HEADER TRANSCRIPTION 14-JUL-17 5WGD
TITLE ESTROGEN RECEPTOR ALPHA LIGAND BINDING DOMAIN IN COMPLEX WITH
TITLE 2 ESTRADIOL AND SRC2-LP1
CAVEAT 5WGD ILE E 4 HAS WRONG CHIRALITY AT ATOM CB ILE F 3 HAS WRONG
CAVEAT 2 5WGD CHIRALITY AT ATOM CB THE MODELED PEPTIDE SRC2-LP1 HAVE
CAVEAT 3 5WGD DIFFERENT SEQUENCE IDENTITY BETWEEN THE CHAINS E AND F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 5 GROUP A MEMBER 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: (ACE)HKILHKLLQDS(NH2);
COMPND 10 CHAIN: E;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: (ACE)AILHKLLQDS(NH2);
COMPND 14 CHAIN: F;
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: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630
KEYWDS BREAST CANCER, STAPLED PEPTIDES, SYNTHETIC PEPTIDES, HORMONE,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.FANNING,T.E.SPELTZ,C.G.MAYNE,Z.SIDDIQUI,G.L.GREENE,E.TAJKHORSHID,
AUTHOR 2 T.W.MOORE
REVDAT 3 04-OCT-23 5WGD 1 REMARK
REVDAT 2 26-FEB-20 5WGD 1 REMARK LINK SITE
REVDAT 1 13-JUN-18 5WGD 0
JRNL AUTH T.E.SPELTZ,C.G.MAYNE,S.W.FANNING,Z.SIDDIQUI,E.TAJKHORSHID,
JRNL AUTH 2 G.L.GREENE,T.W.MOORE
JRNL TITL A "CROSS-STITCHED" PEPTIDE WITH IMPROVED HELICITY AND
JRNL TITL 2 PROTEOLYTIC STABILITY.
JRNL REF ORG. BIOMOL. CHEM. V. 16 3702 2018
JRNL REFN ESSN 1477-0539
JRNL PMID 29725689
JRNL DOI 10.1039/C8OB00790J
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 42687
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2083
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 26.6019 - 4.4420 0.94 2895 134 0.1777 0.1860
REMARK 3 2 4.4420 - 3.5283 0.99 2961 162 0.1435 0.1678
REMARK 3 3 3.5283 - 3.0831 0.99 2969 145 0.1647 0.1951
REMARK 3 4 3.0831 - 2.8015 0.98 2943 148 0.1744 0.2094
REMARK 3 5 2.8015 - 2.6009 0.99 2980 144 0.1872 0.2500
REMARK 3 6 2.6009 - 2.4477 0.98 2913 169 0.1761 0.2356
REMARK 3 7 2.4477 - 2.3252 0.98 2938 126 0.1747 0.1964
REMARK 3 8 2.3252 - 2.2240 0.97 2883 161 0.1745 0.2055
REMARK 3 9 2.2240 - 2.1384 0.96 2885 149 0.1695 0.2088
REMARK 3 10 2.1384 - 2.0647 0.95 2846 141 0.1837 0.2086
REMARK 3 11 2.0647 - 2.0001 0.95 2804 139 0.2012 0.2642
REMARK 3 12 2.0001 - 1.9430 0.93 2721 166 0.2066 0.2586
REMARK 3 13 1.9430 - 1.8918 0.84 2529 136 0.2266 0.2635
REMARK 3 14 1.8918 - 1.8457 0.66 1979 99 0.2601 0.2929
REMARK 3 15 1.8457 - 1.8038 0.46 1358 64 0.2674 0.3654
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 3856
REMARK 3 ANGLE : 1.294 5234
REMARK 3 CHIRALITY : 0.087 629
REMARK 3 PLANARITY : 0.004 647
REMARK 3 DIHEDRAL : 13.767 1476
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 308 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9359 9.8127 50.8525
REMARK 3 T TENSOR
REMARK 3 T11: 0.2710 T22: 0.3198
REMARK 3 T33: 0.3305 T12: 0.0096
REMARK 3 T13: -0.0629 T23: 0.1482
REMARK 3 L TENSOR
REMARK 3 L11: 3.7785 L22: 3.8852
REMARK 3 L33: 4.0491 L12: 0.6897
REMARK 3 L13: 0.3364 L23: -1.9229
REMARK 3 S TENSOR
REMARK 3 S11: 0.3643 S12: 0.8972 S13: 1.0373
REMARK 3 S21: -0.3650 S22: 0.2010 S23: 0.8095
REMARK 3 S31: -0.4646 S32: -0.5116 S33: -0.2643
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 322 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9234 -6.8265 51.4401
REMARK 3 T TENSOR
REMARK 3 T11: 0.1760 T22: 0.1958
REMARK 3 T33: 0.2080 T12: 0.0008
REMARK 3 T13: 0.0520 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 7.0034 L22: 6.6760
REMARK 3 L33: 1.7600 L12: -5.6516
REMARK 3 L13: 2.5373 L23: -1.6472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: 0.1091 S13: 0.3198
