HEADER TRANSCRIPTION 08-JAN-15 4S15
TITLE CRYSTAL STRUCTURE OF THE ORPHAN NUCLEAR RECEPTOR RORALPHA LIGAND-
TITLE 2 BINDING DOMAIN IN COMPLEX WITH 4ALPHA-CABOXYL, 4BETA-METHYL-
TITLE 3 ZYMOSTEROL (4ACD8)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 1, RAR-RELATED ORPHAN RECEPTOR A, RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NUCLEAR RECEPTOR-INTERACTING PROTEIN 1;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: LXXLL BINDING MOTIF;
COMPND 13 SYNONYM: NUCLEAR FACTOR RIP140, RECEPTOR-INTERACTING PROTEIN 140;
COMPND 14 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: NR1F1, RORA, RZRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET46;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS TRANSCRIPTION FACTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.HUANG,F.R.SANTORI,D.R.LITTMAN,F.RASTINEJAD
REVDAT 3 28-FEB-24 4S15 1 REMARK SEQADV
REVDAT 2 25-FEB-15 4S15 1 JRNL
REVDAT 1 11-FEB-15 4S15 0
JRNL AUTH F.R.SANTORI,P.HUANG,S.A.VAN DE PAVERT,E.F.DOUGLASS,
JRNL AUTH 2 D.J.LEAVER,B.A.HAUBRICH,R.KEBER,G.LORBEK,T.KONIJN,
JRNL AUTH 3 B.N.ROSALES,D.ROZMAN,S.HORVAT,A.RAHIER,R.E.MEBIUS,
JRNL AUTH 4 F.RASTINEJAD,W.D.NES,D.R.LITTMAN
JRNL TITL IDENTIFICATION OF NATURAL ROR GAMMA LIGANDS THAT REGULATE
JRNL TITL 2 THE DEVELOPMENT OF LYMPHOID CELLS.
JRNL REF CELL METAB V. 21 286 2015
JRNL REFN ISSN 1550-4131
JRNL PMID 25651181
JRNL DOI 10.1016/J.CMET.2015.01.004
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 51607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2641
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 46.2512 - 5.0604 0.96 2675 149 0.1801 0.2195
REMARK 3 2 5.0604 - 4.0173 0.98 2623 134 0.1437 0.1678
REMARK 3 3 4.0173 - 3.5097 0.99 2620 139 0.1522 0.1782
REMARK 3 4 3.5097 - 3.1889 1.00 2597 147 0.1706 0.1983
REMARK 3 5 3.1889 - 2.9604 1.00 2594 128 0.1885 0.2717
REMARK 3 6 2.9604 - 2.7859 1.00 2591 150 0.1864 0.2137
REMARK 3 7 2.7859 - 2.6464 1.00 2611 132 0.1889 0.2485
REMARK 3 8 2.6464 - 2.5312 1.00 2588 149 0.1804 0.2300
REMARK 3 9 2.5312 - 2.4337 1.00 2558 136 0.1747 0.2322
REMARK 3 10 2.4337 - 2.3498 1.00 2587 143 0.1708 0.2218
REMARK 3 11 2.3498 - 2.2763 1.00 2606 114 0.1686 0.2089
REMARK 3 12 2.2763 - 2.2112 1.00 2600 119 0.1630 0.1839
REMARK 3 13 2.2112 - 2.1530 1.00 2553 141 0.1690 0.2152
REMARK 3 14 2.1530 - 2.1005 1.00 2549 158 0.1747 0.2029
REMARK 3 15 2.1005 - 2.0527 1.00 2577 131 0.1914 0.2372
REMARK 3 16 2.0527 - 2.0091 1.00 2556 141 0.2005 0.2786
REMARK 3 17 2.0091 - 1.9689 0.99 2535 139 0.2054 0.2365
REMARK 3 18 1.9689 - 1.9317 0.99 2519 155 0.2213 0.2481
REMARK 3 19 1.9317 - 1.8972 0.95 2427 136 0.2535 0.2908
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.160
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 : 0.005 4417
REMARK 3 ANGLE : 0.907 5982
REMARK 3 CHIRALITY : 0.037 678
REMARK 3 PLANARITY : 0.003 750
REMARK 3 DIHEDRAL : 14.891 1697
