HEADER TRANSCRIPTION 07-JUN-16 5KCU
TITLE CRYSTAL STRUCTURE OF THE ER-ALPHA LIGAND-BINDING DOMAIN (Y537S) IN
TITLE 2 COMPLEX WITH AN N-ETHYL, ALPHA-NAPHTHYL OBHS-N DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN;
COMPND 5 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 6 GROUP A MEMBER 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NCOA2;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: NUCLEAR RECEPTOR-INTERACTING PEPTIDE;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESR1, ESR, NR3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS NUCLEAR RECEPTOR, TRANSCRIPTION FACTOR, LIGAND BINDING, PROTEIN-
KEYWDS 2 LIGAND COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.NWACHUKWU,S.SRINIVASAN,N.E.BRUNO,V.DHARMARAJAN,D.GOSWAMI,
AUTHOR 2 I.KASTRATI,S.NOVICK,J.NOWAK,H.B.ZHOU,N.BOONMUEN,Y.ZHAO,J.MIN,
AUTHOR 3 J.FRASOR,B.S.KATZENELLENBOGEN,P.R.GRIFFIN,J.A.KATZENELLENBOGEN,
AUTHOR 4 K.W.NETTLES
REVDAT 5 06-MAR-24 5KCU 1 REMARK
REVDAT 4 26-FEB-20 5KCU 1 REMARK
REVDAT 3 28-DEC-16 5KCU 1 JRNL
REVDAT 2 21-DEC-16 5KCU 1 JRNL
REVDAT 1 16-NOV-16 5KCU 0
SPRSDE 16-NOV-16 5KCU 5BP6
JRNL AUTH S.SRINIVASAN,J.C.NWACHUKWU,N.E.BRUNO,V.DHARMARAJAN,
JRNL AUTH 2 D.GOSWAMI,I.KASTRATI,S.NOVICK,J.NOWAK,V.CAVETT,H.B.ZHOU,
JRNL AUTH 3 N.BOONMUEN,Y.ZHAO,J.MIN,J.FRASOR,B.S.KATZENELLENBOGEN,
JRNL AUTH 4 P.R.GRIFFIN,J.A.KATZENELLENBOGEN,K.W.NETTLES
JRNL TITL FULL ANTAGONISM OF THE ESTROGEN RECEPTOR WITHOUT A
JRNL TITL 2 PROTOTYPICAL LIGAND SIDE CHAIN.
JRNL REF NAT. CHEM. BIOL. V. 13 111 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 27870835
JRNL DOI 10.1038/NCHEMBIO.2236
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1690
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 29121
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1863
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 46.9855 - 4.7720 0.98 2309 154 0.1744 0.2437
REMARK 3 2 4.7720 - 3.7882 0.97 2262 148 0.1591 0.2210
REMARK 3 3 3.7882 - 3.3095 0.99 2272 158 0.1934 0.2241
REMARK 3 4 3.3095 - 3.0070 0.99 2279 160 0.2067 0.2353
REMARK 3 5 3.0070 - 2.7915 0.96 2227 140 0.2117 0.2753
REMARK 3 6 2.7915 - 2.6269 0.95 2171 152 0.2203 0.2819
REMARK 3 7 2.6269 - 2.4953 0.95 2180 152 0.2188 0.2914
REMARK 3 8 2.4953 - 2.3867 0.93 2149 134 0.2211 0.2688
REMARK 3 9 2.3867 - 2.2949 0.90 2029 149 0.2136 0.2817
REMARK 3 10 2.2949 - 2.2157 0.89 2046 146 0.2427 0.2826
REMARK 3 11 2.2157 - 2.1464 0.79 1806 128 0.2361 0.3486
REMARK 3 12 2.1464 - 2.0850 0.80 1837 124 0.2651 0.2985
REMARK 3 13 2.0850 - 2.0301 0.75 1691 118 0.2858 0.3457
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.15
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 3882
REMARK 3 ANGLE : 0.881 5268
REMARK 3 CHIRALITY : 0.031 622
REMARK 3 PLANARITY : 0.003 649
REMARK 3 DIHEDRAL : 14.337 1433
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0574 -16.0721 5.9964
REMARK 3 T TENSOR
REMARK 3 T11: 0.5674 T22: 0.4907
REMARK 3 T33: 0.3193 T12: -0.1436
REMARK 3 T13: 0.0328 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 4.6162 L22: 4.9028
