HEADER TRANSCRIPTION 07-OCT-14 4WLB
TITLE CRYSTAL STRUCTURE OF RORC IN COMPLEX WITH A PARTIAL INVERSE AGONIST
TITLE 2 COMPOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ROR-GAMMA LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-GAMMA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SRC-1 PEPTIDE;
COMPND 11 CHAIN: D, E;
COMPND 12 FRAGMENT: SRC-1 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: RORC, NR1F3, RORG, RZRG;
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: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS NUCLEAR RECEPTOR LIGAND BINDING DOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BOENIG,S.G.HYMOWITZ,J.R.KIEFER
REVDAT 4 27-DEC-23 4WLB 1 REMARK
REVDAT 3 22-NOV-17 4WLB 1 SOURCE JRNL REMARK
REVDAT 2 17-DEC-14 4WLB 1 JRNL
REVDAT 1 12-NOV-14 4WLB 0
JRNL AUTH M.B.VAN NIEL,B.P.FAUBER,M.CARTWRIGHT,S.GAINES,J.C.KILLEN,
JRNL AUTH 2 O.RENE,S.I.WARD,G.DE LEON BOENIG,Y.DENG,C.EIDENSCHENK,
JRNL AUTH 3 C.EVERETT,E.GANCIA,A.GANGULI,A.GOBBI,J.HAWKINS,A.R.JOHNSON,
JRNL AUTH 4 J.R.KIEFER,H.LA,P.LOCKEY,M.NORMAN,W.OUYANG,A.QIN,N.WAKES,
JRNL AUTH 5 B.WASZKOWYCZ,H.WONG
JRNL TITL A REVERSED SULFONAMIDE SERIES OF SELECTIVE RORC INVERSE
JRNL TITL 2 AGONISTS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 5769 2014
JRNL REFN ESSN 1464-3405
JRNL PMID 25453817
JRNL DOI 10.1016/J.BMCL.2014.10.037
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 53814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.080
REMARK 3 FREE R VALUE TEST SET COUNT : 5427
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 39.0500 - 5.2828 1.00 1914 218 0.1821 0.2273
REMARK 3 2 5.2828 - 4.1947 0.99 1800 200 0.1318 0.1482
REMARK 3 3 4.1947 - 3.6649 0.99 1836 173 0.1371 0.1872
REMARK 3 4 3.6649 - 3.3300 0.99 1789 184 0.1546 0.1859
REMARK 3 5 3.3300 - 3.0914 1.00 1771 217 0.1632 0.1950
REMARK 3 6 3.0914 - 2.9092 1.00 1758 213 0.1724 0.2167
REMARK 3 7 2.9092 - 2.7636 1.00 1791 197 0.1647 0.2152
REMARK 3 8 2.7636 - 2.6433 1.00 1737 202 0.1663 0.2209
REMARK 3 9 2.6433 - 2.5416 1.00 1771 200 0.1581 0.2118
REMARK 3 10 2.5416 - 2.4539 1.00 1787 179 0.1567 0.2163
REMARK 3 11 2.4539 - 2.3772 1.00 1742 199 0.1444 0.2154
REMARK 3 12 2.3772 - 2.3092 1.00 1772 199 0.1497 0.1795
REMARK 3 13 2.3092 - 2.2484 0.96 1688 170 0.1977 0.2964
REMARK 3 14 2.2484 - 2.1936 0.97 1710 186 0.2111 0.2763
REMARK 3 15 2.1936 - 2.1437 1.00 1751 200 0.1717 0.2189
REMARK 3 16 2.1437 - 2.0981 1.00 1747 180 0.1780 0.2247
REMARK 3 17 2.0981 - 2.0561 0.99 1781 186 0.2087 0.2609
REMARK 3 18 2.0561 - 2.0173 1.00 1726 194 0.1934 0.2393
REMARK 3 19 2.0173 - 1.9813 1.00 1764 196 0.1839 0.2303
REMARK 3 20 1.9813 - 1.9477 0.99 1674 232 0.2029 0.2891
REMARK 3 21 1.9477 - 1.9163 0.96 1684 166 0.2910 0.3707
REMARK 3 22 1.9163 - 1.8868 0.94 1654 202 0.3488 0.4100
REMARK 3 23 1.8868 - 1.8591 0.98 1697 182 0.2638 0.3142
REMARK 3 24 1.8591 - 1.8329 0.97 1667 213 0.2540 0.2769
REMARK 3 25 1.8329 - 1.8081 0.95 1652 181 0.2336 0.2496
REMARK 3 26 1.8081 - 1.7846 0.83 1438 177 0.2163 0.2660
REMARK 3 27 1.7846 - 1.7623 0.68 1169 129 0.2154 0.2630
REMARK 3 28 1.7623 - 1.7411 0.54 954 111 0.2263 0.3085
REMARK 3 29 1.7411 - 1.7209 0.40 691 72 0.2338 0.3020
REMARK 3 30 1.7209 - 1.7015 0.28 472 69 0.2567 0.3548
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.63
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 : 0.007 4396
REMARK 3 ANGLE : 1.034 5945