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 269 THROUGH 287 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2594 25.6592 -4.9829
REMARK 3 T TENSOR
REMARK 3 T11: 0.2720 T22: 0.2318
REMARK 3 T33: 0.2056 T12: 0.0387
REMARK 3 T13: 0.0753 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 4.0896 L22: 2.6918
REMARK 3 L33: 5.2003 L12: -0.1370
REMARK 3 L13: -2.4322 L23: -0.3409
REMARK 3 S TENSOR
REMARK 3 S11: 0.1713 S12: 0.4255 S13: 0.1359
REMARK 3 S21: -0.5115 S22: 0.0020 S23: -0.1762
REMARK 3 S31: 0.0067 S32: -0.0934 S33: 0.0146
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 288 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9302 21.0467 3.4791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 0.2347
REMARK 3 T33: 0.2575 T12: -0.0007
REMARK 3 T13: -0.0463 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 5.9299 L22: 1.8725
REMARK 3 L33: 1.5952 L12: 0.5260
REMARK 3 L13: -0.9689 L23: 0.2251
REMARK 3 S TENSOR
REMARK 3 S11: -0.0619 S12: 0.2575 S13: -0.4982
REMARK 3 S21: -0.2011 S22: -0.1612 S23: -0.1568
REMARK 3 S31: 0.0116 S32: 0.0943 S33: 0.1605
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 305 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0206 29.2094 17.2084
REMARK 3 T TENSOR
REMARK 3 T11: 0.1535 T22: 0.1101
REMARK 3 T33: 0.1417 T12: 0.0068
REMARK 3 T13: 0.0006 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 2.6428 L22: 0.8799
REMARK 3 L33: 1.6952 L12: -0.6833
REMARK 3 L13: -1.4169 L23: 0.8761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0986 S12: -0.0728 S13: -0.1695
REMARK 3 S21: 0.0588 S22: -0.0232 S23: 0.1668
REMARK 3 S31: 0.0835 S32: -0.0472 S33: 0.0571
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 341 THROUGH 387 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6311 31.7860 7.2711
REMARK 3 T TENSOR
REMARK 3 T11: 0.1954 T22: 0.1584
REMARK 3 T33: 0.1263 T12: -0.0035
REMARK 3 T13: 0.0161 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 3.0757 L22: 1.6617
REMARK 3 L33: 1.0968 L12: 0.6332
REMARK 3 L13: -0.3333 L23: 0.1810
REMARK 3 S TENSOR
REMARK 3 S11: 0.0356 S12: 0.0567 S13: 0.0678
REMARK 3 S21: -0.1644 S22: -0.0185 S23: -0.0563
REMARK 3 S31: -0.1418 S32: 0.0772 S33: -0.0070
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 388 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0792 38.0483 7.6676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1895 T22: 0.2009
REMARK 3 T33: 0.1989 T12: 0.0356
REMARK 3 T13: -0.0170 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.8765 L22: 2.0253
REMARK 3 L33: 4.4458 L12: -1.1733
REMARK 3 L13: -1.8050 L23: 0.9550
REMARK 3 S TENSOR
REMARK 3 S11: 0.2062 S12: 0.4411 S13: 0.0870
REMARK 3 S21: -0.1456 S22: -0.1701 S23: 0.1215
REMARK 3 S31: -0.3212 S32: -0.1555 S33: -0.0510
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 414 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9879 36.7468 1.8097
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.2045
