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HEADER HYDROLASE 08-FEB-22 7R4E
TITLE RVX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
TITLE 2 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: RVX PHOSPHYLATION PRODUCT COVALENTLY ATTACHED TO
COMPND 8 SER203
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL: HEK293F;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, TERNARY COMPLEX, REACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM
REVDAT 1 27-APR-22 7R4E 0
JRNL AUTH C.LINDGREN,N.FORSGREN,N.HOSTER,C.AKFUR,E.ARTURSSON,
JRNL AUTH 2 L.EDVINSSON,R.SVENSSON,F.WOREK,F.EKSTROM,A.LINUSSON
JRNL TITL BROAD-SPECTRUM ANTIDOTE DISCOVERY BY UNTANGLING THE
JRNL TITL 2 REACTIVATION MECHANISM OF NERVE AGENT INHIBITED
JRNL TITL 3 ACETYLCHOLINESTERASE.
JRNL REF CHEMISTRY 2022
JRNL REFN ISSN 0947-6539
JRNL PMID 35420233
JRNL DOI 10.1002/CHEM.202200678
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.335
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 40697
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.949
REMARK 3 FREE R VALUE TEST SET COUNT : 793
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 29.1069 - 5.4415 1.00 6939 135 0.1589 0.1899
REMARK 3 2 5.4415 - 4.3236 1.00 6702 132 0.1346 0.1468
REMARK 3 3 4.3236 - 3.7784 1.00 6595 125 0.1470 0.1991
REMARK 3 4 3.7784 - 3.4335 0.99 6578 142 0.1748 0.2267
REMARK 3 5 3.4335 - 3.1878 1.00 6571 115 0.2031 0.2653
REMARK 3 6 3.1878 - 3.0000 0.99 6519 144 0.2230 0.2949
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) : 0.315
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.787
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.45
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 : 0.009 8837
REMARK 3 ANGLE : 1.044 12057
REMARK 3 CHIRALITY : 0.057 1289
REMARK 3 PLANARITY : 0.007 1576
REMARK 3 DIHEDRAL : 12.553 7088
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6333 13.6036 44.2823
REMARK 3 T TENSOR
REMARK 3 T11: 0.5795 T22: 0.5448
REMARK 3 T33: 0.3358 T12: 0.0053
REMARK 3 T13: 0.0444 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 2.0336 L22: 1.7318
REMARK 3 L33: 5.7225 L12: 0.4778
REMARK 3 L13: -1.0739 L23: -0.2573
REMARK 3 S TENSOR
REMARK 3 S11: -0.5637 S12: -0.6587 S13: 0.3418
REMARK 3 S21: 0.6552 S22: 0.3736 S23: 0.0607
REMARK 3 S31: -0.1751 S32: -0.3990 S33: -0.0270
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1609 15.3259 27.9661
REMARK 3 T TENSOR
REMARK 3 T11: 0.3216 T22: 0.3459
REMARK 3 T33: 0.2144 T12: 0.0012
REMARK 3 T13: -0.0258 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 3.5245 L22: 2.0639
REMARK 3 L33: 5.3475 L12: 0.2262
REMARK 3 L13: -0.4336 L23: -0.5621
REMARK 3 S TENSOR
REMARK 3 S11: -0.1560 S12: -0.2158 S13: 0.2342
REMARK 3 S21: 0.1686 S22: 0.1112 S23: -0.0257
REMARK 3 S31: -0.0035 S32: 0.1141 S33: 0.0179
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1299 3.0860 21.1794
REMARK 3 T TENSOR
REMARK 3 T11: 0.4120 T22: 0.2245
REMARK 3 T33: 0.2919 T12: 0.0536
REMARK 3 T13: -0.0164 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 4.1644 L22: 1.6534
REMARK 3 L33: 5.3510 L12: 0.9523
REMARK 3 L13: -0.2028 L23: -0.5406
REMARK 3 S TENSOR
REMARK 3 S11: -0.1123 S12: -0.1055 S13: -0.4225
REMARK 3 S21: 0.0642 S22: 0.0918 S23: -0.1457
REMARK 3 S31: 0.5679 S32: -0.0095 S33: 0.0548
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9405 16.2017 10.5695
REMARK 3 T TENSOR
REMARK 3 T11: 0.4079 T22: 0.6275
REMARK 3 T33: 0.3579 T12: 0.0395
