HEADER TRANSCRIPTION 13-OCT-16 5TMZ
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN (Y537S) IN
TITLE 2 COMPLEX WITH THE ESTRADIOL DERIVATIVE, (8S,9S,13S,14S,17S)-16-(3-
TITLE 3 METHOXYBENZYL)-13-METHYL-7,8,9,11,12,13,14,15,16,17-DECAHYDRO-6H-
TITLE 4 CYCLOPENTA[A]PHENANTHRENE-3,17-DIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN (UNP RESIDUES 298-554);
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 (UNP RESIDUES 686-
COMPND 13 698);
COMPND 14 SYNONYM: NCOA-2,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75,BHLHE75,
COMPND 15 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2,HTIF2;
COMPND 16 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,R.ERUMBI,S.SRINIVASAN,N.E.BRUNO,J.NOWAK,T.IZARD,
AUTHOR 2 D.J.KOJETIN,O.ELEMENTO,J.A.KATZENELLENBOGEN,K.W.NETTLES
REVDAT 4 06-MAR-24 5TMZ 1 REMARK
REVDAT 3 22-NOV-17 5TMZ 1 REMARK
REVDAT 2 01-FEB-17 5TMZ 1 JRNL
REVDAT 1 18-JAN-17 5TMZ 0
JRNL AUTH J.C.NWACHUKWU,S.SRINIVASAN,N.E.BRUNO,J.NOWAK,N.J.WRIGHT,
JRNL AUTH 2 F.MINUTOLO,E.S.RANGARAJAN,T.IZARD,X.Q.YAO,B.J.GRANT,
JRNL AUTH 3 D.J.KOJETIN,O.ELEMENTO,J.A.KATZENELLENBOGEN,K.W.NETTLES
JRNL TITL SYSTEMS STRUCTURAL BIOLOGY ANALYSIS OF LIGAND EFFECTS ON ER
JRNL TITL 2 ALPHA PREDICTS CELLULAR RESPONSE TO ENVIRONMENTAL ESTROGENS
JRNL TITL 3 AND ANTI-HORMONE THERAPIES.
JRNL REF CELL CHEM BIOL V. 24 35 2017
JRNL REFN ESSN 2451-9456
JRNL PMID 28042045
JRNL DOI 10.1016/J.CHEMBIOL.2016.11.014
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 22490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.290
REMARK 3 FREE R VALUE TEST SET COUNT : 1865
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 46.4535 - 5.1865 0.99 1754 163 0.1676 0.1987
REMARK 3 2 5.1865 - 4.1175 1.00 1734 164 0.1547 0.2116
REMARK 3 3 4.1175 - 3.5973 0.98 1708 142 0.1641 0.2230
REMARK 3 4 3.5973 - 3.2684 0.99 1697 162 0.1938 0.2387
REMARK 3 5 3.2684 - 3.0342 0.99 1740 151 0.2024 0.2492
REMARK 3 6 3.0342 - 2.8554 0.98 1700 150 0.2092 0.2605
REMARK 3 7 2.8554 - 2.7124 0.94 1618 158 0.2138 0.2785
REMARK 3 8 2.7124 - 2.5943 0.96 1646 130 0.2118 0.2681
REMARK 3 9 2.5943 - 2.4945 0.94 1617 155 0.2229 0.2974
REMARK 3 10 2.4945 - 2.4084 0.94 1622 153 0.2140 0.2614
REMARK 3 11 2.4084 - 2.3331 0.91 1561 143 0.2195 0.2807
REMARK 3 12 2.3331 - 2.2664 0.83 1416 118 0.2149 0.3039
REMARK 3 13 2.2664 - 2.2067 0.47 812 76 0.2148 0.3181
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.35
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 4128
REMARK 3 ANGLE : 0.449 5597
REMARK 3 CHIRALITY : 0.033 662
REMARK 3 PLANARITY : 0.003 692
REMARK 3 DIHEDRAL : 13.255 2497
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 304 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7831 19.1471 -4.8547
REMARK 3 T TENSOR
REMARK 3 T11: 0.3156 T22: 0.3685
REMARK 3 T33: 0.3137 T12: 0.5666
REMARK 3 T13: -0.1523 T23: 0.1039
REMARK 3 L TENSOR
REMARK 3 L11: -0.0009 L22: 0.0894
REMARK 3 L33: 0.0147 L12: 0.0094
REMARK 3 L13: 0.0068 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0700 S13: 0.1087
REMARK 3 S21: -0.0050 S22: 0.0061 S23: 0.0982
REMARK 3 S31: -0.0914 S32: -0.0502 S33: 0.0509
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8017 -6.0384 -6.9686
REMARK 3 T TENSOR
REMARK 3 T11: 0.2317 T22: 0.2392
REMARK 3 T33: 0.1631 T12: 0.1769
REMARK 3 T13: -0.0692 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.3963 L22: 0.0869
REMARK 3 L33: 0.0481 L12: 0.1029
REMARK 3 L13: -0.1336 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: 0.0941 S13: -0.1923