REMARK 3 L33: 4.1584 L12: 1.1227
REMARK 3 L13: -1.7230 L23: -0.4110
REMARK 3 S TENSOR
REMARK 3 S11: 0.4679 S12: -1.1368 S13: 0.3078
REMARK 3 S21: 0.8651 S22: -0.7707 S23: 0.4703
REMARK 3 S31: -0.3521 S32: 0.5558 S33: 0.2062
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9712 -20.0898 1.3058
REMARK 3 T TENSOR
REMARK 3 T11: 0.4271 T22: 0.4182
REMARK 3 T33: 0.3315 T12: -0.1161
REMARK 3 T13: 0.0512 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 6.5454 L22: 7.0304
REMARK 3 L33: 4.6109 L12: 1.1020
REMARK 3 L13: -2.0827 L23: -1.7431
REMARK 3 S TENSOR
REMARK 3 S11: -0.2413 S12: 0.1138 S13: -0.1206
REMARK 3 S21: -0.2262 S22: 0.2975 S23: 0.1282
REMARK 3 S31: 0.1549 S32: -0.5555 S33: -0.1057
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2955 -19.1145 -2.1466
REMARK 3 T TENSOR
REMARK 3 T11: 0.3187 T22: 0.2797
REMARK 3 T33: 0.2757 T12: -0.0817
REMARK 3 T13: 0.0787 T23: -0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 4.6706 L22: 3.0362
REMARK 3 L33: 6.8453 L12: 1.2190
REMARK 3 L13: -1.8063 L23: -0.8749
REMARK 3 S TENSOR
REMARK 3 S11: 0.0668 S12: -0.0912 S13: 0.1062
REMARK 3 S21: -0.0614 S22: -0.1897 S23: 0.0566
REMARK 3 S31: 0.1357 S32: -0.0125 S33: 0.1368
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 472 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7119 -23.8259 -6.4751
REMARK 3 T TENSOR
REMARK 3 T11: 0.3913 T22: 0.3209
REMARK 3 T33: 0.2754 T12: -0.0173
REMARK 3 T13: 0.0988 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 5.6415 L22: 5.8791
REMARK 3 L33: 6.1273 L12: 0.6025
REMARK 3 L13: -1.0399 L23: -1.1782
REMARK 3 S TENSOR
REMARK 3 S11: -0.1469 S12: 0.1383 S13: -0.5080
REMARK 3 S21: -0.0432 S22: -0.0207 S23: 0.0875
REMARK 3 S31: 0.6429 S32: 0.0761 S33: 0.1283
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 473 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8660 -8.5089 -3.6559
REMARK 3 T TENSOR
REMARK 3 T11: 0.6313 T22: 0.6726
REMARK 3 T33: 0.5152 T12: -0.2856
REMARK 3 T13: -0.0213 T23: -0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 7.1621 L22: 2.4500
REMARK 3 L33: 5.7637 L12: -1.4804
REMARK 3 L13: 0.7068 L23: -0.4772
REMARK 3 S TENSOR
REMARK 3 S11: 0.2637 S12: -0.4997 S13: 0.5763
REMARK 3 S21: 0.5040 S22: -0.4355 S23: -0.3412
REMARK 3 S31: -1.0031 S32: 0.9307 S33: 0.0965
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 497 THROUGH 529 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0572 -21.7978 -11.6011
REMARK 3 T TENSOR
REMARK 3 T11: 0.4856 T22: 0.2969
REMARK 3 T33: 0.2941 T12: -0.0325
REMARK 3 T13: 0.0279 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 9.9157 L22: 2.9616
REMARK 3 L33: 5.9688 L12: 0.6663
REMARK 3 L13: -0.4870 L23: -0.6161
REMARK 3 S TENSOR
REMARK 3 S11: 0.1615 S12: -0.2766 S13: -0.4246
REMARK 3 S21: 0.0875 S22: -0.3306 S23: 0.0262
REMARK 3 S31: 0.3240 S32: -0.0455 S33: 0.2266
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 530 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8144 -17.6459 -10.0078
REMARK 3 T TENSOR
