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10707 lines (10707 loc) · 847 KB
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HEADER APOPTOSIS/APOPTOSIS INHIBITOR 16-DEC-15 5FDR
TITLE MCL-1 COMPLEXED WITH SMALL MOLECULE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL-
COMPND 3 1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN
COMPND 6 EAT/MCL1,MCL1/EAT;
COMPND 7 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: MCL1, BCL2L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MCL-1, INHIBITOR, APOPTOSIS-APOPTOSIS INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ZHAO
REVDAT 5 27-SEP-23 5FDR 1 REMARK
REVDAT 4 04-DEC-19 5FDR 1 REMARK
REVDAT 3 20-SEP-17 5FDR 1 JRNL REMARK
REVDAT 2 23-MAR-16 5FDR 1 JRNL
REVDAT 1 02-MAR-16 5FDR 0
JRNL AUTH N.F.PELZ,Z.BIAN,B.ZHAO,S.SHAW,J.C.TARR,J.BELMAR,C.GREGG,
JRNL AUTH 2 D.V.CAMPER,C.M.GOODWIN,A.L.ARNOLD,J.L.SENSINTAFFAR,
JRNL AUTH 3 A.FRIBERG,O.W.ROSSANESE,T.LEE,E.T.OLEJNICZAK,S.W.FESIK
JRNL TITL DISCOVERY OF 2-INDOLE-ACYLSULFONAMIDE MYELOID CELL LEUKEMIA
JRNL TITL 2 1 (MCL-1) INHIBITORS USING FRAGMENT-BASED METHODS.
JRNL REF J.MED.CHEM. V. 59 2054 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26878343
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01660
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.490
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 22089
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1079
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 28.7530 - 5.1911 0.98 2747 158 0.2355 0.2899
REMARK 3 2 5.1911 - 4.1242 0.98 2735 139 0.2100 0.2491
REMARK 3 3 4.1242 - 3.6040 0.99 2719 152 0.2061 0.2676
REMARK 3 4 3.6040 - 3.2750 0.98 2669 144 0.2228 0.2915
REMARK 3 5 3.2750 - 3.0405 0.95 2644 133 0.2299 0.2987
REMARK 3 6 3.0405 - 2.8615 0.92 2524 123 0.2432 0.3269
REMARK 3 7 2.8615 - 2.7183 0.91 2527 109 0.2413 0.3027
REMARK 3 8 2.7183 - 2.6000 0.88 2445 121 0.2272 0.3141
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.120
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 : 0.010 5027
REMARK 3 ANGLE : 1.326 6791
REMARK 3 CHIRALITY : 0.070 729
REMARK 3 PLANARITY : 0.009 857
REMARK 3 DIHEDRAL : 19.742 3009
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5063 3.6874 5.0344
REMARK 3 T TENSOR
REMARK 3 T11: 0.2610 T22: 0.2361
REMARK 3 T33: 0.2239 T12: 0.0268
REMARK 3 T13: -0.1508 T23: -0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 2.3953 L22: 3.9194
REMARK 3 L33: 2.3393 L12: -0.3004
REMARK 3 L13: -1.2634 L23: -0.2063
REMARK 3 S TENSOR
REMARK 3 S11: 0.2079 S12: 0.4874 S13: -0.2058
REMARK 3 S21: -0.3739 S22: -0.0814 S23: -0.1273
REMARK 3 S31: -0.2234 S32: -0.2318 S33: -0.2608
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6233 11.3093 19.2484
REMARK 3 T TENSOR
REMARK 3 T11: 0.4774 T22: 0.1709
REMARK 3 T33: 0.2519 T12: 0.0227
REMARK 3 T13: -0.0701 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 6.3397 L22: 0.1843
REMARK 3 L33: 2.5110 L12: 0.1706
REMARK 3 L13: -1.2504 L23: 0.1359
REMARK 3 S TENSOR
REMARK 3 S11: -0.2157 S12: -0.2678 S13: 0.6928
REMARK 3 S21: -0.3370 S22: 0.1878 S23: -0.2402
REMARK 3 S31: -0.4524 S32: 0.4802 S33: 0.2077
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0040 3.5408 8.4730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2156 T22: 0.1858
REMARK 3 T33: 0.1000 T12: -0.0577
REMARK 3 T13: -0.0356 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 3.1204 L22: 3.4579
REMARK 3 L33: 1.8448 L12: -0.1836
REMARK 3 L13: -1.2807 L23: 0.9981
REMARK 3 S TENSOR
REMARK 3 S11: -0.0732 S12: -0.0602 S13: -0.1414
REMARK 3 S21: -0.3340 S22: 0.2292 S23: -0.0724
REMARK 3 S31: -0.0544 S32: 0.1064 S33: -0.1058
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8842 -32.2008 7.6419
REMARK 3 T TENSOR
REMARK 3 T11: 0.4858 T22: 0.1784
REMARK 3 T33: 0.4834 T12: 0.0322
