HEADER SIGNALING PROTEIN/INHIBITOR 04-AUG-13 4M1Y
TITLE CRYSTAL STRUCTURE OF SMALL MOLECULE VINYLSULFONAMIDE 15 COVALENTLY
TITLE 2 BOUND TO K-RAS G12C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: K-RAS GTPASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-169;
COMPND 5 SYNONYM: K-RAS 2, KI-RAS, C-K-RAS, C-KI-RAS, GTPASE KRAS, N-
COMPND 6 TERMINALLY PROCESSED;
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: KRAS, KRAS ISOFORM 2B, KRAS2, RASK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS411
KEYWDS GTPASE, GDP BOUND, SMALL MOLECULE INHIBITOR, COVALENT BINDER,
KEYWDS 2 SIGNALING PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.OSTREM,U.PETERS,M.L.SOS,J.A.WELLS,K.M.SHOKAT
REVDAT 4 20-SEP-23 4M1Y 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4M1Y 1 REMARK
REVDAT 2 18-DEC-13 4M1Y 1 JRNL
REVDAT 1 27-NOV-13 4M1Y 0
JRNL AUTH J.M.OSTREM,U.PETERS,M.L.SOS,J.A.WELLS,K.M.SHOKAT
JRNL TITL K-RAS(G12C) INHIBITORS ALLOSTERICALLY CONTROL GTP AFFINITY
JRNL TITL 2 AND EFFECTOR INTERACTIONS.
JRNL REF NATURE V. 503 548 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 24256730
JRNL DOI 10.1038/NATURE12796
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1402
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 71402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 23.3818 - 3.5905 0.93 4819 137 0.1600 0.1956
REMARK 3 2 3.5905 - 2.8515 0.99 5080 147 0.1587 0.1701
REMARK 3 3 2.8515 - 2.4915 0.99 5095 146 0.1689 0.1931
REMARK 3 4 2.4915 - 2.2639 0.99 5014 142 0.1625 0.1950
REMARK 3 5 2.2639 - 2.1018 0.99 5028 148 0.1630 0.1790
REMARK 3 6 2.1018 - 1.9779 0.98 5010 145 0.1677 0.1811
REMARK 3 7 1.9779 - 1.8789 0.98 5002 139 0.1731 0.1946
REMARK 3 8 1.8789 - 1.7971 0.98 4946 144 0.1751 0.2130
REMARK 3 9 1.7971 - 1.7280 0.98 4975 152 0.1822 0.2059
REMARK 3 10 1.7280 - 1.6684 0.97 4924 147 0.1861 0.2021
REMARK 3 11 1.6684 - 1.6162 0.97 4953 138 0.1822 0.1932
REMARK 3 12 1.6162 - 1.5700 0.97 4917 134 0.1949 0.2145
REMARK 3 13 1.5700 - 1.5287 0.97 4919 146 0.2048 0.2286
REMARK 3 14 1.5287 - 1.4914 0.94 4721 134 0.2179 0.2366
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.67
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 : 0.008 3920
REMARK 3 ANGLE : 1.194 5316
REMARK 3 CHIRALITY : 0.063 605
REMARK 3 PLANARITY : 0.005 666
REMARK 3 DIHEDRAL : 17.751 1469
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6221 16.9562 148.4035
REMARK 3 T TENSOR
REMARK 3 T11: 0.1289 T22: 0.2583
REMARK 3 T33: 0.1747 T12: 0.0387
REMARK 3 T13: 0.0213 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 4.4215 L22: 5.4009
REMARK 3 L33: 3.2872 L12: -0.8205
REMARK 3 L13: 1.9352 L23: -1.2877
REMARK 3 S TENSOR
REMARK 3 S11: 0.1288 S12: -0.0838 S13: -0.2082
REMARK 3 S21: -0.1004 S22: -0.1468 S23: -0.5094
REMARK 3 S31: 0.3024 S32: 0.4686 S33: 0.0717
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6874 26.6604 151.1020
REMARK 3 T TENSOR
REMARK 3 T11: 0.6511 T22: 0.5475
REMARK 3 T33: 0.6289 T12: -0.1056
REMARK 3 T13: -0.0135 T23: 0.1013
REMARK 3 L TENSOR
REMARK 3 L11: 7.8031 L22: 4.1645
REMARK 3 L33: 4.0429 L12: -2.3676
REMARK 3 L13: -1.5796 L23: 4.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1851 S12: 0.3480 S13: 1.1398