REMARK 3 T11: 0.6702 T22: 0.9469
REMARK 3 T33: 0.7825 T12: -0.1975
REMARK 3 T13: -0.0126 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.2127 L22: 4.8959
REMARK 3 L33: 8.7894 L12: -0.5941
REMARK 3 L13: -2.0757 L23: -1.9480
REMARK 3 S TENSOR
REMARK 3 S11: -0.3420 S12: 1.0140 S13: 0.1286
REMARK 3 S21: -0.3064 S22: 0.1760 S23: 0.8693
REMARK 3 S31: 1.4294 S32: -1.4367 S33: -0.0556
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 305 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6602 -19.5679 -32.3377
REMARK 3 T TENSOR
REMARK 3 T11: 0.4614 T22: 0.6372
REMARK 3 T33: 0.5173 T12: 0.0032
REMARK 3 T13: 0.1123 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 4.9558 L22: 4.1670
REMARK 3 L33: 4.7999 L12: -0.6653
REMARK 3 L13: -0.0401 L23: 0.3636
REMARK 3 S TENSOR
REMARK 3 S11: 0.0756 S12: 0.2818 S13: -0.6206
REMARK 3 S21: 0.0624 S22: -0.0499 S23: -0.5108
REMARK 3 S31: 0.4579 S32: 1.2127 S33: -0.1179
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9833 -11.2481 -46.6739
REMARK 3 T TENSOR
REMARK 3 T11: 0.8415 T22: 1.6795
REMARK 3 T33: 1.3361 T12: -0.1461
REMARK 3 T13: -0.2452 T23: 0.1773
REMARK 3 L TENSOR
REMARK 3 L11: 0.2291 L22: 3.5799
REMARK 3 L33: 2.4281 L12: -0.9083
REMARK 3 L13: -0.7455 L23: 2.9446
REMARK 3 S TENSOR
REMARK 3 S11: 0.6672 S12: 2.5902 S13: 0.4806
REMARK 3 S21: -1.2389 S22: -0.3968 S23: 1.9706
REMARK 3 S31: 0.1917 S32: -0.8704 S33: 0.4877
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5886 -24.7375 -31.6235
REMARK 3 T TENSOR
REMARK 3 T11: 0.4807 T22: 0.2972
REMARK 3 T33: 0.3306 T12: 0.0045
REMARK 3 T13: 0.1003 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 2.4294 L22: 4.8109
REMARK 3 L33: 6.5828 L12: 0.7496
REMARK 3 L13: -2.1046 L23: -0.3535
REMARK 3 S TENSOR
REMARK 3 S11: -0.4277 S12: 0.2166 S13: -0.4813
REMARK 3 S21: -0.2672 S22: -0.0153 S23: -0.2740
REMARK 3 S31: 1.2360 S32: 0.1146 S33: 0.3016
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7244 -6.3724 -36.3561
REMARK 3 T TENSOR
REMARK 3 T11: 0.7422 T22: 0.5284
REMARK 3 T33: 0.4216 T12: 0.1008
REMARK 3 T13: 0.0491 T23: 0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 4.9102 L22: 8.1745
REMARK 3 L33: 3.3771 L12: -0.3834
REMARK 3 L13: -2.8877 L23: 3.5149
REMARK 3 S TENSOR
REMARK 3 S11: 0.3939 S12: 0.9901 S13: 0.6808
REMARK 3 S21: -0.4440 S22: 0.2965 S23: 0.6195
REMARK 3 S31: -2.3814 S32: -1.2132 S33: -0.3832
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 412 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4797 -9.3934 -33.5449
REMARK 3 T TENSOR
REMARK 3 T11: 1.0687 T22: 1.8951
REMARK 3 T33: 1.1954 T12: 0.4135
REMARK 3 T13: -0.0468 T23: 0.4277
REMARK 3 L TENSOR
REMARK 3 L11: 3.2134 L22: 2.4712
REMARK 3 L33: 5.0697 L12: -0.6366
REMARK 3 L13: -1.3216 L23: -0.9828
REMARK 3 S TENSOR
REMARK 3 S11: 1.1038 S12: 0.2941 S13: -0.3566
REMARK 3 S21: -0.1892 S22: -0.0805 S23: 0.5795
REMARK 3 S31: 0.4009 S32: -0.2122 S33: -0.2800
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0431 -11.4526 -24.7177
REMARK 3 T TENSOR
REMARK 3 T11: 0.3913 T22: 0.3048
