HEADER TRANSCRIPTION 05-MAY-15 4ZNU
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN (Y537S) IN
TITLE 2 COMPLEX WITH A 2-METHYL-SUBSTITUTED OBHS DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, UNP RESIDUES 301-559;
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-INTERACTING PEPTIDE;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: UNP RESIDUES 686-698;
COMPND 13 SYNONYM: NCOA-2,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75,BHLHE75,
COMPND 14 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2,HTIF2;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESR1, ESR, NR3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, LIGAND BINDING, PROTEIN-
KEYWDS 2 LIGAND COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.NWACHUKWU,S.SRINIVASAN,Y.ZHENG,S.WANG,J.MIN,C.DONG,Z.LIAO,
AUTHOR 2 V.CAVETT,J.NOWAK,R.HOUTMAN,K.E.CARLSON,J.S.JOSAN,O.ELEMENTO,
AUTHOR 3 J.A.KATZENELLENBOGEN,H.B.ZHOU,K.W.NETTLES
REVDAT 2 27-SEP-23 4ZNU 1 REMARK
REVDAT 1 04-MAY-16 4ZNU 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. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.9
REMARK 3 NUMBER OF REFLECTIONS : 15961
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 816
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 0.0000 - 4.3571 0.97 3054 160 0.1749 0.2092
REMARK 3 2 4.3571 - 3.4587 0.99 3069 160 0.1739 0.2201
REMARK 3 3 3.4587 - 3.0216 0.95 2937 168 0.2233 0.2936
REMARK 3 4 3.0216 - 2.7453 0.92 2808 149 0.2451 0.2791
REMARK 3 5 2.7453 - 2.5486 0.71 2181 110 0.2407 0.3123
REMARK 3 6 2.5486 - 2.4000 0.36 1096 69 0.2592 0.3405
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.81
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 : 0.004 3867
REMARK 3 ANGLE : 0.805 5243
REMARK 3 CHIRALITY : 0.053 627
REMARK 3 PLANARITY : 0.003 646
REMARK 3 DIHEDRAL : 15.620 1409
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6025 0.6407 28.7946
REMARK 3 T TENSOR
REMARK 3 T11: 0.4853 T22: 0.9990
REMARK 3 T33: 0.7753 T12: 0.1069
REMARK 3 T13: 0.1145 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 6.5726 L22: 8.2740
REMARK 3 L33: 7.9570 L12: -0.1460
REMARK 3 L13: 5.2973 L23: 0.4677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0786 S12: -0.0982 S13: 0.1514
REMARK 3 S21: -0.1718 S22: 0.6173 S23: -1.2682
REMARK 3 S31: 0.7660 S32: 2.4076 S33: -0.6049
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0207 8.2328 10.3199
REMARK 3 T TENSOR
REMARK 3 T11: 0.6411 T22: 0.9674
REMARK 3 T33: 0.5428 T12: 0.0017
REMARK 3 T13: -0.1361 T23: 0.0953
REMARK 3 L TENSOR
REMARK 3 L11: 3.8426 L22: 5.1310
REMARK 3 L33: 5.3261 L12: 0.5163
REMARK 3 L13: -1.6597 L23: 0.1723
REMARK 3 S TENSOR
REMARK 3 S11: 0.1346 S12: 1.3039 S13: 0.2995
REMARK 3 S21: -1.0115 S22: -0.0195 S23: 1.0563
REMARK 3 S31: -0.7974 S32: -0.9092 S33: -0.0071
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 393 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2084 -2.5275 22.6369
REMARK 3 T TENSOR
REMARK 3 T11: 0.4145 T22: 0.3602
REMARK 3 T33: 0.4153 T12: -0.0556
REMARK 3 T13: 0.0672 T23: -0.0557
REMARK 3 L TENSOR
REMARK 3 L11: 4.0466 L22: 5.6643
REMARK 3 L33: 9.1346 L12: 0.1672
REMARK 3 L13: -0.9316 L23: -0.9293
REMARK 3 S TENSOR
REMARK 3 S11: -0.2810 S12: 0.1579 S13: -0.6478
