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Chemical substance (1) PDB-CCD (1) Gene (2) KEGG GENES (2) Protein sequence (8) UniProt (2) SWISS-PROT (2) PDBSTR (4) DNA sequence (4) EMBL (4) Protein domain (5) InterPro (4) PROSITE (1) Literature (1) PubMed (1) All databases (21)
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HEADER TRANSCRIPTION 03-SEP-15 5DK9
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
TITLE 2 WITH A PHENYLAMINO-SUBSTITUTED ETHYL TRIARYL-ETHYLENE DERIVATIVE 4,
TITLE 3 4'-{2-[3-(PHENYLAMINO)PHENYL]BUT-1-ENE-1,1-DIYL}DIPHENOL
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: NUCLEAR RECEPTOR COACTIVATOR 2;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: NUCLEAR RECEPTOR-INTERACTING PEPTIDE;
COMPND 13 SYNONYM: NCOA-2,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75,BHLHE75,
COMPND 14 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2,HTIF2;
COMPND 15 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
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, LIGAND BINDING, PROTEIN-
KEYWDS 2 LIGAND COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.NWACHUKWU,S.SRINIVASAN,Y.ZHENG,S.WANG,J.MIN,C.DONG,Z.LIAO,
AUTHOR 2 V.CAVETT,J.NOWAK,R.HOUTMAN,K.E.CARLSON,J.S.JOSAN,O.ELEMENTO,
AUTHOR 3 J.A.KATZENELLENBOGEN,H.B.ZHOU,K.W.NETTLES
REVDAT 2 27-SEP-23 5DK9 1 HEADER REMARK
REVDAT 1 04-MAY-16 5DK9 0
JRNL AUTH J.C.NWACHUKWU,S.SRINIVASAN,Y.ZHENG,S.WANG,J.MIN,C.DONG,
JRNL AUTH 2 Z.LIAO,J.NOWAK,N.J.WRIGHT,R.HOUTMAN,K.E.CARLSON,J.S.JOSAN,
JRNL AUTH 3 O.ELEMENTO,J.A.KATZENELLENBOGEN,H.B.ZHOU,K.W.NETTLES
JRNL TITL PREDICTIVE FEATURES OF LIGAND-SPECIFIC SIGNALING THROUGH THE
JRNL TITL 2 ESTROGEN RECEPTOR.
JRNL REF MOL.SYST.BIOL. V. 12 864 2016
JRNL REFN ESSN 1744-4292
JRNL PMID 27107013
JRNL DOI 10.15252/MSB.20156701
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 19803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
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 (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 998
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 46.3894 - 4.3544 0.95 2911 151 0.1845 0.2073
REMARK 3 2 4.3544 - 3.4566 0.94 2810 142 0.1788 0.2273
REMARK 3 3 3.4566 - 3.0197 0.97 2904 161 0.2135 0.2433
REMARK 3 4 3.0197 - 2.7437 0.96 2866 154 0.2156 0.2506
REMARK 3 5 2.7437 - 2.5470 0.94 2792 148 0.2328 0.2537
REMARK 3 6 2.5470 - 2.3969 0.89 2640 143 0.2493 0.2896
REMARK 3 7 2.3969 - 2.2768 0.64 1882 99 0.2737 0.2924
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.02
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 : 0.003 3929
REMARK 3 ANGLE : 0.767 5313
REMARK 3 CHIRALITY : 0.051 625
REMARK 3 PLANARITY : 0.003 657
REMARK 3 DIHEDRAL : 18.217 1471
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 306:336)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3445 5.4330 -6.6485
REMARK 3 T TENSOR
REMARK 3 T11: 0.3294 T22: 0.6019
REMARK 3 T33: 0.1153 T12: 0.1339
REMARK 3 T13: -0.0610 T23: 0.1225
REMARK 3 L TENSOR
REMARK 3 L11: 2.3625 L22: 2.9395
REMARK 3 L33: 4.3778 L12: 2.0085
REMARK 3 L13: -0.8917 L23: 0.9340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: 0.7004 S13: 0.0390
REMARK 3 S21: -0.1556 S22: -0.2435 S23: -0.3064
REMARK 3 S31: -0.1223 S32: -0.3775 S33: 0.1763
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 337:530)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3279 3.3654 4.5898
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.1452
REMARK 3 T33: 0.1000 T12: 0.0080
REMARK 3 T13: -0.0547 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 6.7668 L22: 2.8118
REMARK 3 L33: 6.8893 L12: -0.6672
REMARK 3 L13: -3.5611 L23: 1.7588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: 0.2280 S13: -0.1374
REMARK 3 S21: 0.0474 S22: -0.1663 S23: -0.0242