REMARK 3 T33: 0.3057 T12: 0.0146
REMARK 3 T13: 0.0088 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 3.4625 L22: 4.5462
REMARK 3 L33: 8.6626 L12: 0.2902
REMARK 3 L13: -2.0123 L23: -0.3762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: 0.0353 S13: 0.2343
REMARK 3 S21: 0.2670 S22: -0.0063 S23: 0.3762
REMARK 3 S31: -0.9232 S32: -0.1084 S33: -0.0506
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 456 THROUGH 470 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3410 -33.9264 -15.0417
REMARK 3 T TENSOR
REMARK 3 T11: 1.2418 T22: 0.7752
REMARK 3 T33: 0.8464 T12: -0.1005
REMARK 3 T13: 0.1063 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 3.3810 L22: 1.5917
REMARK 3 L33: 6.7250 L12: 0.5139
REMARK 3 L13: -0.6425 L23: 0.2372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0801 S12: -1.0721 S13: -0.1411
REMARK 3 S21: 1.8215 S22: 0.3415 S23: -0.6665
REMARK 3 S31: 0.8709 S32: 0.6393 S33: -0.3083
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 471 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9476 -19.9152 -16.7412
REMARK 3 T TENSOR
REMARK 3 T11: 0.4211 T22: 0.7602
REMARK 3 T33: 0.5022 T12: 0.1044
REMARK 3 T13: -0.0312 T23: 0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 4.2897 L22: 3.7081
REMARK 3 L33: 7.0031 L12: 2.8567
REMARK 3 L13: 0.6418 L23: 4.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0925 S12: -0.0460 S13: -0.3359
REMARK 3 S21: 0.6456 S22: -0.0449 S23: -1.0306
REMARK 3 S31: 0.4892 S32: 1.7418 S33: 0.0846
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 526 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1203 -14.7571 -18.2201
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.2007
REMARK 3 T33: 0.2353 T12: 0.0282
REMARK 3 T13: 0.0427 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 4.2426 L22: 6.1798
REMARK 3 L33: 7.5341 L12: 1.5058
REMARK 3 L13: -0.9802 L23: 0.5331
REMARK 3 S TENSOR
REMARK 3 S11: -0.2333 S12: 0.0992 S13: -0.0153
REMARK 3 S21: -0.2050 S22: -0.0033 S23: 0.1238
REMARK 3 S31: -0.5796 S32: -0.0187 S33: 0.1725
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 527 THROUGH 545 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1265 -30.1672 -34.2805
REMARK 3 T TENSOR
REMARK 3 T11: 1.0707 T22: 0.9447
REMARK 3 T33: 0.7919 T12: -0.5561
REMARK 3 T13: -0.0667 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 3.0946 L22: 2.0366
REMARK 3 L33: 6.2206 L12: -0.9899
REMARK 3 L13: 0.3916 L23: 1.0294
REMARK 3 S TENSOR
REMARK 3 S11: -0.3685 S12: -0.1017 S13: -1.5331
REMARK 3 S21: -0.5306 S22: 1.2140 S23: 1.8904
REMARK 3 S31: 0.9541 S32: -1.9203 S33: -0.0435
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 687 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3340 -5.7408 -1.6934
REMARK 3 T TENSOR
REMARK 3 T11: 0.7215 T22: 0.8751
REMARK 3 T33: 1.2150 T12: 0.2247
REMARK 3 T13: 0.3012 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 6.9699 L22: 7.1818
REMARK 3 L33: 1.2394 L12: 4.7278
REMARK 3 L13: -0.4430 L23: 0.8319
REMARK 3 S TENSOR
REMARK 3 S11: 1.0069 S12: 0.0985 S13: 1.3278