REMARK 3 T13: -0.0051 T23: -0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 1.5893 L22: 3.1631
REMARK 3 L33: 4.5911 L12: -2.2389
REMARK 3 L13: 0.9344 L23: -0.9627
REMARK 3 S TENSOR
REMARK 3 S11: 0.4995 S12: 0.1297 S13: -0.7549
REMARK 3 S21: 0.1481 S22: 0.0089 S23: -0.2920
REMARK 3 S31: 1.1661 S32: 0.1327 S33: -0.2674
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6495 -28.2816 1.7751
REMARK 3 T TENSOR
REMARK 3 T11: 0.3953 T22: 0.0489
REMARK 3 T33: 0.5290 T12: -0.0093
REMARK 3 T13: 0.0257 T23: -0.2750
REMARK 3 L TENSOR
REMARK 3 L11: 0.1191 L22: 2.4226
REMARK 3 L33: 2.6130 L12: -0.3188
REMARK 3 L13: 0.1163 L23: 1.0576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0700 S12: 0.2010 S13: -0.1120
REMARK 3 S21: -0.0525 S22: -0.0514 S23: -0.4193
REMARK 3 S31: 0.2919 S32: 0.6816 S33: -0.3349
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 224 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7374 -19.9866 22.1007
REMARK 3 T TENSOR
REMARK 3 T11: 0.1776 T22: 0.1908
REMARK 3 T33: 0.3426 T12: 0.0106
REMARK 3 T13: -0.0075 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 4.5215 L22: 4.5162
REMARK 3 L33: 6.7120 L12: 0.8319
REMARK 3 L13: -0.3749 L23: -0.7309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1485 S12: -0.5399 S13: -0.1321
REMARK 3 S21: 0.3186 S22: -0.5603 S23: -0.3416
REMARK 3 S31: -0.3808 S32: 0.0742 S33: 0.2354
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8768 -23.3285 9.0144
REMARK 3 T TENSOR
REMARK 3 T11: 0.2818 T22: 0.1419
REMARK 3 T33: 0.4717 T12: 0.0497
REMARK 3 T13: 0.0172 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 2.3311 L22: 3.6516
REMARK 3 L33: 4.6876 L12: 0.3820
REMARK 3 L13: 1.0279 L23: 0.1815
REMARK 3 S TENSOR
REMARK 3 S11: -0.1464 S12: 0.0302 S13: 0.1559
REMARK 3 S21: 0.1799 S22: -0.0912 S23: 0.4581
REMARK 3 S31: 0.0065 S32: -0.3139 S33: 0.2009
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 172 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2399 -11.2852 46.4263
REMARK 3 T TENSOR
REMARK 3 T11: 0.4153 T22: 0.2387
REMARK 3 T33: 0.2003 T12: -0.0225
REMARK 3 T13: 0.0173 T23: 0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 6.5438 L22: 5.7967
REMARK 3 L33: 5.9723 L12: -0.1181
REMARK 3 L13: 0.7993 L23: -0.5282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: -1.2424 S13: -0.2179
REMARK 3 S21: 0.7528 S22: 0.0023 S23: 0.4498
REMARK 3 S31: -0.0053 S32: 0.1950 S33: -0.0337
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 204 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9075 -4.9765 36.8288
REMARK 3 T TENSOR
REMARK 3 T11: 0.1969 T22: 0.2052
REMARK 3 T33: 0.3400 T12: 0.0250
REMARK 3 T13: 0.1011 T23: -0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 3.9029 L22: 2.5481
REMARK 3 L33: 2.5689 L12: 0.7396
REMARK 3 L13: 1.7063 L23: -0.1246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0776 S12: -0.0837 S13: 0.4220
REMARK 3 S21: 0.1917 S22: -0.2269 S23: 0.4846
REMARK 3 S31: -0.0675 S32: -0.2912 S33: 0.2856
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 240 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1281 -13.2620 28.9909
REMARK 3 T TENSOR
REMARK 3 T11: 0.3841 T22: 0.2903
REMARK 3 T33: 0.2113 T12: 0.0110
REMARK 3 T13: 0.1771 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 2.6322 L22: 1.7904
REMARK 3 L33: 2.9166 L12: -1.2209
REMARK 3 L13: 0.7340 L23: 0.3899
REMARK 3 S TENSOR
REMARK 3 S11: 0.0932 S12: 0.4298 S13: -0.2599
REMARK 3 S21: -0.7395 S22: 0.6096 S23: -0.0444
REMARK 3 S31: 0.2516 S32: 0.0774 S33: -0.2892
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 261 THROUGH 283 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7335 -9.8246 35.9616
REMARK 3 T TENSOR
REMARK 3 T11: 0.3206 T22: 0.2356
REMARK 3 T33: -0.1240 T12: 0.0291
REMARK 3 T13: 0.0679 T23: -0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 7.5642 L22: 2.8063
