HEADER TRANSCRIPTION 21-SEP-15 5DVS
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
TITLE 2 WITH A 2-METHYL-SUBSTITUTED TRIARYL-IMINE 4,4'-[(2-METHYLPHENYL)
TITLE 3 CARBONIMIDOYL]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,N.J.WRIGHT,S.SRINIVASAN,Y.ZHENG,S.WANG,J.MIN,C.DONG,
AUTHOR 2 Z.LIAO,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 06-MAR-24 5DVS 1 REMARK
REVDAT 1 04-MAY-16 5DVS 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 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 20857
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1864
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 46.9381 - 5.3426 0.97 1605 155 0.1924 0.2373
REMARK 3 2 5.3426 - 4.2415 0.98 1594 158 0.1786 0.2276
REMARK 3 3 4.2415 - 3.7056 0.93 1502 151 0.1876 0.2140
REMARK 3 4 3.7056 - 3.3669 0.97 1555 153 0.2159 0.2830
REMARK 3 5 3.3669 - 3.1256 0.97 1560 145 0.2398 0.2732
REMARK 3 6 3.1256 - 2.9413 0.96 1520 158 0.2345 0.2860
REMARK 3 7 2.9413 - 2.7941 0.94 1512 151 0.2449 0.3268
REMARK 3 8 2.7941 - 2.6724 0.88 1414 140 0.2636 0.3498
REMARK 3 9 2.6724 - 2.5696 0.90 1440 135 0.2591 0.3111
REMARK 3 10 2.5696 - 2.4809 0.89 1443 131 0.2615 0.2941
REMARK 3 11 2.4809 - 2.4033 0.87 1362 143 0.2537 0.3113
REMARK 3 12 2.4033 - 2.3346 0.83 1338 122 0.2706 0.3384
REMARK 3 13 2.3346 - 2.2732 0.72 1148 122 0.2959 0.3275
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 3738
REMARK 3 ANGLE : 0.539 5064
REMARK 3 CHIRALITY : 0.020 606
REMARK 3 PLANARITY : 0.003 627
REMARK 3 DIHEDRAL : 12.014 1331
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3997 -18.0096 6.3307
REMARK 3 T TENSOR
REMARK 3 T11: 0.4450 T22: 0.4438
REMARK 3 T33: 0.2874 T12: 0.0636
REMARK 3 T13: 0.0416 T23: -0.0779
REMARK 3 L TENSOR
REMARK 3 L11: 7.5496 L22: 6.5065
REMARK 3 L33: 5.8221 L12: 3.5518
REMARK 3 L13: -2.6323 L23: -3.1659
REMARK 3 S TENSOR
REMARK 3 S11: 0.4116 S12: -0.8019 S13: -0.2279
REMARK 3 S21: 0.5514 S22: -0.6326 S23: 0.0315
REMARK 3 S31: -0.3165 S32: 0.3321 S33: 0.2260
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8072 -19.2554 -0.8347
REMARK 3 T TENSOR
REMARK 3 T11: 0.4498 T22: 0.4061
REMARK 3 T33: 0.2866 T12: -0.0435
REMARK 3 T13: 0.0733 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 4.5061 L22: 4.7951
REMARK 3 L33: 5.0404 L12: 0.9696
REMARK 3 L13: -1.2781 L23: -1.6659
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: -0.1121 S13: 0.1487
REMARK 3 S21: -0.0625 S22: -0.0056 S23: 0.1364
REMARK 3 S31: -0.0266 S32: -0.0929 S33: -0.0010
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 472 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7560 -23.7890 -6.2222
REMARK 3 T TENSOR
REMARK 3 T11: 0.4943 T22: 0.3814
REMARK 3 T33: 0.3407 T12: -0.0086
REMARK 3 T13: 0.1102 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 4.5485 L22: 3.3468
REMARK 3 L33: 5.1377 L12: 0.0971
REMARK 3 L13: -1.1612 L23: -0.9899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0965 S12: 0.1363 S13: -0.3703
REMARK 3 S21: -0.0834 S22: -0.0698 S23: 0.0641
REMARK 3 S31: 0.4237 S32: 0.2851 S33: 0.1649
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 473 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8985 -16.9228 -8.1720
