HEADER TRANSCRIPTION 31-AUG-15 5DIE
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN IN COMPLEX
TITLE 2 WITH A TRIFLUORO-SUBSTITUTED A-CD RING ESTROGEN DERIVATIVE (1S,3AR,
TITLE 3 5S,7AS)-7A-METHYL-5-(2,3,5-TRIFLUORO-4-HYDROXYPHENYL)OCTAHYDRO-1H-
TITLE 4 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: 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 06-MAR-24 5DIE 1 HEADER REMARK
REVDAT 1 04-MAY-16 5DIE 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. 2.24 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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.130
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 22567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2010
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 46.4585 - 5.3969 1.00 1660 160 0.1838 0.2394
REMARK 3 2 5.3969 - 4.2846 1.00 1629 160 0.1673 0.1973
REMARK 3 3 4.2846 - 3.7433 1.00 1622 154 0.1670 0.2166
REMARK 3 4 3.7433 - 3.4012 0.99 1619 159 0.1976 0.2406
REMARK 3 5 3.4012 - 3.1574 0.98 1584 155 0.2227 0.2433
REMARK 3 6 3.1574 - 2.9713 0.98 1578 154 0.2322 0.2769
REMARK 3 7 2.9713 - 2.8225 0.96 1534 143 0.2170 0.2803
REMARK 3 8 2.8225 - 2.6997 0.96 1549 152 0.2404 0.2840
REMARK 3 9 2.6997 - 2.5958 0.92 1514 144 0.2286 0.2779
REMARK 3 10 2.5958 - 2.5062 0.90 1414 147 0.2456 0.2518
REMARK 3 11 2.5062 - 2.4278 0.86 1403 140 0.2437 0.2583
REMARK 3 12 2.4278 - 2.3584 0.80 1292 122 0.2590 0.2760
REMARK 3 13 2.3584 - 2.2963 0.75 1206 118 0.2762 0.3709
REMARK 3 14 2.2963 - 2.2403 0.60 953 102 0.3122 0.3700
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.01
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 4014
REMARK 3 ANGLE : 0.684 5433
REMARK 3 CHIRALITY : 0.025 641
REMARK 3 PLANARITY : 0.002 671
REMARK 3 DIHEDRAL : 13.890 1505
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 305 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3525 1.2180 32.0160
REMARK 3 T TENSOR
REMARK 3 T11: 0.4724 T22: 0.3237
REMARK 3 T33: 0.3190 T12: 0.0837
REMARK 3 T13: 0.0147 T23: 0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 3.0924 L22: 4.2937
REMARK 3 L33: 2.2391 L12: 2.0294
REMARK 3 L13: 0.0886 L23: 1.7429
REMARK 3 S TENSOR
REMARK 3 S11: 0.2043 S12: -0.4967 S13: 0.9480
REMARK 3 S21: 0.5194 S22: -0.0969 S23: 0.5840
REMARK 3 S31: -0.0944 S32: 0.1229 S33: 0.0265
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9357 -1.1424 23.2229
REMARK 3 T TENSOR
REMARK 3 T11: 0.2828 T22: 0.2848
REMARK 3 T33: 0.2316 T12: 0.0253
REMARK 3 T13: 0.0454 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 3.0205 L22: 3.2188
REMARK 3 L33: 2.2487 L12: 0.9671
REMARK 3 L13: -0.3950 L23: 0.1305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: -0.1381 S13: 0.0488
REMARK 3 S21: 0.1834 S22: 0.0286 S23: 0.1005
REMARK 3 S31: -0.0361 S32: 0.1124 S33: -0.0150
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 456 THROUGH 470 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0280 16.4785 12.6540
REMARK 3 T TENSOR
REMARK 3 T11: 0.5818 T22: 0.6138
REMARK 3 T33: 0.7453 T12: -0.0104
REMARK 3 T13: 0.0860 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 6.0112 L22: 5.5905
REMARK 3 L33: 4.6494 L12: 5.7630
REMARK 3 L13: 0.6647 L23: 0.3288
REMARK 3 S TENSOR
REMARK 3 S11: 0.2812 S12: 1.1011 S13: 1.5467
REMARK 3 S21: -0.5145 S22: -0.1016 S23: -0.5441
REMARK 3 S31: -0.5486 S32: 0.1201 S33: -0.4151
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 471 THROUGH 531 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7876 2.8363 17.5198