REMARK 3 S21: -0.2750 S22: 0.0131 S23: -0.6534
REMARK 3 S31: 0.1354 S32: 0.0044 S33: -0.0020
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8509 2.4905 56.0915
REMARK 3 T TENSOR
REMARK 3 T11: 0.1368 T22: 0.1519
REMARK 3 T33: 0.0965 T12: -0.0194
REMARK 3 T13: 0.0261 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 6.4524 L22: 5.7644
REMARK 3 L33: 0.8651 L12: -4.8660
REMARK 3 L13: 1.0669 L23: -1.2197
REMARK 3 S TENSOR
REMARK 3 S11: 0.2394 S12: 0.2826 S13: -0.0263
REMARK 3 S21: -0.4382 S22: -0.1552 S23: -0.1524
REMARK 3 S31: -0.0198 S32: 0.2234 S33: -0.0541
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.8324 9.2752 61.2977
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.1091
REMARK 3 T33: 0.0823 T12: -0.0117
REMARK 3 T13: 0.0312 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.6512 L22: 5.3452
REMARK 3 L33: 1.9223 L12: 0.3611
REMARK 3 L13: -0.0919 L23: 0.6179
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: -0.0212 S13: 0.2247
REMARK 3 S21: 0.0183 S22: -0.0055 S23: 0.1983
REMARK 3 S31: -0.2085 S32: 0.0385 S33: -0.0339
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 395 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2121 -11.9736 55.4434
REMARK 3 T TENSOR
REMARK 3 T11: 0.1737 T22: 0.1063
REMARK 3 T33: 0.2218 T12: 0.0033
REMARK 3 T13: 0.0374 T23: -0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 2.2810 L22: 3.9800
REMARK 3 L33: 2.8338 L12: 0.5533
REMARK 3 L13: -0.4435 L23: -0.4207
REMARK 3 S TENSOR
REMARK 3 S11: -0.1880 S12: 0.1295 S13: -0.6861
REMARK 3 S21: -0.4005 S22: -0.1022 S23: 0.1810
REMARK 3 S31: 0.4756 S32: 0.1086 S33: 0.0654
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 408 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7320 -14.6461 63.1754
REMARK 3 T TENSOR
REMARK 3 T11: 0.2707 T22: 0.1530
REMARK 3 T33: 0.2860 T12: 0.0492
REMARK 3 T13: 0.0866 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 1.9465 L22: 1.4872
REMARK 3 L33: 8.6686 L12: -0.6693
REMARK 3 L13: 3.6061 L23: -1.2577
REMARK 3 S TENSOR
REMARK 3 S11: 0.1104 S12: -0.0592 S13: -0.5305
REMARK 3 S21: -0.0554 S22: 0.2103 S23: -0.0315
REMARK 3 S31: 0.5160 S32: 0.0989 S33: -0.2539
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 421 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2345 -10.8413 65.4097
REMARK 3 T TENSOR
REMARK 3 T11: 0.1687 T22: 0.1158
REMARK 3 T33: 0.2073 T12: 0.0011
REMARK 3 T13: 0.0456 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.1079 L22: 3.2734
REMARK 3 L33: 3.2934 L12: -0.3510
REMARK 3 L13: 1.4411 L23: -0.3474
REMARK 3 S TENSOR
REMARK 3 S11: -0.1664 S12: -0.1927 S13: -0.7225
REMARK 3 S21: 0.1724 S22: 0.0032 S23: 0.3595
REMARK 3 S31: 0.1650 S32: 0.0110 S33: 0.1147
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 439 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1555 4.7401 61.4634
REMARK 3 T TENSOR
REMARK 3 T11: 0.0961 T22: 0.1263
REMARK 3 T33: 0.0848 T12: 0.0070
REMARK 3 T13: 0.0129 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 4.9988 L22: 2.7157
REMARK 3 L33: 2.5317 L12: 1.3068
REMARK 3 L13: 0.4791 L23: 0.6029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: 0.0025 S13: 0.0717
REMARK 3 S21: 0.0250 S22: -0.1117 S23: 0.0877
REMARK 3 S31: -0.1468 S32: -0.2451 S33: 0.1005
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 474 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0313 6.5305 60.1066
REMARK 3 T TENSOR
REMARK 3 T11: 0.1410 T22: 0.2517
REMARK 3 T33: 0.1391 T12: 0.0600