REMARK 3 T TENSOR
REMARK 3 T11: 0.5890 T22: 0.4009
REMARK 3 T33: 0.2812 T12: -0.0678
REMARK 3 T13: 0.0949 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 5.7445 L22: 2.1712
REMARK 3 L33: 4.1397 L12: -0.2289
REMARK 3 L13: -0.5001 L23: -0.7769
REMARK 3 S TENSOR
REMARK 3 S11: 0.1211 S12: 0.0339 S13: 0.0725
REMARK 3 S21: 0.1097 S22: -0.1662 S23: 0.0013
REMARK 3 S31: -0.0005 S32: 0.0981 S33: 0.0566
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 306 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7455 -20.7892 -25.9084
REMARK 3 T TENSOR
REMARK 3 T11: 0.4639 T22: 0.9598
REMARK 3 T33: 0.7376 T12: 0.0944
REMARK 3 T13: 0.1243 T23: 0.1226
REMARK 3 L TENSOR
REMARK 3 L11: 7.6539 L22: 5.4196
REMARK 3 L33: 7.0520 L12: -1.5759
REMARK 3 L13: 7.2461 L23: -2.0445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0326 S12: 1.2055 S13: 0.2412
REMARK 3 S21: -0.1164 S22: -0.6656 S23: -1.2690
REMARK 3 S31: 0.6107 S32: 2.4020 S33: 0.5039
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9386 -14.0244 -43.6320
REMARK 3 T TENSOR
REMARK 3 T11: 0.5230 T22: 0.6581
REMARK 3 T33: 0.5060 T12: -0.0499
REMARK 3 T13: -0.0151 T23: 0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 7.9967 L22: 6.7065
REMARK 3 L33: 8.4388 L12: -0.2127
REMARK 3 L13: 1.8483 L23: -2.4621
REMARK 3 S TENSOR
REMARK 3 S11: -0.2321 S12: 1.1801 S13: 0.4584
REMARK 3 S21: -0.6167 S22: 0.1257 S23: 0.5732
REMARK 3 S31: -0.0261 S32: -0.3431 S33: 0.1662
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 340 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9010 -24.6153 -34.6772
REMARK 3 T TENSOR
REMARK 3 T11: 0.6349 T22: 0.3540
REMARK 3 T33: 0.3304 T12: -0.0425
REMARK 3 T13: 0.1455 T23: -0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 5.4177 L22: 6.3674
REMARK 3 L33: 8.4783 L12: -0.4774
REMARK 3 L13: 0.8041 L23: -2.8938
REMARK 3 S TENSOR
REMARK 3 S11: -0.2389 S12: 0.6834 S13: -0.6239
REMARK 3 S21: -0.2936 S22: 0.0487 S23: 0.0431
REMARK 3 S31: 1.2353 S32: 0.1986 S33: 0.2166
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3302 -19.4937 -28.4125
REMARK 3 T TENSOR
REMARK 3 T11: 0.4345 T22: 0.3848
REMARK 3 T33: 0.2236 T12: -0.0311
REMARK 3 T13: 0.0503 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 3.1359 L22: 6.0054
REMARK 3 L33: 7.0037 L12: -1.0464
REMARK 3 L13: -1.0816 L23: -0.2996
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: 0.1618 S13: -0.1166
REMARK 3 S21: -0.0986 S22: -0.2056 S23: -0.0712
REMARK 3 S31: 0.3028 S32: -0.1440 S33: 0.1922
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 402 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8329 -8.1072 -36.5213
REMARK 3 T TENSOR
REMARK 3 T11: 0.6033 T22: 0.7582
REMARK 3 T33: 0.5049 T12: 0.2762
REMARK 3 T13: 0.1480 T23: 0.1595
REMARK 3 L TENSOR
REMARK 3 L11: 7.8761 L22: 2.6861
REMARK 3 L33: 8.2138 L12: -3.9342
REMARK 3 L13: -3.3070 L23: 3.8032
REMARK 3 S TENSOR
REMARK 3 S11: 1.0526 S12: 1.5050 S13: 0.3860
REMARK 3 S21: -0.1069 S22: -0.0277 S23: 0.6571
REMARK 3 S31: -1.4170 S32: -1.7342 S33: -0.7873
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 422 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2663 -6.8736 -24.5000