REMARK 3 T TENSOR
REMARK 3 T11: 0.3411 T22: 0.3591
REMARK 3 T33: 0.2425 T12: 0.0107
REMARK 3 T13: 0.0228 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 5.8134 L22: 1.4788
REMARK 3 L33: 0.8649 L12: 0.3323
REMARK 3 L13: -0.3776 L23: -0.3753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: -0.1997 S13: 0.3114
REMARK 3 S21: 0.1023 S22: -0.0345 S23: -0.1044
REMARK 3 S31: -0.1412 S32: 0.0700 S33: -0.0253
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 532 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3497 7.1842 17.1692
REMARK 3 T TENSOR
REMARK 3 T11: 0.3876 T22: 0.3686
REMARK 3 T33: 0.6228 T12: 0.0556
REMARK 3 T13: 0.0097 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 5.4650 L22: 3.1352
REMARK 3 L33: 1.9519 L12: 1.9877
REMARK 3 L13: -0.9447 L23: 1.1755
REMARK 3 S TENSOR
REMARK 3 S11: 0.2816 S12: 0.3775 S13: 0.8387
REMARK 3 S21: -0.1222 S22: -0.1645 S23: 1.0240
REMARK 3 S31: -0.3396 S32: -0.4776 S33: 0.2178
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 305 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0114 -6.0577 -1.4578
REMARK 3 T TENSOR
REMARK 3 T11: 0.4654 T22: 0.5710
REMARK 3 T33: 0.5785 T12: 0.0771
REMARK 3 T13: 0.1023 T23: -0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 7.8415 L22: 2.8721
REMARK 3 L33: 8.0300 L12: -1.1226
REMARK 3 L13: 2.7318 L23: 0.8776
REMARK 3 S TENSOR
REMARK 3 S11: 0.2891 S12: 0.7504 S13: -0.6827
REMARK 3 S21: -0.0329 S22: 0.0303 S23: -0.6115
REMARK 3 S31: 0.9318 S32: 1.1611 S33: -0.3271
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 323 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2082 9.4963 -16.7377
REMARK 3 T TENSOR
REMARK 3 T11: 0.8581 T22: 0.6030
REMARK 3 T33: 0.2610 T12: -0.0142
REMARK 3 T13: -0.0244 T23: 0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 4.2960 L22: 7.9140
REMARK 3 L33: 4.8113 L12: 0.3573
REMARK 3 L13: 4.3037 L23: 0.2874
REMARK 3 S TENSOR
REMARK 3 S11: -0.5957 S12: 0.1898 S13: 0.5033
REMARK 3 S21: -1.0002 S22: -0.0627 S23: 0.8415
REMARK 3 S31: -1.6404 S32: -0.1947 S33: -0.5308
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9513 4.6684 -4.0953
REMARK 3 T TENSOR
REMARK 3 T11: 0.3370 T22: 0.2838
REMARK 3 T33: 0.2392 T12: 0.0206
REMARK 3 T13: 0.0323 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 3.1106 L22: 3.3395
REMARK 3 L33: 3.4548 L12: -0.1850
REMARK 3 L13: 0.7689 L23: 0.2170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0275 S12: 0.0439 S13: -0.0515
REMARK 3 S21: -0.3650 S22: -0.0521 S23: 0.1168
REMARK 3 S31: -0.1628 S32: 0.0361 S33: 0.1070
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 456 THROUGH 472 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6198 -16.5739 9.0668
REMARK 3 T TENSOR
REMARK 3 T11: 1.0034 T22: 0.6118
REMARK 3 T33: 0.7591 T12: 0.0916
REMARK 3 T13: 0.1228 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 2.7459 L22: 3.2471
REMARK 3 L33: 1.4907 L12: -2.8790
REMARK 3 L13: -1.5911 L23: 1.8858
REMARK 3 S TENSOR
REMARK 3 S11: -0.7087 S12: 0.8487 S13: -0.7973
REMARK 3 S21: 2.6910 S22: -0.0069 S23: -0.9915
REMARK 3 S31: 1.1919 S32: -0.2892 S33: 0.9065
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 473 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3754 -2.5212 8.4592
REMARK 3 T TENSOR
REMARK 3 T11: 0.2932 T22: 0.4580
REMARK 3 T33: 0.3662 T12: 0.0814
REMARK 3 T13: 0.0078 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 6.0537 L22: 6.7514