REMARK 3 S21: -0.0641 S22: -0.0052 S23: -0.0263
REMARK 3 S31: 1.0594 S32: -0.2600 S33: 0.2832
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 394 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3275 15.1912 18.1110
REMARK 3 T TENSOR
REMARK 3 T11: 0.6042 T22: 0.5112
REMARK 3 T33: 0.3653 T12: 0.0270
REMARK 3 T13: -0.0760 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 9.7591 L22: 9.6322
REMARK 3 L33: 7.6816 L12: -0.4386
REMARK 3 L13: -1.5070 L23: 0.8060
REMARK 3 S TENSOR
REMARK 3 S11: -0.5033 S12: 0.6682 S13: 0.8597
REMARK 3 S21: -0.4725 S22: 0.3455 S23: 0.3719
REMARK 3 S31: -1.9916 S32: -0.6100 S33: 0.0499
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0431 12.5473 21.0334
REMARK 3 T TENSOR
REMARK 3 T11: 0.6732 T22: 1.4125
REMARK 3 T33: 0.8256 T12: 0.3041
REMARK 3 T13: -0.1482 T23: 0.1123
REMARK 3 L TENSOR
REMARK 3 L11: 6.7588 L22: 4.7767
REMARK 3 L33: 9.0613 L12: -1.1412
REMARK 3 L13: -4.0716 L23: -4.1905
REMARK 3 S TENSOR
REMARK 3 S11: -0.2472 S12: 0.3461 S13: -0.6938
REMARK 3 S21: -0.1138 S22: 1.2412 S23: 1.3293
REMARK 3 S31: -0.6923 S32: -2.3569 S33: -1.0087
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6580 15.0329 29.3644
REMARK 3 T TENSOR
REMARK 3 T11: 0.6377 T22: 0.5327
REMARK 3 T33: 0.5882 T12: 0.1261
REMARK 3 T13: 0.0007 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 2.4307 L22: 2.7182
REMARK 3 L33: 6.2822 L12: 1.9595
REMARK 3 L13: 4.2261 L23: 1.9143
REMARK 3 S TENSOR
REMARK 3 S11: -0.8141 S12: -0.7572 S13: 1.7400
REMARK 3 S21: -0.0674 S22: 0.1775 S23: 0.9718
REMARK 3 S31: -1.3549 S32: -0.9451 S33: 0.6083
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 438 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0733 6.8822 30.7137
REMARK 3 T TENSOR
REMARK 3 T11: 0.3182 T22: 0.4759
REMARK 3 T33: 0.3579 T12: -0.0093
REMARK 3 T13: -0.0155 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 5.9123 L22: 4.5267
REMARK 3 L33: 9.5023 L12: -1.3679
REMARK 3 L13: 0.7294 L23: 2.1845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0613 S13: 0.0963
REMARK 3 S21: -0.1145 S22: -0.1171 S23: 0.0098
REMARK 3 S31: -0.3061 S32: 1.0863 S33: 0.1312
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 456 THROUGH 467 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9988 -11.9077 39.2369
REMARK 3 T TENSOR
REMARK 3 T11: 1.6713 T22: 1.1751
REMARK 3 T33: 0.7181 T12: -0.0421
REMARK 3 T13: 0.3362 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 3.5890 L22: 3.5599
REMARK 3 L33: 4.8295 L12: 0.9670
REMARK 3 L13: -2.2463 L23: 2.3641
REMARK 3 S TENSOR
REMARK 3 S11: -0.6598 S12: -1.0689 S13: -1.0241
REMARK 3 S21: 1.3674 S22: -0.3286 S23: 0.0895
REMARK 3 S31: 2.7868 S32: -0.4617 S33: 1.1213
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 468 THROUGH 497 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9160 1.2443 38.6728
REMARK 3 T TENSOR
REMARK 3 T11: 0.3614 T22: 0.6594
REMARK 3 T33: 0.4038 T12: 0.0845
REMARK 3 T13: -0.0226 T23: 0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 5.7067 L22: 8.4994
REMARK 3 L33: 8.5690 L12: 0.1193
REMARK 3 L13: 0.4440 L23: 1.9664
REMARK 3 S TENSOR
REMARK 3 S11: -0.2601 S12: 0.2386 S13: -0.2957
REMARK 3 S21: 0.6754 S22: 0.2522 S23: -0.8609
REMARK 3 S31: 0.6739 S32: 0.9752 S33: 0.1168