REMARK 3 L33: 0.9911 L12: 2.1741
REMARK 3 L13: 0.8507 L23: 1.2407
REMARK 3 S TENSOR
REMARK 3 S11: -0.0588 S12: -0.2114 S13: -0.5736
REMARK 3 S21: -0.0197 S22: -0.3574 S23: 0.1376
REMARK 3 S31: -0.1932 S32: -0.1579 S33: 0.1859
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 284 THROUGH 308 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8234 -12.2466 38.5153
REMARK 3 T TENSOR
REMARK 3 T11: 0.2487 T22: 0.2224
REMARK 3 T33: 0.3003 T12: 0.0989
REMARK 3 T13: 0.0603 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 7.3241 L22: 8.1864
REMARK 3 L33: 4.4591 L12: 3.5741
REMARK 3 L13: 2.6470 L23: 2.0821
REMARK 3 S TENSOR
REMARK 3 S11: -0.2770 S12: -0.2788 S13: -0.5709
REMARK 3 S21: 0.4854 S22: 0.4548 S23: -0.6806
REMARK 3 S31: 0.3581 S32: 0.3172 S33: -0.1662
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 309 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2773 4.3890 45.8402
REMARK 3 T TENSOR
REMARK 3 T11: 0.0292 T22: 0.4233
REMARK 3 T33: 0.0466 T12: 0.2280
REMARK 3 T13: 0.1363 T23: -0.2665
REMARK 3 L TENSOR
REMARK 3 L11: 1.6100 L22: 5.4104
REMARK 3 L33: 2.2574 L12: -1.1421
REMARK 3 L13: -0.6431 L23: 1.2595
REMARK 3 S TENSOR
REMARK 3 S11: 0.0249 S12: -0.4484 S13: 0.0799
REMARK 3 S21: 0.0974 S22: 0.6783 S23: -0.5902
REMARK 3 S31: -0.1347 S32: -0.0448 S33: 0.1071
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 172 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.1948 30.0116 42.1266
REMARK 3 T TENSOR
REMARK 3 T11: 0.5101 T22: 0.2256
REMARK 3 T33: 1.1796 T12: 0.1596
REMARK 3 T13: -0.1588 T23: -0.3073
REMARK 3 L TENSOR
REMARK 3 L11: 1.1845 L22: 1.8422
REMARK 3 L33: 3.7458 L12: 0.0456
REMARK 3 L13: -1.4337 L23: -0.4372
REMARK 3 S TENSOR
REMARK 3 S11: 0.4377 S12: -0.4465 S13: 1.4638
REMARK 3 S21: 0.6207 S22: -0.1383 S23: -0.5164
REMARK 3 S31: -1.1761 S32: -0.2050 S33: -0.1715
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 203 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1724 18.2001 39.4181
REMARK 3 T TENSOR
REMARK 3 T11: 0.2934 T22: 0.1508
REMARK 3 T33: 0.4270 T12: 0.0062
REMARK 3 T13: -0.0105 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 2.2364 L22: 2.8278
REMARK 3 L33: 0.2567 L12: -1.4206
REMARK 3 L13: -0.2659 L23: 0.2300
REMARK 3 S TENSOR
REMARK 3 S11: -0.3519 S12: -0.0301 S13: 0.8107
REMARK 3 S21: 0.1567 S22: 0.1259 S23: -0.5704
REMARK 3 S31: -0.1200 S32: 0.2945 S33: 0.0643
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 236 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9056 19.5096 25.3029
REMARK 3 T TENSOR
REMARK 3 T11: 0.2960 T22: 0.3767
REMARK 3 T33: 0.4003 T12: 0.0381
REMARK 3 T13: -0.0554 T23: -0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 6.2603 L22: 4.7427
REMARK 3 L33: 7.2056 L12: -0.8852
REMARK 3 L13: -0.2941 L23: -2.1145
REMARK 3 S TENSOR
REMARK 3 S11: -0.1183 S12: 1.0258 S13: 0.7048
REMARK 3 S21: -0.7707 S22: -0.3872 S23: -0.2359
REMARK 3 S31: 0.1925 S32: -0.5001 S33: 0.2252
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 255 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0325 19.9783 39.4338
REMARK 3 T TENSOR
REMARK 3 T11: 0.2412 T22: 0.1754
REMARK 3 T33: 0.3604 T12: 0.0059
REMARK 3 T13: 0.0057 T23: -0.1357
REMARK 3 L TENSOR
REMARK 3 L11: 4.1132 L22: 3.2713
REMARK 3 L33: 6.0415 L12: -0.9058
REMARK 3 L13: -0.1770 L23: -0.2284
REMARK 3 S TENSOR
REMARK 3 S11: -0.2483 S12: -0.3663 S13: 0.6889
REMARK 3 S21: -0.0795 S22: 0.0343 S23: -0.0505
REMARK 3 S31: -0.3596 S32: -0.4782 S33: 0.2627
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 5FDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22089
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 4HW2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, BIS-TRIS, MAGNESIUM
REMARK 280 CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 57.50250
