HEADER TRANSLATION 13-AUG-19 6U06
TITLE DISCOVERY OF LYSINE-TARGETED EIF4E INHIBITORS THROUGH COVALENT DOCKING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MRNA CAP-BINDING PROTEIN,EIF-4F 25 KDA SUBUNIT;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COVALENT LYSINE INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: EIF4E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CAP-BINDING SITE, ANTI-NEOPLASTIC, INHIBITOR, TRANSLATION INITIATION
KEYWDS 2 BLOCKING, TRANSLATION, TRANSLATION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.B.WAN,B.K.SHOICHET,J.TAUNTON
REVDAT 5 11-OCT-23 6U06 1 REMARK
REVDAT 4 25-MAR-20 6U06 1 JRNL
REVDAT 3 11-MAR-20 6U06 1 JRNL
REVDAT 2 18-DEC-19 6U06 1 REMARK
REVDAT 1 16-OCT-19 6U06 0
JRNL AUTH X.WAN,T.YANG,A.CUESTA,X.PANG,T.E.BALIUS,J.J.IRWIN,
JRNL AUTH 2 B.K.SHOICHET,J.TAUNTON
JRNL TITL DISCOVERY OF LYSINE-TARGETED EIF4E INHIBITORS THROUGH
JRNL TITL 2 COVALENT DOCKING.
JRNL REF J.AM.CHEM.SOC. V. 142 4960 2020
JRNL REFN ESSN 1520-5126
JRNL PMID 32105459
JRNL DOI 10.1021/JACS.9B10377
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX-1.13-2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 55775
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2721
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 73.1320 - 5.2295 0.98 2857 166 0.1807 0.1957
REMARK 3 2 5.2295 - 4.1509 0.95 2729 146 0.1586 0.2078
REMARK 3 3 4.1509 - 3.6262 0.96 2824 154 0.1707 0.2236
REMARK 3 4 3.6262 - 3.2947 0.97 2816 131 0.1919 0.2361
REMARK 3 5 3.2947 - 3.0585 0.96 2766 173 0.2064 0.2441
REMARK 3 6 3.0585 - 2.8782 0.96 2778 157 0.2066 0.2585
REMARK 3 7 2.8782 - 2.7340 0.98 2828 125 0.2138 0.3004
REMARK 3 8 2.7340 - 2.6150 0.96 2826 163 0.2178 0.2798
REMARK 3 9 2.6150 - 2.5143 0.96 2771 137 0.2169 0.2483
REMARK 3 10 2.5143 - 2.4276 0.96 2810 137 0.2093 0.2414
REMARK 3 11 2.4276 - 2.3517 0.95 2769 132 0.2137 0.2898
REMARK 3 12 2.3517 - 2.2844 0.96 2769 140 0.2163 0.2461
REMARK 3 13 2.2844 - 2.2243 0.96 2770 165 0.2191 0.2629
REMARK 3 14 2.2243 - 2.1700 0.94 2791 129 0.2280 0.2914
REMARK 3 15 2.1700 - 2.1207 0.97 2774 127 0.2474 0.2888
REMARK 3 16 2.1207 - 2.0756 0.94 2820 158 0.2468 0.2933
REMARK 3 17 2.0756 - 2.0340 0.96 2764 119 0.2568 0.3289
REMARK 3 18 2.0340 - 1.9956 0.96 2770 133 0.2546 0.3080
REMARK 3 19 1.9956 - 1.9600 0.95 2822 129 0.2669 0.3017
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.47
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 34
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2314 -22.0894 -7.6744
REMARK 3 T TENSOR
REMARK 3 T11: 0.2121 T22: 0.4284
REMARK 3 T33: 0.4169 T12: 0.1423
REMARK 3 T13: -0.0544 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 4.0488 L22: 3.4057
REMARK 3 L33: 7.3255 L12: -0.1914
REMARK 3 L13: 1.2531 L23: -1.1690
REMARK 3 S TENSOR
REMARK 3 S11: 0.4631 S12: -0.3962 S13: -0.3310
REMARK 3 S21: -0.1852 S22: -0.4273 S23: -0.0446
REMARK 3 S31: 1.0318 S32: 0.1849 S33: -0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3079 3.4720 -14.5752
REMARK 3 T TENSOR
REMARK 3 T11: 0.2518 T22: 0.1741
REMARK 3 T33: 0.5651 T12: -0.0528
REMARK 3 T13: -0.0261 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.7999 L22: 2.6271
REMARK 3 L33: 1.5107 L12: -0.8621
REMARK 3 L13: 0.1273 L23: -0.6804
REMARK 3 S TENSOR
REMARK 3 S11: -0.2668 S12: -0.1703 S13: 0.7390
REMARK 3 S21: 0.2767 S22: 0.3494 S23: -0.2029
REMARK 3 S31: -0.4356 S32: 0.3599 S33: -0.0020
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2350 1.3854 -13.7260
REMARK 3 T TENSOR
REMARK 3 T11: 0.4366 T22: 0.3001
REMARK 3 T33: 0.8596 T12: -0.0147
REMARK 3 T13: -0.3037 T23: -0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 0.4355 L22: 5.3943
REMARK 3 L33: 1.5786 L12: -1.1834
REMARK 3 L13: 0.3638 L23: -2.6079
REMARK 3 S TENSOR
REMARK 3 S11: -0.4768 S12: -0.1126 S13: 1.1078
REMARK 3 S21: -0.1658 S22: -0.0422 S23: 0.6516
REMARK 3 S31: -0.6892 S32: -0.1343 S33: 0.0621