REMARK 3 S21: -0.4884 S22: -1.6010 S23: 0.7652
REMARK 3 S31: -0.3839 S32: -1.8521 S33: 0.5364
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 688 THROUGH 696 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0218 -36.6135 -36.0441
REMARK 3 T TENSOR
REMARK 3 T11: 1.0164 T22: 0.6918
REMARK 3 T33: 0.9763 T12: 0.0912
REMARK 3 T13: 0.1253 T23: -0.1701
REMARK 3 L TENSOR
REMARK 3 L11: 4.2080 L22: 0.8858
REMARK 3 L33: 6.1155 L12: 1.2317
REMARK 3 L13: 4.8924 L23: 0.9518
REMARK 3 S TENSOR
REMARK 3 S11: 0.5848 S12: 1.8479 S13: -2.4036
REMARK 3 S21: -0.0768 S22: 0.0647 S23: 1.1345
REMARK 3 S31: -0.1242 S32: 1.6212 S33: -0.4537
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 5KCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE I-BEAM
REMARK 200 SINGLE CRYSTAL ASYMMETRIC CUT
REMARK 200 4.965 DEGS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31432
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.73400
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 (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
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 41.11100
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: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 SER A 305
REMARK 465 ASP A 332
REMARK 465 PRO A 333
REMARK 465 THR A 334
REMARK 465 ARG A 335
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 VAL A 533
REMARK 465 VAL A 534
REMARK 465 PRO A 535
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 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 MET B 528
REMARK 465 LYS B 529
REMARK 465 CYS B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 VAL B 533
REMARK 465 VAL B 534
REMARK 465 ALA B 546
REMARK 465 HIS B 547
REMARK 465 ARG B 548
REMARK 465 LEU B 549
REMARK 465 HIS B 550
REMARK 465 ALA B 551
REMARK 465 PRO B 552
REMARK 465 THR B 553
REMARK 465 SER B 554
REMARK 465 LYS C 686
REMARK 465 SER C 697
REMARK 465 SER C 698
REMARK 465 SER C 699
REMARK 465 LYS D 686
REMARK 465 HIS D 687
REMARK 465 SER D 697
REMARK 465 SER D 698
REMARK 465 SER D 699
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 306 CG CD1 CD2
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 GLU A 397 CG CD OE1 OE2
REMARK 470 GLN A 414 CG CD OE1 NE2
REMARK 470 GLU A 419 CG CD OE1 OE2
REMARK 470 MET A 421 CG SD CE
REMARK 470 LYS A 529 CG CD CE NZ
REMARK 470 LYS A 531 CG CD CE NZ
REMARK 470 ASN A 532 CG OD1 ND2
REMARK 470 LEU A 536 CG CD1 CD2
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 330 CG CD OE1 OE2
REMARK 470 ASP B 332 CG OD1 OD2
REMARK 470 ARG B 335 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 337 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 343 CG SD CE
REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 411 CG OD1 OD2
REMARK 470 LYS B 416 CG CD CE NZ
REMARK 470 CYS B 417 SG
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 LYS B 472 CG CD CE NZ
REMARK 470 LYS D 688 CG CD CE NZ
REMARK 470 HIS D 691 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 692 CG CD NE CZ NH1 NH2