REMARK 290 SMTRY3 2 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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 170
REMARK 465 GLY A 326
REMARK 465 GLY A 327
REMARK 465 GLY B 170
REMARK 465 LYS B 197
REMARK 465 PRO B 198
REMARK 465 GLU B 322
REMARK 465 ASP B 323
REMARK 465 LEU B 324
REMARK 465 GLU B 325
REMARK 465 GLY B 326
REMARK 465 GLY B 327
REMARK 465 GLY C 170
REMARK 465 ASP C 171
REMARK 465 ALA C 193
REMARK 465 LYS C 194
REMARK 465 ASP C 195
REMARK 465 THR C 196
REMARK 465 LYS C 197
REMARK 465 PRO C 198
REMARK 465 MET C 199
REMARK 465 GLY C 200
REMARK 465 ARG C 201
REMARK 465 SER C 202
REMARK 465 GLU C 325
REMARK 465 GLY C 326
REMARK 465 GLY C 327
REMARK 465 GLY D 170
REMARK 465 ASP D 171
REMARK 465 LYS D 197
REMARK 465 PRO D 198
REMARK 465 GLU D 322
REMARK 465 ASP D 323
REMARK 465 LEU D 324
REMARK 465 GLU D 325
REMARK 465 GLY D 326
REMARK 465 GLY D 327
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 ASP A 195 CG OD1 OD2
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 LYS B 194 CG CD CE NZ
REMARK 470 ASP B 195 CG OD1 OD2
REMARK 470 THR B 196 OG1 CG2
REMARK 470 SER B 202 OG
REMARK 470 VAL B 321 CG1 CG2
REMARK 470 LYS D 194 CG CD CE NZ
REMARK 470 ASP D 195 CG OD1 OD2
REMARK 470 THR D 196 OG1 CG2
REMARK 470 VAL D 321 CG1 CG2
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 LEU A 179 OG SER A 183 2.06
REMARK 500 NH2 ARG A 310 OE2 GLU A 317 2.10
REMARK 500 O LEU A 235 NH1 ARG D 248 2.13
REMARK 500 NH2 ARG A 176 O ARG A 201 2.14
REMARK 500 NH1 ARG B 176 OE1 GLU B 180 2.14
REMARK 500 O LEU D 179 OG SER D 183 2.17
REMARK 500 NH2 ARG B 215 O PHE B 319 2.18
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 OE1 GLU A 292 NH2 ARG B 207 2755 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 292 CD GLU B 292 OE1 -0.087
REMARK 500 GLU B 292 CD GLU B 292 OE2 -0.084
REMARK 500 VAL C 321 CB VAL C 321 CG1 -0.131
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 201 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
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 ASP A 195 70.90 -64.57
REMARK 500 LYS A 197 142.15 81.69
REMARK 500 ARG A 201 130.48 65.10
REMARK 500 ASP A 236 72.60 51.97
REMARK 500 HIS A 320 92.97 0.58
REMARK 500 VAL A 321 100.93 -54.23
REMARK 500 ARG B 201 -90.77 85.53
REMARK 500 ALA B 204 -50.56 118.89
REMARK 500 ASP B 236 72.61 51.55
REMARK 500 GLU B 292 -76.11 -31.86
REMARK 500 ASP C 236 71.72 50.62
REMARK 500 HIS C 320 140.69 -6.46
REMARK 500 THR D 191 -167.01 -108.47
REMARK 500 ALA D 193 -154.64 -161.32
REMARK 500 ARG D 201 -118.48 47.74
REMARK 500 SER D 202 42.09 -94.90
REMARK 500 ASP D 236 76.78 51.42
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 5X3 A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5X3 D 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HW2 RELATED DB: PDB
REMARK 900 4HW2 CONTAINS THE SAME PROTEIN
DBREF 5FDR A 172 327 UNP Q07820 MCL1_HUMAN 172 327
DBREF 5FDR B 172 327 UNP Q07820 MCL1_HUMAN 172 327
DBREF 5FDR C 172 327 UNP Q07820 MCL1_HUMAN 172 327
DBREF 5FDR D 172 327 UNP Q07820 MCL1_HUMAN 172 327
SEQADV 5FDR GLY A 170 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR ASP A 171 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR GLY B 170 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR ASP B 171 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR GLY C 170 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR ASP C 171 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR GLY D 170 UNP Q07820 EXPRESSION TAG
SEQADV 5FDR ASP D 171 UNP Q07820 EXPRESSION TAG
SEQRES 1 A 158 GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE
SEQRES 2 A 158 SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP
SEQRES 3 A 158 THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS
SEQRES 4 A 158 ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN
SEQRES 5 A 158 ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS
SEQRES 6 A 158 LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER
SEQRES 7 A 158 ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN
SEQRES 8 A 158 TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE
SEQRES 9 A 158 VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS
SEQRES 10 A 158 ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL
SEQRES 11 A 158 ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP
SEQRES 12 A 158 ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU
SEQRES 13 A 158 GLY GLY
SEQRES 1 B 158 GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE
SEQRES 2 B 158 SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP
SEQRES 3 B 158 THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS
SEQRES 4 B 158 ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN
SEQRES 5 B 158 ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS
SEQRES 6 B 158 LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER
SEQRES 7 B 158 ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN
SEQRES 8 B 158 TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE
SEQRES 9 B 158 VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS
SEQRES 10 B 158 ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL
SEQRES 11 B 158 ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP
SEQRES 12 B 158 ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU
SEQRES 13 B 158 GLY GLY
SEQRES 1 C 158 GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE
SEQRES 2 C 158 SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP
SEQRES 3 C 158 THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS
SEQRES 4 C 158 ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN
SEQRES 5 C 158 ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS
SEQRES 6 C 158 LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER
SEQRES 7 C 158 ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN
SEQRES 8 C 158 TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE
SEQRES 9 C 158 VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS
SEQRES 10 C 158 ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL
SEQRES 11 C 158 ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP
SEQRES 12 C 158 ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU
SEQRES 13 C 158 GLY GLY
SEQRES 1 D 158 GLY ASP ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE
SEQRES 2 D 158 SER ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP
SEQRES 3 D 158 THR LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS
SEQRES 4 D 158 ALA LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN
SEQRES 5 D 158 ARG ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS
SEQRES 6 D 158 LEU ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER
SEQRES 7 D 158 ARG VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN
SEQRES 8 D 158 TRP GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE
SEQRES 9 D 158 VAL ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS
SEQRES 10 D 158 ILE GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL
SEQRES 11 D 158 ARG THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP
SEQRES 12 D 158 ASP GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU
SEQRES 13 D 158 GLY GLY
HET 5X3 A 400 44
HET 5X3 B 400 44
HET 5X3 C 400 44
HET 5X3 D 400 44
HETNAM 5X3 5-[[6-CHLORANYL-3-[3-(4-CHLORANYL-3,5-DIMETHYL-
HETNAM 2 5X3 PHENOXY)PROPYL]-7-(3,5-DIMETHYL-1~{H}-PYRAZOL-4-YL)-
HETNAM 3 5X3 1~{H}-INDOL-2-YL]CARBONYLSULFAMOYL]FURAN-2-CARBOXYLIC
HETNAM 4 5X3 ACID
FORMUL 5 5X3 4(C30 H28 CL2 N4 O7 S)
HELIX 1 AA1 GLU A 173 GLY A 192 1 20
HELIX 2 AA2 GLY A 203 HIS A 224 1 22
HELIX 3 AA3 HIS A 224 ASP A 236 1 13
HELIX 4 AA4 ASN A 239 SER A 255 1 17
HELIX 5 AA5 ASN A 260 ILE A 281 1 22
HELIX 6 AA6 GLN A 283 SER A 285 5 3
HELIX 7 AA7 CYS A 286 GLN A 309 1 24