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 498 THROUGH 527 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9231 6.9533 35.7682
REMARK 3 T TENSOR
REMARK 3 T11: 0.3726 T22: 0.3480
REMARK 3 T33: 0.2498 T12: -0.0260
REMARK 3 T13: 0.0369 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 7.4985 L22: 6.0016
REMARK 3 L33: 7.8962 L12: 0.4608
REMARK 3 L13: 1.0569 L23: -0.1190
REMARK 3 S TENSOR
REMARK 3 S11: 0.2710 S12: -0.2207 S13: -0.0071
REMARK 3 S21: 0.2806 S22: -0.3656 S23: 0.1652
REMARK 3 S31: 0.1084 S32: -0.4206 S33: 0.1543
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 528 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1186 -7.6398 20.6928
REMARK 3 T TENSOR
REMARK 3 T11: 0.6858 T22: 1.1751
REMARK 3 T33: 1.2336 T12: -0.3736
REMARK 3 T13: -0.0727 T23: -0.2396
REMARK 3 L TENSOR
REMARK 3 L11: 8.8388 L22: 3.9473
REMARK 3 L33: 3.5754 L12: -4.3134
REMARK 3 L13: -0.5916 L23: -0.1680
REMARK 3 S TENSOR
REMARK 3 S11: 0.3587 S12: -2.0271 S13: 0.1504
REMARK 3 S21: 0.2765 S22: -0.3282 S23: 0.4949
REMARK 3 S31: 0.1683 S32: -1.1815 S33: -0.2121
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 688 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6676 -14.8556 18.9230
REMARK 3 T TENSOR
REMARK 3 T11: 1.1183 T22: 0.6046
REMARK 3 T33: 0.9902 T12: 0.1676
REMARK 3 T13: 0.1729 T23: -0.2153
REMARK 3 L TENSOR
REMARK 3 L11: 2.0154 L22: 2.0257
REMARK 3 L33: 8.5249 L12: -3.9517
REMARK 3 L13: 4.5786 L23: 1.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.6433 S12: 0.5726 S13: -2.9760
REMARK 3 S21: -0.6530 S22: 1.0297 S23: -0.0026
REMARK 3 S31: 1.1881 S32: 1.1751 S33: -0.4003
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 306 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6881 16.7567 59.6934
REMARK 3 T TENSOR
REMARK 3 T11: 0.7727 T22: 0.6213
REMARK 3 T33: 0.4948 T12: -0.2048
REMARK 3 T13: -0.0392 T23: -0.1327
REMARK 3 L TENSOR
REMARK 3 L11: 6.6271 L22: 7.2441
REMARK 3 L33: 8.0852 L12: 1.7491
REMARK 3 L13: -1.6649 L23: -5.2006
REMARK 3 S TENSOR
REMARK 3 S11: 1.0378 S12: -0.9851 S13: 0.8671
REMARK 3 S21: 2.0923 S22: -0.8627 S23: -0.0733
REMARK 3 S31: -0.6124 S32: 0.8281 S33: -0.0884
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9816 -5.1056 61.1114
REMARK 3 T TENSOR
REMARK 3 T11: 0.6777 T22: 0.5694
REMARK 3 T33: 0.5241 T12: -0.1295
REMARK 3 T13: 0.2066 T23: -0.1112
REMARK 3 L TENSOR
REMARK 3 L11: 5.8731 L22: 9.7136
REMARK 3 L33: 5.2311 L12: 2.2904
REMARK 3 L13: 2.1731 L23: 0.8661
REMARK 3 S TENSOR
REMARK 3 S11: -0.2611 S12: -0.7861 S13: -0.6131
REMARK 3 S21: 0.1817 S22: -0.5289 S23: 1.1427
REMARK 3 S31: 0.4755 S32: -0.5455 S33: 0.7866
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1988 5.8150 54.6348
REMARK 3 T TENSOR
REMARK 3 T11: 0.4488 T22: 0.3731
REMARK 3 T33: 0.3255 T12: -0.0287
REMARK 3 T13: 0.0442 T23: -0.0835
REMARK 3 L TENSOR
REMARK 3 L11: 4.6565 L22: 0.8945
REMARK 3 L33: 5.6939 L12: 0.0448
REMARK 3 L13: -1.4511 L23: -2.5824
REMARK 3 S TENSOR
REMARK 3 S11: -0.2413 S12: 0.1356 S13: -0.0669
REMARK 3 S21: -0.2766 S22: 0.0256 S23: -0.0008
REMARK 3 S31: -0.1176 S32: -0.7073 S33: 0.1705
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 397 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7063 5.2669 49.9502
REMARK 3 T TENSOR
REMARK 3 T11: 0.3965 T22: 0.3610
