HEADER TRANSCRIPTION 07-JUL-16 5KRL
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN (Y537S) IN
TITLE 2 COMPLEX WITH THE A-CD RING ESTROGEN, (1S,7AS)-5-(2-CHLORO-4-
TITLE 3 HYDROXYPHENYL)-7A-METHYL-2,3,3A,4,7,7A-HEXAHYDRO-1H-INDEN-1-OL
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,J.NOWAK,D.J.KOJETIN,O.ELEMENTO,
AUTHOR 2 J.A.KATZENELLENBOGEN,K.W.NETTLES
REVDAT 3 06-MAR-24 5KRL 1 REMARK
REVDAT 2 01-FEB-17 5KRL 1 JRNL
REVDAT 1 18-JAN-17 5KRL 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. 2.40 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 19236
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) : 0.182
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1636
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 46.6440 - 5.4919 0.99 1533 142 0.1896 0.2162
REMARK 3 2 5.4919 - 4.3601 1.00 1512 146 0.1531 0.1870
REMARK 3 3 4.3601 - 3.8093 0.99 1516 138 0.1513 0.1706
REMARK 3 4 3.8093 - 3.4611 0.99 1474 138 0.1697 0.1925
REMARK 3 5 3.4611 - 3.2131 0.99 1501 142 0.1875 0.2196
REMARK 3 6 3.2131 - 3.0237 0.99 1480 136 0.2015 0.2353
REMARK 3 7 3.0237 - 2.8723 0.98 1488 134 0.1944 0.2342
REMARK 3 8 2.8723 - 2.7473 0.97 1447 140 0.2041 0.2328
REMARK 3 9 2.7473 - 2.6415 0.97 1454 133 0.2112 0.2848
REMARK 3 10 2.6415 - 2.5504 0.96 1430 138 0.2053 0.2751
REMARK 3 11 2.5504 - 2.4706 0.93 1412 120 0.2007 0.2308
REMARK 3 12 2.4706 - 2.4000 0.90 1353 129 0.2034 0.2879
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.29
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 : 0.006 3869
REMARK 3 ANGLE : 0.938 5240
REMARK 3 CHIRALITY : 0.212 630
REMARK 3 PLANARITY : 0.002 646
REMARK 3 DIHEDRAL : 13.657 1409
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 305 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9216 0.2592 32.0586
REMARK 3 T TENSOR
REMARK 3 T11: 0.2324 T22: 0.3060
REMARK 3 T33: 0.1758 T12: 0.0566
REMARK 3 T13: -0.0163 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 3.1398 L22: 7.3227
REMARK 3 L33: 4.2205 L12: 2.6166
REMARK 3 L13: 1.2237 L23: 2.0314
REMARK 3 S TENSOR
REMARK 3 S11: 0.5237 S12: -0.7713 S13: 1.2185
REMARK 3 S21: 0.9686 S22: -0.2476 S23: 0.9339
REMARK 3 S31: 0.1384 S32: 0.4047 S33: -0.0413
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2541 -3.0824 23.3288
REMARK 3 T TENSOR
REMARK 3 T11: 0.1281 T22: 0.1961
REMARK 3 T33: 0.0924 T12: 0.0168
REMARK 3 T13: 0.0143 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 4.1783 L22: 5.0880
REMARK 3 L33: 2.7026 L12: 0.6276
REMARK 3 L13: -0.8363 L23: -0.4317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0453 S12: -0.1536 S13: -0.1636
REMARK 3 S21: 0.2018 S22: -0.0497 S23: 0.1398
REMARK 3 S31: 0.0248 S32: -0.1355 S33: 0.0065
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 438 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6058 2.0240 18.5631
REMARK 3 T TENSOR
REMARK 3 T11: 0.1707 T22: 0.1541
REMARK 3 T33: 0.1056 T12: -0.0053
REMARK 3 T13: 0.0131 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 7.7507 L22: 1.9081
REMARK 3 L33: 1.5683 L12: 0.7235
REMARK 3 L13: -0.8893 L23: 0.0882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0086 S12: -0.1066 S13: 0.4957
REMARK 3 S21: -0.0189 S22: 0.0085 S23: 0.0670
REMARK 3 S31: -0.1513 S32: 0.0482 S33: 0.0155
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 305 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1303 -7.6508 -1.0019
REMARK 3 T TENSOR
REMARK 3 T11: 0.3772 T22: 0.5609
REMARK 3 T33: 0.6608 T12: 0.0276
REMARK 3 T13: 0.1624 T23: -0.1727
REMARK 3 L TENSOR
REMARK 3 L11: 4.9670 L22: 6.6191
REMARK 3 L33: 2.0086 L12: -0.9225
REMARK 3 L13: 7.1619 L23: -1.2257
REMARK 3 S TENSOR
REMARK 3 S11: 0.8563 S12: 0.7416 S13: -0.8870
REMARK 3 S21: -0.2024 S22: 0.3153 S23: -1.4076
REMARK 3 S31: 0.9703 S32: 0.7505 S33: -0.8782
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1529 5.7138 -15.1118
REMARK 3 T TENSOR
REMARK 3 T11: 0.7657 T22: 0.5799
REMARK 3 T33: 0.0741 T12: -0.2503
REMARK 3 T13: -0.0327 T23: 0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 2.4680 L22: 4.2345
REMARK 3 L33: 2.5702 L12: -0.4651