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9787 -9.0281 -10.6601
REMARK 3 T TENSOR
REMARK 3 T11: 0.1707 T22: 0.2440
REMARK 3 T33: 0.2441 T12: -0.0042
REMARK 3 T13: -0.0333 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 2.0915 L22: 2.1381
REMARK 3 L33: 2.6099 L12: 0.5913
REMARK 3 L13: 0.8254 L23: -0.5852
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.3629 S13: 0.3802
REMARK 3 S21: 0.1597 S22: -0.0954 S23: -0.1334
REMARK 3 S31: -0.1953 S32: -0.1751 S33: 0.1025
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8279 -1.0662 -26.3133
REMARK 3 T TENSOR
REMARK 3 T11: 0.3394 T22: 0.3995
REMARK 3 T33: 0.4299 T12: -0.1540
REMARK 3 T13: -0.0426 T23: 0.1014
REMARK 3 L TENSOR
REMARK 3 L11: 3.7131 L22: 2.6470
REMARK 3 L33: 5.7662 L12: -0.2900
REMARK 3 L13: 1.9532 L23: -1.1746
REMARK 3 S TENSOR
REMARK 3 S11: -0.2617 S12: 0.7359 S13: 0.7574
REMARK 3 S21: -0.5770 S22: 0.3308 S23: -0.1249
REMARK 3 S31: -0.9366 S32: 0.7605 S33: 0.1469
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8467 -13.2235 -20.9590
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.2474
REMARK 3 T33: 0.2800 T12: -0.0451
REMARK 3 T13: -0.0432 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.4592 L22: 1.6786
REMARK 3 L33: 2.0162 L12: 0.2395
REMARK 3 L13: 0.8317 L23: -0.3983
REMARK 3 S TENSOR
REMARK 3 S11: -0.1892 S12: 0.1126 S13: 0.1386
REMARK 3 S21: -0.2508 S22: 0.1250 S23: 0.2207
REMARK 3 S31: 0.0816 S32: -0.3728 S33: 0.0243
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8975 -8.9951 -26.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.2428 T22: 0.2928
REMARK 3 T33: 0.2674 T12: -0.0613
REMARK 3 T13: -0.0113 T23: 0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 2.5656 L22: 1.7238
REMARK 3 L33: 3.1132 L12: 0.6652
REMARK 3 L13: -1.0222 L23: -0.0701
REMARK 3 S TENSOR
REMARK 3 S11: -0.1984 S12: 0.4876 S13: 0.3711
REMARK 3 S21: -0.3356 S22: 0.1770 S23: -0.2031
REMARK 3 S31: -0.0616 S32: 0.0555 S33: 0.0362
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8466 -19.1367 -31.2012
REMARK 3 T TENSOR
REMARK 3 T11: 0.4204 T22: 0.4387
REMARK 3 T33: 0.3040 T12: -0.1266
REMARK 3 T13: -0.0199 T23: -0.1120
REMARK 3 L TENSOR
REMARK 3 L11: 0.3167 L22: 0.3599
REMARK 3 L33: 2.5985 L12: 0.1196
REMARK 3 L13: -0.8740 L23: -0.3826
REMARK 3 S TENSOR
REMARK 3 S11: -0.1369 S12: 1.0924 S13: -0.5436
REMARK 3 S21: -0.3779 S22: -0.0409 S23: 0.0911
REMARK 3 S31: 0.3541 S32: -0.2024 S33: 0.1412
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5135 -5.9201 -36.1005
REMARK 3 T TENSOR
REMARK 3 T11: 0.5468 T22: 0.6188
REMARK 3 T33: 0.3708 T12: -0.1132
REMARK 3 T13: -0.1271 T23: 0.0676
REMARK 3 L TENSOR
REMARK 3 L11: 4.2733 L22: 0.4406
REMARK 3 L33: 3.0557 L12: 0.7865
REMARK 3 L13: 0.0632 L23: 0.1776
REMARK 3 S TENSOR
REMARK 3 S11: -0.3864 S12: 0.7037 S13: 0.5390
REMARK 3 S21: -0.8135 S22: 0.0496 S23: 0.0585
REMARK 3 S31: -0.5336 S32: -0.7145 S33: 0.1312
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 30 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3257 -38.0987 -69.1534
REMARK 3 T TENSOR
REMARK 3 T11: 0.3821 T22: 0.3063
REMARK 3 T33: 0.4236 T12: 0.0563
REMARK 3 T13: -0.0130 T23: -0.1164
REMARK 3 L TENSOR
REMARK 3 L11: 3.4551 L22: 4.4300
REMARK 3 L33: 6.8617 L12: -0.2483
REMARK 3 L13: -0.6461 L23: 0.7740
REMARK 3 S TENSOR
REMARK 3 S11: -0.3876 S12: 0.0646 S13: -0.0524
REMARK 3 S21: -0.4745 S22: 0.5753 S23: -0.4952
REMARK 3 S31: 0.3281 S32: 1.0461 S33: -0.1692
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2019 -28.7999 -62.2538
REMARK 3 T TENSOR
REMARK 3 T11: 0.2735 T22: 0.3417
REMARK 3 T33: 0.6301 T12: -0.0261
REMARK 3 T13: -0.0779 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 0.5905 L22: 0.4912
REMARK 3 L33: 1.4754 L12: 0.2739
REMARK 3 L13: -0.7179 L23: 0.1920
REMARK 3 S TENSOR
REMARK 3 S11: 0.4098 S12: 0.2528 S13: -0.5460
REMARK 3 S21: -0.1936 S22: -0.3171 S23: 1.0342