REMARK 3 T13: 0.0012 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 5.9857 L22: 2.8486
REMARK 3 L33: 2.7409 L12: 1.2586
REMARK 3 L13: -0.3707 L23: -0.1464
REMARK 3 S TENSOR
REMARK 3 S11: 0.0685 S12: 0.4305 S13: 0.3798
REMARK 3 S21: -0.3535 S22: -0.0993 S23: -0.0147
REMARK 3 S31: -0.3724 S32: -0.2602 S33: -0.0376
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 497 THROUGH 530 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1241 -1.4424 69.1733
REMARK 3 T TENSOR
REMARK 3 T11: 0.1238 T22: 0.1456
REMARK 3 T33: 0.0750 T12: 0.0020
REMARK 3 T13: 0.0155 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 5.6956 L22: 0.6980
REMARK 3 L33: 0.2016 L12: -0.3538
REMARK 3 L13: -0.2944 L23: 0.1759
REMARK 3 S TENSOR
REMARK 3 S11: -0.1340 S12: -0.1725 S13: -0.0999
REMARK 3 S21: 0.0339 S22: 0.0801 S23: -0.0231
REMARK 3 S31: 0.0285 S32: 0.0564 S33: 0.0326
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 537 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.9424 0.5801 65.4339
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.2104
REMARK 3 T33: 0.2608 T12: -0.0119
REMARK 3 T13: -0.0200 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 7.6330 L22: 3.5546
REMARK 3 L33: 4.3171 L12: -5.0197
REMARK 3 L13: 2.9835 L23: -1.1431
REMARK 3 S TENSOR
REMARK 3 S11: 0.6066 S12: 0.1831 S13: -0.3470
REMARK 3 S21: -0.2897 S22: 0.0216 S23: 0.1274
REMARK 3 S31: 0.2984 S32: 0.0848 S33: -0.2377
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 538 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6380 9.6159 65.6502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1875 T22: 0.1660
REMARK 3 T33: 0.3192 T12: -0.0192
REMARK 3 T13: 0.0053 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 8.5588 L22: 2.9089
REMARK 3 L33: 7.0822 L12: -3.1488
REMARK 3 L13: -1.7405 L23: -0.3180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: -0.3377 S13: 0.4232
REMARK 3 S21: 0.2945 S22: 0.0041 S23: -0.4403
REMARK 3 S31: -0.4778 S32: 0.2129 S33: -0.1626
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 307 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0578 -1.1624 89.4415
REMARK 3 T TENSOR
REMARK 3 T11: 0.2369 T22: 0.3275
REMARK 3 T33: 0.1857 T12: 0.0501
REMARK 3 T13: 0.0502 T23: 0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 4.0818 L22: 1.9652
REMARK 3 L33: 3.8125 L12: -0.4106
REMARK 3 L13: 2.5620 L23: -0.8325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: -0.8241 S13: -0.6413
REMARK 3 S21: 0.4618 S22: 0.2291 S23: 0.5138
REMARK 3 S31: 0.0241 S32: -0.7569 S33: -0.3410
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5321 0.4017 94.9538
REMARK 3 T TENSOR
REMARK 3 T11: 0.2593 T22: 0.1523
REMARK 3 T33: 0.1163 T12: 0.0429
REMARK 3 T13: -0.0374 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 4.9643 L22: 3.8665
REMARK 3 L33: 3.9268 L12: 1.6793
REMARK 3 L13: 3.2009 L23: 0.8564
REMARK 3 S TENSOR
REMARK 3 S11: -0.2749 S12: 0.0142 S13: 0.1501
REMARK 3 S21: 0.5179 S22: 0.1135 S23: -0.2077
REMARK 3 S31: -0.1326 S32: 0.1989 S33: 0.0882
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 364 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7777 -14.0409 84.7976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3695 T22: 0.2117
REMARK 3 T33: 0.3576 T12: -0.0749
REMARK 3 T13: -0.0604 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 8.5880 L22: 5.0604
REMARK 3 L33: 2.7122 L12: -6.5876
REMARK 3 L13: -1.8487 L23: 1.5314
REMARK 3 S TENSOR