REMARK 3 CHIRALITY : 0.037 652
REMARK 3 PLANARITY : 0.004 752
REMARK 3 DIHEDRAL : 14.804 1633
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 239 THROUGH 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1377 30.2731 -20.4084
REMARK 3 T TENSOR
REMARK 3 T11: 0.1363 T22: 0.1187
REMARK 3 T33: 0.1271 T12: -0.0127
REMARK 3 T13: 0.0318 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 2.0247 L22: 4.3470
REMARK 3 L33: 0.3823 L12: 0.2257
REMARK 3 L13: -0.1123 L23: 0.2190
REMARK 3 S TENSOR
REMARK 3 S11: -0.0522 S12: 0.1120 S13: 0.3810
REMARK 3 S21: -0.5062 S22: 0.0953 S23: -0.4134
REMARK 3 S31: -0.1479 S32: -0.0064 S33: -0.0195
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 264 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8856 2.6190 -12.2264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.1077
REMARK 3 T33: 0.0836 T12: -0.0285
REMARK 3 T13: -0.0008 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 0.6180 L22: 1.0145
REMARK 3 L33: 0.7969 L12: -0.3122
REMARK 3 L13: 0.3160 L23: -0.0998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0235 S12: 0.0039 S13: -0.0496
REMARK 3 S21: -0.1681 S22: 0.0240 S23: 0.1936
REMARK 3 S31: 0.1925 S32: -0.1072 S33: 0.0047
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2832 17.2138 -9.8263
REMARK 3 T TENSOR
REMARK 3 T11: 0.0490 T22: 0.0750
REMARK 3 T33: 0.0884 T12: -0.0155
REMARK 3 T13: -0.0157 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.0124 L22: 1.6850
REMARK 3 L33: 0.9799 L12: 0.2756
REMARK 3 L13: 0.6557 L23: 0.3291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.1374 S13: -0.0759
REMARK 3 S21: 0.0226 S22: 0.0393 S23: -0.3160
REMARK 3 S31: -0.0137 S32: 0.0886 S33: 0.0505
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 348 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1536 7.3783 -4.3917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0888 T22: 0.1159
REMARK 3 T33: 0.0859 T12: -0.0318
REMARK 3 T13: 0.0221 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 1.0686 L22: 1.3654
REMARK 3 L33: 0.9534 L12: 0.0148
REMARK 3 L13: 0.0156 L23: 0.3095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0546 S12: 0.0222 S13: -0.0220
REMARK 3 S21: -0.0082 S22: 0.0069 S23: 0.1798
REMARK 3 S31: 0.1288 S32: -0.2078 S33: 0.0473
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 390 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3171 27.6877 -9.7864
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.0730
REMARK 3 T33: 0.1019 T12: -0.0063
REMARK 3 T13: -0.0364 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 2.0340 L22: 1.4143
REMARK 3 L33: 0.6217 L12: -0.3761
REMARK 3 L13: 0.4328 L23: -0.1722
REMARK 3 S TENSOR
REMARK 3 S11: -0.1095 S12: -0.0113 S13: 0.2860
REMARK 3 S21: 0.0805 S22: 0.0251 S23: -0.1479
REMARK 3 S31: -0.0419 S32: -0.0174 S33: 0.0658
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6799 29.4416 -6.3582
REMARK 3 T TENSOR
REMARK 3 T11: 0.0953 T22: 0.1160
REMARK 3 T33: 0.1921 T12: 0.0125
REMARK 3 T13: -0.0234 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.7062 L22: 2.9251
REMARK 3 L33: 4.0707 L12: -1.1133
REMARK 3 L13: 1.3510 L23: -1.9281
REMARK 3 S TENSOR
REMARK 3 S11: -0.1013 S12: -0.2243 S13: 0.2429
REMARK 3 S21: 0.3198 S22: 0.1749 S23: 0.2813
REMARK 3 S31: 0.0662 S32: -0.1929 S33: 0.0612
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 450 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4548 2.4449 0.8923