REMARK 3 T33: 0.1925 T12: -0.0076
REMARK 3 T13: 0.0546 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 4.2971 L22: 3.9033
REMARK 3 L33: 3.8652 L12: 0.4753
REMARK 3 L13: 0.3155 L23: 0.8186
REMARK 3 S TENSOR
REMARK 3 S11: 0.2776 S12: -0.0433 S13: 0.4034
REMARK 3 S21: 0.0021 S22: -0.3895 S23: -0.1317
REMARK 3 S31: -0.4428 S32: 0.0515 S33: -0.0216
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 439 THROUGH 463 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3318 36.2552 -8.0432
REMARK 3 T TENSOR
REMARK 3 T11: 0.3742 T22: 0.2622
REMARK 3 T33: 0.2133 T12: 0.0566
REMARK 3 T13: 0.0961 T23: 0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 5.9531 L22: 3.2995
REMARK 3 L33: 5.8982 L12: 1.1466
REMARK 3 L13: 2.5078 L23: 1.0632
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.4376 S13: -0.0307
REMARK 3 S21: -0.6340 S22: 0.0023 S23: -0.1613
REMARK 3 S31: -0.4473 S32: -0.0085 S33: -0.0611
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 464 THROUGH 512 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8685 40.2429 15.1717
REMARK 3 T TENSOR
REMARK 3 T11: 0.2213 T22: 0.1592
REMARK 3 T33: 0.2255 T12: -0.0042
REMARK 3 T13: 0.0216 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.0287 L22: 1.3072
REMARK 3 L33: 2.6009 L12: -0.4311
REMARK 3 L13: -0.8689 L23: 0.1758
REMARK 3 S TENSOR
REMARK 3 S11: 0.1692 S12: 0.0757 S13: 0.1533
REMARK 3 S21: -0.1717 S22: 0.0377 S23: -0.1630
REMARK 3 S31: -0.2317 S32: 0.1093 S33: -0.1100
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 498 THROUGH 506 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6394 29.2733 19.1048
REMARK 3 T TENSOR
REMARK 3 T11: 0.2320 T22: 0.1938
REMARK 3 T33: 0.2276 T12: -0.0226
REMARK 3 T13: -0.0186 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 2.0857 L22: 2.0048
REMARK 3 L33: 2.4375 L12: 1.8395
REMARK 3 L13: -1.0596 L23: -1.7243
REMARK 3 S TENSOR
REMARK 3 S11: 0.2425 S12: 0.1270 S13: 0.4528
REMARK 3 S21: 0.3100 S22: -0.1628 S23: -0.3505
REMARK 3 S31: -0.3354 S32: 0.5557 S33: -0.0246
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 269 THROUGH 287 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5681 14.5785 26.1648
REMARK 3 T TENSOR
REMARK 3 T11: 0.2874 T22: 0.6295
REMARK 3 T33: 0.5056 T12: 0.0915
REMARK 3 T13: 0.1990 T23: 0.1122
REMARK 3 L TENSOR
REMARK 3 L11: 5.8387 L22: 5.3092
REMARK 3 L33: 1.9816 L12: -2.7650
REMARK 3 L13: 0.1327 L23: 1.3924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0656 S12: 0.2304 S13: 0.2562
REMARK 3 S21: -0.9267 S22: -0.1753 S23: -1.2085
REMARK 3 S31: 0.2653 S32: 1.1439 S33: -0.1689
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 288 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2161 29.1697 36.6293
REMARK 3 T TENSOR
REMARK 3 T11: 0.3497 T22: 0.3627
REMARK 3 T33: 0.3534 T12: -0.0885
REMARK 3 T13: 0.0162 T23: -0.1032
REMARK 3 L TENSOR
REMARK 3 L11: 1.9613 L22: 4.5881
REMARK 3 L33: 5.7369 L12: -0.6762