REMARK 3 S31: 0.2997 S32: -0.6172 S33: 0.1074
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 56 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9376 -33.3292 -63.2852
REMARK 3 T TENSOR
REMARK 3 T11: 0.2923 T22: 0.2775
REMARK 3 T33: 0.8689 T12: -0.1103
REMARK 3 T13: -0.0694 T23: -0.4767
REMARK 3 L TENSOR
REMARK 3 L11: 9.1661 L22: 0.3082
REMARK 3 L33: 1.5498 L12: -1.2842
REMARK 3 L13: -3.6132 L23: 0.5056
REMARK 3 S TENSOR
REMARK 3 S11: -0.1369 S12: -0.5020 S13: 0.3334
REMARK 3 S21: 0.1727 S22: -0.4355 S23: 1.3635
REMARK 3 S31: -0.1202 S32: -0.7286 S33: 0.1615
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1028 -25.8314 -66.2136
REMARK 3 T TENSOR
REMARK 3 T11: 0.2325 T22: 0.1847
REMARK 3 T33: 0.2463 T12: 0.0185
REMARK 3 T13: 0.0026 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 2.2098 L22: 2.0348
REMARK 3 L33: 3.0705 L12: 0.3509
REMARK 3 L13: -0.5066 L23: 0.1063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: 0.1754 S13: -0.0248
REMARK 3 S21: 0.0054 S22: -0.0154 S23: 0.1198
REMARK 3 S31: -0.0942 S32: -0.2492 S33: 0.1068
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2129 -37.1388 -50.4871
REMARK 3 T TENSOR
REMARK 3 T11: 0.5262 T22: 0.1917
REMARK 3 T33: 0.3420 T12: -0.0742
REMARK 3 T13: 0.0792 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.4482 L22: 1.1805
REMARK 3 L33: 5.4109 L12: 0.4584
REMARK 3 L13: -2.1646 L23: 1.0707
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: 0.0237 S13: -0.2554
REMARK 3 S21: 0.7236 S22: -0.0059 S23: 0.1474
REMARK 3 S31: 0.6004 S32: -0.1972 S33: 0.1055
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7310 -13.8716 -53.7549
REMARK 3 T TENSOR
REMARK 3 T11: 0.4669 T22: 0.1721
REMARK 3 T33: 0.3769 T12: 0.0093
REMARK 3 T13: -0.0250 T23: -0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 0.6800 L22: 1.1981
REMARK 3 L33: 1.0958 L12: -0.8082
REMARK 3 L13: -0.0649 L23: -0.4399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: -0.1269 S13: 0.2511
REMARK 3 S21: 0.0724 S22: -0.0388 S23: 0.2019
REMARK 3 S31: -0.1908 S32: -0.1698 S33: -0.0439
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 126 THROUGH 156 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3971 -26.5699 -55.2292
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.1884
REMARK 3 T33: 0.3055 T12: -0.0072
REMARK 3 T13: -0.0248 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.4178 L22: 1.2959
REMARK 3 L33: 2.2459 L12: -0.2909
REMARK 3 L13: -0.0800 L23: 0.3619
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: -0.2492 S13: -0.0038
REMARK 3 S21: 0.1640 S22: 0.1336 S23: -0.0622
REMARK 3 S31: 0.0544 S32: 0.1478 S33: 0.0324
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 157 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3499 -25.2551 -48.9222
REMARK 3 T TENSOR
REMARK 3 T11: 0.4363 T22: 0.1960
REMARK 3 T33: 0.3218 T12: -0.0092
REMARK 3 T13: 0.0320 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 2.3344 L22: 2.5071
REMARK 3 L33: 2.8255 L12: -1.1836
REMARK 3 L13: 1.1776 L23: -0.9684
REMARK 3 S TENSOR
REMARK 3 S11: -0.1340 S12: -0.2257 S13: 0.1046
REMARK 3 S21: 0.9395 S22: 0.0404 S23: 0.2798
REMARK 3 S31: -0.0775 S32: -0.4156 S33: -0.0414
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4354 -24.9719 -45.1193
REMARK 3 T TENSOR
REMARK 3 T11: 0.4549 T22: 0.3910
REMARK 3 T33: 0.3294 T12: 0.0094
REMARK 3 T13: -0.0998 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.1268 L22: 0.7479
REMARK 3 L33: 4.8029 L12: -0.1535
REMARK 3 L13: 0.7707 L23: -1.3749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.6213 S13: 0.2467
REMARK 3 S21: 0.6515 S22: 0.1953 S23: -0.5016
REMARK 3 S31: 0.0467 S32: 0.3795 S33: 0.1318
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 187 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1619 -21.2643 -42.8080
REMARK 3 T TENSOR
REMARK 3 T11: 0.5109 T22: 0.2727
REMARK 3 T33: 0.2704 T12: 0.0064