REMARK 3 S21: -0.0036 S22: -0.1044 S23: -0.1579
REMARK 3 S31: 0.1020 S32: 0.1014 S33: -0.0541
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6107 7.9075 2.1508
REMARK 3 T TENSOR
REMARK 3 T11: 0.0875 T22: 0.0861
REMARK 3 T33: 0.1478 T12: -0.0040
REMARK 3 T13: 0.0368 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.0541 L22: 0.0495
REMARK 3 L33: 0.3004 L12: 0.0215
REMARK 3 L13: -0.0891 L23: -0.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1099 S12: -0.0446 S13: 0.0897
REMARK 3 S21: 0.0006 S22: -0.0917 S23: -0.0576
REMARK 3 S31: -0.0492 S32: 0.3243 S33: -0.0098
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 395 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2719 -9.5378 -2.9259
REMARK 3 T TENSOR
REMARK 3 T11: 0.2773 T22: 0.1231
REMARK 3 T33: 0.1973 T12: -0.0064
REMARK 3 T13: 0.0540 T23: -0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 0.0269 L22: 0.0864
REMARK 3 L33: 0.0737 L12: -0.0211
REMARK 3 L13: 0.0285 L23: -0.0475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0758 S12: 0.0346 S13: -0.0243
REMARK 3 S21: -0.0520 S22: -0.0723 S23: -0.0015
REMARK 3 S31: 0.0802 S32: 0.0147 S33: -0.0275
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0599 -14.7369 7.9369
REMARK 3 T TENSOR
REMARK 3 T11: 0.8571 T22: 0.4152
REMARK 3 T33: 0.6560 T12: 0.1626
REMARK 3 T13: 0.1890 T23: 0.0795
REMARK 3 L TENSOR
REMARK 3 L11: -0.0007 L22: 0.0005
REMARK 3 L33: 0.0008 L12: -0.0010
REMARK 3 L13: 0.0003 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.0250 S13: -0.0041
REMARK 3 S21: 0.0116 S22: -0.0030 S23: -0.0453
REMARK 3 S31: 0.0087 S32: 0.0408 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 471 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2829 2.1627 5.8227
REMARK 3 T TENSOR
REMARK 3 T11: 0.0844 T22: 0.0098
REMARK 3 T33: 0.1788 T12: 0.0774
REMARK 3 T13: 0.0059 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.2875 L22: 0.1324
REMARK 3 L33: 0.4953 L12: -0.1689
REMARK 3 L13: -0.1595 L23: 0.1839
REMARK 3 S TENSOR
REMARK 3 S11: -0.1163 S12: 0.0623 S13: -0.0157
REMARK 3 S21: 0.1641 S22: -0.1109 S23: 0.0925
REMARK 3 S31: 0.3293 S32: -0.2087 S33: -0.3260
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 472 THROUGH 529 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0167 7.1877 8.2651
REMARK 3 T TENSOR
REMARK 3 T11: 0.0714 T22: 0.2311
REMARK 3 T33: 0.0767 T12: 0.1125
REMARK 3 T13: -0.1175 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.3204 L22: 0.2234
REMARK 3 L33: 0.2227 L12: -0.1277
REMARK 3 L13: 0.0276 L23: 0.1491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0941 S12: 0.1727 S13: 0.1056
REMARK 3 S21: -0.1124 S22: -0.2828 S23: 0.0134
REMARK 3 S31: -0.0563 S32: -0.2982 S33: -0.3942
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9200 3.8994 8.8309
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.4033
REMARK 3 T33: 0.3312 T12: 0.0198
REMARK 3 T13: -0.0167 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.0584 L22: 0.0484
REMARK 3 L33: 0.0621 L12: 0.0309
REMARK 3 L13: -0.0515 L23: -0.0213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0522 S12: -0.1181 S13: 0.0666
REMARK 3 S21: -0.0170 S22: -0.1629 S23: -0.1050
REMARK 3 S31: 0.0542 S32: 0.0933 S33: -0.0258
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 687 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3603 17.8315 1.1843
REMARK 3 T TENSOR
REMARK 3 T11: 0.1985 T22: 0.1998
REMARK 3 T33: 0.4783 T12: -0.1555
REMARK 3 T13: 0.0902 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 0.0540 L22: 0.0312
REMARK 3 L33: 0.0177 L12: 0.0409