HELIX 8 AA8 ARG A 310 HIS A 320 1 11
HELIX 9 AA9 ASP B 172 GLY B 192 1 21
HELIX 10 AB1 ALA B 204 HIS B 224 1 21
HELIX 11 AB2 HIS B 224 ASP B 236 1 13
HELIX 12 AB3 ASN B 239 SER B 245 1 7
HELIX 13 AB4 LEU B 246 SER B 255 1 10
HELIX 14 AB5 ASN B 260 ILE B 281 1 22
HELIX 15 AB6 GLN B 283 SER B 285 5 3
HELIX 16 AB7 CYS B 286 GLN B 309 1 24
HELIX 17 AB8 ARG B 310 PHE B 319 1 10
HELIX 18 AB9 GLU C 173 THR C 191 1 19
HELIX 19 AC1 ALA C 204 HIS C 224 1 21
HELIX 20 AC2 HIS C 224 ASP C 236 1 13
HELIX 21 AC3 ASN C 239 SER C 255 1 17
HELIX 22 AC4 ASN C 260 ILE C 281 1 22
HELIX 23 AC5 GLN C 283 SER C 285 5 3
HELIX 24 AC6 CYS C 286 GLN C 309 1 24
HELIX 25 AC7 ARG C 310 HIS C 320 1 11
HELIX 26 AC8 GLU D 173 THR D 191 1 19
HELIX 27 AC9 SER D 202 HIS D 224 1 23
HELIX 28 AD1 HIS D 224 ASP D 236 1 13
HELIX 29 AD2 ASN D 239 LEU D 246 1 8
HELIX 30 AD3 LEU D 246 SER D 255 1 10
HELIX 31 AD4 ASN D 260 ILE D 281 1 22
HELIX 32 AD5 GLN D 283 SER D 285 5 3
HELIX 33 AD6 CYS D 286 GLN D 309 1 24
HELIX 34 AD7 ARG D 310 HIS D 320 1 11
CISPEP 1 ARG A 201 SER A 202 0 -3.86
SITE 1 AC1 16 HIS A 224 ALA A 227 PHE A 228 MET A 231
SITE 2 AC1 16 MET A 250 VAL A 253 ASN A 260 GLY A 262
SITE 3 AC1 16 ARG A 263 THR A 266 LEU A 267 PHE A 270
SITE 4 AC1 16 GLY A 271 THR B 226 ASP C 256 GLY C 257
SITE 1 AC2 14 GLY A 219 ARG A 222 ASN A 223 ALA B 227
SITE 2 AC2 14 PHE B 228 MET B 231 VAL B 249 MET B 250
SITE 3 AC2 14 VAL B 253 ASP B 256 GLY B 257 ARG B 263
SITE 4 AC2 14 LEU B 267 PHE B 270
SITE 1 AC3 15 ASP A 256 GLY A 257 HIS C 224 ALA C 227
SITE 2 AC3 15 PHE C 228 MET C 231 MET C 250 VAL C 253
SITE 3 AC3 15 ASN C 260 GLY C 262 ARG C 263 THR C 266
SITE 4 AC3 15 LEU C 267 PHE C 270 THR D 226
SITE 1 AC4 16 GLY C 219 ARG C 222 ASN C 223 ALA D 227
SITE 2 AC4 16 PHE D 228 MET D 231 MET D 250 VAL D 253
SITE 3 AC4 16 PHE D 254 ASP D 256 GLY D 257 ARG D 263
SITE 4 AC4 16 THR D 266 LEU D 267 PHE D 270 ILE D 294
CRYST1 35.040 115.005 95.327 90.00 91.17 90.00 P 1 21 1 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 0.028539 0.000000 0.000581 0.00000
SCALE2 0.000000 0.008695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010492 0.00000
ATOM 1 N ASP A 171 54.865 8.760 2.964 1.00 58.92 N
ANISOU 1 N ASP A 171 6088 6132 10168 -807 623 -421 N
ATOM 2 CA ASP A 171 53.489 9.119 3.313 1.00 64.59 C
ANISOU 2 CA ASP A 171 7112 6907 10523 -764 451 -414 C
ATOM 3 C ASP A 171 52.990 10.403 2.671 1.00 75.03 C
ANISOU 3 C ASP A 171 8717 8156 11634 -767 685 -354 C
ATOM 4 O ASP A 171 51.876 10.820 2.954 1.00 77.41 O
ANISOU 4 O ASP A 171 9257 8493 11662 -726 566 -335 O
ATOM 5 CB ASP A 171 53.306 9.296 4.821 1.00 61.85 C
ANISOU 5 CB ASP A 171 6697 6584 10220 -892 91 -440 C
ATOM 6 CG ASP A 171 54.056 8.333 5.617 1.00 58.25 C
ANISOU 6 CG ASP A 171 5932 6173 10027 -927 -142 -471 C
ATOM 7 OD1 ASP A 171 54.105 7.193 5.220 1.00 62.11 O
ANISOU 7 OD1 ASP A 171 6341 6710 10546 -793 -129 -479 O
ATOM 8 OD2 ASP A 171 54.607 8.736 6.634 1.00 51.39 O
ANISOU 8 OD2 ASP A 171 4906 5286 9332 -1088 -337 -489 O
ATOM 9 N ASP A 172 53.795 11.067 1.843 1.00 77.49 N
ANISOU 9 N ASP A 172 9005 8356 12082 -810 1031 -311 N
ATOM 10 CA ASP A 172 53.161 12.040 0.964 1.00 78.84 C
ANISOU 10 CA ASP A 172 9502 8471 11981 -736 1287 -229 C
ATOM 11 C ASP A 172 52.241 11.352 -0.038 1.00 65.88 C
ANISOU 11 C ASP A 172 8095 6948 9988 -505 1339 -215 C
ATOM 12 O ASP A 172 51.549 12.037 -0.805 1.00 72.32 O
ANISOU 12 O ASP A 172 9204 7756 10517 -401 1503 -135 O
ATOM 13 CB ASP A 172 54.220 12.891 0.254 1.00 86.75 C
ANISOU 13 CB ASP A 172 10450 9311 13201 -828 1683 -172 C
ATOM 14 CG ASP A 172 55.020 13.746 1.222 1.00 92.01 C
ANISOU 14 CG ASP A 172 10910 9849 14199 -1084 1627 -200 C
ATOM 15 OD1 ASP A 172 55.485 14.835 0.819 1.00 88.75 O
ANISOU 15 OD1 ASP A 172 10555 9274 13892 -1184 1927 -143 O
ATOM 16 OD2 ASP A 172 55.177 13.330 2.389 1.00 92.83 O