REMARK 3 T13: 0.0257 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 1.7287 L22: 3.0747
REMARK 3 L33: 4.1346 L12: 0.9848
REMARK 3 L13: -0.6562 L23: -0.1980
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: -0.2662 S13: 0.1996
REMARK 3 S21: 0.6348 S22: -0.1174 S23: 0.2822
REMARK 3 S31: -0.0837 S32: -0.3670 S33: -0.0963
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 28 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0788 -3.9576 0.2918
REMARK 3 T TENSOR
REMARK 3 T11: 0.3383 T22: 0.5707
REMARK 3 T33: 0.3254 T12: 0.0412
REMARK 3 T13: -0.0319 T23: -0.1074
REMARK 3 L TENSOR
REMARK 3 L11: 3.8939 L22: 4.4946
REMARK 3 L33: 9.2784 L12: -0.7824
REMARK 3 L13: -1.0178 L23: -0.9153
REMARK 3 S TENSOR
REMARK 3 S11: 0.2433 S12: -0.9241 S13: 0.4506
REMARK 3 S21: 0.3153 S22: -0.1783 S23: -0.4269
REMARK 3 S31: -1.6044 S32: -0.1915 S33: 0.0401
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2972 -30.8735 8.2817
REMARK 3 T TENSOR
REMARK 3 T11: 0.3475 T22: 0.7202
REMARK 3 T33: 0.7172 T12: 0.0083
REMARK 3 T13: -0.0335 T23: 0.2859
REMARK 3 L TENSOR
REMARK 3 L11: 4.0085 L22: 7.9775
REMARK 3 L33: 1.9041 L12: 3.0027
REMARK 3 L13: 1.7332 L23: 1.8390
REMARK 3 S TENSOR
REMARK 3 S11: 0.1786 S12: 0.0178 S13: -1.1343
REMARK 3 S21: 0.5897 S22: 0.5339 S23: -0.1870
REMARK 3 S31: 0.5454 S32: -0.0798 S33: -0.1707
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 60 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7506 -18.8527 4.1476
REMARK 3 T TENSOR
REMARK 3 T11: 0.2241 T22: 0.6126
REMARK 3 T33: 0.3308 T12: 0.0208
REMARK 3 T13: 0.0102 T23: 0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 2.7522 L22: 1.9054
REMARK 3 L33: 1.7409 L12: 0.8798
REMARK 3 L13: -0.0587 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: -0.1089 S12: -0.5508 S13: -0.4048
REMARK 3 S21: -0.1057 S22: 0.0925 S23: 0.0018
REMARK 3 S31: 0.1568 S32: -0.0605 S33: -0.0517
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4296 -25.3240 20.1825
REMARK 3 T TENSOR
REMARK 3 T11: 0.3211 T22: 1.6889
REMARK 3 T33: 0.3022 T12: 0.0538
REMARK 3 T13: -0.2322 T23: 0.4696
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 1.1540
REMARK 3 L33: 4.3202 L12: 0.4378
REMARK 3 L13: -0.5262 L23: 0.4194
REMARK 3 S TENSOR
REMARK 3 S11: 0.3138 S12: -1.2100 S13: -0.7943
REMARK 3 S21: 0.5963 S22: -0.0116 S23: -0.0872
REMARK 3 S31: 0.5448 S32: -0.0233 S33: -0.3120
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 111 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.7738 -16.4891 16.6351
REMARK 3 T TENSOR
REMARK 3 T11: -0.0615 T22: 1.6165
REMARK 3 T33: 0.4294 T12: -0.0129
REMARK 3 T13: 0.1604 T23: 0.2367
REMARK 3 L TENSOR
REMARK 3 L11: 0.2199 L22: 1.8546
REMARK 3 L33: 0.3339 L12: -0.6017
REMARK 3 L13: -0.0379 L23: -0.1661
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: -0.6855 S13: -0.1464
REMARK 3 S21: 0.1472 S22: 0.0227 S23: 0.7741
REMARK 3 S31: -0.0268 S32: -0.2517 S33: 0.0801
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 126 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3019 -14.7347 17.0219
REMARK 3 T TENSOR
REMARK 3 T11: 0.3690 T22: 1.1446
REMARK 3 T33: 0.2583 T12: -0.0271
REMARK 3 T13: 0.0421 T23: 0.0788
REMARK 3 L TENSOR
REMARK 3 L11: 0.5696 L22: 2.2717
REMARK 3 L33: 2.6602 L12: -0.4907
REMARK 3 L13: 0.4121 L23: 0.1777
REMARK 3 S TENSOR
REMARK 3 S11: 0.2236 S12: -1.4260 S13: -0.1290
REMARK 3 S21: 0.5477 S22: -0.1023 S23: 0.3049
REMARK 3 S31: -0.0985 S32: 0.0905 S33: -0.0765
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 173 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5517 -11.9038 25.9990
REMARK 3 T TENSOR
REMARK 3 T11: 0.6910 T22: 1.3666
REMARK 3 T33: 0.3052 T12: -0.0567
REMARK 3 T13: 0.0604 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.4805 L22: 1.2607
REMARK 3 L33: 1.4250 L12: -0.0947
REMARK 3 L13: 0.5696 L23: 0.2133
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: -1.0617 S13: 0.3245