REMARK 3 T33: 0.3014 T12: -0.0779
REMARK 3 T13: 0.0480 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 5.9436 L22: 5.5784
REMARK 3 L33: 6.1455 L12: 0.1726
REMARK 3 L13: -0.3674 L23: -0.7796
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: 0.3108 S13: 0.0661
REMARK 3 S21: -0.2918 S22: -0.2020 S23: 0.1815
REMARK 3 S31: 0.2820 S32: -0.1883 S33: 0.1386
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 398 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5592 -13.5731 53.1652
REMARK 3 T TENSOR
REMARK 3 T11: 1.1669 T22: 0.4308
REMARK 3 T33: 0.8690 T12: -0.0683
REMARK 3 T13: 0.2405 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 4.2654 L22: 1.7203
REMARK 3 L33: 4.5271 L12: -1.3273
REMARK 3 L13: -0.5015 L23: -1.0837
REMARK 3 S TENSOR
REMARK 3 S11: -0.3611 S12: 0.2424 S13: -1.4790
REMARK 3 S21: -0.0729 S22: 0.0369 S23: 0.5794
REMARK 3 S31: 2.2649 S32: -0.3182 S33: 0.2780
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2667 -9.3565 47.4072
REMARK 3 T TENSOR
REMARK 3 T11: 0.9027 T22: 0.4886
REMARK 3 T33: 0.6059 T12: 0.0397
REMARK 3 T13: 0.1405 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 2.3985 L22: 2.8584
REMARK 3 L33: 6.4081 L12: 6.5802
REMARK 3 L13: 5.5897 L23: 1.9262
REMARK 3 S TENSOR
REMARK 3 S11: 0.3417 S12: 0.2536 S13: -1.5265
REMARK 3 S21: 0.4486 S22: -0.2714 S23: -0.3727
REMARK 3 S31: 1.7296 S32: 0.1675 S33: -0.0356
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 438 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6003 7.6022 50.1204
REMARK 3 T TENSOR
REMARK 3 T11: 0.4016 T22: 0.3217
REMARK 3 T33: 0.3399 T12: -0.1163
REMARK 3 T13: -0.0056 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 9.1905 L22: 5.9008
REMARK 3 L33: 7.9749 L12: -0.6249
REMARK 3 L13: -5.4027 L23: 0.5116
REMARK 3 S TENSOR
REMARK 3 S11: 0.0768 S12: 0.2287 S13: -0.0245
REMARK 3 S21: 0.2770 S22: -0.1493 S23: 0.1822
REMARK 3 S31: -0.3913 S32: 0.3561 S33: 0.1470
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1182 12.8026 51.4458
REMARK 3 T TENSOR
REMARK 3 T11: 0.5219 T22: 0.5596
REMARK 3 T33: 0.4687 T12: -0.1720
REMARK 3 T13: -0.1247 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 5.8942 L22: 5.7718
REMARK 3 L33: 5.0105 L12: -0.7020
REMARK 3 L13: -0.4466 L23: -1.6388
REMARK 3 S TENSOR
REMARK 3 S11: -0.2596 S12: -0.7027 S13: 0.6078
REMARK 3 S21: 1.0598 S22: -0.2312 S23: -0.6387
REMARK 3 S31: -0.8078 S32: 0.6250 S33: 0.4175
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 527 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2539 0.7386 43.0076
REMARK 3 T TENSOR
REMARK 3 T11: 0.4419 T22: 0.2992
REMARK 3 T33: 0.2367 T12: -0.0117
REMARK 3 T13: 0.0179 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 9.8875 L22: 4.1140
REMARK 3 L33: 4.4906 L12: 1.5440
REMARK 3 L13: -2.7665 L23: -0.3344
REMARK 3 S TENSOR
REMARK 3 S11: -0.1213 S12: 0.1406 S13: -0.6777
REMARK 3 S21: 0.0196 S22: -0.0431 S23: -0.0589
REMARK 3 S31: 0.4457 S32: 0.0493 S33: 0.1280
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 528 THROUGH 537 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8626 -3.5801 47.6102
REMARK 3 T TENSOR
REMARK 3 T11: 1.1387 T22: 1.0248
REMARK 3 T33: 0.7897 T12: -0.3274
REMARK 3 T13: 0.0813 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 2.6015 L22: 2.0099