REMARK 3 T TENSOR
REMARK 3 T11: 0.7753 T22: 0.5024
REMARK 3 T33: 0.5504 T12: 0.1222
REMARK 3 T13: 0.1143 T23: 0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 9.6322 L22: 2.1386
REMARK 3 L33: 9.8334 L12: 2.9007
REMARK 3 L13: 5.0986 L23: 1.9673
REMARK 3 S TENSOR
REMARK 3 S11: -0.2745 S12: -0.6932 S13: 1.1481
REMARK 3 S21: 0.1434 S22: 0.0637 S23: 0.6598
REMARK 3 S31: -1.5997 S32: -0.7054 S33: 0.1292
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9179 -19.8209 -21.4992
REMARK 3 T TENSOR
REMARK 3 T11: 0.4938 T22: 0.5402
REMARK 3 T33: 0.3946 T12: 0.0689
REMARK 3 T13: 0.0764 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 3.7547 L22: 2.3360
REMARK 3 L33: 7.2153 L12: 0.8520
REMARK 3 L13: 1.0315 L23: 1.7998
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: -0.2896 S13: -0.1184
REMARK 3 S21: 1.1692 S22: -0.0720 S23: 0.1747
REMARK 3 S31: 0.5332 S32: 0.3794 S33: 0.0045
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 531 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5080 -16.3448 -18.7759
REMARK 3 T TENSOR
REMARK 3 T11: 0.3872 T22: 0.3169
REMARK 3 T33: 0.1838 T12: 0.0091
REMARK 3 T13: 0.0837 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 6.3746 L22: 3.5360
REMARK 3 L33: 7.6137 L12: 0.5921
REMARK 3 L13: 1.7324 L23: 0.7220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.1649 S13: 0.2158
REMARK 3 S21: 0.2956 S22: -0.0662 S23: 0.0656
REMARK 3 S31: -0.0649 S32: 0.5682 S33: 0.1450
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 532 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9350 -29.9372 -33.1372
REMARK 3 T TENSOR
REMARK 3 T11: 0.8767 T22: 0.8300
REMARK 3 T33: 0.5532 T12: -0.1730
REMARK 3 T13: 0.0165 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.3577 L22: 9.1235
REMARK 3 L33: 5.1312 L12: 2.4423
REMARK 3 L13: -1.1323 L23: 4.2765
REMARK 3 S TENSOR
REMARK 3 S11: 0.1456 S12: -0.0071 S13: -0.8676
REMARK 3 S21: 0.0389 S22: -0.4986 S23: -0.8572
REMARK 3 S31: 0.5892 S32: -1.8616 S33: 0.3644
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 688 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6170 -5.7774 -0.6438
REMARK 3 T TENSOR
REMARK 3 T11: 0.6969 T22: 0.9284
REMARK 3 T33: 0.8270 T12: 0.0350
REMARK 3 T13: 0.1681 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.9861 L22: 5.7569
REMARK 3 L33: 5.0424 L12: 0.0453
REMARK 3 L13: 0.5454 L23: 5.3181
REMARK 3 S TENSOR
REMARK 3 S11: 0.9464 S12: 0.3486 S13: 1.3285
REMARK 3 S21: 0.6103 S22: -1.5216 S23: -0.0531
REMARK 3 S31: -0.3114 S32: -2.5265 S33: 0.5871
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 688 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7872 -36.9608 -35.2927
REMARK 3 T TENSOR
REMARK 3 T11: 0.9874 T22: 0.5796
REMARK 3 T33: 0.6591 T12: -0.0027
REMARK 3 T13: 0.1118 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 6.6904 L22: 9.7854
REMARK 3 L33: 6.4186 L12: 0.7589
REMARK 3 L13: 6.0086 L23: 3.7525
REMARK 3 S TENSOR
REMARK 3 S11: -0.2881 S12: 0.9159 S13: -1.0250
REMARK 3 S21: -0.2703 S22: -0.1314 S23: 0.5655
REMARK 3 S31: 0.9318 S32: 0.7691 S33: 0.3688
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 5DVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213902.