REMARK 3 L13: -0.0315 L23: -0.0245
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: -0.0279 S13: -0.0139
REMARK 3 S21: 0.0166 S22: -0.0486 S23: -0.0522
REMARK 3 S31: -0.0165 S32: 0.0581 S33: -0.0097
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 304 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6968 0.8918 25.1265
REMARK 3 T TENSOR
REMARK 3 T11: 0.2851 T22: 0.6588
REMARK 3 T33: 0.3163 T12: -0.1975
REMARK 3 T13: 0.0426 T23: -0.1511
REMARK 3 L TENSOR
REMARK 3 L11: 0.0236 L22: 0.0443
REMARK 3 L33: 0.1128 L12: -0.0293
REMARK 3 L13: 0.0482 L23: -0.0575
REMARK 3 S TENSOR
REMARK 3 S11: 0.0851 S12: -0.0253 S13: -0.1165
REMARK 3 S21: -0.0386 S22: 0.0928 S23: 0.0934
REMARK 3 S31: 0.0856 S32: -0.0507 S33: 0.0091
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3397 10.0343 43.9029
REMARK 3 T TENSOR
REMARK 3 T11: 0.2783 T22: 0.3588
REMARK 3 T33: 0.2282 T12: 0.0195
REMARK 3 T13: -0.0198 T23: -0.0908
REMARK 3 L TENSOR
REMARK 3 L11: -0.0000 L22: 0.0043
REMARK 3 L33: 0.0045 L12: 0.0027
REMARK 3 L13: 0.0020 L23: 0.0085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0372 S12: -0.0607 S13: 0.0036
REMARK 3 S21: -0.0422 S22: 0.0490 S23: -0.1290
REMARK 3 S31: 0.0006 S32: 0.1106 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1346 -0.8717 31.3723
REMARK 3 T TENSOR
REMARK 3 T11: 0.3272 T22: 0.0767
REMARK 3 T33: 0.1524 T12: -0.0097
REMARK 3 T13: 0.0814 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.2943 L22: 0.4092
REMARK 3 L33: 0.4384 L12: 0.0337
REMARK 3 L13: -0.3122 L23: 0.0854
REMARK 3 S TENSOR
REMARK 3 S11: -0.3253 S12: -0.2146 S13: -0.2887
REMARK 3 S21: 0.0173 S22: -0.0739 S23: 0.0342
REMARK 3 S31: 0.6179 S32: 0.1157 S33: -0.4985
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0173 17.3491 35.8422
REMARK 3 T TENSOR
REMARK 3 T11: 0.3825 T22: 0.2220
REMARK 3 T33: 0.1311 T12: -0.1237
REMARK 3 T13: -0.0527 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 0.0381 L22: 0.0596
REMARK 3 L33: 0.0091 L12: 0.0201
REMARK 3 L13: 0.0155 L23: 0.0224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.0910 S13: -0.0014
REMARK 3 S21: 0.0783 S22: 0.0393 S23: -0.0476
REMARK 3 S31: -0.0318 S32: 0.0947 S33: 0.0250
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 412 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5125 15.7396 33.6386
REMARK 3 T TENSOR
REMARK 3 T11: 0.6121 T22: 0.8561
REMARK 3 T33: 0.8532 T12: -0.2833
REMARK 3 T13: 0.0373 T23: -0.3322
REMARK 3 L TENSOR
REMARK 3 L11: 0.0013 L22: 0.0003
REMARK 3 L33: 0.0003 L12: 0.0007
REMARK 3 L13: 0.0010 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.0171 S13: 0.0043
REMARK 3 S21: -0.0053 S22: 0.0330 S23: 0.0095
REMARK 3 S31: -0.0174 S32: 0.0214 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9773 16.1360 25.4489
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.0999
REMARK 3 T33: 0.1917 T12: -0.1825
REMARK 3 T13: 0.0327 T23: -0.0994
REMARK 3 L TENSOR
REMARK 3 L11: 0.0327 L22: 0.0179
REMARK 3 L33: 0.0327 L12: 0.0052
REMARK 3 L13: 0.0092 L23: 0.0058
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.0010 S13: 0.0191
REMARK 3 S21: -0.0623 S22: 0.0115 S23: -0.0613
REMARK 3 S31: -0.1185 S32: 0.1111 S33: -0.0386
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 438 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7563 8.4875 23.4918
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.1816
REMARK 3 T33: 0.1421 T12: 0.0289
REMARK 3 T13: 0.0025 T23: -0.0927
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0050
REMARK 3 L33: 0.1610 L12: -0.0029