REMARK 3 T13: 0.0151 T23: 0.0905
REMARK 3 L TENSOR
REMARK 3 L11: 4.3202 L22: 1.7201
REMARK 3 L33: 4.7017 L12: 1.9107
REMARK 3 L13: 0.6048 L23: 0.4325
REMARK 3 S TENSOR
REMARK 3 S11: -0.4060 S12: 0.8688 S13: 0.2890
REMARK 3 S21: -0.3052 S22: 0.1645 S23: -0.2866
REMARK 3 S31: -0.2766 S32: 0.7643 S33: 0.1465
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9286 -0.9766 11.1923
REMARK 3 T TENSOR
REMARK 3 T11: 0.6244 T22: 0.3356
REMARK 3 T33: 0.4567 T12: -0.0304
REMARK 3 T13: 0.0470 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 6.4991 L22: 0.4548
REMARK 3 L33: 4.4486 L12: -0.5240
REMARK 3 L13: 0.6026 L23: 0.2433
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: 0.2985 S13: -1.1284
REMARK 3 S21: -0.2907 S22: 0.0342 S23: 0.2070
REMARK 3 S31: 0.8754 S32: 0.4628 S33: 0.0361
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4321 21.7321 -3.9839
REMARK 3 T TENSOR
REMARK 3 T11: 0.3338 T22: 0.4806
REMARK 3 T33: 0.2759 T12: -0.0321
REMARK 3 T13: -0.0613 T23: 0.0886
REMARK 3 L TENSOR
REMARK 3 L11: 3.1388 L22: 8.5341
REMARK 3 L33: 4.0064 L12: -1.6876
REMARK 3 L13: -1.9180 L23: 2.8043
REMARK 3 S TENSOR
REMARK 3 S11: 0.1656 S12: 0.1268 S13: 0.1810
REMARK 3 S21: -0.6090 S22: 0.0729 S23: -0.1768
REMARK 3 S31: -0.3103 S32: 0.1172 S33: -0.2143
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2934 13.8841 2.4931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2644 T22: 0.4960
REMARK 3 T33: 0.3056 T12: -0.0731
REMARK 3 T13: -0.0595 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 1.2899 L22: 2.4025
REMARK 3 L33: 4.0313 L12: -0.1601
REMARK 3 L13: 0.1012 L23: -0.4248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0959 S12: 0.2278 S13: -0.0502
REMARK 3 S21: -0.2202 S22: 0.0417 S23: 0.2190
REMARK 3 S31: 0.2546 S32: -0.2737 S33: -0.1393
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 441 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3682 16.9504 20.5949
REMARK 3 T TENSOR
REMARK 3 T11: 0.3214 T22: 0.6619
REMARK 3 T33: 0.3636 T12: 0.0235
REMARK 3 T13: -0.0022 T23: 0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 1.3749 L22: 3.0549
REMARK 3 L33: 4.4670 L12: -0.0226
REMARK 3 L13: 0.4943 L23: -1.0961
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: -0.1879 S13: 0.0163
REMARK 3 S21: 0.0527 S22: 0.1148 S23: 0.4508
REMARK 3 S31: -0.0632 S32: -0.9949 S33: -0.1561
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1624 1.1601 13.5060
REMARK 3 T TENSOR
REMARK 3 T11: 0.4090 T22: 0.7450
REMARK 3 T33: 0.5314 T12: -0.2473
REMARK 3 T13: -0.0360 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 5.0790 L22: 8.0260
REMARK 3 L33: 4.4010 L12: -1.1009
REMARK 3 L13: 2.8013 L23: -0.7381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.1112 S13: -0.7158
REMARK 3 S21: -0.1142 S22: 0.1621 S23: 0.9039
REMARK 3 S31: 0.5129 S32: -1.6026 S33: 0.0769
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2528 6.1997 -1.5407
REMARK 3 T TENSOR
REMARK 3 T11: 0.5557 T22: 0.7386
REMARK 3 T33: 0.3403 T12: 0.0208
REMARK 3 T13: -0.1834 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 0.9232 L22: 3.1101
REMARK 3 L33: 9.3988 L12: -0.3465
REMARK 3 L13: -2.5473 L23: 3.1724
REMARK 3 S TENSOR
REMARK 3 S11: 0.1152 S12: 0.1845 S13: -0.1391
REMARK 3 S21: -0.4575 S22: -0.1758 S23: 0.1680
REMARK 3 S31: 0.2149 S32: -0.3925 S33: 0.0540
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8430 5.9741 -61.9762
REMARK 3 T TENSOR
REMARK 3 T11: 0.4752 T22: 0.7260