REMARK 3 S21: 0.7330 S22: 0.0890 S23: 0.0384
REMARK 3 S31: 0.0898 S32: 0.0831 S33: -0.0893
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 30 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6946 -22.6794 -77.9011
REMARK 3 T TENSOR
REMARK 3 T11: 0.5049 T22: 0.4546
REMARK 3 T33: 0.3173 T12: 0.1188
REMARK 3 T13: -0.0853 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 3.6635 L22: 4.2506
REMARK 3 L33: 6.3623 L12: -0.3668
REMARK 3 L13: -0.4437 L23: 0.1759
REMARK 3 S TENSOR
REMARK 3 S11: -0.3936 S12: -0.1463 S13: -0.1899
REMARK 3 S21: -0.5217 S22: -0.2810 S23: 0.0080
REMARK 3 S31: -0.4370 S32: -1.3991 S33: 0.0883
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 43 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6680 -3.5192 -85.0012
REMARK 3 T TENSOR
REMARK 3 T11: 0.5131 T22: 0.4306
REMARK 3 T33: 0.5351 T12: 0.0191
REMARK 3 T13: 0.1529 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 3.8303 L22: 3.4191
REMARK 3 L33: -0.0248 L12: 1.8438
REMARK 3 L13: 0.0257 L23: 0.1317
REMARK 3 S TENSOR
REMARK 3 S11: 0.2628 S12: -0.0811 S13: 0.0752
REMARK 3 S21: -0.1482 S22: -0.1893 S23: -0.7378
REMARK 3 S31: 0.0509 S32: 0.3090 S33: 0.0022
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 60 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6612 -6.4364 -80.9365
REMARK 3 T TENSOR
REMARK 3 T11: 0.4952 T22: 0.2317
REMARK 3 T33: 0.3708 T12: 0.0710
REMARK 3 T13: 0.1297 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.1190 L22: 1.4072
REMARK 3 L33: 2.4376 L12: -0.0513
REMARK 3 L13: 0.1850 L23: -0.0341
REMARK 3 S TENSOR
REMARK 3 S11: 0.1364 S12: -0.0022 S13: 0.1275
REMARK 3 S21: -0.3749 S22: -0.0196 S23: -0.5143
REMARK 3 S31: -0.0809 S32: 0.1810 S33: -0.0871
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 96 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3682 -12.9917 -96.7125
REMARK 3 T TENSOR
REMARK 3 T11: 0.8256 T22: 0.6200
REMARK 3 T33: 0.4771 T12: 0.1563
REMARK 3 T13: 0.2634 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.0814 L22: 1.2224
REMARK 3 L33: 4.2945 L12: 0.1434
REMARK 3 L13: -0.5940 L23: -1.5200
REMARK 3 S TENSOR
REMARK 3 S11: 0.1839 S12: 0.7355 S13: -0.0433
REMARK 3 S21: -0.7033 S22: 0.1331 S23: -0.6732
REMARK 3 S31: 0.5618 S32: 0.8596 S33: 0.0022
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 111 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6358 6.2274 -93.1698
REMARK 3 T TENSOR
REMARK 3 T11: 1.2238 T22: 0.3751
REMARK 3 T33: 0.5640 T12: 0.1589
REMARK 3 T13: 0.0864 T23: 0.0898
REMARK 3 L TENSOR
REMARK 3 L11: 1.3641 L22: 1.7190
REMARK 3 L33: 1.1696 L12: -0.4699
REMARK 3 L13: -0.1885 L23: 1.4051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: 0.3128 S13: 0.7320
REMARK 3 S21: -0.3951 S22: -0.1722 S23: 0.0197
REMARK 3 S31: -0.4139 S32: -0.0253 S33: 0.1109
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 126 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7431 -6.6446 -93.8413
REMARK 3 T TENSOR
REMARK 3 T11: 0.8527 T22: 0.3590
REMARK 3 T33: 0.2547 T12: 0.0961
REMARK 3 T13: 0.1002 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.7227 L22: 0.1996
REMARK 3 L33: 2.3835 L12: -0.3390
REMARK 3 L13: 0.1925 L23: 0.5393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.5457 S13: 0.3363
REMARK 3 S21: -1.0560 S22: 0.1656 S23: 0.1156
REMARK 3 S31: 0.0600 S32: -0.0771 S33: -0.1379
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 173 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2513 -8.6092-102.3247
REMARK 3 T TENSOR
REMARK 3 T11: 0.8035 T22: 0.7115
REMARK 3 T33: 0.3182 T12: 0.1131
REMARK 3 T13: 0.0031 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.0721 L22: 0.3037
REMARK 3 L33: 3.3449 L12: -0.0542
REMARK 3 L13: -0.1645 L23: 1.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1740 S12: 0.5855 S13: 0.3142
REMARK 3 S21: -0.8524 S22: 0.4049 S23: 0.1106
REMARK 3 S31: -0.5754 S32: -0.3773 S33: -0.0994