REMARK 3 S11: -0.2705 S12: -0.0387 S13: -1.3575
REMARK 3 S21: -0.2389 S22: 0.1576 S23: 0.9307
REMARK 3 S31: 0.4756 S32: -0.5500 S33: 0.1365
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9471 -2.9910 85.2791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.1366
REMARK 3 T33: 0.0629 T12: 0.0072
REMARK 3 T13: -0.0188 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.7527 L22: 5.1856
REMARK 3 L33: 3.3688 L12: -0.7952
REMARK 3 L13: 0.4215 L23: 0.2622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0335 S12: 0.0129 S13: -0.1579
REMARK 3 S21: 0.2044 S22: -0.0116 S23: -0.2056
REMARK 3 S31: 0.0987 S32: 0.1777 S33: -0.0238
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1623 15.3727 91.5989
REMARK 3 T TENSOR
REMARK 3 T11: 0.5996 T22: 0.0274
REMARK 3 T33: 0.1591 T12: 0.0852
REMARK 3 T13: -0.1129 T23: -0.1395
REMARK 3 L TENSOR
REMARK 3 L11: 2.5461 L22: 1.7748
REMARK 3 L33: 0.7450 L12: -0.7028
REMARK 3 L13: 1.0743 L23: -0.9318
REMARK 3 S TENSOR
REMARK 3 S11: -0.3737 S12: -0.4338 S13: 0.7774
REMARK 3 S21: 0.9427 S22: 0.3112 S23: -0.0954
REMARK 3 S31: -0.9604 S32: -0.2326 S33: 0.3165
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 408 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7221 17.1439 90.7050
REMARK 3 T TENSOR
REMARK 3 T11: 0.5787 T22: 0.2429
REMARK 3 T33: 0.4416 T12: -0.1200
REMARK 3 T13: -0.2457 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 2.9425 L22: 3.6819
REMARK 3 L33: 2.1806 L12: -2.9952
REMARK 3 L13: -1.4810 L23: 1.0195
REMARK 3 S TENSOR
REMARK 3 S11: -0.2003 S12: -0.0897 S13: 0.8238
REMARK 3 S21: 0.1857 S22: 0.0461 S23: -1.1086
REMARK 3 S31: -0.8830 S32: 0.4068 S33: 0.0662
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6556 14.3093 81.1188
REMARK 3 T TENSOR
REMARK 3 T11: 0.2916 T22: 0.1252
REMARK 3 T33: 0.1405 T12: -0.0301
REMARK 3 T13: -0.0167 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 7.1990 L22: 5.2785
REMARK 3 L33: 5.0152 L12: 0.0800
REMARK 3 L13: 3.3616 L23: 0.1276
REMARK 3 S TENSOR
REMARK 3 S11: -0.1981 S12: -0.0259 S13: 0.2865
REMARK 3 S21: 0.0790 S22: -0.0149 S23: -0.1342
REMARK 3 S31: -0.6452 S32: 0.0385 S33: 0.2171
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9276 -0.8916 79.4853
REMARK 3 T TENSOR
REMARK 3 T11: 0.1118 T22: 0.1347
REMARK 3 T33: 0.0710 T12: -0.0221
REMARK 3 T13: -0.0063 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 4.0540 L22: 7.2299
REMARK 3 L33: 5.0339 L12: -1.4409
REMARK 3 L13: 0.0657 L23: 0.9370
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: 0.1727 S13: -0.2014
REMARK 3 S21: -0.1443 S22: -0.1461 S23: 0.1184
REMARK 3 S31: -0.0248 S32: -0.0290 S33: 0.1906
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6425 -1.8912 74.9800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0836 T22: 0.2164
REMARK 3 T33: 0.1489 T12: -0.0321
REMARK 3 T13: 0.0168 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 7.2562 L22: 6.3382
REMARK 3 L33: 3.3621 L12: -5.1775
REMARK 3 L13: 1.0202 L23: -1.4157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: -0.1181 S13: -0.3517
REMARK 3 S21: 0.0207 S22: -0.0850 S23: 0.2923
REMARK 3 S31: 0.2032 S32: -0.1268 S33: 0.1206
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 530 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4675 4.8192 76.8052
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.1083
REMARK 3 T33: 0.0819 T12: -0.0264
REMARK 3 T13: 0.0389 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.9808 L22: 2.2803
REMARK 3 L33: 4.6842 L12: -0.2791