REMARK 3 L13: -0.8191 L23: 4.4842
REMARK 3 S TENSOR
REMARK 3 S11: 0.4570 S12: 0.0287 S13: 0.4965
REMARK 3 S21: -0.4078 S22: 0.4985 S23: -1.3332
REMARK 3 S31: -0.4809 S32: 0.3033 S33: 0.2078
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 299 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5357 27.1871 35.9634
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.1318
REMARK 3 T33: 0.1571 T12: -0.0140
REMARK 3 T13: -0.0331 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 2.7757 L22: 1.4977
REMARK 3 L33: 1.2071 L12: -0.1744
REMARK 3 L13: 0.4466 L23: 0.2356
REMARK 3 S TENSOR
REMARK 3 S11: -0.1510 S12: -0.2321 S13: 0.2364
REMARK 3 S21: 0.0812 S22: -0.0151 S23: 0.0924
REMARK 3 S31: -0.1985 S32: 0.0088 S33: 0.0677
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 341 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3249 11.9674 25.7752
REMARK 3 T TENSOR
REMARK 3 T11: 0.1844 T22: 0.1685
REMARK 3 T33: 0.2028 T12: 0.0256
REMARK 3 T13: 0.0328 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 2.3987 L22: 4.4458
REMARK 3 L33: 3.9317 L12: 0.7806
REMARK 3 L13: 0.7665 L23: 1.1898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: 0.1422 S13: -0.1477
REMARK 3 S21: -0.3422 S22: -0.0026 S23: -0.3183
REMARK 3 S31: 0.0105 S32: 0.1154 S33: 0.0376
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3361 21.6620 45.1663
REMARK 3 T TENSOR
REMARK 3 T11: 0.2899 T22: 0.2082
REMARK 3 T33: 0.1594 T12: -0.0044
REMARK 3 T13: -0.0420 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 3.1130 L22: 2.4638
REMARK 3 L33: 2.4095 L12: -0.7458
REMARK 3 L13: 0.4144 L23: -0.2440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: -0.1569 S13: -0.0454
REMARK 3 S21: 0.4118 S22: -0.0047 S23: -0.1406
REMARK 3 S31: -0.1034 S32: 0.1223 S33: 0.0655
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 414 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6352 8.3003 30.4378
REMARK 3 T TENSOR
REMARK 3 T11: 0.1589 T22: 0.2588
REMARK 3 T33: 0.2219 T12: 0.0294
REMARK 3 T13: 0.0227 T23: 0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 4.0487 L22: 3.5110
REMARK 3 L33: 3.1478 L12: 2.0946
REMARK 3 L13: 1.4253 L23: 1.2914
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: 0.1119 S13: -0.1474
REMARK 3 S21: -0.0741 S22: 0.1376 S23: -0.2619
REMARK 3 S31: 0.0138 S32: 0.4457 S33: 0.0042
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 465 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1371 5.2937 33.2766
REMARK 3 T TENSOR
REMARK 3 T11: 0.2388 T22: 0.4181
REMARK 3 T33: 0.5246 T12: 0.0859
REMARK 3 T13: -0.0259 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 4.7306 L22: 4.5743
REMARK 3 L33: 5.3038 L12: 0.8321
REMARK 3 L13: 1.5198 L23: 1.1584
REMARK 3 S TENSOR
REMARK 3 S11: 0.2623 S12: -0.1160 S13: -0.5460
REMARK 3 S21: 0.5418 S22: 0.1574 S23: -1.2476
REMARK 3 S31: 0.4739 S32: 0.9167 S33: -0.0612