REMARK 3 S21: -1.6559 S22: 0.5853 S23: -0.8202
REMARK 3 S31: -0.1739 S32: 0.1412 S33: -0.4803
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2230 10.2094 151.9911
REMARK 3 T TENSOR
REMARK 3 T11: 0.2601 T22: 0.3855
REMARK 3 T33: 0.2321 T12: 0.0562
REMARK 3 T13: 0.0204 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 1.1178 L22: 5.9329
REMARK 3 L33: 2.1011 L12: 0.3541
REMARK 3 L13: 0.3742 L23: -2.4558
REMARK 3 S TENSOR
REMARK 3 S11: 0.2500 S12: 0.1685 S13: 0.1819
REMARK 3 S21: 0.0904 S22: -0.2255 S23: -0.0637
REMARK 3 S31: -0.0714 S32: 0.3866 S33: -0.0060
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3245 13.2858 134.7906
REMARK 3 T TENSOR
REMARK 3 T11: 0.5857 T22: 0.5611
REMARK 3 T33: 0.6244 T12: 0.0215
REMARK 3 T13: 0.0102 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 7.6565 L22: 8.6362
REMARK 3 L33: 7.6964 L12: -0.5432
REMARK 3 L13: 0.4632 L23: -0.0189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0723 S12: 0.9309 S13: 0.9185
REMARK 3 S21: 0.1506 S22: 0.0250 S23: -1.2782
REMARK 3 S31: -0.4840 S32: 0.9467 S33: 0.0784
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 75 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6589 19.8005 140.7844
REMARK 3 T TENSOR
REMARK 3 T11: 0.2441 T22: 0.1451
REMARK 3 T33: 0.2095 T12: 0.0393
REMARK 3 T13: -0.0847 T23: -0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 2.4203 L22: 2.5553
REMARK 3 L33: 2.4478 L12: -1.1694
REMARK 3 L13: 0.5049 L23: -0.2808
REMARK 3 S TENSOR
REMARK 3 S11: 0.3135 S12: 0.3759 S13: -0.4585
REMARK 3 S21: -0.7378 S22: -0.1750 S23: 0.4260
REMARK 3 S31: 0.2899 S32: 0.1097 S33: 0.0196
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4423 22.1974 148.0935
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.1196
REMARK 3 T33: 0.1533 T12: -0.0056
REMARK 3 T13: -0.0146 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 3.2041 L22: 3.2003
REMARK 3 L33: 2.5977 L12: -0.7047
REMARK 3 L13: 0.8076 L23: -0.7978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0832 S12: 0.0386 S13: -0.2330
REMARK 3 S21: 0.0061 S22: 0.0296 S23: 0.2000
REMARK 3 S31: 0.1315 S32: 0.0298 S33: -0.0360
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7624 16.5672 153.1675
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.1839
REMARK 3 T33: 0.1891 T12: -0.0087
REMARK 3 T13: 0.0233 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 3.6782 L22: 4.3314
REMARK 3 L33: 2.5372 L12: -1.4042
REMARK 3 L13: 1.4322 L23: -0.5837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.1950 S13: -0.3608
REMARK 3 S21: 0.1672 S22: 0.0904 S23: 0.3260
REMARK 3 S31: 0.1560 S32: -0.0330 S33: -0.0395
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7336 18.2850 179.8471
REMARK 3 T TENSOR
REMARK 3 T11: 0.2746 T22: 0.1416
REMARK 3 T33: 0.2910 T12: 0.0390
REMARK 3 T13: 0.0190 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 3.3429 L22: 4.3289
REMARK 3 L33: 2.8349 L12: -0.4279
REMARK 3 L13: -0.0926 L23: 0.2323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0761 S12: -0.3298 S13: 0.7278
REMARK 3 S21: 0.0338 S22: 0.0790 S23: 0.3860
REMARK 3 S31: -0.5893 S32: -0.1989 S33: -0.1024