REMARK 3 L13: 2.4702 L23: -0.8887
REMARK 3 S TENSOR
REMARK 3 S11: -0.1317 S12: 0.2214 S13: 0.3550
REMARK 3 S21: 0.0425 S22: -0.0733 S23: -0.2553
REMARK 3 S31: -0.1424 S32: 0.4190 S33: 0.1298
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 531 THROUGH 537 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.4976 0.8594 95.8403
REMARK 3 T TENSOR
REMARK 3 T11: 0.3736 T22: 0.5220
REMARK 3 T33: 0.5046 T12: -0.0923
REMARK 3 T13: -0.2416 T23: -0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 6.9333 L22: 0.6230
REMARK 3 L33: 2.2372 L12: -0.1014
REMARK 3 L13: 1.7646 L23: -1.0745
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: -0.2109 S13: 0.9215
REMARK 3 S21: 0.2301 S22: 0.2983 S23: 0.1900
REMARK 3 S31: -0.1520 S32: 0.1420 S33: 0.3372
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 538 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9130 -6.9807 89.2173
REMARK 3 T TENSOR
REMARK 3 T11: 0.2561 T22: 0.2826
REMARK 3 T33: 0.2993 T12: -0.0104
REMARK 3 T13: -0.0803 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 6.9236 L22: 5.0920
REMARK 3 L33: 2.1642 L12: 2.0922
REMARK 3 L13: 3.7536 L23: 1.6608
REMARK 3 S TENSOR
REMARK 3 S11: 0.1510 S12: -0.0089 S13: -0.7680
REMARK 3 S21: 0.3571 S22: -0.2376 S23: -0.9411
REMARK 3 S31: 0.3831 S32: 0.8309 S33: 0.1302
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 5WGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000228993.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45402
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 5DXE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3,350, MGCL2, TRIS PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.15K
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 41.91550
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: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 MET A 294
REMARK 465 ASP A 295
REMARK 465 PRO A 296
REMARK 465 MET A 297
REMARK 465 ILE A 298
REMARK 465 LYS A 299
REMARK 465 ARG A 300
REMARK 465 SER A 301
REMARK 465 LYS A 302
REMARK 465 LYS A 303
REMARK 465 ASN A 304
REMARK 465 SER A 305
REMARK 465 LEU A 306
REMARK 465 ALA A 307
REMARK 465 PHE A 461
REMARK 465 LEU A 462
REMARK 465 SER A 463
REMARK 465 SER A 464
REMARK 465 THR A 465
REMARK 465 LEU A 466
REMARK 465 LYS A 467
REMARK 465 SER A 468
REMARK 465 LEU A 469
REMARK 465 GLU A 470
REMARK 465 GLU A 471
REMARK 465 LYS A 472
REMARK 465 ARG A 548
REMARK 465 LEU A 549
REMARK 465 HIS A 550
REMARK 465 ALA A 551
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
REMARK 465 MET B 294
REMARK 465 ASP B 295
REMARK 465 PRO B 296
REMARK 465 MET B 297
REMARK 465 ILE B 298
REMARK 465 LYS B 299
REMARK 465 ARG B 300
REMARK 465 SER B 301
REMARK 465 LYS B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 SER B 305
REMARK 465 LEU B 306
REMARK 465 GLU B 330
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 PRO B 336
REMARK 465 PHE B 337
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 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 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 309 OG
REMARK 470 LEU A 310 CG CD1 CD2
REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 362 CE NZ
REMARK 470 GLU A 397 CG CD OE1 OE2
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 MET A 437 CG SD CE
REMARK 470 TYR A 459 CD1 CE1 OH
REMARK 470 ASP A 473 CG OD1 OD2
REMARK 470 LYS A 492 CG CD CE NZ
REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 397 CG CD OE1 OE2
REMARK 470 ASP B 411 CG OD1 OD2