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 466 THROUGH 494 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4850 9.5256 37.6304
REMARK 3 T TENSOR
REMARK 3 T11: 0.1886 T22: 0.1657
REMARK 3 T33: 0.2329 T12: -0.0144
REMARK 3 T13: 0.0158 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 6.0053 L22: 2.8285
REMARK 3 L33: 1.2994 L12: -1.5208
REMARK 3 L13: 0.9028 L23: -0.9228
REMARK 3 S TENSOR
REMARK 3 S11: 0.1561 S12: -0.2769 S13: -0.2388
REMARK 3 S21: 0.0147 S22: -0.1120 S23: -0.1021
REMARK 3 S31: 0.1073 S32: 0.0857 S33: 0.0428
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 495 THROUGH 518 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5724 15.5917 23.8848
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2076
REMARK 3 T33: 0.1807 T12: -0.0009
REMARK 3 T13: -0.0465 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.9675 L22: 3.8354
REMARK 3 L33: 1.2671 L12: -1.2289
REMARK 3 L13: -0.4582 L23: 0.2147
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.1003 S13: -0.1516
REMARK 3 S21: -0.3335 S22: -0.1355 S23: 0.2492
REMARK 3 S31: -0.0579 S32: -0.0213 S33: 0.0767
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 498 THROUGH 506 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5205 15.9642 14.1289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3342 T22: 0.2297
REMARK 3 T33: 0.2133 T12: 0.0269
REMARK 3 T13: 0.0499 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 7.2072 L22: 2.0740
REMARK 3 L33: 6.4333 L12: -1.8613
REMARK 3 L13: 0.1110 L23: -0.8108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: 0.1711 S13: -0.1222
REMARK 3 S21: -0.1275 S22: -0.3754 S23: -0.1302
REMARK 3 S31: 0.6626 S32: 0.3875 S33: 0.3920
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 4S15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000088048.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51703
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.897
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM MGCL2, 9%-21% PEG 3350, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 35.59700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.55200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.15250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.55200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.59700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.15250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 268
REMARK 465 SER A 513
REMARK 465 GLU A 514
REMARK 465 PHE A 515
REMARK 465 GLU A 516
REMARK 465 PRO A 517
REMARK 465 ALA A 518
REMARK 465 MET A 519
REMARK 465 GLN A 520
REMARK 465 ILE A 521
REMARK 465 ASP A 522
REMARK 465 GLY A 523
REMARK 465 LYS C 507
REMARK 465 ASN C 508
REMARK 465 GLU C 509
REMARK 465 GLY B 268
REMARK 465 MET B 519
REMARK 465 GLN B 520
REMARK 465 ILE B 521
REMARK 465 ASP B 522
REMARK 465 GLY B 523
REMARK 465 LYS D 507
REMARK 465 ASN D 508
REMARK 465 GLU D 509