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0504 25.2725 179.8156
REMARK 3 T TENSOR
REMARK 3 T11: 0.7213 T22: 0.3249
REMARK 3 T33: 0.6548 T12: -0.0273
REMARK 3 T13: 0.1363 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 3.5081 L22: 0.8746
REMARK 3 L33: 2.8385 L12: -1.7516
REMARK 3 L13: 0.4997 L23: 0.0198
REMARK 3 S TENSOR
REMARK 3 S11: 0.1636 S12: -0.3694 S13: 0.4755
REMARK 3 S21: 0.5882 S22: 0.3106 S23: 0.1223
REMARK 3 S31: -1.4334 S32: -0.4119 S33: -0.4109
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2990 18.6976 181.0809
REMARK 3 T TENSOR
REMARK 3 T11: 0.3512 T22: 0.3989
REMARK 3 T33: 0.5594 T12: 0.0575
REMARK 3 T13: -0.0435 T23: -0.1036
REMARK 3 L TENSOR
REMARK 3 L11: 7.2968 L22: 5.3796
REMARK 3 L33: 8.6791 L12: 0.9757
REMARK 3 L13: -2.0515 L23: -3.1649
REMARK 3 S TENSOR
REMARK 3 S11: 0.0577 S12: -0.3896 S13: -0.0109
REMARK 3 S21: 0.6822 S22: 0.1053 S23: 0.3065
REMARK 3 S31: -0.5764 S32: -0.7633 S33: -0.2780
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2813 11.1376 177.8334
REMARK 3 T TENSOR
REMARK 3 T11: 0.1780 T22: 0.2476
REMARK 3 T33: 0.4168 T12: 0.0421
REMARK 3 T13: -0.0209 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 5.3474 L22: 1.1559
REMARK 3 L33: 2.0092 L12: -0.2034
REMARK 3 L13: 1.5968 L23: 0.1591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: -0.3967 S13: -0.0323
REMARK 3 S21: -0.1083 S22: 0.0284 S23: 0.8686
REMARK 3 S31: -0.1124 S32: -0.5599 S33: 0.0249
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5777 1.6386 176.1246
REMARK 3 T TENSOR
REMARK 3 T11: 0.1509 T22: 0.1486
REMARK 3 T33: 0.2533 T12: -0.0020
REMARK 3 T13: -0.0136 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 3.4048 L22: 4.2778
REMARK 3 L33: 4.4021 L12: -2.6693
REMARK 3 L13: 3.0514 L23: -1.2098
REMARK 3 S TENSOR
REMARK 3 S11: 0.1044 S12: -0.1698 S13: -0.5166
REMARK 3 S21: -0.2140 S22: 0.0616 S23: 0.7782
REMARK 3 S31: 0.1319 S32: -0.3018 S33: -0.0963
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 104 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9242 7.0068 175.1603
REMARK 3 T TENSOR
REMARK 3 T11: 0.1781 T22: 0.1149
REMARK 3 T33: 0.1144 T12: 0.0149
REMARK 3 T13: 0.0127 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 4.5031 L22: 5.2505
REMARK 3 L33: 2.9267 L12: -0.3833
REMARK 3 L13: 0.0061 L23: -0.2938
REMARK 3 S TENSOR
REMARK 3 S11: 0.1358 S12: 0.2412 S13: 0.1153
REMARK 3 S21: -0.3155 S22: -0.1352 S23: 0.1713
REMARK 3 S31: 0.1049 S32: 0.0669 S33: 0.0305
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3107 1.4059 167.2771
REMARK 3 T TENSOR
REMARK 3 T11: 0.2888 T22: 0.2476
REMARK 3 T33: 0.1608 T12: 0.0034
REMARK 3 T13: 0.0408 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 3.2458 L22: 6.6294
REMARK 3 L33: 6.7022 L12: 0.8183
REMARK 3 L13: 4.3327 L23: 1.9007
REMARK 3 S TENSOR
REMARK 3 S11: 0.2047 S12: 0.2377 S13: -0.5603
REMARK 3 S21: -0.6583 S22: 0.1377 S23: -0.2334
REMARK 3 S31: 0.1736 S32: 0.5846 S33: -0.2718
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3009 13.0372 175.6355
REMARK 3 T TENSOR
REMARK 3 T11: 0.2481 T22: 0.1955
REMARK 3 T33: 0.2472 T12: -0.0232
REMARK 3 T13: 0.0092 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 3.7803 L22: 4.1718