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 OE2 GLU B 339 CB CYS B 417 1.59
REMARK 500 O HOH B 740 O HOH B 742 2.00
REMARK 500 O LEU B 308 NZ LYS B 481 2.02
REMARK 500 O HOH B 743 O HOH B 746 2.05
REMARK 500 O HOH B 701 O HOH B 745 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 742 O HOH B 744 1556 1.92
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 419 86.33 -68.93
REMARK 500 TYR B 526 33.37 -76.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 334 ARG B 335 55.20
REMARK 500 ARG B 335 PRO B 336 139.29
REMARK 500 GLU B 339 ALA B 340 135.09
REMARK 500 VAL B 418 GLU B 419 -148.42
REMARK 500 GLY B 420 MET B 421 -145.83
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 OB8 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OB8 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KCC RELATED DB: PDB
REMARK 900 RELATED ID: 5KCD RELATED DB: PDB
REMARK 900 RELATED ID: 5KCF RELATED DB: PDB
REMARK 900 RELATED ID: 5KCT RELATED DB: PDB
REMARK 900 RELATED ID: 5KCW RELATED DB: PDB
REMARK 900 RELATED ID: 5KD9 RELATED DB: PDB
DBREF 5KCU A 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KCU B 298 554 UNP P03372 ESR1_HUMAN 125 381
DBREF 5KCU C 686 699 PDB 5KCU 5KCU 686 699
DBREF 5KCU D 686 699 PDB 5KCU 5KCU 686 699
SEQADV 5KCU SER A 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQADV 5KCU SER B 537 UNP P03372 TYR 364 ENGINEERED MUTATION
SEQRES 1 A 257 ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER LEU
SEQRES 2 A 257 THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA GLU
SEQRES 3 A 257 PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG PRO
SEQRES 4 A 257 PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN LEU
SEQRES 5 A 257 ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA LYS
SEQRES 6 A 257 ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP GLN
SEQRES 7 A 257 VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU ILE LEU MET
SEQRES 8 A 257 ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY LYS
SEQRES 9 A 257 LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN
SEQRES 10 A 257 GLY LYS CYS VAL GLU GLY MET VAL GLU ILE PHE ASP MET
SEQRES 11 A 257 LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN LEU
SEQRES 12 A 257 GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE LEU
SEQRES 13 A 257 LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR LEU
SEQRES 14 A 257 LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU
SEQRES 15 A 257 ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA LYS
SEQRES 16 A 257 ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU ALA
SEQRES 17 A 257 GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET SER
SEQRES 18 A 257 ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CYS LYS
SEQRES 19 A 257 ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET LEU
SEQRES 20 A 257 ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 B 257 ILE LYS ARG SER LYS LYS ASN SER LEU ALA LEU SER LEU
SEQRES 2 B 257 THR ALA ASP GLN MET VAL SER ALA LEU LEU ASP ALA GLU