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 MET A 429 45.79 -86.66
REMARK 500 GLU A 438 60.05 -100.26
REMARK 500 TYR A 495 60.93 -119.00
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 4D8 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4D8 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4S14 RELATED DB: PDB
DBREF 4S15 A 269 523 UNP P35398 RORA_HUMAN 269 523
DBREF 4S15 C 498 509 UNP P48552 NRIP1_HUMAN 499 510
DBREF 4S15 B 269 523 UNP P35398 RORA_HUMAN 269 523
DBREF 4S15 D 498 509 UNP P48552 NRIP1_HUMAN 499 510
SEQADV 4S15 GLY A 268 UNP P35398 EXPRESSION TAG
SEQADV 4S15 GLY B 268 UNP P35398 EXPRESSION TAG
SEQRES 1 A 256 GLY SER MET ALA GLU LEU GLU HIS LEU ALA GLN ASN ILE
SEQRES 2 A 256 SER LYS SER HIS LEU GLU THR CYS GLN TYR LEU ARG GLU
SEQRES 3 A 256 GLU LEU GLN GLN ILE THR TRP GLN THR PHE LEU GLN GLU
SEQRES 4 A 256 GLU ILE GLU ASN TYR GLN ASN LYS GLN ARG GLU VAL MET
SEQRES 5 A 256 TRP GLN LEU CYS ALA ILE LYS ILE THR GLU ALA ILE GLN
SEQRES 6 A 256 TYR VAL VAL GLU PHE ALA LYS ARG ILE ASP GLY PHE MET
SEQRES 7 A 256 GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS ALA
SEQRES 8 A 256 GLY SER LEU GLU VAL VAL PHE ILE ARG MET CYS ARG ALA
SEQRES 9 A 256 PHE ASP SER GLN ASN ASN THR VAL TYR PHE ASP GLY LYS
SEQRES 10 A 256 TYR ALA SER PRO ASP VAL PHE LYS SER LEU GLY CYS GLU
SEQRES 11 A 256 ASP PHE ILE SER PHE VAL PHE GLU PHE GLY LYS SER LEU
SEQRES 12 A 256 CYS SER MET HIS LEU THR GLU ASP GLU ILE ALA LEU PHE
SEQRES 13 A 256 SER ALA PHE VAL LEU MET SER ALA ASP ARG SER TRP LEU
SEQRES 14 A 256 GLN GLU LYS VAL LYS ILE GLU LYS LEU GLN GLN LYS ILE
SEQRES 15 A 256 GLN LEU ALA LEU GLN HIS VAL LEU GLN LYS ASN HIS ARG
SEQRES 16 A 256 GLU ASP GLY ILE LEU THR LYS LEU ILE CYS LYS VAL SER
SEQRES 17 A 256 THR LEU ARG ALA LEU CYS GLY ARG HIS THR GLU LYS LEU
SEQRES 18 A 256 MET ALA PHE LYS ALA ILE TYR PRO ASP ILE VAL ARG LEU
SEQRES 19 A 256 HIS PHE PRO PRO LEU TYR LYS GLU LEU PHE THR SER GLU
SEQRES 20 A 256 PHE GLU PRO ALA MET GLN ILE ASP GLY
SEQRES 1 C 12 THR LEU LEU GLN LEU LEU LEU GLY HIS LYS ASN GLU
SEQRES 1 B 256 GLY SER MET ALA GLU LEU GLU HIS LEU ALA GLN ASN ILE
SEQRES 2 B 256 SER LYS SER HIS LEU GLU THR CYS GLN TYR LEU ARG GLU
SEQRES 3 B 256 GLU LEU GLN GLN ILE THR TRP GLN THR PHE LEU GLN GLU
SEQRES 4 B 256 GLU ILE GLU ASN TYR GLN ASN LYS GLN ARG GLU VAL MET
SEQRES 5 B 256 TRP GLN LEU CYS ALA ILE LYS ILE THR GLU ALA ILE GLN
SEQRES 6 B 256 TYR VAL VAL GLU PHE ALA LYS ARG ILE ASP GLY PHE MET
SEQRES 7 B 256 GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS ALA
SEQRES 8 B 256 GLY SER LEU GLU VAL VAL PHE ILE ARG MET CYS ARG ALA
SEQRES 9 B 256 PHE ASP SER GLN ASN ASN THR VAL TYR PHE ASP GLY LYS
SEQRES 10 B 256 TYR ALA SER PRO ASP VAL PHE LYS SER LEU GLY CYS GLU
SEQRES 11 B 256 ASP PHE ILE SER PHE VAL PHE GLU PHE GLY LYS SER LEU
SEQRES 12 B 256 CYS SER MET HIS LEU THR GLU ASP GLU ILE ALA LEU PHE
SEQRES 13 B 256 SER ALA PHE VAL LEU MET SER ALA ASP ARG SER TRP LEU