REMARK 3 L13: 0.0192 L23: -0.0295
REMARK 3 S TENSOR
REMARK 3 S11: -0.1137 S12: 0.0094 S13: -0.0344
REMARK 3 S21: 0.0048 S22: -0.0315 S23: -0.0134
REMARK 3 S31: -0.0828 S32: -0.2822 S33: -0.0923
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 456 THROUGH 465 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6111 -9.7809 14.9334
REMARK 3 T TENSOR
REMARK 3 T11: 0.5142 T22: 0.4289
REMARK 3 T33: 0.4200 T12: -0.1775
REMARK 3 T13: 0.1641 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 0.0043 L22: 0.0081
REMARK 3 L33: 0.0010 L12: -0.0005
REMARK 3 L13: -0.0002 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.0062 S13: 0.0005
REMARK 3 S21: -0.0164 S22: 0.0332 S23: 0.0132
REMARK 3 S31: 0.0240 S32: 0.0055 S33: -0.0001
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 466 THROUGH 531 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9284 4.7056 18.1930
REMARK 3 T TENSOR
REMARK 3 T11: -0.2454 T22: 0.2162
REMARK 3 T33: 0.1363 T12: 0.1496
REMARK 3 T13: -0.1180 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.1324 L22: 0.0096
REMARK 3 L33: 0.2960 L12: 0.0044
REMARK 3 L13: 0.0733 L23: 0.0435
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: -0.0350 S13: 0.0667
REMARK 3 S21: -0.0456 S22: -0.1278 S23: 0.0657
REMARK 3 S31: 0.0135 S32: -0.3692 S33: -0.3688
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 532 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3028 -5.8926 33.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.5433 T22: 0.3763
REMARK 3 T33: 0.3811 T12: 0.4026
REMARK 3 T13: 0.0349 T23: 0.1343
REMARK 3 L TENSOR
REMARK 3 L11: 0.0248 L22: 0.0583
REMARK 3 L33: 0.0211 L12: -0.0333
REMARK 3 L13: 0.0220 L23: -0.0348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0329 S12: -0.0033 S13: 0.0176
REMARK 3 S21: -0.0084 S22: 0.0223 S23: 0.0044
REMARK 3 S31: 0.0161 S32: 0.0458 S33: 0.0109
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 688 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0565 -13.4544 35.5691
REMARK 3 T TENSOR
REMARK 3 T11: 0.7366 T22: 0.1127
REMARK 3 T33: 0.3144 T12: -0.1328
REMARK 3 T13: 0.2355 T23: 0.2027
REMARK 3 L TENSOR
REMARK 3 L11: 0.0056 L22: 0.0241
REMARK 3 L33: 0.0237 L12: -0.0104
REMARK 3 L13: -0.0071 L23: 0.0160
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0081 S13: -0.0221
REMARK 3 S21: -0.0229 S22: -0.0119 S23: -0.0104
REMARK 3 S31: 0.0204 S32: -0.0241 S33: -0.0129
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 5TMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-14
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) : 0.979
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, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24431
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.43
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 41.33000
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: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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 LEU A 462
REMARK 465 SER A 463
REMARK 465 SER A 464
REMARK 465 THR A 465
REMARK 465 LEU A 466
REMARK 465 LYS A 467
REMARK 465 SER A 468
REMARK 465 LEU A 469
REMARK 465 GLU A 470
REMARK 465 LEU A 549
REMARK 465 HIS A 550
REMARK 465 ALA A 551
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
REMARK 465 LYS C 686
REMARK 465 SER C 697
REMARK 465 SER C 698
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 LEU B 462
REMARK 465 SER B 463
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 D 686
REMARK 465 HIS D 687
REMARK 465 SER D 698