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 187 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8258 -1.1720-104.3430
REMARK 3 T TENSOR
REMARK 3 T11: 1.0406 T22: 0.8505
REMARK 3 T33: 0.4237 T12: 0.1458
REMARK 3 T13: 0.1300 T23: 0.2113
REMARK 3 L TENSOR
REMARK 3 L11: 2.7303 L22: 1.8244
REMARK 3 L33: 2.1080 L12: -1.6233
REMARK 3 L13: -0.7207 L23: 1.6476
REMARK 3 S TENSOR
REMARK 3 S11: 0.4038 S12: 1.7851 S13: 1.1693
REMARK 3 S21: -0.9531 S22: 0.0187 S23: -0.4258
REMARK 3 S31: -0.5698 S32: 0.0879 S33: -0.2376
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 6U06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1000243628.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11685
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55811
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 146.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
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: PHENIX
REMARK 200 STARTING MODEL: 4DT6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, MPD, PEG 6K, NDSB-256, PH 7.2,
REMARK 280 BATCH MODE, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 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 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 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 VAL A 28
REMARK 465 ALA A 29
REMARK 465 LYS A 206
REMARK 465 SER A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 THR A 211
REMARK 465 VAL B 28
REMARK 465 ALA B 29
REMARK 465 LYS B 206
REMARK 465 SER B 207
REMARK 465 GLY B 208
REMARK 465 SER B 209
REMARK 465 THR B 210
REMARK 465 THR B 211
REMARK 465 ALA C 204
REMARK 465 THR C 205
REMARK 465 LYS C 206
REMARK 465 SER C 207
REMARK 465 GLY C 208
REMARK 465 SER C 209
REMARK 465 THR C 210
REMARK 465 THR C 211
REMARK 465 VAL D 28
REMARK 465 ALA D 29
REMARK 465 THR D 55
REMARK 465 SER D 207
REMARK 465 GLY D 208
REMARK 465 SER D 209
REMARK 465 THR D 210
REMARK 465 THR D 211
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 ASN A 30 CG OD1 ND2
REMARK 470 HIS A 33 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 VAL C 28 CG1 CG2
REMARK 470 LYS C 49 CG CD CE NZ
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 THR C 55 OG1 CG2
REMARK 470 TRP C 56 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 56 CZ3 CH2
REMARK 470 GLN C 57 CG CD OE1 NE2
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 173 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 185 CG CD OE1 OE2
REMARK 470 LYS C 192 CG CD CE NZ
REMARK 470 VAL C 194 CG1 CG2
REMARK 470 THR C 203 OG1 CG2
REMARK 470 LYS C 212 CG CD CE NZ
REMARK 470 ASN D 30 CG OD1 ND2
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 TRP D 56 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 56 CZ3 CH2
REMARK 470 GLU D 185 CG CD OE1 OE2
REMARK 470 ARG D 186 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 192 CG CD CE NZ
REMARK 470 LYS D 206 CG CD CE NZ
REMARK 470 LYS D 212 CG CD CE NZ
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 67 31.07 -149.73
REMARK 500 ASP A 143 -132.78 61.53
REMARK 500 SER B 64 148.63 -178.69
REMARK 500 ASP B 67 27.21 -144.78
REMARK 500 ASP B 143 -131.86 58.83
REMARK 500 ALA C 58 -8.09 68.10
REMARK 500 ASP C 67 23.39 -146.97
REMARK 500 ASP C 143 -132.64 62.91
REMARK 500 ASP D 67 26.16 -145.70
REMARK 500 ASP D 143 -131.38 61.98
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 EI8 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EI8 B 301 and LYS B
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EI8 C 301 and LYS C
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EI8 D 301 and LYS D
REMARK 800 162
DBREF 6U06 A 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 6U06 B 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 6U06 C 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 6U06 D 28 217 UNP P63073 IF4E_MOUSE 28 217