SEQRES 14 B 256 GLN GLU LYS VAL LYS ILE GLU LYS LEU GLN GLN LYS ILE
SEQRES 15 B 256 GLN LEU ALA LEU GLN HIS VAL LEU GLN LYS ASN HIS ARG
SEQRES 16 B 256 GLU ASP GLY ILE LEU THR LYS LEU ILE CYS LYS VAL SER
SEQRES 17 B 256 THR LEU ARG ALA LEU CYS GLY ARG HIS THR GLU LYS LEU
SEQRES 18 B 256 MET ALA PHE LYS ALA ILE TYR PRO ASP ILE VAL ARG LEU
SEQRES 19 B 256 HIS PHE PRO PRO LEU TYR LYS GLU LEU PHE THR SER GLU
SEQRES 20 B 256 PHE GLU PRO ALA MET GLN ILE ASP GLY
SEQRES 1 D 12 THR LEU LEU GLN LEU LEU LEU GLY HIS LYS ASN GLU
HET 4D8 A 601 32
HET GOL A 602 6
HET 4D8 B 601 32
HET GOL B 602 6
HETNAM 4D8 (3BETA,4ALPHA,5BETA,14BETA)-3-HYDROXY-4-METHYLCHOLESTA-
HETNAM 2 4D8 8,24-DIENE-4-CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN 4D8 4ALPHA-CARBOXY-4BETA-METHYL-ZYMOSTEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 4D8 2(C29 H46 O3)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 9 HOH *310(H2 O)
HELIX 1 1 SER A 269 CYS A 288 1 20
HELIX 2 2 LEU A 291 ILE A 298 1 8
HELIX 3 3 LEU A 304 ASN A 313 1 10
HELIX 4 4 GLN A 315 ARG A 340 1 26
HELIX 5 5 ILE A 341 GLU A 346 1 6
HELIX 6 6 CYS A 348 CYS A 369 1 22
HELIX 7 7 SER A 387 GLY A 395 5 9
HELIX 8 8 CYS A 396 SER A 412 1 17
HELIX 9 9 THR A 416 MET A 429 1 14
HELIX 10 10 GLU A 438 ASN A 460 1 23
HELIX 11 11 ASP A 464 TYR A 495 1 32
HELIX 12 12 TYR A 495 PHE A 503 1 9
HELIX 13 13 PRO A 504 THR A 512 1 9
HELIX 14 14 LEU C 499 GLY C 505 1 7
HELIX 15 15 MET B 270 CYS B 288 1 19
HELIX 16 16 LEU B 291 GLN B 297 1 7
HELIX 17 17 LEU B 304 ASN B 313 1 10
HELIX 18 18 GLN B 315 ARG B 340 1 26
HELIX 19 19 CYS B 348 MET B 368 1 21
HELIX 20 20 SER B 387 GLY B 395 5 9
HELIX 21 21 CYS B 396 SER B 412 1 17
HELIX 22 22 THR B 416 MET B 429 1 14
HELIX 23 23 GLU B 438 LYS B 459 1 22
HELIX 24 24 GLY B 465 TYR B 495 1 31
HELIX 25 25 TYR B 495 PHE B 503 1 9
HELIX 26 26 PRO B 504 THR B 512 1 9
HELIX 27 27 LEU D 499 GLY D 505 1 7
SHEET 1 A 3 PHE A 372 ASP A 373 0
SHEET 2 A 3 THR A 378 PHE A 381 -1 O THR A 378 N ASP A 373
SHEET 3 A 3 LYS A 384 ALA A 386 -1 O ALA A 386 N VAL A 379
SHEET 1 B 3 PHE B 372 ASP B 373 0
SHEET 2 B 3 THR B 378 PHE B 381 -1 O THR B 378 N ASP B 373
SHEET 3 B 3 LYS B 384 ALA B 386 -1 O ALA B 386 N VAL B 379
SITE 1 AC1 11 GLN A 289 TYR A 290 ILE A 327 ALA A 330
SITE 2 AC1 11 MET A 368 VAL A 379 TYR A 380 VAL A 403
SITE 3 AC1 11 GOL A 602 HOH A 757 HOH A 764
SITE 1 AC2 7 CYS A 288 GLN A 289 TYR A 290 ARG A 367
SITE 2 AC2 7 ARG A 370 4D8 A 601 HOH A 706
SITE 1 AC3 13 GLN B 289 TYR B 290 TRP B 320 ILE B 327
SITE 2 AC3 13 ALA B 330 MET B 368 VAL B 379 TYR B 380
SITE 3 AC3 13 LEU B 394 PHE B 399 VAL B 403 GOL B 602
SITE 4 AC3 13 HOH B 751
SITE 1 AC4 6 CYS B 288 GLN B 289 TYR B 290 ARG B 367
SITE 2 AC4 6 ARG B 370 4D8 B 601
CRYST1 71.194 80.305 113.104 90.00 90.00 90.00 P 21 21 21 8
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 0.014046 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