REMARK 3 L33: 6.1565 L12: 3.0833
REMARK 3 L13: 4.5824 L23: 4.7474
REMARK 3 S TENSOR
REMARK 3 S11: -0.1153 S12: 0.4228 S13: 0.2336
REMARK 3 S21: -0.4072 S22: 0.3236 S23: -0.5266
REMARK 3 S31: -0.5165 S32: 0.6127 S33: -0.2088
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 152 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3915 19.1437 166.9633
REMARK 3 T TENSOR
REMARK 3 T11: 0.4543 T22: 0.2964
REMARK 3 T33: 0.3054 T12: 0.0703
REMARK 3 T13: -0.0527 T23: 0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 7.6274 L22: 3.7119
REMARK 3 L33: 2.6674 L12: 0.2270
REMARK 3 L13: 1.2644 L23: -1.2349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 1.1538 S13: 0.6360
REMARK 3 S21: -0.9912 S22: -0.1108 S23: 0.2720
REMARK 3 S31: -0.3894 S32: -0.0623 S33: 0.2212
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1277 29.7080 203.7878
REMARK 3 T TENSOR
REMARK 3 T11: 0.3486 T22: 0.6154
REMARK 3 T33: 0.2312 T12: 0.0601
REMARK 3 T13: 0.0113 T23: 0.2297
REMARK 3 L TENSOR
REMARK 3 L11: 1.2755 L22: 2.8784
REMARK 3 L33: 4.0553 L12: -0.9527
REMARK 3 L13: 1.7950 L23: -0.4664
REMARK 3 S TENSOR
REMARK 3 S11: -0.1312 S12: -1.2829 S13: -0.7363
REMARK 3 S21: 0.7147 S22: -0.0649 S23: 0.1067
REMARK 3 S31: 0.3402 S32: -0.1938 S33: -0.2867
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8003 32.3129 208.0529
REMARK 3 T TENSOR
REMARK 3 T11: 0.5161 T22: 0.7920
REMARK 3 T33: 0.4237 T12: 0.0281
REMARK 3 T13: 0.0241 T23: 0.1438
REMARK 3 L TENSOR
REMARK 3 L11: 2.0560 L22: 6.8646
REMARK 3 L33: 3.2458 L12: 0.7675
REMARK 3 L13: 0.1258 L23: -0.1855
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -1.0108 S13: -0.4059
REMARK 3 S21: 0.7688 S22: -0.0270 S23: 0.8308
REMARK 3 S31: -0.0495 S32: -0.1903 S33: -0.0334
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 77 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6853 39.6036 193.6629
REMARK 3 T TENSOR
REMARK 3 T11: 0.2199 T22: 0.2123
REMARK 3 T33: 0.1297 T12: 0.0572
REMARK 3 T13: 0.0023 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 4.2995 L22: 4.5788
REMARK 3 L33: 7.0484 L12: 1.3832
REMARK 3 L13: 2.2210 L23: 2.1079
REMARK 3 S TENSOR
REMARK 3 S11: -0.2310 S12: -0.6254 S13: 0.2426
REMARK 3 S21: 0.1031 S22: 0.0840 S23: 0.3329
REMARK 3 S31: -0.7533 S32: -0.3397 S33: 0.1726
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 104 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5064 35.8074 189.2499
REMARK 3 T TENSOR
REMARK 3 T11: 0.1415 T22: 0.1710
REMARK 3 T33: 0.1305 T12: 0.0067
REMARK 3 T13: 0.0201 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 6.5854 L22: 6.0425
REMARK 3 L33: 4.3249 L12: 1.5093
REMARK 3 L13: 2.1090 L23: -0.8319
REMARK 3 S TENSOR
REMARK 3 S11: -0.1603 S12: 0.0567 S13: -0.1947
REMARK 3 S21: -0.1285 S22: 0.0331 S23: -0.3474
REMARK 3 S31: -0.2088 S32: 0.0553 S33: 0.0723
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 144 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7644 30.8054 199.2061
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.3428
REMARK 3 T33: 0.2856 T12: 0.0263
REMARK 3 T13: -0.0489 T23: 0.1260
REMARK 3 L TENSOR
REMARK 3 L11: 7.4526 L22: 5.4137
REMARK 3 L33: 7.0283 L12: 1.9462
REMARK 3 L13: 3.7179 L23: 2.8853