ANISOU 16 OD2 ASP A 172 10807 10014 14452 -1189 1281 -279 O
ATOM 17 N GLU A 173 52.237 10.019 -0.035 1.00 52.73 N
ANISOU 17 N GLU A 173 6305 5387 8343 -426 1196 -292 N
ATOM 18 CA GLU A 173 51.288 9.177 -0.742 1.00 45.66 C
ANISOU 18 CA GLU A 173 5599 4617 7132 -241 1150 -323 C
ATOM 19 C GLU A 173 50.541 8.179 0.137 1.00 33.56 C
ANISOU 19 C GLU A 173 4001 3197 5554 -217 779 -399 C
ATOM 20 O GLU A 173 49.400 7.845 -0.176 1.00 32.29 O
ANISOU 20 O GLU A 173 4034 3140 5094 -100 672 -416 O
ATOM 21 CB GLU A 173 52.021 8.391 -1.838 1.00 43.35 C
ANISOU 21 CB GLU A 173 5258 4312 6899 -153 1418 -361 C
ATOM 22 CG GLU A 173 51.111 7.594 -2.754 1.00 57.79 C
ANISOU 22 CG GLU A 173 7320 6260 8376 26 1411 -415 C
ATOM 23 CD GLU A 173 50.290 8.470 -3.684 1.00 61.73 C
ANISOU 23 CD GLU A 173 8168 6798 8487 133 1550 -332 C
ATOM 24 OE1 GLU A 173 50.847 9.455 -4.225 1.00 58.88 O
ANISOU 24 OE1 GLU A 173 7890 6333 8149 114 1853 -232 O
ATOM 25 OE2 GLU A 173 49.076 8.187 -3.845 1.00 56.16 O
ANISOU 25 OE2 GLU A 173 7646 6225 7468 236 1352 -357 O
ATOM 26 N LEU A 174 51.110 7.747 1.260 1.00 33.15 N
ANISOU 26 N LEU A 174 3687 3126 5784 -327 572 -435 N
ATOM 27 CA LEU A 174 50.362 6.856 2.130 1.00 31.10 C
ANISOU 27 CA LEU A 174 3397 2955 5466 -301 244 -484 C
ATOM 28 C LEU A 174 49.291 7.613 2.916 1.00 48.56 C
ANISOU 28 C LEU A 174 5775 5198 7479 -334 50 -449 C
ATOM 29 O LEU A 174 48.198 7.082 3.157 1.00 27.70 O
ANISOU 29 O LEU A 174 3236 2644 4645 -259 -132 -471 O
ATOM 30 CB LEU A 174 51.328 6.125 3.051 1.00 31.58 C
ANISOU 30 CB LEU A 174 3142 2989 5869 -383 89 -512 C
ATOM 31 CG LEU A 174 50.603 5.270 4.072 1.00 34.72 C
ANISOU 31 CG LEU A 174 3520 3457 6214 -362 -239 -540 C
ATOM 32 CD1 LEU A 174 49.981 4.111 3.314 1.00 29.15 C
ANISOU 32 CD1 LEU A 174 2903 2805 5366 -214 -205 -600 C
ATOM 33 CD2 LEU A 174 51.556 4.767 5.120 1.00 43.03 C
ANISOU 33 CD2 LEU A 174 4283 4485 7582 -443 -422 -535 C
ATOM 34 N TYR A 175 49.585 8.857 3.325 1.00 43.72 N
ANISOU 34 N TYR A 175 5187 4498 6925 -452 103 -398 N
ATOM 35 CA TYR A 175 48.544 9.715 3.882 1.00 28.76 C
ANISOU 35 CA TYR A 175 3496 2607 4824 -461 -3 -359 C
ATOM 36 C TYR A 175 47.468 10.019 2.858 1.00 33.27 C
ANISOU 36 C TYR A 175 4331 3236 5074 -298 121 -307 C
ATOM 37 O TYR A 175 46.279 10.014 3.179 1.00 43.95 O
ANISOU 37 O TYR A 175 5814 4661 6223 -227 -34 -295 O
ATOM 38 CB TYR A 175 49.148 11.023 4.387 1.00 29.98 C
ANISOU 38 CB TYR A 175 3649 2628 5116 -623 79 -329 C
ATOM 39 CG TYR A 175 48.121 12.040 4.867 1.00 29.12 C
ANISOU 39 CG TYR A 175 3779 2487 4801 -621 35 -285 C
ATOM 40 CD1 TYR A 175 47.632 11.998 6.171 1.00 27.91 C
ANISOU 40 CD1 TYR A 175 3629 2350 4624 -687 -227 -321 C
ATOM 41 CD2 TYR A 175 47.659 13.057 4.025 1.00 29.82 C
ANISOU 41 CD2 TYR A 175 4098 2515 4718 -542 276 -197 C
ATOM 42 CE1 TYR A 175 46.709 12.908 6.630 1.00 27.35 C
ANISOU 42 CE1 TYR A 175 3775 2233 4382 -677 -238 -285 C
ATOM 43 CE2 TYR A 175 46.736 14.003 4.482 1.00 43.86 C
ANISOU 43 CE2 TYR A 175 6086 4244 6335 -524 256 -146 C
ATOM 44 CZ TYR A 175 46.263 13.929 5.791 1.00 49.13 C
ANISOU 44 CZ TYR A 175 6744 4924 7000 -594 5 -198 C
ATOM 45 OH TYR A 175 45.343 14.857 6.261 1.00 30.24 O
ANISOU 45 OH TYR A 175 4563 2468 4459 -567 13 -153 O
ATOM 46 N ARG A 176 47.859 10.304 1.621 1.00 35.77 N
ANISOU 46 N ARG A 176 4729 3525 5338 -232 402 -269 N
ATOM 47 CA ARG A 176 46.862 10.715 0.646 1.00 32.55 C
ANISOU 47 CA ARG A 176 4588 3179 4599 -69 504 -201 C
ATOM 48 C ARG A 176 45.985 9.532 0.248 1.00 30.71 C
ANISOU 48 C ARG A 176 4388 3107 4173 62 341 -270 C
ATOM 49 O ARG A 176 44.769 9.671 0.099 1.00 29.94 O
ANISOU 49 O ARG A 176 4446 3105 3824 168 231 -240 O
ATOM 50 CB ARG A 176 47.554 11.351 -0.564 1.00 34.11 C
ANISOU 50 CB ARG A 176 4893 3299 4770 -30 863 -130 C
ATOM 51 CG ARG A 176 46.613 11.739 -1.705 1.00 47.96 C
ANISOU 51 CG ARG A 176 6941 5131 6151 162 973 -43 C
