(H2 O)
HELIX 1 AA1 SER A 305 LEU A 310 5 6
HELIX 2 AA2 THR A 311 GLU A 323 1 13
HELIX 3 AA3 SER A 338 LYS A 362 1 25
HELIX 4 AA4 GLY A 366 LEU A 370 5 5
HELIX 5 AA5 THR A 371 SER A 395 1 25
HELIX 6 AA6 ARG A 412 LYS A 416 1 5
HELIX 7 AA7 GLY A 420 MET A 438 1 19
HELIX 8 AA8 GLN A 441 SER A 456 1 16
HELIX 9 AA9 ASP A 473 ALA A 493 1 21
HELIX 10 AB1 THR A 496 ASN A 532 1 37
HELIX 11 AB2 SER A 537 ALA A 546 1 10
HELIX 12 AB3 HIS A 547 ARG A 548 5 2
HELIX 13 AB4 LEU B 306 LEU B 310 5 5
HELIX 14 AB5 THR B 311 ALA B 322 1 12
HELIX 15 AB6 SER B 338 LYS B 362 1 25
HELIX 16 AB7 GLY B 366 LEU B 370 5 5
HELIX 17 AB8 THR B 371 SER B 395 1 25
HELIX 18 AB9 VAL B 422 MET B 438 1 17
HELIX 19 AC1 GLN B 441 SER B 456 1 16
HELIX 20 AC2 LEU B 469 ALA B 493 1 25
HELIX 21 AC3 THR B 496 TYR B 526 1 31
HELIX 22 AC4 SER B 537 ALA B 546 1 10
HELIX 23 AC5 LYS C 688 LEU C 694 1 7
HELIX 24 AC6 ILE D 689 ASP D 696 1 8
SHEET 1 AA1 2 LYS A 401 ALA A 405 0
SHEET 2 AA1 2 LEU A 408 ASP A 411 -1 O LEU A 410 N LEU A 402
SHEET 1 AA2 2 LYS B 401 ALA B 405 0
SHEET 2 AA2 2 LEU B 408 ASP B 411 -1 O LEU B 410 N LEU B 402
SITE 1 AC1 16 MET A 343 LEU A 346 THR A 347 ALA A 350
SITE 2 AC1 16 GLU A 353 MET A 388 ARG A 394 GLU A 419
SITE 3 AC1 16 GLY A 420 MET A 421 ILE A 424 PHE A 425
SITE 4 AC1 16 LEU A 428 GLY A 521 HIS A 524 LEU A 540
SITE 1 AC2 13 LEU B 346 THR B 347 ALA B 350 GLU B 353
SITE 2 AC2 13 LEU B 387 ARG B 394 MET B 421 ILE B 424
SITE 3 AC2 13 GLY B 521 LEU B 525 LEU B 540 LEU B 544
SITE 4 AC2 13 HOH B 752
CRYST1 54.872 81.560 58.914 90.00 110.18 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 0.018224 0.000000 0.006698 0.00000
SCALE2 0.000000 0.012261 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018084 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