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: -0.4899 S13: -0.5449
REMARK 3 S21: 0.5006 S22: 0.2171 S23: -0.2598
REMARK 3 S31: 0.1462 S32: 0.5532 S33: -0.0580
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 4M1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71411
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : 0.03100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.1890
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : 0.38100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.673
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.0
REMARK 200 STARTING MODEL: PDB ENTRY 3GFT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 31% PEG4000, 0.2M NH4CH3COO, 0.1M NA
REMARK 280 -CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 34.06050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.77000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.06050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.77000
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
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 374 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 TYR A 32
REMARK 465 ASP A 33
REMARK 465 PRO A 34
REMARK 465 THR A 35
REMARK 465 ILE A 36
REMARK 465 GLN A 61
REMARK 465 LYS A 169
REMARK 465 GLY B 0
REMARK 465 ASP B 30
REMARK 465 GLU B 31
REMARK 465 TYR B 32
REMARK 465 ASP B 33
REMARK 465 PRO B 34
REMARK 465 THR B 35
REMARK 465 ILE B 36
REMARK 465 GLU B 37
REMARK 465 GLY C 0
REMARK 465 ASP C 30
REMARK 465 GLU C 31
REMARK 465 TYR C 32
REMARK 465 ASP C 33
REMARK 465 PRO C 34
REMARK 465 THR C 35
REMARK 465 ILE C 36
REMARK 465 GLU C 37
REMARK 465 ASP C 38
REMARK 465 GLN C 61
REMARK 465 GLU C 62
REMARK 465 GLU C 63
REMARK 465 TYR C 64
REMARK 465 SER C 65
REMARK 465 ALA C 66
REMARK 465 MET C 67
REMARK 465 GLU C 168
REMARK 465 LYS C 169
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 VAL A 29 CG1 CG2
REMARK 470 ARG A 68 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 105 CG OD1 OD2
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 SER B 39 OG
REMARK 470 ASP B 105 CG OD1 OD2
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 LYS B 169 CG CD CE NZ
REMARK 470 MET C 1 CG SD CE
REMARK 470 LYS C 5 CG CD CE NZ
REMARK 470 ASN C 26 CG OD1 ND2
REMARK 470 SER C 39 OG
REMARK 470 LEU C 52 CG CD1 CD2
REMARK 470 ARG C 68 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 102 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 105 CG OD1 OD2
REMARK 470 SER C 106 OG
REMARK 470 GLU C 107 CG CD OE1 OE2
REMARK 470 ASP C 108 CG OD1 OD2
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 HH22 ARG A 149 O HOH A 327 1.52
REMARK 500 HZ3 LYS A 42 O HOH A 414 1.58
REMARK 500 O HOH A 403 O HOH A 404 1.90
REMARK 500 OE1 GLU B 143 O HOH B 343 1.98
REMARK 500 O HOH C 303 O HOH C 338 2.09
REMARK 500 O HOH B 400 O HOH B 405 2.10
REMARK 500 O HOH A 418 O HOH A 421 2.11
REMARK 500 NH2 ARG C 73 O HOH C 357 2.12
REMARK 500 O HOH C 319 O HOH C 342 2.12
REMARK 500 OH TYR C 71 O HOH C 350 2.15
REMARK 500 O HOH A 344 O HOH A 406 2.17
REMARK 500 OD1 ASP C 92 O HOH C 341 2.18
REMARK 500 OE1 GLU B 168 O HOH B 358 2.19
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 HG1 THR A 50 HG1 THR A 50 2859 1.10