REMARK 3 T33: 0.3749 T12: 0.0156
REMARK 3 T13: -0.0949 T23: -0.1625
REMARK 3 L TENSOR
REMARK 3 L11: 4.4271 L22: 1.3373
REMARK 3 L33: 4.1920 L12: -1.1420
REMARK 3 L13: -1.5312 L23: 0.0106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1868 S12: 0.8588 S13: -0.1638
REMARK 3 S21: -0.1264 S22: -0.1952 S23: 0.3608
REMARK 3 S31: -0.2184 S32: -0.7860 S33: -0.0332
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6896 1.2215 -51.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.4093 T22: 0.5798
REMARK 3 T33: 0.3067 T12: -0.0461
REMARK 3 T13: -0.0600 T23: -0.1013
REMARK 3 L TENSOR
REMARK 3 L11: 1.4567 L22: 2.4088
REMARK 3 L33: 4.2041 L12: -0.1077
REMARK 3 L13: 0.2742 L23: 0.6872
REMARK 3 S TENSOR
REMARK 3 S11: 0.0624 S12: 0.2430 S13: -0.2072
REMARK 3 S21: 0.0740 S22: -0.2167 S23: 0.2603
REMARK 3 S31: 0.4380 S32: -0.3266 S33: 0.1005
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5008 2.9453 -47.9872
REMARK 3 T TENSOR
REMARK 3 T11: 0.4097 T22: 0.6087
REMARK 3 T33: 0.2924 T12: 0.0078
REMARK 3 T13: -0.0566 T23: -0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 2.7328 L22: 4.1060
REMARK 3 L33: 3.1490 L12: -1.9022
REMARK 3 L13: 0.1670 L23: 0.5347
REMARK 3 S TENSOR
REMARK 3 S11: 0.1432 S12: 0.0705 S13: -0.0985
REMARK 3 S21: 0.0503 S22: 0.0320 S23: -0.3130
REMARK 3 S31: 0.2923 S32: 0.5142 S33: -0.1522
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2459 10.6260 -37.0414
REMARK 3 T TENSOR
REMARK 3 T11: 0.4082 T22: 0.6519
REMARK 3 T33: 0.3784 T12: -0.0621
REMARK 3 T13: -0.1146 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 2.0017 L22: 1.8784
REMARK 3 L33: 2.8597 L12: -0.7374
REMARK 3 L13: -0.0523 L23: 0.0122
REMARK 3 S TENSOR
REMARK 3 S11: 0.3145 S12: 0.1068 S13: 0.1521
REMARK 3 S21: 0.0797 S22: -0.1787 S23: -0.1788
REMARK 3 S31: -0.1072 S32: 0.4800 S33: -0.1208
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3653 -5.2915 -18.3442
REMARK 3 T TENSOR
REMARK 3 T11: 0.8279 T22: 0.4553
REMARK 3 T33: 0.3395 T12: -0.0352
REMARK 3 T13: -0.1274 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 6.2569 L22: 4.5581
REMARK 3 L33: 2.8353 L12: 2.4268
REMARK 3 L13: 1.8854 L23: 0.2583
REMARK 3 S TENSOR
REMARK 3 S11: 0.4151 S12: -0.6674 S13: -0.4022
REMARK 3 S21: 0.3252 S22: -0.1231 S23: -0.0903
REMARK 3 S31: 0.6491 S32: -0.2106 S33: -0.3301
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1931 8.3939 -33.4674
REMARK 3 T TENSOR
REMARK 3 T11: 0.4176 T22: 0.5315
REMARK 3 T33: 0.3028 T12: 0.0099
REMARK 3 T13: 0.0092 T23: -0.1409
REMARK 3 L TENSOR
REMARK 3 L11: 2.7454 L22: 3.6695
REMARK 3 L33: 4.2914 L12: 0.8748
REMARK 3 L13: -0.2101 L23: -0.4860
REMARK 3 S TENSOR
REMARK 3 S11: 0.1587 S12: -0.1109 S13: 0.0402
REMARK 3 S21: 0.0393 S22: -0.1008 S23: 0.4064
REMARK 3 S31: 0.2722 S32: -0.6730 S33: -0.0652
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7830 22.3711 -28.9014
REMARK 3 T TENSOR
REMARK 3 T11: 0.4549 T22: 0.3749
REMARK 3 T33: 0.3331 T12: 0.0231
REMARK 3 T13: 0.0214 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 5.0362 L22: 7.2481
REMARK 3 L33: 9.0981 L12: -0.0331
REMARK 3 L13: 2.4339 L23: -2.1781
REMARK 3 S TENSOR
REMARK 3 S11: 0.5115 S12: -0.2789 S13: 0.5395
REMARK 3 S21: -0.0253 S22: -0.0758 S23: 0.5575
REMARK 3 S31: -0.1607 S32: -0.4506 S33: -0.4401
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8481 11.5854 -21.7175
REMARK 3 T TENSOR
REMARK 3 T11: 0.6252 T22: 0.7450
REMARK 3 T33: 0.2499 T12: -0.0207