REMARK 3 L33: 3.8722 L12: 2.5068
REMARK 3 L13: 0.4286 L23: 1.5930
REMARK 3 S TENSOR
REMARK 3 S11: 0.1411 S12: -0.2060 S13: -0.5862
REMARK 3 S21: -0.0051 S22: -0.2797 S23: -0.8219
REMARK 3 S31: 0.3080 S32: 0.4008 S33: 0.0136
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 528 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1473 5.4169 7.2886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2897 T22: 0.3344
REMARK 3 T33: 0.2898 T12: 0.0210
REMARK 3 T13: 0.0581 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 4.5596 L22: 3.0902
REMARK 3 L33: 3.3072 L12: 0.6810
REMARK 3 L13: 0.8289 L23: 0.7609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: 0.0398 S13: 0.2943
REMARK 3 S21: -0.0293 S22: -0.1047 S23: 0.2617
REMARK 3 S31: -0.0877 S32: -0.3084 S33: 0.0497
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 529 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3753 -4.3822 -7.6689
REMARK 3 T TENSOR
REMARK 3 T11: 0.5077 T22: 0.5458
REMARK 3 T33: 0.7752 T12: -0.0318
REMARK 3 T13: -0.0306 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 6.3436 L22: 6.0082
REMARK 3 L33: 8.6255 L12: -0.4825
REMARK 3 L13: -0.7521 L23: 1.1113
REMARK 3 S TENSOR
REMARK 3 S11: 0.2757 S12: 0.0047 S13: 0.0808
REMARK 3 S21: -0.2884 S22: -0.0385 S23: 1.2849
REMARK 3 S31: 0.6517 S32: -1.2367 S33: 0.0382
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 687 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0655 18.4806 27.0058
REMARK 3 T TENSOR
REMARK 3 T11: 0.4274 T22: 0.3723
REMARK 3 T33: 0.6510 T12: 0.0178
REMARK 3 T13: 0.1588 T23: -0.1086
REMARK 3 L TENSOR
REMARK 3 L11: 4.6416 L22: 7.1514
REMARK 3 L33: 5.0338 L12: -4.3123
REMARK 3 L13: -4.5354 L23: 3.1658
REMARK 3 S TENSOR
REMARK 3 S11: 0.5083 S12: -0.4875 S13: 0.3948
REMARK 3 S21: -0.2930 S22: -0.3962 S23: 0.2054
REMARK 3 S31: -0.9293 S32: -0.2860 S33: -0.1349
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 687 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1453 -15.0908 -11.2343
REMARK 3 T TENSOR
REMARK 3 T11: 0.9345 T22: 0.4994
REMARK 3 T33: 0.6733 T12: 0.0068
REMARK 3 T13: -0.0256 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 9.4869 L22: 2.6759
REMARK 3 L33: 6.0807 L12: -3.4428
REMARK 3 L13: 5.1588 L23: 0.2895
REMARK 3 S TENSOR
REMARK 3 S11: 0.8898 S12: 0.9968 S13: -1.5443
REMARK 3 S21: -0.5865 S22: -0.5914 S23: 0.2779
REMARK 3 S31: 1.8839 S32: -0.0704 S33: -0.3650
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 5DIE 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_1000213244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-10
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 : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23934
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 (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
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 (%) : 67.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
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 (%): 45.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
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 42.02650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 PRO B 333
REMARK 465 THR B 334
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 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 SER C 697
REMARK 465 SER C 698
REMARK 465 SER C 699
REMARK 465 LYS D 686