REMARK 500 O HOH A 418 O HOH B 398 4759 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 ASP A 108 74.87 -118.95
REMARK 500 ARG A 149 -2.24 76.90
REMARK 500 LYS B 117 33.06 70.28
REMARK 500 SER B 122 49.73 -92.26
REMARK 500 ARG B 149 -1.01 77.44
REMARK 500 THR C 58 4.20 -68.00
REMARK 500 ASP C 108 70.30 -100.87
REMARK 500 LYS C 117 35.57 74.12
REMARK 500 SER C 122 48.43 -81.96
REMARK 500 ARG C 149 -0.49 76.63
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 GDP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 21S B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L8G RELATED DB: PDB
REMARK 900 RELATED MUTANT OF PROTEIN
REMARK 900 RELATED ID: 4LUC RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4LYF RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4LYJ RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4M1O RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4L9W RELATED DB: PDB
REMARK 900 MUTANT IN RELATED PROTEIN
REMARK 900 RELATED ID: 4L9S RELATED DB: PDB
REMARK 900 MUTANT IN RELATED PROTEIN
REMARK 900 RELATED ID: 4LPK RELATED DB: PDB
REMARK 900 WILD-TYPE OF PROTEIN
REMARK 900 RELATED ID: 4LV6 RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4M1S RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4M1T RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4M1W RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4LYH RELATED DB: PDB
REMARK 900 PROTEIN BOUND TO RELATED COMPOUND
REMARK 900 RELATED ID: 4LRW RELATED DB: PDB
REMARK 900 PROTEIN WITHOUT SMALL MOLECULE BOUND
REMARK 900 RELATED ID: 4M21 RELATED DB: PDB
REMARK 900 RELATED COMPOUND BOUND TO PROTEIN
REMARK 900 RELATED ID: 4M22 RELATED DB: PDB
REMARK 900 RELATED COMPOUND BOUND TO PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IN THE STRUCTURE REPRESENTS ISOFORM 2B OF GTPASE KRAS.
REMARK 999 THIS ISOFORM DIFFERS FROM THE CANONICAL SEQUENCE AS FOLLOW: 151-153
REMARK 999 (RVE TO GVD) AND 165-169 (QYRLK TO KHKEK)
DBREF 4M1Y A 1 169 UNP P01116 RASK_HUMAN 1 169
DBREF 4M1Y B 1 169 UNP P01116 RASK_HUMAN 1 169
DBREF 4M1Y C 1 169 UNP P01116 RASK_HUMAN 1 169
SEQADV 4M1Y GLY A 0 UNP P01116 EXPRESSION TAG
SEQADV 4M1Y CYS A 12 UNP P01116 GLY 12 VARIANT
SEQADV 4M1Y SER A 51 UNP P01116 CYS 51 ENGINEERED MUTATION
SEQADV 4M1Y LEU A 80 UNP P01116 CYS 80 ENGINEERED MUTATION
SEQADV 4M1Y SER A 118 UNP P01116 CYS 118 ENGINEERED MUTATION
SEQADV 4M1Y GLY A 151 UNP P01116 ARG 151 SEE REMARK 999
SEQADV 4M1Y ASP A 153 UNP P01116 GLU 153 SEE REMARK 999
SEQADV 4M1Y LYS A 165 UNP P01116 GLN 165 SEE REMARK 999
SEQADV 4M1Y HIS A 166 UNP P01116 TYR 166 SEE REMARK 999
SEQADV 4M1Y LYS A 167 UNP P01116 ARG 167 SEE REMARK 999
SEQADV 4M1Y GLU A 168 UNP P01116 LEU 168 SEE REMARK 999
SEQADV 4M1Y GLY B 0 UNP P01116 EXPRESSION TAG
SEQADV 4M1Y CYS B 12 UNP P01116 GLY 12 VARIANT
SEQADV 4M1Y SER B 51 UNP P01116 CYS 51 ENGINEERED MUTATION
SEQADV 4M1Y LEU B 80 UNP P01116 CYS 80 ENGINEERED MUTATION
SEQADV 4M1Y SER B 118 UNP P01116 CYS 118 ENGINEERED MUTATION
SEQADV 4M1Y GLY B 151 UNP P01116 ARG 151 SEE REMARK 999
SEQADV 4M1Y ASP B 153 UNP P01116 GLU 153 SEE REMARK 999
SEQADV 4M1Y LYS B 165 UNP P01116 GLN 165 SEE REMARK 999