SEQRES 1 A 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 A 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 A 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 A 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 A 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 A 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 A 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 A 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 A 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 A 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 A 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 A 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 A 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 A 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 A 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 B 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 B 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 B 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 B 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 B 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 B 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 B 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 B 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 B 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 B 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 B 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 B 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 B 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 B 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 B 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 C 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 C 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 C 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 C 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 C 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 C 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 C 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 C 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 C 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 C 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 C 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 C 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 C 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 C 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 C 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 D 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 D 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 D 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 D 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 D 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 D 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 D 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 D 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 D 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 D 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 D 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 D 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 D 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 D 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 D 190 THR THR LYS ASN ARG PHE VAL VAL
HET EI8 A 301 33
HET EI8 B 301 33
HET EI8 C 301 33
HET EI8 D 301 33
HETNAM EI8 3-{[(4-CYANOPHENYL)METHYL](1-OXO-1,2-
HETNAM 2 EI8 DIHYDROISOQUINOLIN-7-YL)SULFAMOYL}BENZENE-1-SULFONYL
HETNAM 3 EI8 FLUORIDE
FORMUL 5 EI8 4(C23 H16 F N3 O5 S2)
FORMUL 9 HOH *156(H2 O)
HELIX 1 AA1 ASN A 30 ILE A 35 1 6
HELIX 2 AA2 TRP A 56 ALA A 58 5 3
HELIX 3 AA3 VAL A 69 ILE A 79 1 11
HELIX 4 AA4 LEU A 81 LEU A 85 5 5
HELIX 5 AA5 GLN A 120 ASP A 125 1 6
HELIX 6 AA6 ASP A 125 GLY A 139 1 15
HELIX 7 AA7 PHE A 142 ASP A 147 5 6
HELIX 8 AA8 ASN A 172 LEU A 187 1 16
HELIX 9 AA9 HIS A 200 THR A 205 1 6