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.1361
REMARK 3 T33: -0.0233 T12: 0.0410
REMARK 3 T13: -0.0589 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.2785 L22: 2.0630
REMARK 3 L33: 1.0538 L12: -0.5215
REMARK 3 L13: -0.1548 L23: 0.4031
REMARK 3 S TENSOR
REMARK 3 S11: -0.1128 S12: -0.0101 S13: 0.0778
REMARK 3 S21: 0.5564 S22: 0.1447 S23: -0.6360
REMARK 3 S31: 0.3625 S32: 0.0307 S33: 0.0655
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 239 THROUGH 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5609 -36.7651 -4.9148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2266 T22: 0.1032
REMARK 3 T33: 0.1159 T12: -0.0101
REMARK 3 T13: -0.0367 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.2527 L22: 4.7332
REMARK 3 L33: 1.0319 L12: -0.7594
REMARK 3 L13: 0.4436 L23: -0.4132
REMARK 3 S TENSOR
REMARK 3 S11: 0.1716 S12: -0.0813 S13: -0.2358
REMARK 3 S21: 0.6789 S22: -0.0181 S23: 0.0930
REMARK 3 S31: 0.1794 S32: 0.0382 S33: -0.2437
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 264 THROUGH 291 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5601 -7.7739 -20.9207
REMARK 3 T TENSOR
REMARK 3 T11: 0.1095 T22: 0.1787
REMARK 3 T33: 0.2547 T12: 0.0114
REMARK 3 T13: 0.0445 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 1.0605 L22: 1.9558
REMARK 3 L33: 0.8682 L12: 0.0439
REMARK 3 L13: 0.7501 L23: -0.4988
REMARK 3 S TENSOR
REMARK 3 S11: -0.1752 S12: 0.0497 S13: 0.0335
REMARK 3 S21: 0.0837 S22: 0.3347 S23: 0.6323
REMARK 3 S31: -0.0425 S32: -0.3133 S33: -0.0639
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 292 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5526 -10.5586 -13.6000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1008 T22: 0.0938
REMARK 3 T33: 0.0514 T12: -0.0091
REMARK 3 T13: -0.0100 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.8936 L22: 3.2150
REMARK 3 L33: 1.1012 L12: 0.4437
REMARK 3 L13: 0.2676 L23: -1.0842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.0535 S13: 0.0469
REMARK 3 S21: 0.3070 S22: 0.0057 S23: -0.0536
REMARK 3 S31: -0.0523 S32: -0.0739 S33: -0.0682
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 317 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8059 -24.0624 -11.2264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1341 T22: 0.0223
REMARK 3 T33: 0.2889 T12: -0.0002
REMARK 3 T13: -0.1347 T23: 0.0993
REMARK 3 L TENSOR
REMARK 3 L11: 2.3350 L22: 1.5235
REMARK 3 L33: 0.5987 L12: 0.3767
REMARK 3 L13: -0.0427 L23: -0.0322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0982 S12: 0.1038 S13: -0.7561
REMARK 3 S21: 0.3193 S22: -0.1023 S23: -0.5963
REMARK 3 S31: 0.1128 S32: 0.1371 S33: -0.1235
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 348 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2991 -13.9276 -27.6464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1397 T22: 0.1260
REMARK 3 T33: 0.0910 T12: -0.0169
REMARK 3 T13: -0.0324 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 1.3148 L22: 1.7116
REMARK 3 L33: 0.2556 L12: 0.3990
REMARK 3 L13: 0.3841 L23: -0.1776
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: 0.1733 S13: 0.0329
REMARK 3 S21: -0.3593 S22: 0.1351 S23: 0.2432
REMARK 3 S31: 0.0142 S32: 0.0108 S33: -0.0494
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 390 THROUGH 414 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7441 -30.2357 -14.9412
REMARK 3 T TENSOR