REMARK 3 L13: 0.4020 L23: 0.2741
REMARK 3 S TENSOR
REMARK 3 S11: -0.5682 S12: 0.1533 S13: -0.0626
REMARK 3 S21: -0.9674 S22: 0.3532 S23: 0.8160
REMARK 3 S31: -0.9732 S32: 0.3075 S33: 0.1718
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8964 -1.0013 -11.7924
REMARK 3 T TENSOR
REMARK 3 T11: 0.4105 T22: 0.3324
REMARK 3 T33: 0.1916 T12: -0.1194
REMARK 3 T13: -0.0208 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 5.9525 L22: 5.7744
REMARK 3 L33: 6.5375 L12: -0.4808
REMARK 3 L13: 3.1924 L23: -0.3148
REMARK 3 S TENSOR
REMARK 3 S11: -0.5733 S12: 0.6103 S13: 0.1624
REMARK 3 S21: -0.5271 S22: 0.3133 S23: 0.2508
REMARK 3 S31: -0.2586 S32: -0.0863 S33: 0.2110
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 364 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4261 -15.5903 -1.4423
REMARK 3 T TENSOR
REMARK 3 T11: 0.5213 T22: 0.3291
REMARK 3 T33: 0.6139 T12: 0.1758
REMARK 3 T13: -0.0621 T23: -0.1557
REMARK 3 L TENSOR
REMARK 3 L11: 4.4254 L22: 5.7784
REMARK 3 L33: 2.7666 L12: 5.0188
REMARK 3 L13: 0.7909 L23: 1.3287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: 0.0133 S13: -1.4869
REMARK 3 S21: 0.1564 S22: 0.7288 S23: -0.6404
REMARK 3 S31: 0.5573 S32: 1.1737 S33: -0.3773
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7203 5.0704 -5.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.3771 T22: 0.2296
REMARK 3 T33: 0.1674 T12: -0.0486
REMARK 3 T13: -0.0168 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 4.1579 L22: 5.7056
REMARK 3 L33: 5.2831 L12: 1.0803
REMARK 3 L13: 1.0792 L23: 0.3133
REMARK 3 S TENSOR
REMARK 3 S11: -0.2450 S12: 0.3055 S13: 0.3587
REMARK 3 S21: -0.7726 S22: 0.0090 S23: 0.5073
REMARK 3 S31: -0.6486 S32: -0.0895 S33: 0.2089
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6483 12.7238 2.2055
REMARK 3 T TENSOR
REMARK 3 T11: 0.4078 T22: 0.2316
REMARK 3 T33: 0.1937 T12: 0.0448
REMARK 3 T13: 0.0283 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.1508 L22: 9.2178
REMARK 3 L33: 6.4654 L12: 1.5892
REMARK 3 L13: 6.5658 L23: 0.3607
REMARK 3 S TENSOR
REMARK 3 S11: -0.7821 S12: -0.3771 S13: 0.9799
REMARK 3 S21: -0.2882 S22: 0.1963 S23: 0.3223
REMARK 3 S31: -1.0433 S32: -0.2811 S33: 0.4705
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7442 -3.3783 6.1360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1133 T22: 0.2530
REMARK 3 T33: 0.1778 T12: 0.0355
REMARK 3 T13: 0.0555 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 5.8825 L22: 4.9854
REMARK 3 L33: 5.1693 L12: 0.7410
REMARK 3 L13: 2.8027 L23: 1.4548
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: 0.1748 S13: -0.5292
REMARK 3 S21: -0.1672 S22: -0.0050 S23: -0.3281
REMARK 3 S31: 0.2255 S32: 0.2491 S33: -0.0421
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1088 0.4668 1.9659
REMARK 3 T TENSOR
REMARK 3 T11: 0.2077 T22: 0.3006
REMARK 3 T33: 0.1794 T12: 0.0120
REMARK 3 T13: 0.0243 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 4.6034 L22: 2.8612
REMARK 3 L33: 5.4993 L12: 0.8932
REMARK 3 L13: 2.2182 L23: 1.3964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: -0.0667 S13: 0.0129
REMARK 3 S21: -0.3514 S22: -0.1754 S23: 0.4436
REMARK 3 S31: -0.0139 S32: -0.9698 S33: 0.1779
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 687 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1316 16.8040 27.1515
REMARK 3 T TENSOR
REMARK 3 T11: 0.4418 T22: 0.3894
REMARK 3 T33: 0.5316 T12: 0.1043
REMARK 3 T13: 0.0752 T23: -0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 7.1928 L22: 6.7406
REMARK 3 L33: 7.4618 L12: -1.4936
REMARK 3 L13: -7.1456 L23: 1.1971
REMARK 3 S TENSOR
REMARK 3 S11: -0.2171 S12: -0.6669 S13: 1.6270
REMARK 3 S21: 0.9445 S22: 0.2747 S23: 0.7798
REMARK 3 S31: -1.3141 S32: -0.6984 S33: -0.0672
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 688 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9056 -16.2806 -10.8541
REMARK 3 T TENSOR
REMARK 3 T11: 0.6136 T22: 0.3270
REMARK 3 T33: 0.5057 T12: -0.0600
REMARK 3 T13: 0.0593 T23: -0.1294
REMARK 3 L TENSOR
REMARK 3 L11: 2.0098 L22: 2.0100
REMARK 3 L33: 9.9523 L12: 2.8230