REMARK 3 S31: 0.0655 S32: -0.4281 S33: 0.1013
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 532:548)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7421 4.8534 8.5676
REMARK 3 T TENSOR
REMARK 3 T11: -0.0344 T22: 0.6583
REMARK 3 T33: 0.4742 T12: -0.1435
REMARK 3 T13: -0.0868 T23: 0.1373
REMARK 3 L TENSOR
REMARK 3 L11: 2.7754 L22: 3.7758
REMARK 3 L33: 3.2942 L12: -2.1954
REMARK 3 L13: 1.4119 L23: -1.9003
REMARK 3 S TENSOR
REMARK 3 S11: 0.2038 S12: -0.8509 S13: -0.5589
REMARK 3 S21: 0.5870 S22: 0.0489 S23: -0.3879
REMARK 3 S31: 0.7820 S32: 0.7566 S33: -0.1234
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 305:351)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7226 5.6782 36.2435
REMARK 3 T TENSOR
REMARK 3 T11: 0.2268 T22: 0.2137
REMARK 3 T33: 0.1830 T12: -0.0017
REMARK 3 T13: 0.0835 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 5.8513 L22: 4.0668
REMARK 3 L33: 7.5080 L12: -1.5001
REMARK 3 L13: 0.4478 L23: -0.1495
REMARK 3 S TENSOR
REMARK 3 S11: -0.3606 S12: -0.4508 S13: 0.1589
REMARK 3 S21: 0.5796 S22: 0.1860 S23: 0.0491
REMARK 3 S31: -0.0423 S32: -0.0270 S33: 0.1072
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 352:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3553 6.2454 28.2044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.1621
REMARK 3 T33: 0.0876 T12: -0.0016
REMARK 3 T13: 0.0109 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 4.4586 L22: 5.0527
REMARK 3 L33: 7.6128 L12: -1.6168
REMARK 3 L13: -1.5388 L23: 0.5562
REMARK 3 S TENSOR
REMARK 3 S11: -0.1666 S12: -0.1737 S13: 0.0657
REMARK 3 S21: -0.0768 S22: 0.0830 S23: -0.1086
REMARK 3 S31: -0.0639 S32: 0.0331 S33: 0.0680
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 470:548)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2560 3.4829 20.9771
REMARK 3 T TENSOR
REMARK 3 T11: 0.1931 T22: 0.2671
REMARK 3 T33: 0.1713 T12: 0.0156
REMARK 3 T13: 0.0119 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 2.9148 L22: 3.9740
REMARK 3 L33: 5.6847 L12: -0.7965
REMARK 3 L13: -1.7109 L23: -0.3826
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: -0.1898 S13: -0.2419
REMARK 3 S21: -0.0369 S22: -0.1324 S23: -0.0473
REMARK 3 S31: 0.5102 S32: -0.2991 S33: 0.1172
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 5DK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JAN-13
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 : 21608
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.78800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2QA8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
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 40.96000
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: 5030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 SER A 305
REMARK 465 PHE A 461
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 LYS A 531
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 PHE B 461
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 VAL B 533
REMARK 465 VAL B 534
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 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 LEU A 306 CG CD1 CD2
REMARK 470 LEU A 310 CG CD1 CD2
REMARK 470 GLN A 314 CG CD OE1 NE2
REMARK 470 GLN A 414 CG CD OE1 NE2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 TYR A 459 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 337 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 412 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 GLU B 471 CG CD OE1 OE2
REMARK 470 LYS B 481 CG CD CE NZ
REMARK 470 LYS B 492 CG CD CE NZ
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 ASN B 532 CG OD1 ND2
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 688 CG CD CE NZ