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 TYR B 459 OH
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 GLU B 542 CG CD OE1 OE2
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 11 OD2
REMARK 470 ASP F 10 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 NZ LYS F 6 CG ASP F 10 1.37
REMARK 500 NZ LYS E 7 CG ASP E 11 1.38
REMARK 500 O HOH A 904 O HOH B 835 2.08
REMARK 500 O HOH B 838 O HOH B 855 2.10
REMARK 500 OD1 ASN B 359 OG SER F 11 2.12
REMARK 500 O HOH B 833 O HOH B 871 2.15
REMARK 500 O HOH F 103 O HOH F 104 2.16
REMARK 500 O HOH B 768 O HOH B 846 2.17
REMARK 500 O HOH B 831 O HOH B 868 2.18
REMARK 500 O HOH A 853 O HOH B 799 2.19
REMARK 500 O HOH B 834 O HOH B 847 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS E 6 NE2 HIS E 6 CD2 -0.066
REMARK 500 LEU F 7 CA LEU F 7 C -0.162
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 34.25 -92.21
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 B 879 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 880 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH B 881 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH B 882 DISTANCE = 8.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EST A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EST B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand NH2 E 13 bound to SER E
REMARK 800 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand NH2 F 12 bound to SER F
REMARK 800 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE F 1 and ALA F 2
DBREF 5WGD A 297 554 UNP P03372 ESR1_HUMAN 124 381
DBREF 5WGD B 297 554 UNP P03372 ESR1_HUMAN 124 381
DBREF 5WGD E 1 13 PDB 5WGD 5WGD 1 13
DBREF 5WGD F 1 12 PDB 5WGD 5WGD 1 12
SEQADV 5WGD MET A 294 UNP P03372 INITIATING METHIONINE
SEQADV 5WGD ASP A 295 UNP P03372 EXPRESSION TAG
SEQADV 5WGD PRO A 296 UNP P03372 EXPRESSION TAG
SEQADV 5WGD SER A 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQADV 5WGD MET B 294 UNP P03372 INITIATING METHIONINE
SEQADV 5WGD ASP B 295 UNP P03372 EXPRESSION TAG
SEQADV 5WGD PRO B 296 UNP P03372 EXPRESSION TAG
SEQADV 5WGD SER B 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQRES 1 A 261 MET ASP PRO MET ILE LYS ARG SER LYS LYS ASN SER LEU
SEQRES 2 A 261 ALA LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU
SEQRES 3 A 261 LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP
SEQRES 4 A 261 PRO THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU
SEQRES 5 A 261 LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE
SEQRES 6 A 261 ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR
SEQRES 7 A 261 LEU HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU
SEQRES 8 A 261 GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU
SEQRES 9 A 261 HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU
SEQRES 10 A 261 ASP ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU
SEQRES 11 A 261 ILE PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG
SEQRES 12 A 261 MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS
SEQRES 13 A 261 SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU
SEQRES 14 A 261 SER SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE
SEQRES 15 A 261 HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS
SEQRES 16 A 261 LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS
SEQRES 17 A 261 GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE
SEQRES 18 A 261 ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER