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 SER A 305 OG
REMARK 470 LEU A 306 CG CD1 CD2
REMARK 470 LEU A 310 CG CD1 CD2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 ASP B 332 CG OD1 OD2
REMARK 470 ARG B 335 CG CD NE CZ NH1 NH2
REMARK 470 THR B 460 OG1 CG2
REMARK 470 LYS B 467 CG CD CE NZ
REMARK 470 GLU B 470 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 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 HIS D 687 CG ND1 CD2 CE1 NE2
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 TYR B 459 O HOH B 701 1.87
REMARK 500 OD1 ASP A 480 O HOH A 701 2.06
REMARK 500 O HOH C 702 O HOH C 703 2.12
REMARK 500 OE2 GLU B 385 O HOH B 702 2.14
REMARK 500 O HOH A 719 O HOH A 747 2.14
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 LEU A 306 -66.64 57.58
REMARK 500 GLU A 330 32.71 -91.89
REMARK 500 LEU B 306 -102.30 65.06
REMARK 500 VAL B 458 18.06 -66.94
REMARK 500 SER B 468 -122.86 178.74
REMARK 500 LEU B 469 63.64 -119.15
REMARK 500 GLU B 471 -161.68 58.97
REMARK 500 LYS B 472 -53.13 52.97
REMARK 500 CYS B 530 30.32 -79.44
REMARK 500 LYS B 531 6.28 -152.59
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 5CJ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5CJ 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: 5DK9 RELATED DB: PDB
REMARK 900 RELATED ID: 5DIG RELATED DB: PDB
REMARK 900 RELATED ID: 5DID RELATED DB: PDB
REMARK 900 RELATED ID: 5DI7 RELATED DB: PDB
DBREF 5DIE A 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DIE B 298 554 UNP P03372 ESR1_HUMAN 298 554
DBREF 5DIE C 686 699 UNP Q15596 NCOA2_HUMAN 686 699
DBREF 5DIE D 686 699 UNP Q15596 NCOA2_HUMAN 686 699
SEQADV 5DIE SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 5DIE 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 5CJ A 601 21
HET 5CJ B 601 21
HETNAM 5CJ (1S,3AR,5S,7AS)-7A-METHYL-5-(2,3,5-TRIFLUORO-4-
HETNAM 2 5CJ HYDROXYPHENYL)OCTAHYDRO-1H-INDEN-1-OL
FORMUL 5 5CJ 2(C16 H19 F3 O2)
FORMUL 7 HOH *95(H2 O)
HELIX 1 AA1 THR A 311 ALA A 322 1 12
HELIX 2 AA2 SER A 338 LYS A 362 1 25
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 MET A 421 ASN A 439 1 19
HELIX 6 AA6 GLN A 441 SER A 456 1 16
HELIX 7 AA7 GLU A 471 ALA A 493 1 23
HELIX 8 AA8 THR A 496 CYS A 530 1 35
HELIX 9 AA9 SER A 537 ALA A 546 1 10
HELIX 10 AB1 LEU B 306 LEU B 310 5 5
HELIX 11 AB2 THR B 311 ALA B 322 1 12
HELIX 12 AB3 SER B 338 LYS B 362 1 25
HELIX 13 AB4 GLY B 366 LEU B 370 5 5
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 MET B 421 ASN B 439 1 19
HELIX 17 AB8 GLN B 441 SER B 456 1 16
HELIX 18 AB9 LYS B 472 ALA B 493 1 22
HELIX 19 AC1 THR B 496 CYS B 530 1 35
HELIX 20 AC2 SER B 537 ALA B 546 1 10
HELIX 21 AC3 LYS C 688 LEU C 694 1 7
HELIX 22 AC4 LYS D 688 ASP D 696 1 9
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 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 GLU B 470 GLU B 471 0 17.62
SITE 1 AC1 12 MET A 343 LEU A 346 LEU A 349 ALA A 350
SITE 2 AC1 12 GLU A 353 LEU A 387 MET A 388 LEU A 391
SITE 3 AC1 12 ARG A 394 GLY A 521 HIS A 524 HOH A 718
SITE 1 AC2 12 LEU B 346 LEU B 349 ALA B 350 GLU B 353
SITE 2 AC2 12 LEU B 387 MET B 388 LEU B 391 ARG B 394
SITE 3 AC2 12 MET B 421 GLY B 521 HIS B 524 HOH B 707
CRYST1 56.137 84.053 58.536 90.00 108.35 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 0.017814 0.000000 0.005908 0.00000
SCALE2 0.000000 0.011897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017999 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