REMARK 3 L13: 7.4251 L23: -0.6250
REMARK 3 S TENSOR
REMARK 3 S11: 0.4405 S12: 1.0426 S13: -1.6385
REMARK 3 S21: -0.8582 S22: -0.4867 S23: 0.3073
REMARK 3 S31: 1.7232 S32: -0.0198 S33: 0.0939
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 5KRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-11
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 : 23493
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
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 (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
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 (%): 40.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
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 41.36000
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: 5080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 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 TYR B 331
REMARK 465 ASP B 332
REMARK 465 PRO B 333
REMARK 465 THR B 334
REMARK 465 ARG B 335
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 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 LEU A 306 CG CD1 CD2
REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 416 CG CD CE NZ
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 LYS A 472 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 330 CG CD OE1 OE2
REMARK 470 PHE B 337 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 372 CG CD1 CD2
REMARK 470 GLU B 397 CG CD OE1 OE2
REMARK 470 LYS B 416 CG CD CE NZ
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 472 CG CD CE NZ
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 ASN B 532 CG OD1 ND2
REMARK 470 ASP B 545 CG OD1 OD2
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 687 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 688 CG CD CE NZ
REMARK 470 LYS D 688 CG CD CE NZ
REMARK 470 ARG D 692 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 695 CG CD OE1 NE2
REMARK 470 ASP D 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 CB ASN B 532 N VAL B 534 1.64
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 GLU A 330 41.03 -91.97
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 6WR A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WR B 601
DBREF 5KRL A 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KRL B 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KRL C 686 699 PDB 5KRL 5KRL 686 699
DBREF 5KRL D 686 699 PDB 5KRL 5KRL 686 699
SEQADV 5KRL SER A 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQADV 5KRL 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 6WR A 601 18
HET 6WR B 601 18
HETNAM 6WR (1~{S},3~{A}~{R},7~{A}~{S})-5-(2-CHLORANYL-4-OXIDANYL-
HETNAM 2 6WR PHENYL)-2,3,3~{A},4,7,7~{A}-HEXAHYDRO-1~{H}-INDEN-1-OL
FORMUL 5 6WR 2(C15 H17 CL O2)
FORMUL 7 HOH *226(H2 O)
HELIX 1 AA1 SER A 305 LEU A 310 1 6
HELIX 2 AA2 THR A 311 ALA A 322 1 12
HELIX 3 AA3 SER A 338 ARG A 363 1 26
HELIX 4 AA4 THR A 371 SER A 395 1 25
HELIX 5 AA5 ARG A 412 LYS A 416 1 5
HELIX 6 AA6 MET A 421 ASN A 439 1 19
HELIX 7 AA7 GLN A 441 SER A 456 1 16
HELIX 8 AA8 GLU A 471 ALA A 493 1 23
HELIX 9 AA9 THR A 496 LYS A 531 1 36
HELIX 10 AB1 SER A 537 ALA A 546 1 10
HELIX 11 AB2 HIS A 547 ARG A 548 5 2
HELIX 12 AB3 SER B 305 SER B 309 5 5
HELIX 13 AB4 THR B 311 ALA B 322 1 12
HELIX 14 AB5 SER B 338 LYS B 362 1 25
HELIX 15 AB6 THR B 371 SER B 395 1 25
HELIX 16 AB7 ASN B 413 VAL B 418 5 6
HELIX 17 AB8 GLY B 420 ASN B 439 1 20
HELIX 18 AB9 GLN B 441 SER B 456 1 16
HELIX 19 AC1 LYS B 472 ALA B 493 1 22
HELIX 20 AC2 THR B 496 LYS B 531 1 36
HELIX 21 AC3 SER B 537 ALA B 546 1 10
HELIX 22 AC4 LYS C 688 LEU C 694 1 7
HELIX 23 AC5 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 7 MET A 343 LEU A 346 GLU A 353 LEU A 387
SITE 2 AC1 7 MET A 388 GLY A 521 HIS A 524
SITE 1 AC2 4 LEU B 346 GLU B 353 MET B 388 HIS B 524
CRYST1 55.860 82.720 58.580 90.00 109.36 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 0.017902 0.000000 0.006290 0.00000
SCALE2 0.000000 0.012089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018094 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