REMARK 3 T11: -0.1155 T22: 0.0887
REMARK 3 T33: 0.3293 T12: -0.0189
REMARK 3 T13: -0.0716 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.2965 L22: 2.3048
REMARK 3 L33: 1.1918 L12: 0.7459
REMARK 3 L13: 0.1273 L23: -0.0215
REMARK 3 S TENSOR
REMARK 3 S11: -0.2137 S12: 0.0146 S13: -0.2818
REMARK 3 S21: -0.2809 S22: 0.2439 S23: -0.8925
REMARK 3 S31: 0.0068 S32: 0.1392 S33: -0.2514
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 415 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2326 -39.3696 -12.1073
REMARK 3 T TENSOR
REMARK 3 T11: 0.0987 T22: 0.0651
REMARK 3 T33: 0.3652 T12: 0.0120
REMARK 3 T13: -0.0681 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 1.8603 L22: 1.6421
REMARK 3 L33: 1.5261 L12: -0.1852
REMARK 3 L13: 0.6520 L23: -0.2130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: -0.1019 S13: -0.0468
REMARK 3 S21: 0.0849 S22: -0.0124 S23: -0.7882
REMARK 3 S31: 0.2691 S32: 0.0550 S33: -0.3527
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 436 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8279 -36.1496 -24.2931
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 0.1095
REMARK 3 T33: 0.1707 T12: -0.0080
REMARK 3 T13: 0.0414 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 3.0187 L22: 3.1123
REMARK 3 L33: 2.1354 L12: 2.2504
REMARK 3 L13: -1.2953 L23: -1.0505
REMARK 3 S TENSOR
REMARK 3 S11: 0.3226 S12: 0.1534 S13: -0.2381
REMARK 3 S21: -0.4146 S22: 0.0287 S23: -0.3473
REMARK 3 S31: -0.1654 S32: 0.1373 S33: 0.0719
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 450 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0520 -9.1493 -21.2433
REMARK 3 T TENSOR
REMARK 3 T11: 0.0934 T22: 0.1649
REMARK 3 T33: 0.1208 T12: -0.0345
REMARK 3 T13: 0.0466 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.5645 L22: 1.7555
REMARK 3 L33: 1.4037 L12: -0.2849
REMARK 3 L13: -0.2975 L23: -0.0110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0925 S12: 0.0667 S13: -0.0914
REMARK 3 S21: -0.0900 S22: 0.1649 S23: -0.5910
REMARK 3 S31: -0.0699 S32: 0.2020 S33: -0.0275
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 8 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0979 9.4259 -12.9110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.1722
REMARK 3 T33: 0.2542 T12: -0.0235
REMARK 3 T13: 0.0581 T23: -0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 3.4258 L22: 4.4708
REMARK 3 L33: 2.8816 L12: -1.0959
REMARK 3 L13: 2.0324 L23: 0.3198
REMARK 3 S TENSOR
REMARK 3 S11: 0.3257 S12: 0.1248 S13: 0.3660
REMARK 3 S21: -0.2382 S22: -0.1304 S23: -0.6216
REMARK 3 S31: -0.1059 S32: 0.1879 S33: 0.0114
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7953 -16.1074 -2.8942
REMARK 3 T TENSOR
REMARK 3 T11: 0.3648 T22: 0.2319
REMARK 3 T33: 0.2088 T12: -0.0226
REMARK 3 T13: -0.1375 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 3.8640 L22: 4.5281
REMARK 3 L33: 3.4746 L12: -0.1081
REMARK 3 L13: -1.0028 L23: -0.9648
REMARK 3 S TENSOR
REMARK 3 S11: 0.1690 S12: -0.3174 S13: -0.0255
REMARK 3 S21: 0.4586 S22: -0.0048 S23: -0.6497
REMARK 3 S31: 0.4154 S32: 0.0945 S33: 0.0758
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 4WLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62573
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.76600
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM FORMATE, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 291K