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 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 687 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 ARG B 335 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 LEU B 466 CG CD1 CD2
REMARK 470 LYS B 467 CG CD CE NZ
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 PRO A 333 53.02 -92.91
REMARK 500 PRO A 336 105.59 -58.55
REMARK 500 CYS A 530 43.71 -90.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 779 DISTANCE = 6.21 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 7FQ A 601
REMARK 610 7FQ B 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7FQ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7FQ B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TMR RELATED DB: PDB
REMARK 900 RELATED ID: 5TMS RELATED DB: PDB
REMARK 900 RELATED ID: 5TMT RELATED DB: PDB
REMARK 900 RELATED ID: 5TMU RELATED DB: PDB
REMARK 900 RELATED ID: 5TMV RELATED DB: PDB
REMARK 900 RELATED ID: 5TMW RELATED DB: PDB
REMARK 900 RELATED ID: 5TN1 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN3 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN4 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN5 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN6 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN7 RELATED DB: PDB
REMARK 900 RELATED ID: 5TN8 RELATED DB: PDB
DBREF 5TMZ A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5TMZ C 686 698 UNP Q15596 NCOA2_HUMAN 686 698
DBREF 5TMZ B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5TMZ D 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 5TMZ SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 5TMZ 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 C 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 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 D 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET 7FQ A 601 21
HET 7FQ B 601 21
HETNAM 7FQ (9BETA,13ALPHA,14BETA,16ALPHA,17ALPHA)-16-[(4-
HETNAM 2 7FQ METHOXYPHENYL)METHYL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL
FORMUL 5 7FQ 2(C26 H32 O3)
FORMUL 7 HOH *148(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 ASN A 413 VAL A 418 5 6
HELIX 5 AA5 MET A 421 ASN A 439 1 19
HELIX 6 AA6 GLN A 441 SER A 456 1 16
HELIX 7 AA7 GLY A 457 PHE A 461 5 5
HELIX 8 AA8 LYS A 472 ALA A 493 1 22
HELIX 9 AA9 THR A 496 CYS A 530 1 35
HELIX 10 AB1 SER A 537 ALA A 546 1 10
HELIX 11 AB2 LYS C 688 ASP C 696 1 9
HELIX 12 AB3 THR B 311 ALA B 322 1 12
HELIX 13 AB4 SER B 338 ARG B 363 1 26
HELIX 14 AB5 THR B 371 SER B 395 1 25
HELIX 15 AB6 ASN B 413 VAL B 418 5 6
HELIX 16 AB7 GLY B 420 MET B 438 1 19
HELIX 17 AB8 GLN B 441 SER B 456 1 16
HELIX 18 AB9 GLY B 457 PHE B 461 5 5
HELIX 19 AC1 THR B 465 ALA B 493 1 29
HELIX 20 AC2 THR B 496 ASN B 532 1 37
HELIX 21 AC3 SER B 537 ARG B 548 1 12
HELIX 22 AC4 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 408 N ALA B 405
SITE 1 AC1 10 MET A 343 LEU A 346 GLU A 353 LEU A 387
SITE 2 AC1 10 ARG A 394 MET A 421 HIS A 524 LEU A 525
SITE 3 AC1 10 MET A 528 HOH A 721
SITE 1 AC2 13 MET B 343 LEU B 346 ALA B 350 GLU B 353
SITE 2 AC2 13 LEU B 387 MET B 388 LEU B 391 ARG B 394
SITE 3 AC2 13 MET B 421 ILE B 424 HIS B 524 MET B 528
SITE 4 AC2 13 HOH B 728
CRYST1 54.630 82.660 58.460 90.00 110.83 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 0.018305 0.000000 0.006964 0.00000
SCALE2 0.000000 0.012098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018302 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