REMARK 3 L33: 6.8218 L12: 0.1521
REMARK 3 L13: 1.9501 L23: 7.5192
REMARK 3 S TENSOR
REMARK 3 S11: -0.3159 S12: 0.8127 S13: -0.9176
REMARK 3 S21: 1.2927 S22: 0.2374 S23: 2.5842
REMARK 3 S31: 0.9896 S32: -0.9768 S33: -0.0918
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 538 THROUGH 551 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9759 6.2797 42.0638
REMARK 3 T TENSOR
REMARK 3 T11: 0.6826 T22: 1.3628
REMARK 3 T33: 0.8030 T12: -0.2057
REMARK 3 T13: -0.0479 T23: -0.0931
REMARK 3 L TENSOR
REMARK 3 L11: 8.1674 L22: 8.8614
REMARK 3 L33: 4.2047 L12: 2.2845
REMARK 3 L13: 5.8276 L23: 1.3849
REMARK 3 S TENSOR
REMARK 3 S11: -1.1655 S12: 2.2861 S13: -0.8369
REMARK 3 S21: -1.4320 S22: 0.3175 S23: 1.1509
REMARK 3 S31: -0.3317 S32: 2.2247 S33: 0.1078
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 688 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5534 16.4967 54.3796
REMARK 3 T TENSOR
REMARK 3 T11: 0.8685 T22: 0.9295
REMARK 3 T33: 1.0864 T12: 0.1334
REMARK 3 T13: 0.0795 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 5.9798 L22: 5.7749
REMARK 3 L33: 1.9888 L12: 2.6118
REMARK 3 L13: 2.0851 L23: 2.2497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0952 S12: -0.8503 S13: 1.6898
REMARK 3 S21: 1.1845 S22: -0.6410 S23: 1.1418
REMARK 3 S31: -1.5012 S32: -2.5546 S33: 0.3689
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 4ZNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209590.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19202
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78700
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: 2B1V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
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 41.13500
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: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 SER A 301
REMARK 465 LYS A 302
REMARK 465 LYS A 303
REMARK 465 ASN A 304
REMARK 465 SER A 305
REMARK 465 PHE A 461
REMARK 465 LEU A 462
REMARK 465 SER A 463
REMARK 465 SER A 464
REMARK 465 LYS A 529
REMARK 465 CYS A 530
REMARK 465 LYS A 531
REMARK 465 ASN A 532
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 ARG A 555
REMARK 465 GLY A 556
REMARK 465 GLY A 557
REMARK 465 ALA A 558
REMARK 465 SER A 559
REMARK 465 LYS C 686
REMARK 465 HIS C 687
REMARK 465 SER C 697
REMARK 465 SER C 698
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 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 GLU B 471
REMARK 465 LYS B 472
REMARK 465 LYS B 529
REMARK 465 CYS B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 PRO B 552
REMARK 465 THR B 553
REMARK 465 SER B 554
REMARK 465 ARG B 555
REMARK 465 GLY B 556
REMARK 465 GLY B 557
REMARK 465 ALA B 558
REMARK 465 SER B 559
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 SER A 309 OG
REMARK 470 THR A 334 OG1 CG2
REMARK 470 PHE A 337 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 373 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 394 O
REMARK 470 MET A 396 O
REMARK 470 GLU A 397 CG CD OE1 OE2
REMARK 470 LYS A 416 CG CD CE NZ
REMARK 470 LEU A 466 CG CD1 CD2
REMARK 470 LYS A 467 CG CD CE NZ
REMARK 470 SER A 468 CB OG
REMARK 470 ARG A 477 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 481 CG CD CE NZ