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 33.39350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.92700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.12900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.92700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.39350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.12900
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, 3, 4
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: B, E
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 86.25800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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 246
REMARK 465 HIS A 247
REMARK 465 HIS A 248
REMARK 465 HIS A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 GLY A 253
REMARK 465 GLU A 254
REMARK 465 ASN A 255
REMARK 465 LEU A 256
REMARK 465 TYR A 257
REMARK 465 PHE A 258
REMARK 465 GLN A 259
REMARK 465 GLY A 508
REMARK 465 ASN A 509
REMARK 465 SER A 510
REMARK 465 MET B 246
REMARK 465 HIS B 247
REMARK 465 HIS B 248
REMARK 465 HIS B 249
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 GLY B 253
REMARK 465 GLU B 254
REMARK 465 ASN B 255
REMARK 465 LEU B 256
REMARK 465 TYR B 257
REMARK 465 PHE B 258
REMARK 465 GLN B 259
REMARK 465 GLY B 508
REMARK 465 ASN B 509
REMARK 465 SER B 510
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 ARG A 437 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 469 CG CD CE NZ
REMARK 470 ARG B 294 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 437 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 O HOH A 821 O HOH A 894 2.15
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 GLN A 286 -93.15 75.21
REMARK 500 HIS A 411 62.61 36.65
REMARK 500 GLN B 286 -73.28 75.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3QQ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3QQ B 601
DBREF 4WLB A 262 507 UNP P51449 RORG_HUMAN 241 486
DBREF 4WLB B 262 507 UNP P51449 RORG_HUMAN 241 486
DBREF 4WLB D 8 15 PDB 4WLB 4WLB 8 15
DBREF 4WLB E 8 15 PDB 4WLB 4WLB 8 15
SEQADV 4WLB MET A 246 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 247 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 248 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 249 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 250 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 251 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS A 252 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY A 253 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLU A 254 UNP P51449 EXPRESSION TAG
SEQADV 4WLB ASN A 255 UNP P51449 EXPRESSION TAG
SEQADV 4WLB LEU A 256 UNP P51449 EXPRESSION TAG
SEQADV 4WLB TYR A 257 UNP P51449 EXPRESSION TAG
SEQADV 4WLB PHE A 258 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLN A 259 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY A 260 UNP P51449 EXPRESSION TAG
SEQADV 4WLB SER A 261 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY A 508 UNP P51449 EXPRESSION TAG
SEQADV 4WLB ASN A 509 UNP P51449 EXPRESSION TAG
SEQADV 4WLB SER A 510 UNP P51449 EXPRESSION TAG
SEQADV 4WLB MET B 246 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 247 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 248 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 249 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 250 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 251 UNP P51449 EXPRESSION TAG