SEQRES 19 A 261 MET LYS CYS LYS ASN VAL VAL PRO LEU SER ASP LEU LEU
SEQRES 20 A 261 LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA PRO THR
SEQRES 21 A 261 SER
SEQRES 1 B 261 MET ASP PRO MET ILE LYS ARG SER LYS LYS ASN SER LEU
SEQRES 2 B 261 ALA LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU
SEQRES 3 B 261 LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP
SEQRES 4 B 261 PRO THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU
SEQRES 5 B 261 LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE
SEQRES 6 B 261 ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR
SEQRES 7 B 261 LEU HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU
SEQRES 8 B 261 GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU
SEQRES 9 B 261 HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU
SEQRES 10 B 261 ASP ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU
SEQRES 11 B 261 ILE PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG
SEQRES 12 B 261 MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS
SEQRES 13 B 261 SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU
SEQRES 14 B 261 SER SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE
SEQRES 15 B 261 HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS
SEQRES 16 B 261 LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS
SEQRES 17 B 261 GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE
SEQRES 18 B 261 ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER
SEQRES 19 B 261 MET LYS CYS LYS ASN VAL VAL PRO LEU SER ASP LEU LEU
SEQRES 20 B 261 LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA PRO THR
SEQRES 21 B 261 SER
SEQRES 1 E 13 ACE HIS LYS ILE LEU HIS LYS LEU LEU GLN ASP SER NH2
SEQRES 1 F 12 ACE ALA ILE LEU HIS LYS LEU LEU GLN ASP SER NH2
HET ACE E 1 3
HET NH2 E 13 1
HET ACE F 1 2
HET NH2 F 12 1
HET EST A 601 20
HET EST B 601 20
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM EST ESTRADIOL
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 NH2 2(H2 N)
FORMUL 5 EST 2(C18 H24 O2)
FORMUL 7 HOH *416(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 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 HIS A 474 ALA A 493 1 20
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 THR B 311 ALA B 322 1 12
HELIX 12 AB3 GLU B 339 ARG B 363 1 25
HELIX 13 AB4 GLY B 366 LEU B 370 5 5
HELIX 14 AB5 THR B 371 MET B 396 1 26
HELIX 15 AB6 ASN B 413 VAL B 418 5 6
HELIX 16 AB7 GLY B 420 ASN B 439 1 20
HELIX 17 AB8 GLN B 441 SER B 456 1 16
HELIX 18 AB9 HIS B 474 ALA B 493 1 20
HELIX 19 AC1 THR B 496 LYS B 531 1 36
HELIX 20 AC2 SER B 537 ALA B 546 1 10
HELIX 21 AC3 LYS E 3 LEU E 9 1 7
HELIX 22 AC4 ALA F 2 SER F 11 1 10
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
LINK C ACE E 1 N HIS E 2 1555 1555 1.32
LINK C SER E 12 N NH2 E 13 1555 1555 1.33
LINK C ACE F 1 N ALA F 2 1555 1555 1.30
LINK C SER F 11 N NH2 F 12 1555 1555 1.31
SITE 1 AC1 7 MET A 343 LEU A 346 GLU A 353 ARG A 394
SITE 2 AC1 7 HIS A 524 LEU A 525 HOH A 788
SITE 1 AC2 7 MET B 343 LEU B 346 GLU B 353 ARG B 394
SITE 2 AC2 7 HIS B 524 LEU B 525 HOH B 791
SITE 1 AC3 3 GLN E 10 ASP E 11 SER E 12
SITE 1 AC4 4 LYS B 362 LEU F 8 ASP F 10 SER F 11
SITE 1 AC5 4 ILE F 3 LEU F 4 HIS F 5 LYS F 6
CRYST1 56.037 83.831 58.375 90.00 108.32 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 0.017845 0.000000 0.005907 0.00000
SCALE2 0.000000 0.011929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018045 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