REMARK 3 T13: 0.0278 T23: -0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 5.1644 L22: 1.5566
REMARK 3 L33: 3.3503 L12: -0.3300
REMARK 3 L13: 4.1463 L23: -0.4912
REMARK 3 S TENSOR
REMARK 3 S11: -0.1599 S12: 0.1254 S13: -0.0872
REMARK 3 S21: 0.2309 S22: -0.0820 S23: -0.0896
REMARK 3 S31: 0.3297 S32: 0.3702 S33: 0.2736
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 7R4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40881
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.107
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-30 % (W/V) PEG750MME 0.1 M HEPES PH
REMARK 280 7.0-7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.47800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.77450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.49850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.77450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.47800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.49850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 THR B 543
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 323 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 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 ARG A 3 31.10 -98.98
REMARK 500 PHE A 47 -11.83 78.18
REMARK 500 PHE A 80 116.74 -161.01
REMARK 500 ASP A 95 93.54 -64.69
REMARK 500 CYS A 96 3.05 -152.89
REMARK 500 TYR A 133 31.83 -96.78
REMARK 500 RVX A 203 -120.83 50.42
REMARK 500 CYS A 257 76.37 -118.12
REMARK 500 ASP A 306 -80.51 -123.58
REMARK 500 PHE A 321 28.15 -140.75
REMARK 500 ASP A 323 42.48 -76.26
REMARK 500 VAL A 407 -65.75 -138.04
REMARK 500 ASP A 488 113.00 -170.43
REMARK 500 ARG A 493 49.02 -88.17
REMARK 500 ASP A 494 93.13 -170.97
REMARK 500 GLN A 508 56.10 33.49
REMARK 500 ALA A 542 50.77 -98.23
REMARK 500 PRO B 41 48.87 -86.34
REMARK 500 ALA B 109 -70.23 -63.47
REMARK 500 PHE B 123 12.18 56.85
REMARK 500 ALA B 127 143.53 -175.47
REMARK 500 ALA B 167 64.87 -156.81
REMARK 500 RVX B 203 -122.78 59.47
REMARK 500 HIS B 223 -30.81 -132.44
REMARK 500 THR B 275 37.11 -92.87
REMARK 500 THR B 275 37.11 -94.89
REMARK 500 TRP B 286 2.17 -63.42
REMARK 500 PRO B 301 158.98 -49.90
REMARK 500 ASP B 306 -87.13 -103.28
REMARK 500 TYR B 341 32.62 -96.96
REMARK 500 SER B 347 139.83 173.95
REMARK 500 VAL B 367 75.23 -119.07
REMARK 500 VAL B 407 -63.91 -130.23
REMARK 500 HIS B 447 104.41 -58.18
REMARK 500 PRO B 498 90.97 -53.16
REMARK 500 SER B 541 49.45 -84.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 I1X A 601
REMARK 610 I1X B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7QYN RELATED DB: PDB
REMARK 900 7QYN CONTAINS THE NON-INHIBITED PROTEIN IN COMPLEX WITH THE SAME
REMARK 900 REACTIVATOR
REMARK 900 RELATED ID: 7R0A RELATED DB: PDB
REMARK 900 7R0A CONTAINS THE SAME PROTEIN, ALBEIT SARIN-INHIBITED, IN COMPLEX
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)
REMARK 900 PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R2F RELATED DB: PDB
REMARK 900 7R2F CONTAINS THE SAME PROTEIN, ALBEIT TABUN-INHIBITED, IN COMPLEX
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)
REMARK 900 PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R3C RELATED DB: PDB
REMARK 900 7R3C CONTAINS THE SAME PROTEIN, ALBEIT VX-INHIBITED, IN COMPLEX
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)
REMARK 900 PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R02 RELATED DB: PDB
REMARK 900 7R02 CONTAINS THE NON-INHIBITED PROTEIN IN COMPLEX WITH N-(3-