SEQADV 4WLB HIS B 252 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY B 253 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLU B 254 UNP P51449 EXPRESSION TAG
SEQADV 4WLB ASN B 255 UNP P51449 EXPRESSION TAG
SEQADV 4WLB LEU B 256 UNP P51449 EXPRESSION TAG
SEQADV 4WLB TYR B 257 UNP P51449 EXPRESSION TAG
SEQADV 4WLB PHE B 258 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLN B 259 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY B 260 UNP P51449 EXPRESSION TAG
SEQADV 4WLB SER B 261 UNP P51449 EXPRESSION TAG
SEQADV 4WLB GLY B 508 UNP P51449 EXPRESSION TAG
SEQADV 4WLB ASN B 509 UNP P51449 EXPRESSION TAG
SEQADV 4WLB SER B 510 UNP P51449 EXPRESSION TAG
SEQRES 1 A 265 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 A 265 GLN GLY SER ALA PRO TYR ALA SER LEU THR GLU ILE GLU
SEQRES 3 A 265 HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG GLU THR
SEQRES 4 A 265 CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN ARG SER
SEQRES 5 A 265 ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR GLN ARG
SEQRES 6 A 265 LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA HIS HIS
SEQRES 7 A 265 LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS
SEQRES 8 A 265 ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN ASP GLN
SEQRES 9 A 265 ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL VAL LEU
SEQRES 10 A 265 VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN ARG THR
SEQRES 11 A 265 VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU LEU PHE
SEQRES 12 A 265 ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER ILE PHE
SEQRES 13 A 265 ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE SER GLU
SEQRES 14 A 265 ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU ILE ASN
SEQRES 15 A 265 ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU
SEQRES 16 A 265 GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS
SEQRES 17 A 265 LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA LYS LEU
SEQRES 18 A 265 PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER GLN HIS
SEQRES 19 A 265 VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE
SEQRES 20 A 265 VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU
SEQRES 21 A 265 PHE SER GLY ASN SER
SEQRES 1 B 265 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 B 265 GLN GLY SER ALA PRO TYR ALA SER LEU THR GLU ILE GLU
SEQRES 3 B 265 HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG GLU THR
SEQRES 4 B 265 CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN ARG SER
SEQRES 5 B 265 ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR GLN ARG
SEQRES 6 B 265 LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA HIS HIS
SEQRES 7 B 265 LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS
SEQRES 8 B 265 ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN ASP GLN
SEQRES 9 B 265 ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL VAL LEU
SEQRES 10 B 265 VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN ARG THR
SEQRES 11 B 265 VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU LEU PHE
SEQRES 12 B 265 ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER ILE PHE
SEQRES 13 B 265 ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE SER GLU
SEQRES 14 B 265 ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU ILE ASN
SEQRES 15 B 265 ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU
SEQRES 16 B 265 GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS
SEQRES 17 B 265 LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA LYS LEU
SEQRES 18 B 265 PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER GLN HIS
SEQRES 19 B 265 VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE
SEQRES 20 B 265 VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU
SEQRES 21 B 265 PHE SER GLY ASN SER
SEQRES 1 D 8 SER LEU LEU LYS LYS LEU LEU ASP
SEQRES 1 E 8 SER LEU LEU LYS LYS LEU LEU ASP
HET 3QQ A 601 33
HET TLA A 602 10
HET TLA A 603 10
HET 3QQ B 601 33
HETNAM 3QQ N-(4-FLUOROBENZYL)-N-(2-METHYLPROPYL)-6-{[1-
HETNAM 2 3QQ (METHYLSULFONYL)PIPERIDIN-4-YL]AMINO}PYRIDINE-3-
HETNAM 3 3QQ SULFONAMIDE
HETNAM TLA L(+)-TARTARIC ACID
FORMUL 5 3QQ 2(C22 H31 F N4 O4 S2)
FORMUL 6 TLA 2(C4 H6 O6)
FORMUL 9 HOH *425(H2 O)
HELIX 1 AA1 SER A 266 GLU A 283 1 18
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 SER A 301 ARG A 310 1 10
HELIX 4 AA4 SER A 312 LEU A 338 1 27
HELIX 5 AA5 GLY A 340 LEU A 344 5 5
HELIX 6 AA6 CYS A 345 MET A 365 1 21
HELIX 7 AA7 GLY A 384 GLY A 392 5 9
HELIX 8 AA8 CYS A 393 ALA A 409 1 17
HELIX 9 AA9 SER A 413 ILE A 426 1 14
HELIX 10 AB1 GLU A 435 THR A 457 1 23
HELIX 11 AB2 ARG A 459 LEU A 466 5 8
HELIX 12 AB3 GLY A 470 HIS A 490 1 21
HELIX 13 AB4 HIS A 490 PHE A 498 1 9
HELIX 14 AB5 PRO A 499 SER A 507 1 9
HELIX 15 AB6 SER B 266 GLU B 283 1 18
HELIX 16 AB7 ARG B 288 GLN B 295 1 8
HELIX 17 AB8 ARG B 296 ASN B 298 5 3
HELIX 18 AB9 SER B 301 LYS B 311 1 11
HELIX 19 AC1 SER B 312 LEU B 338 1 27
HELIX 20 AC2 CYS B 345 MET B 365 1 21
HELIX 21 AC3 GLY B 384 GLY B 392 5 9
HELIX 22 AC4 CYS B 393 ALA B 409 1 17
HELIX 23 AC5 SER B 413 ILE B 426 1 14
HELIX 24 AC6 GLU B 435 THR B 457 1 23
HELIX 25 AC7 ARG B 459 LEU B 466 5 8
HELIX 26 AC8 GLY B 470 HIS B 490 1 21
HELIX 27 AC9 HIS B 490 PHE B 498 1 9
HELIX 28 AD1 PRO B 499 SER B 507 1 9
HELIX 29 AD2 LEU D 9 ASP D 15 1 7
HELIX 30 AD3 LEU E 9 ASP E 15 1 7
SHEET 1 AA1 3 TYR A 369 ASN A 370 0
SHEET 2 AA1 3 THR A 375 PHE A 378 -1 O THR A 375 N ASN A 370
SHEET 3 AA1 3 LYS A 381 GLY A 383 -1 O GLY A 383 N VAL A 376
SHEET 1 AA2 3 TYR B 369 ASN B 370 0
SHEET 2 AA2 3 THR B 375 PHE B 378 -1 O THR B 375 N ASN B 370
SHEET 3 AA2 3 LYS B 381 GLY B 383 -1 O LYS B 381 N PHE B 378
SSBOND 1 CYS A 455 CYS B 455 1555 1565 2.09
SITE 1 AC1 17 CYS A 285 GLN A 286 LEU A 287 TRP A 317
SITE 2 AC1 17 CYS A 320 HIS A 323 ARG A 364 MET A 365
SITE 3 AC1 17 ARG A 367 ALA A 368 PHE A 378 PHE A 388
SITE 4 AC1 17 LEU A 396 ILE A 397 ILE A 400 HIS A 479
SITE 5 AC1 17 HOH A 885
SITE 1 AC2 14 ARG A 294 ASN A 298 HOH A 721 HOH A 725
SITE 2 AC2 14 HOH A 741 HOH A 882 HOH A 892 HOH A 912
SITE 3 AC2 14 SER B 301 GLU B 303 GLU B 304 THR B 457
SITE 4 AC2 14 HIS B 458 ARG B 459
SITE 1 AC3 10 ARG A 296 ALA A 371 SER A 408 HIS A 411
SITE 2 AC3 10 HOH A 716 HOH A 737 HOH A 771 ARG B 374
SITE 3 AC3 10 HIS B 405 HOH B 703
SITE 1 AC4 17 CYS B 285 GLN B 286 LEU B 287 TRP B 317
SITE 2 AC4 17 CYS B 320 HIS B 323 ARG B 364 ARG B 367
SITE 3 AC4 17 ALA B 368 PHE B 378 PHE B 388 LEU B 396
SITE 4 AC4 17 ILE B 400 PHE B 401 HIS B 479 HOH B 768
SITE 5 AC4 17 HOH B 794
CRYST1 66.787 86.258 91.854 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 0.014973 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011593 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010887 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