SEQRES 3 B 257 PRO PRO ILE LEU TYR SER GLU TYR ASP PRO THR ARG PRO
SEQRES 4 B 257 PHE SER GLU ALA SER MET MET GLY LEU LEU THR ASN LEU
SEQRES 5 B 257 ALA ASP ARG GLU LEU VAL HIS MET ILE ASN TRP ALA LYS
SEQRES 6 B 257 ARG VAL PRO GLY PHE VAL ASP LEU THR LEU HIS ASP GLN
SEQRES 7 B 257 VAL HIS LEU LEU GLU CYS ALA TRP LEU GLU ILE LEU MET
SEQRES 8 B 257 ILE GLY LEU VAL TRP ARG SER MET GLU HIS PRO GLY LYS
SEQRES 9 B 257 LEU LEU PHE ALA PRO ASN LEU LEU LEU ASP ARG ASN GLN
SEQRES 10 B 257 GLY LYS CYS VAL GLU GLY MET VAL GLU ILE PHE ASP MET
SEQRES 11 B 257 LEU LEU ALA THR SER SER ARG PHE ARG MET MET ASN LEU
SEQRES 12 B 257 GLN GLY GLU GLU PHE VAL CYS LEU LYS SER ILE ILE LEU
SEQRES 13 B 257 LEU ASN SER GLY VAL TYR THR PHE LEU SER SER THR LEU
SEQRES 14 B 257 LYS SER LEU GLU GLU LYS ASP HIS ILE HIS ARG VAL LEU
SEQRES 15 B 257 ASP LYS ILE THR ASP THR LEU ILE HIS LEU MET ALA LYS
SEQRES 16 B 257 ALA GLY LEU THR LEU GLN GLN GLN HIS GLN ARG LEU ALA
SEQRES 17 B 257 GLN LEU LEU LEU ILE LEU SER HIS ILE ARG HIS MET SER
SEQRES 18 B 257 ASN LYS GLY MET GLU HIS LEU TYR SER MET LYS CYS LYS
SEQRES 19 B 257 ASN VAL VAL PRO LEU SER ASP LEU LEU LEU GLU MET LEU
SEQRES 20 B 257 ASP ALA HIS ARG LEU HIS ALA PRO THR SER
SEQRES 1 C 14 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 2 C 14 SER
SEQRES 1 D 14 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER
SEQRES 2 D 14 SER
HET OB8 A 601 37
HET OB8 B 601 37
HETNAM OB8 (1S,2R,4S)-N-ETHYL-5,6-BIS(4-HYDROXYPHENYL)-N-
HETNAM 2 OB8 (NAPHTHALEN-2-YL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2-
HETNAM 3 OB8 SULFONAMIDE
FORMUL 5 OB8 2(C30 H27 N O5 S)
FORMUL 7 HOH *99(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 ARG A 394 1 24
HELIX 4 AA4 ASP A 411 LYS A 416 1 6
HELIX 5 AA5 GLY A 420 ASN A 439 1 20
HELIX 6 AA6 GLN A 441 SER A 456 1 16
HELIX 7 AA7 ASP A 473 ALA A 493 1 21
HELIX 8 AA8 THR A 496 TYR A 526 1 31
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 ALA B 340 ARG B 363 1 24
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 MET B 421 ASN B 439 1 19
HELIX 16 AB7 GLN B 441 SER B 456 1 16
HELIX 17 AB8 GLU B 470 ALA B 493 1 24
HELIX 18 AB9 THR B 496 TYR B 526 1 31
HELIX 19 AC1 SER B 537 LEU B 544 1 8
HELIX 20 AC2 LYS C 688 ASP C 696 1 9
HELIX 21 AC3 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 408 N ALA B 405
CISPEP 1 CYS A 530 LYS A 531 0 -3.29
CISPEP 2 LEU B 469 GLU B 470 0 -11.41
SITE 1 AC1 15 THR A 347 ALA A 350 GLU A 353 LEU A 387
SITE 2 AC1 15 MET A 388 ARG A 394 PHE A 404 GLU A 419
SITE 3 AC1 15 GLY A 420 MET A 421 ILE A 424 GLY A 521
SITE 4 AC1 15 HIS A 524 MET A 528 HOH A 713
SITE 1 AC2 15 LEU B 346 THR B 347 ALA B 350 GLU B 353
SITE 2 AC2 15 LEU B 387 MET B 388 ARG B 394 PHE B 404
SITE 3 AC2 15 VAL B 418 MET B 421 ILE B 424 GLY B 521
SITE 4 AC2 15 HIS B 524 LEU B 540 HOH B 721
CRYST1 55.482 82.222 58.830 90.00 110.83 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018024 0.000000 0.006857 0.00000
SCALE2 0.000000 0.012162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