HELIX 10 AB1 ASN B 30 TYR B 34 5 5
HELIX 11 AB2 THR B 55 ASN B 59 1 5
HELIX 12 AB3 VAL B 69 ASN B 77 1 9
HELIX 13 AB4 LEU B 81 LEU B 85 5 5
HELIX 14 AB5 GLN B 120 ASP B 125 1 6
HELIX 15 AB6 ASP B 125 GLY B 139 1 15
HELIX 16 AB7 PHE B 142 ASP B 147 5 6
HELIX 17 AB8 ASN B 172 LEU B 187 1 16
HELIX 18 AB9 HIS B 200 THR B 205 1 6
HELIX 19 AC1 VAL C 69 ILE C 79 1 11
HELIX 20 AC2 LEU C 81 LEU C 85 5 5
HELIX 21 AC3 GLN C 120 ASP C 125 1 6
HELIX 22 AC4 ASP C 125 GLY C 139 1 15
HELIX 23 AC5 PHE C 142 ASP C 147 5 6
HELIX 24 AC6 ASN C 172 GLY C 188 1 17
HELIX 25 AC7 TRP D 56 LEU D 60 5 5
HELIX 26 AC8 VAL D 69 ILE D 79 1 11
HELIX 27 AC9 LEU D 81 LEU D 85 5 5
HELIX 28 AD1 GLN D 120 ASP D 125 1 6
HELIX 29 AD2 ASP D 125 GLY D 139 1 15
HELIX 30 AD3 PHE D 142 ASP D 147 5 6
HELIX 31 AD4 ASN D 172 LEU D 187 1 16
HELIX 32 AD5 HIS D 200 LYS D 206 1 7
SHEET 1 AA1 8 LEU A 60 THR A 68 0
SHEET 2 AA1 8 PRO A 38 LYS A 49 -1 N LEU A 45 O SER A 64
SHEET 3 AA1 8 CYS A 89 LYS A 95 -1 O SER A 92 N TRP A 46
SHEET 4 AA1 8 VAL A 149 ASN A 155 -1 O VAL A 154 N TYR A 91
SHEET 5 AA1 8 LYS A 162 THR A 167 -1 O TRP A 166 N CYS A 150
SHEET 6 AA1 8 GLY A 111 THR A 116 -1 N ILE A 115 O ILE A 163
SHEET 7 AA1 8 ILE A 195 SER A 199 -1 O GLN A 198 N ARG A 112
SHEET 8 AA1 8 PHE A 215 VAL A 217 -1 O PHE A 215 N TYR A 197
SHEET 1 AA2 8 LEU B 60 THR B 68 0
SHEET 2 AA2 8 PRO B 38 LYS B 49 -1 N TRP B 43 O PHE B 66
SHEET 3 AA2 8 CYS B 89 LYS B 95 -1 O SER B 92 N TRP B 46
SHEET 4 AA2 8 VAL B 149 VAL B 156 -1 O CYS B 150 N LYS B 95
SHEET 5 AA2 8 LYS B 162 THR B 167 -1 O LYS B 162 N ASN B 155
SHEET 6 AA2 8 GLY B 111 THR B 116 -1 N ILE B 115 O ILE B 163
SHEET 7 AA2 8 ILE B 195 SER B 199 -1 O GLY B 196 N LEU B 114
SHEET 8 AA2 8 PHE B 215 VAL B 217 -1 O PHE B 215 N TYR B 197
SHEET 1 AA3 8 LEU C 60 THR C 68 0
SHEET 2 AA3 8 PRO C 38 LYS C 49 -1 N TRP C 43 O PHE C 66
SHEET 3 AA3 8 CYS C 89 LYS C 95 -1 O SER C 92 N TRP C 46
SHEET 4 AA3 8 VAL C 149 VAL C 156 -1 O CYS C 150 N LYS C 95
SHEET 5 AA3 8 ASP C 161 THR C 167 -1 O TRP C 166 N GLY C 151
SHEET 6 AA3 8 GLY C 111 LEU C 117 -1 N ILE C 115 O ILE C 163
SHEET 7 AA3 8 ILE C 195 SER C 199 -1 O GLY C 196 N LEU C 114
SHEET 8 AA3 8 PHE C 215 VAL C 217 -1 O PHE C 215 N TYR C 197
SHEET 1 AA4 8 ARG D 61 THR D 68 0
SHEET 2 AA4 8 PRO D 38 LYS D 49 -1 N LEU D 39 O ASP D 67
SHEET 3 AA4 8 CYS D 89 LYS D 95 -1 O PHE D 94 N ALA D 44
SHEET 4 AA4 8 VAL D 149 VAL D 156 -1 O VAL D 154 N TYR D 91
SHEET 5 AA4 8 ASP D 161 THR D 167 -1 O TRP D 166 N GLY D 151
SHEET 6 AA4 8 GLY D 111 LEU D 117 -1 N LEU D 117 O ASP D 161
SHEET 7 AA4 8 ILE D 195 SER D 199 -1 O GLY D 196 N LEU D 114
SHEET 8 AA4 8 PHE D 215 VAL D 217 -1 O PHE D 215 N TYR D 197
LINK NZ LYS A 162 S2 EI8 A 301 1555 1555 1.60
LINK NZ LYS B 162 S2 EI8 B 301 1555 1555 1.60
LINK NZ LYS C 162 S2 EI8 C 301 1555 1555 1.59
LINK NZ LYS D 162 S2 EI8 D 301 1555 1555 1.60
SITE 1 AC1 13 LEU A 60 ASP A 90 SER A 92 PRO A 100
SITE 2 AC1 13 MET A 101 TRP A 102 GLU A 103 ARG A 112
SITE 3 AC1 13 ASN A 155 ARG A 157 LYS A 162 TRP A 166
SITE 4 AC1 13 HOH A 427
SITE 1 AC2 15 LEU B 60 ASP B 90 SER B 92 PRO B 100
SITE 2 AC2 15 MET B 101 TRP B 102 GLU B 103 ARG B 112
SITE 3 AC2 15 ILE B 115 VAL B 154 ASN B 155 ARG B 157
SITE 4 AC2 15 ASP B 161 ILE B 163 TRP B 166
SITE 1 AC3 14 ASP C 90 SER C 92 PRO C 100 MET C 101
SITE 2 AC3 14 TRP C 102 GLU C 103 ARG C 112 ILE C 115
SITE 3 AC3 14 VAL C 154 ASN C 155 ARG C 157 ASP C 161
SITE 4 AC3 14 ILE C 163 HOH C 406
SITE 1 AC4 14 LEU D 60 ASP D 90 SER D 92 PRO D 100
SITE 2 AC4 14 MET D 101 TRP D 102 GLU D 103 ARG D 112
SITE 3 AC4 14 ILE D 115 VAL D 154 ASN D 155 ARG D 157
SITE 4 AC4 14 ASP D 161 ILE D 163
CRYST1 38.110 38.290 146.820 87.96 94.87 101.64 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.026240 0.005403 0.002132 0.00000
SCALE2 0.000000 0.026664 -0.000503 0.00000
SCALE3 0.000000 0.000000 0.006837 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