ATOM 52 CD ARG A 176 47.232 11.417 -3.076 1.00 53.71 C
ANISOU 52 CD ARG A 176 7748 5865 6793 249 1255 -41 C
ATOM 53 NE ARG A 176 47.339 9.971 -3.262 1.00 57.55 N
ANISOU 53 NE ARG A 176 8113 6452 7302 276 1141 -181 N
ATOM 54 CZ ARG A 176 46.467 9.207 -3.921 1.00 62.27 C
ANISOU 54 CZ ARG A 176 8841 7203 7616 411 1025 -242 C
ATOM 55 NH1 ARG A 176 45.400 9.738 -4.514 1.00 67.20 N
ANISOU 55 NH1 ARG A 176 9711 7927 7896 548 987 -163 N
ATOM 56 NH2 ARG A 176 46.687 7.894 -3.987 1.00 54.12 N
ANISOU 56 NH2 ARG A 176 7684 6218 6660 407 945 -384 N
ATOM 57 N GLN A 177 46.581 8.356 0.073 1.00 29.20 N
ANISOU 57 N GLN A 177 4041 2940 4114 54 326 -367 N
ATOM 58 CA GLN A 177 45.785 7.192 -0.275 1.00 30.90 C
ANISOU 58 CA GLN A 177 4288 3282 4172 153 179 -456 C
ATOM 59 C GLN A 177 44.930 6.755 0.907 1.00 34.11 C
ANISOU 59 C GLN A 177 4622 3738 4599 116 -128 -485 C
ATOM 60 O GLN A 177 43.729 6.487 0.744 1.00 37.36 O
ANISOU 60 O GLN A 177 5138 4260 4799 199 -265 -503 O
ATOM 61 CB GLN A 177 46.707 6.088 -0.762 1.00 29.51 C
ANISOU 61 CB GLN A 177 3978 3080 4153 155 285 -552 C
ATOM 62 CG GLN A 177 46.090 4.730 -0.845 1.00 38.95 C
ANISOU 62 CG GLN A 177 5155 4360 5283 211 120 -673 C
ATOM 63 CD GLN A 177 47.057 3.704 -1.451 1.00 44.19 C
ANISOU 63 CD GLN A 177 5718 4969 6103 231 286 -766 C
ATOM 64 OE1 GLN A 177 47.980 3.227 -0.778 1.00 43.10 O
ANISOU 64 OE1 GLN A 177 5348 4745 6282 164 276 -776 O
ATOM 65 NE2 GLN A 177 46.833 3.355 -2.724 1.00 45.43 N
ANISOU 65 NE2 GLN A 177 6056 5178 6028 332 434 -836 N
ATOM 66 N SER A 178 45.495 6.788 2.119 1.00 25.70 N
ANISOU 66 N SER A 178 3391 2598 3778 -8 -237 -480 N
ATOM 67 CA SER A 178 44.687 6.453 3.283 1.00 23.98 C
ANISOU 67 CA SER A 178 3139 2415 3557 -39 -498 -491 C
ATOM 68 C SER A 178 43.500 7.388 3.387 1.00 35.25 C
ANISOU 68 C SER A 178 4751 3883 4760 13 -537 -421 C
ATOM 69 O SER A 178 42.350 6.938 3.445 1.00 35.58 O
ANISOU 69 O SER A 178 4841 4018 4658 84 -675 -439 O
ATOM 70 CB SER A 178 45.523 6.531 4.564 1.00 23.82 C
ANISOU 70 CB SER A 178 2951 2311 3789 -178 -607 -483 C
ATOM 71 OG SER A 178 46.740 5.819 4.445 1.00 24.90 O
ANISOU 71 OG SER A 178 2888 2403 4169 -215 -554 -522 O
ATOM 72 N LEU A 179 43.756 8.685 3.235 1.00 30.22 N
ANISOU 72 N LEU A 179 4218 3172 4095 -7 -382 -338 N
ATOM 73 CA LEU A 179 42.711 9.691 3.303 1.00 23.80 C
ANISOU 73 CA LEU A 179 3583 2368 3090 60 -379 -251 C
ATOM 74 C LEU A 179 41.672 9.471 2.221 1.00 35.38 C
ANISOU 74 C LEU A 179 5175 3971 4295 231 -377 -233 C
ATOM 75 O LEU A 179 40.484 9.737 2.418 1.00 23.47 O
ANISOU 75 O LEU A 179 3746 2530 2643 312 -480 -188 O
ATOM 76 CB LEU A 179 43.336 11.069 3.134 1.00 25.10 C
ANISOU 76 CB LEU A 179 3847 2399 3292 13 -160 -166 C
ATOM 77 CG LEU A 179 42.278 12.163 3.168 1.00 28.62 C
ANISOU 77 CG LEU A 179 4492 2830 3552 105 -124 -61 C
ATOM 78 CD1 LEU A 179 41.559 12.129 4.498 1.00 23.68 C
ANISOU 78 CD1 LEU A 179 3843 2201 2952 57 -323 -83 C
ATOM 79 CD2 LEU A 179 42.828 13.508 2.820 1.00 26.73 C
ANISOU 79 CD2 LEU A 179 4383 2438 3334 78 132 32 C
ATOM 80 N GLU A 180 42.109 9.013 1.056 1.00 37.02 N
ANISOU 80 N GLU A 180 5405 4224 4438 289 -258 -268 N
ATOM 81 CA GLU A 180 41.168 8.754 -0.018 1.00 38.85 C
ANISOU 81 CA GLU A 180 5765 4603 4395 443 -285 -269 C
ATOM 82 C GLU A 180 40.209 7.629 0.374 1.00 28.24 C
ANISOU 82 C GLU A 180 4325 3374 3029 452 -541 -369 C
ATOM 83 O GLU A 180 38.984 7.794 0.328 1.00 24.47 O
ANISOU 83 O GLU A 180 3904 3002 2392 540 -667 -335 O
ATOM 84 CB GLU A 180 41.964 8.442 -1.279 1.00 46.70 C
ANISOU 84 CB GLU A 180 6820 5603 5320 487 -87 -305 C
ATOM 85 CG GLU A 180 41.201 7.862 -2.427 1.00 62.58 C
ANISOU 85 CG GLU A 180 8955 7776 7046 620 -139 -359 C
ATOM 86 CD GLU A 180 42.156 7.285 -3.457 1.00 77.15 C
ANISOU 86 CD GLU A 180 10841 9602 8870 632 62 -438 C
ATOM 87 OE1 GLU A 180 42.369 7.896 -4.524 1.00 84.67 O