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 A 741 O HOH A 749 1.91
REMARK 500 OH TYR B 328 O HOH B 701 1.93
REMARK 500 N09 5CC B 601 O HOH B 702 1.99
REMARK 500 OE2 GLU B 542 O HOH B 703 2.07
REMARK 500 OD1 ASP B 351 O HOH B 704 2.08
REMARK 500 O LYS A 401 O HOH A 701 2.14
REMARK 500 N VAL B 368 O HOH B 705 2.15
REMARK 500 O HOH B 724 O HOH B 744 2.15
REMARK 500 O HOH A 715 O HOH A 743 2.15
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 HIS B 513 CA - C - O ANGL. DEV. = 15.1 DEGREES
REMARK 500 HIS B 513 CA - C - N ANGL. DEV. = -13.5 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 TYR A 331 40.51 -90.84
REMARK 500 THR A 334 99.17 54.85
REMARK 500 GLU A 419 74.75 -59.38
REMARK 500 MET A 421 -73.32 71.16
REMARK 500 LEU B 306 -33.41 -136.30
REMARK 500 GLU B 330 30.85 -90.48
REMARK 500 PRO B 336 -173.01 -66.33
REMARK 500 GLU B 470 -90.83 -37.18
REMARK 500 GLU B 471 -41.30 29.07
REMARK 500 LYS B 531 -170.11 71.75
REMARK 500 GLN D 695 -67.52 -99.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 470 GLU B 471 147.37
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 5CC A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5CC B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DL4 RELATED DB: PDB
REMARK 900 RELATED ID: 5DKS RELATED DB: PDB
REMARK 900 RELATED ID: 5DKG RELATED DB: PDB
REMARK 900 RELATED ID: 5DKE RELATED DB: PDB
REMARK 900 RELATED ID: 5DKB RELATED DB: PDB
REMARK 900 RELATED ID: 5DIG RELATED DB: PDB
REMARK 900 RELATED ID: 5DIE RELATED DB: PDB
REMARK 900 RELATED ID: 5DID RELATED DB: PDB
REMARK 900 RELATED ID: 5DI7 RELATED DB: PDB
DBREF 5DK9 A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DK9 B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DK9 C 686 699 UNP Q15596 NCOA2_HUMAN 686 699
DBREF 5DK9 D 686 699 UNP Q15596 NCOA2_HUMAN 686 699
SEQADV 5DK9 SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 5DK9 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 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 5CC A 601 31
HET 5CC B 601 31
HETNAM 5CC 4,4'-{2-[3-(PHENYLAMINO)PHENYL]BUT-1-ENE-1,1-
HETNAM 2 5CC DIYL}DIPHENOL
FORMUL 5 5CC 2(C28 H25 N O2)
FORMUL 7 HOH *125(H2 O)
HELIX 1 AA1 THR A 311 ALA A 322 1 12
HELIX 2 AA2 SER A 338 ARG A 363 1 26
HELIX 3 AA3 THR A 371 SER A 395 1 25
HELIX 4 AA4 ARG A 412 LYS A 416 1 5
HELIX 5 AA5 MET A 421 MET A 438 1 18
HELIX 6 AA6 GLN A 441 SER A 456 1 16
HELIX 7 AA7 HIS A 474 ALA A 493 1 20
HELIX 8 AA8 THR A 496 LYS A 529 1 34
HELIX 9 AA9 SER A 537 ALA A 546 1 10
HELIX 10 AB1 THR B 311 GLU B 323 1 13
HELIX 11 AB2 SER B 338 LYS B 362 1 25
HELIX 12 AB3 THR B 371 SER B 395 1 25
HELIX 13 AB4 MET B 421 ASN B 439 1 19
HELIX 14 AB5 GLN B 441 SER B 456 1 16
HELIX 15 AB6 GLU B 471 ALA B 493 1 23
HELIX 16 AB7 THR B 496 LYS B 529 1 34
HELIX 17 AB8 SER B 537 ALA B 546 1 10
HELIX 18 AB9 ILE C 689 ASP C 696 1 8
HELIX 19 AC1 ILE D 689 LEU D 694 1 6
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
CISPEP 1 ASP A 332 PRO A 333 0 -19.98
CISPEP 2 ARG A 335 PRO A 336 0 -3.72
CISPEP 3 GLY A 420 MET A 421 0 -2.61
SITE 1 AC1 17 LEU A 346 THR A 347 ALA A 350 GLU A 353
SITE 2 AC1 17 LEU A 387 ARG A 394 PHE A 404 VAL A 418
SITE 3 AC1 17 GLU A 419 GLY A 420 MET A 421 ILE A 424
SITE 4 AC1 17 LEU A 428 GLY A 521 HIS A 524 MET A 528
SITE 5 AC1 17 LEU A 540
SITE 1 AC2 15 MET B 343 THR B 347 ALA B 350 GLU B 353
SITE 2 AC2 15 LEU B 387 ARG B 394 PHE B 404 GLU B 419
SITE 3 AC2 15 GLY B 420 GLY B 521 HIS B 524 LEU B 525
SITE 4 AC2 15 MET B 528 LEU B 540 HOH B 702
CRYST1 54.490 81.920 58.280 90.00 111.07 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 0.018352 0.000000 0.007070 0.00000
SCALE2 0.000000 0.012207 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018388 0.00000
(ATOM LINES ARE NOT SHOWN.)
END