SEQADV 4M1Y HIS B 166 UNP P01116 TYR 166 SEE REMARK 999
SEQADV 4M1Y LYS B 167 UNP P01116 ARG 167 SEE REMARK 999
SEQADV 4M1Y GLU B 168 UNP P01116 LEU 168 SEE REMARK 999
SEQADV 4M1Y GLY C 0 UNP P01116 EXPRESSION TAG
SEQADV 4M1Y CYS C 12 UNP P01116 GLY 12 VARIANT
SEQADV 4M1Y SER C 51 UNP P01116 CYS 51 ENGINEERED MUTATION
SEQADV 4M1Y LEU C 80 UNP P01116 CYS 80 ENGINEERED MUTATION
SEQADV 4M1Y SER C 118 UNP P01116 CYS 118 ENGINEERED MUTATION
SEQADV 4M1Y GLY C 151 UNP P01116 ARG 151 SEE REMARK 999
SEQADV 4M1Y ASP C 153 UNP P01116 GLU 153 SEE REMARK 999
SEQADV 4M1Y LYS C 165 UNP P01116 GLN 165 SEE REMARK 999
SEQADV 4M1Y HIS C 166 UNP P01116 TYR 166 SEE REMARK 999
SEQADV 4M1Y LYS C 167 UNP P01116 ARG 167 SEE REMARK 999
SEQADV 4M1Y GLU C 168 UNP P01116 LEU 168 SEE REMARK 999
SEQRES 1 A 170 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 A 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 A 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 A 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR SER
SEQRES 5 A 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 A 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 A 170 PHE LEU LEU VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 A 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 A 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 A 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 A 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 A 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 A 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 14 A 170 LYS
SEQRES 1 B 170 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 B 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 B 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 B 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR SER
SEQRES 5 B 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 B 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 B 170 PHE LEU LEU VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 B 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 B 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 B 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 B 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 B 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 B 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 14 B 170 LYS
SEQRES 1 C 170 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 C 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 C 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 C 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR SER
SEQRES 5 C 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 C 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 C 170 PHE LEU LEU VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 C 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 C 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 C 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 C 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 C 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 C 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 14 C 170 LYS
HET GDP A 201 38