REMARK 470 LYS A 492 CG CD CE NZ
REMARK 470 MET A 528 CG SD CE
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 688 CG CD CE NZ
REMARK 470 ARG C 692 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 LYS B 401 CG CD CE NZ
REMARK 470 TYR B 459 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 477 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 538 CG OD1 OD2
REMARK 470 LYS D 688 CG CD CE NZ
REMARK 470 ILE D 689 CG1 CG2 CD1
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 ALA A 307 22.01 -148.50
REMARK 500 ASP A 332 74.90 72.24
REMARK 500 PHE A 337 136.90 68.74
REMARK 500 THR A 496 -104.39 -64.22
REMARK 500 LEU A 497 -43.82 -161.33
REMARK 500 TYR A 526 33.52 -92.60
REMARK 500 VAL A 534 94.60 55.85
REMARK 500 TYR B 459 35.55 -88.99
REMARK 500 TYR B 526 38.17 -91.77
REMARK 500 LEU B 536 121.32 65.55
REMARK 500 LEU B 549 -13.35 -49.65
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 4Q9 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4Q9 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PP6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH RESVERATROL
REMARK 900 RELATED ID: 4ZN7 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZN9 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZNH RELATED DB: PDB
REMARK 900 RELATED ID: 4ZNS RELATED DB: PDB
REMARK 900 RELATED ID: 4ZNT RELATED DB: PDB
REMARK 900 RELATED ID: 4ZNV RELATED DB: PDB
REMARK 900 RELATED ID: 4ZNW RELATED DB: PDB
DBREF 4ZNU A 301 559 UNP P03372 ESR1_HUMAN 301 559
DBREF 4ZNU C 686 698 UNP Q15596 NCOA2_HUMAN 686 698
DBREF 4ZNU B 301 559 UNP P03372 ESR1_HUMAN 301 559
DBREF 4ZNU D 686 698 UNP Q15596 NCOA2_HUMAN 686 698
SEQADV 4ZNU SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 4ZNU SER B 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQRES 1 A 259 SER LYS LYS ASN SER LEU ALA LEU SER LEU THR ALA ASP
SEQRES 2 A 259 GLN MET VAL SER ALA LEU LEU ASP ALA GLU PRO PRO ILE
SEQRES 3 A 259 LEU TYR SER GLU TYR ASP PRO THR ARG PRO PHE SER GLU
SEQRES 4 A 259 ALA SER MET MET GLY LEU LEU THR ASN LEU ALA ASP ARG
SEQRES 5 A 259 GLU LEU VAL HIS MET ILE ASN TRP ALA LYS ARG VAL PRO
SEQRES 6 A 259 GLY PHE VAL ASP LEU THR LEU HIS ASP GLN VAL HIS LEU
SEQRES 7 A 259 LEU GLU CYS ALA TRP LEU GLU ILE LEU MET ILE GLY LEU
SEQRES 8 A 259 VAL TRP ARG SER MET GLU HIS PRO GLY LYS LEU LEU PHE
SEQRES 9 A 259 ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN GLY LYS CYS
SEQRES 10 A 259 VAL GLU GLY MET VAL GLU ILE PHE ASP MET LEU LEU ALA
SEQRES 11 A 259 THR SER SER ARG PHE ARG MET MET ASN LEU GLN GLY GLU
SEQRES 12 A 259 GLU PHE VAL CYS LEU LYS SER ILE ILE LEU LEU ASN SER
SEQRES 13 A 259 GLY VAL TYR THR PHE LEU SER SER THR LEU LYS SER LEU
SEQRES 14 A 259 GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU ASP LYS ILE
SEQRES 15 A 259 THR ASP THR LEU ILE HIS LEU MET ALA LYS ALA GLY LEU
SEQRES 16 A 259 THR LEU GLN GLN GLN HIS GLN ARG LEU ALA GLN LEU LEU
SEQRES 17 A 259 LEU ILE LEU SER HIS ILE ARG HIS MET SER ASN LYS GLY
SEQRES 18 A 259 MET GLU HIS LEU TYR SER MET LYS CYS LYS ASN VAL VAL
SEQRES 19 A 259 PRO LEU SER ASP LEU LEU LEU GLU MET LEU ASP ALA HIS
SEQRES 20 A 259 ARG LEU HIS ALA PRO THR SER ARG GLY GLY ALA SER
SEQRES 1 C 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 1 B 259 SER LYS LYS ASN SER LEU ALA LEU SER LEU THR ALA ASP