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 : 22394
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
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 (%): 39.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
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 41.31900
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: 5150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 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 LYS A 303
REMARK 465 ASN A 304
REMARK 465 SER A 305
REMARK 465 ARG A 335
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 ARG A 548
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 PHE B 337
REMARK 465 SER B 338
REMARK 465 GLY B 415
REMARK 465 LYS B 416
REMARK 465 CYS B 417
REMARK 465 VAL B 418
REMARK 465 GLU B 419
REMARK 465 GLY B 420
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 SER B 468
REMARK 465 LEU B 469
REMARK 465 GLU B 470
REMARK 465 GLU B 471
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 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 GLN A 314 CG CD OE1 NE2
REMARK 470 SER A 317 OG
REMARK 470 GLU A 330 CG CD OE1 OE2
REMARK 470 THR A 334 OG1 CG2
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 470 GLN A 414 CG CD OE1 NE2
REMARK 470 LYS A 416 CG CD CE NZ
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 LYS A 472 CG CD CE NZ
REMARK 470 LYS A 529 CG CD CE NZ
REMARK 470 LYS A 531 CG CD CE NZ
REMARK 470 ASN A 532 CG OD1 ND2
REMARK 470 VAL A 533 CG1 CG2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 LEU B 308 CG CD1 CD2
REMARK 470 SER B 309 OG
REMARK 470 SER B 317 OG
REMARK 470 ASP B 332 CG OD1 OD2
REMARK 470 ARG B 335 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 SER B 341 OG
REMARK 470 VAL B 368 CG1 CG2
REMARK 470 LEU B 370 CG CD1 CD2
REMARK 470 LEU B 372 CG CD1 CD2
REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 397 CG CD OE1 OE2
REMARK 470 LYS B 401 CG CD CE NZ
REMARK 470 GLN B 414 CG CD OE1 NE2
REMARK 470 LYS B 472 CG CD CE NZ
REMARK 470 ARG B 477 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 481 CG CD CE NZ
REMARK 470 LYS B 492 CG CD CE NZ
REMARK 470 LEU B 497 CG CD1 CD2
REMARK 470 GLN B 499 CG CD OE1 NE2
REMARK 470 TYR B 526 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 ASN B 532 CG OD1 ND2
REMARK 470 VAL B 534 CG1 CG2
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 688 CG CD CE NZ
REMARK 470 ASP D 696 CG OD1 OD2
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 ASN A 532 -91.00 56.84
REMARK 500 ALA B 307 14.47 -149.69
REMARK 500 SER B 309 34.53 -99.21
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 VAL A 533 VAL A 534 128.96
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 5G7 A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5G7 B 901
DBREF 5DVS A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DVS B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DVS C 686 699 UNP Q15596 NCOA2_HUMAN 686 699
DBREF 5DVS D 686 699 UNP Q15596 NCOA2_HUMAN 686 699
SEQADV 5DVS SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 5DVS 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 5G7 A 900 23
HET 5G7 B 901 23
HETNAM 5G7 4,4'-[(2-METHYLPHENYL)CARBONIMIDOYL]DIPHENOL
FORMUL 5 5G7 2(C20 H17 N O2)
FORMUL 7 HOH *76(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 ASP A 411 LYS A 416 1 6
HELIX 5 AA5 GLY A 420 ASN A 439 1 20
HELIX 6 AA6 GLN A 441 SER A 456 1 16
HELIX 7 AA7 ASP A 473 ALA A 493 1 21
HELIX 8 AA8 THR A 496 LYS A 531 1 36
HELIX 9 AA9 SER A 537 ALA A 546 1 10
HELIX 10 AB1 THR B 311 ALA B 322 1 12
HELIX 11 AB2 ALA B 340 ARG B 363 1 24
HELIX 12 AB3 THR B 371 SER B 395 1 25
HELIX 13 AB4 VAL B 422 ASN B 439 1 18
HELIX 14 AB5 GLN B 441 SER B 456 1 16
HELIX 15 AB6 ASP B 473 ALA B 493 1 21
HELIX 16 AB7 THR B 496 ASN B 532 1 37
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 ASP D 696 1 8
SHEET 1 AA1 2 LEU A 402 ALA A 405 0
SHEET 2 AA1 2 LEU A 408 LEU A 410 -1 O LEU A 410 N LEU A 402
SHEET 1 AA2 2 LEU B 402 ALA B 405 0
SHEET 2 AA2 2 LEU B 408 LEU B 410 -1 O LEU B 410 N LEU B 402
SITE 1 AC1 12 LEU A 346 THR A 347 ALA A 350 GLU A 353
SITE 2 AC1 12 LEU A 387 ARG A 394 MET A 421 ILE A 424
SITE 3 AC1 12 GLY A 521 LEU A 525 LEU A 540 HOH A1016
SITE 1 AC2 12 MET B 343 LEU B 346 THR B 347 ALA B 350
SITE 2 AC2 12 GLU B 353 LEU B 387 ARG B 394 MET B 421
SITE 3 AC2 12 ILE B 424 GLY B 521 LEU B 536 HOH B1018
CRYST1 55.800 82.638 58.482 90.00 110.61 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 0.017921 0.000000 0.006740 0.00000
SCALE2 0.000000 0.012101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