HET 21S B 201 45
HET GDP B 202 38
HET GDP C 201 38
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM 21S N-{1-[N-(5,7-DICHLORO-2,1,3-BENZOTHIADIAZOL-4-YL)
HETNAM 2 21S GLYCYL]PIPERIDIN-4-YL}ETHANESULFONAMIDE
FORMUL 4 GDP 3(C10 H15 N5 O11 P2)
FORMUL 5 21S C15 H19 CL2 N5 O3 S2
FORMUL 8 HOH *314(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 TYR A 64 GLY A 75 1 12
HELIX 3 3 ASN A 86 ASP A 92 1 7
HELIX 4 4 ASP A 92 ASP A 105 1 14
HELIX 5 5 ASP A 126 GLY A 138 1 13
HELIX 6 6 GLY A 151 GLU A 168 1 18
HELIX 7 7 GLY B 15 ASN B 26 1 12
HELIX 8 8 TYR B 64 GLY B 75 1 12
HELIX 9 9 ASN B 86 ASP B 92 1 7
HELIX 10 10 ASP B 92 LYS B 104 1 13
HELIX 11 11 ASP B 126 GLY B 138 1 13
HELIX 12 12 GLY B 151 LYS B 169 1 19
HELIX 13 13 GLY C 15 ASN C 26 1 12
HELIX 14 14 ASP C 69 GLY C 75 1 7
HELIX 15 15 ASN C 86 ASP C 105 1 20
HELIX 16 16 ASP C 126 GLY C 138 1 13
HELIX 17 17 GLY C 151 LYS C 167 1 17
SHEET 1 A 6 SER A 39 ILE A 46 0
SHEET 2 A 6 GLU A 49 THR A 58 -1 O SER A 51 N VAL A 44
SHEET 3 A 6 THR A 2 VAL A 9 1 N VAL A 8 O LEU A 56
SHEET 4 A 6 GLY A 77 ALA A 83 1 O VAL A 81 N VAL A 9
SHEET 5 A 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 A 6 PHE A 141 GLU A 143 1 O ILE A 142 N LEU A 113
SHEET 1 B 6 ARG B 41 ILE B 46 0
SHEET 2 B 6 GLU B 49 ILE B 55 -1 O SER B 51 N VAL B 44
SHEET 3 B 6 THR B 2 GLY B 10 1 N TYR B 4 O LEU B 52
SHEET 4 B 6 GLY B 77 ALA B 83 1 O LEU B 79 N VAL B 9
SHEET 5 B 6 MET B 111 ASN B 116 1 O ASN B 116 N PHE B 82
SHEET 6 B 6 PHE B 141 GLU B 143 1 O ILE B 142 N LEU B 113
SHEET 1 C 6 TYR C 40 ILE C 46 0
SHEET 2 C 6 GLU C 49 ASP C 57 -1 O LEU C 53 N LYS C 42
SHEET 3 C 6 THR C 2 VAL C 9 1 N TYR C 4 O ASP C 54
SHEET 4 C 6 GLY C 77 ALA C 83 1 O VAL C 81 N VAL C 9
SHEET 5 C 6 MET C 111 ASN C 116 1 O VAL C 114 N LEU C 80
SHEET 6 C 6 PHE C 141 GLU C 143 1 O ILE C 142 N LEU C 113
LINK SG CYS B 12 C14 21S B 201 1555 1555 1.83
SITE 1 AC1 26 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 26 SER A 17 ALA A 18 PHE A 28 VAL A 29
SITE 3 AC1 26 ASP A 30 ASN A 116 LYS A 117 ASP A 119
SITE 4 AC1 26 LEU A 120 SER A 145 ALA A 146 LYS A 147
SITE 5 AC1 26 HOH A 324 HOH A 331 HOH A 343 HOH A 345
SITE 6 AC1 26 HOH A 357 HOH A 359 HOH A 361 HOH A 400
SITE 7 AC1 26 HOH A 403 HOH A 430
SITE 1 AC2 10 VAL B 8 VAL B 9 GLY B 10 CYS B 12
SITE 2 AC2 10 THR B 58 GLU B 62 ARG B 68 TYR B 71
SITE 3 AC2 10 TYR B 96 GLN B 99
SITE 1 AC3 22 GLY B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC3 22 SER B 17 ALA B 18 PHE B 28 ASN B 116
SITE 3 AC3 22 LYS B 117 ASP B 119 LEU B 120 SER B 145
SITE 4 AC3 22 ALA B 146 LYS B 147 HOH B 353 HOH B 364
SITE 5 AC3 22 HOH B 369 HOH B 397 HOH B 406 HOH B 409
SITE 6 AC3 22 HOH B 410 HOH B 412
SITE 1 AC4 16 GLY C 13 VAL C 14 GLY C 15 LYS C 16
SITE 2 AC4 16 SER C 17 ALA C 18 PHE C 28 ALA C 59
SITE 3 AC4 16 ASN C 116 LYS C 117 ASP C 119 SER C 145
SITE 4 AC4 16 ALA C 146 LYS C 147 HOH C 311 HOH C 327
CRYST1 68.121 83.540 86.224 90.00 110.88 90.00 C 1 2 1 12
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 0.014680 0.000000 0.005600 0.00000
SCALE2 0.000000 0.011970 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012413 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