SEQRES 2 B 259 GLN MET VAL SER ALA LEU LEU ASP ALA GLU PRO PRO ILE
SEQRES 3 B 259 LEU TYR SER GLU TYR ASP PRO THR ARG PRO PHE SER GLU
SEQRES 4 B 259 ALA SER MET MET GLY LEU LEU THR ASN LEU ALA ASP ARG
SEQRES 5 B 259 GLU LEU VAL HIS MET ILE ASN TRP ALA LYS ARG VAL PRO
SEQRES 6 B 259 GLY PHE VAL ASP LEU THR LEU HIS ASP GLN VAL HIS LEU
SEQRES 7 B 259 LEU GLU CYS ALA TRP LEU GLU ILE LEU MET ILE GLY LEU
SEQRES 8 B 259 VAL TRP ARG SER MET GLU HIS PRO GLY LYS LEU LEU PHE
SEQRES 9 B 259 ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN GLY LYS CYS
SEQRES 10 B 259 VAL GLU GLY MET VAL GLU ILE PHE ASP MET LEU LEU ALA
SEQRES 11 B 259 THR SER SER ARG PHE ARG MET MET ASN LEU GLN GLY GLU
SEQRES 12 B 259 GLU PHE VAL CYS LEU LYS SER ILE ILE LEU LEU ASN SER
SEQRES 13 B 259 GLY VAL TYR THR PHE LEU SER SER THR LEU LYS SER LEU
SEQRES 14 B 259 GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU ASP LYS ILE
SEQRES 15 B 259 THR ASP THR LEU ILE HIS LEU MET ALA LYS ALA GLY LEU
SEQRES 16 B 259 THR LEU GLN GLN GLN HIS GLN ARG LEU ALA GLN LEU LEU
SEQRES 17 B 259 LEU ILE LEU SER HIS ILE ARG HIS MET SER ASN LYS GLY
SEQRES 18 B 259 MET GLU HIS LEU TYR SER MET LYS CYS LYS ASN VAL VAL
SEQRES 19 B 259 PRO LEU SER ASP LEU LEU LEU GLU MET LEU ASP ALA HIS
SEQRES 20 B 259 ARG LEU HIS ALA PRO THR SER ARG GLY GLY ALA SER
SEQRES 1 D 13 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
HET 4Q9 A 601 32
HET 4Q9 B 601 32
HETNAM 4Q9 2-METHYLPHENYL (1S,2R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-
HETNAM 2 4Q9 OXABICYCLO[2.2.1]HEPT-5-ENE-2-SULFONATE
FORMUL 5 4Q9 2(C25 H22 O6 S)
FORMUL 7 HOH *40(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 GLY A 366 LEU A 370 5 5
HELIX 4 AA4 THR A 371 ARG A 394 1 24
HELIX 5 AA5 ASP A 411 LYS A 416 1 6
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 LYS A 467 ALA A 493 1 27
HELIX 9 AA9 LEU A 497 TYR A 526 1 30
HELIX 10 AB1 SER A 537 ALA A 546 1 10
HELIX 11 AB2 ILE C 689 LEU C 694 1 6
HELIX 12 AB3 GLN C 695 ASP C 696 5 2
HELIX 13 AB4 LEU B 306 LEU B 310 5 5
HELIX 14 AB5 THR B 311 ALA B 322 1 12
HELIX 15 AB6 SER B 338 ARG B 363 1 26
HELIX 16 AB7 THR B 371 SER B 395 1 25
HELIX 17 AB8 ASP B 411 LYS B 416 1 6
HELIX 18 AB9 GLY B 420 ASN B 439 1 20
HELIX 19 AC1 GLN B 441 SER B 456 1 16
HELIX 20 AC2 HIS B 474 ALA B 493 1 20
HELIX 21 AC3 THR B 496 TYR B 526 1 31
HELIX 22 AC4 SER B 537 LEU B 549 1 13
HELIX 23 AC5 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
CISPEP 1 TYR A 331 ASP A 332 0 8.31
CISPEP 2 SER B 456 GLY B 457 0 -3.52
SITE 1 AC1 15 MET A 343 THR A 347 ALA A 350 GLU A 353
SITE 2 AC1 15 LEU A 387 MET A 388 ARG A 394 PHE A 404
SITE 3 AC1 15 VAL A 418 MET A 421 ILE A 424 GLY A 521
SITE 4 AC1 15 HIS A 524 LEU A 540 HOH A 707
SITE 1 AC2 16 MET B 343 THR B 347 ALA B 350 GLU B 353
SITE 2 AC2 16 LEU B 387 MET B 388 ARG B 394 VAL B 418
SITE 3 AC2 16 GLU B 419 MET B 421 ILE B 424 GLY B 521
SITE 4 AC2 16 HIS B 524 LEU B 525 LEU B 540 HOH B 703
CRYST1 55.960 82.270 58.500 90.00 111.05 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 0.017870 0.000000 0.006878 0.00000
SCALE2 0.000000 0.012155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018316 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