REMARK 900 (DIETHYLAMINO)PROPYL)-4-METHYL-3-NITROBENZAMIDE
DBREF 7R4E A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7R4E B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU RVX ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU RVX ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
MODRES 7R4E RVX A 203 SER MODIFIED RESIDUE
MODRES 7R4E RVX B 203 SER MODIFIED RESIDUE
HET RVX A 203 14
HET RVX B 203 14
HET I1X A 601 16
HET NAG A 602 14
HET NAG A 603 14
HET PG0 A 604 8
HET PG0 A 605 8
HET TOE A 606 11
HET TOE A 607 11
HET P15 A 608 20
HET I1X B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET PG0 B 604 8
HET PG0 B 605 8
HET PG0 B 606 8
HET TOE B 607 11
HETNAM RVX O-[METHYL(2-METHYLPROPOXY)PHOSPHORYL]-L-SERINE
HETNAM I1X 4-METHYL-3-NITRO-~{N}-[(2~{E},4~{E})-5-[2-
HETNAM 2 I1X [(OXIDANYLAMINO)METHYL]PYRIDIN-1-YL]PENTA-2,4-
HETNAM 3 I1X DIENYL]BENZAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN PG0 PEG 6000
FORMUL 1 RVX 2(C8 H18 N O5 P)
FORMUL 3 I1X 2(C19 H23 N4 O4 1+)
FORMUL 4 NAG 4(C8 H15 N O6)
FORMUL 6 PG0 5(C5 H12 O3)
FORMUL 8 TOE 3(C7 H16 O4)
FORMUL 10 P15 C13 H28 O7
FORMUL 18 HOH *121(H2 O)
HELIX 1 AA1 VAL A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 GLY A 143 1 9
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 ILE A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 RVX A 203 SER A 215 1 13
HELIX 9 AA9 LEU A 216 LEU A 221 5 6
HELIX 10 AB1 ALA A 241 VAL A 255 1 15
HELIX 11 AB2 ASP A 266 THR A 275 1 10
HELIX 12 AB3 PRO A 277 TRP A 286 1 10
HELIX 13 AB4 HIS A 287 LEU A 289 5 3
HELIX 14 AB5 THR A 311 GLY A 319 1 9
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 GLY A 456 1 7
HELIX 22 AC4 LEU A 457 ASN A 464 5 8
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 ALA A 542 1 9
HELIX 26 AC8 ASP B 5 GLN B 7 5 3
HELIX 27 AC9 VAL B 42 ARG B 46 5 5
HELIX 28 AD1 PHE B 80 MET B 85 1 6
HELIX 29 AD2 LEU B 130 ASP B 134 5 5
HELIX 30 AD3 GLY B 135 GLY B 143 1 9
HELIX 31 AD4 GLY B 154 LEU B 159 1 6
HELIX 32 AD5 ASN B 170 ILE B 187 1 18
HELIX 33 AD6 ALA B 188 PHE B 190 5 3
HELIX 34 AD7 RVX B 203 LEU B 214 1 12
HELIX 35 AD8 SER B 215 PHE B 222 5 8
HELIX 36 AD9 ALA B 241 LEU B 254 1 14
HELIX 37 AE1 ASP B 266 THR B 275 1 10
HELIX 38 AE2 PRO B 277 ASP B 283 1 7
HELIX 39 AE3 HIS B 284 VAL B 288 5 5
HELIX 40 AE4 THR B 311 GLY B 319 1 9
HELIX 41 AE5 SER B 336 GLY B 342 5 7
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASN B 464 5 9
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 SER B 541 1 17
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 VAL A 520 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 239 SER A 240 0
SHEET 2 AA3 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA511 ILE B 20 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O THR B 198 N ILE B 116
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 SER B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.07
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.08
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.08
LINK C GLU A 202 N RVX A 203 1555 1555 1.33
LINK C RVX A 203 N ALA A 204 1555 1555 1.33
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A 603 1555 1555 1.47
LINK C GLU B 202 N RVX B 203 1555 1555 1.33
LINK C RVX B 203 N ALA B 204 1555 1555 1.33
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.47
LINK ND2 ASN B 464 C1 NAG B 603 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -7.30
CISPEP 2 TYR B 105 PRO B 106 0 9.31
CISPEP 3 CYS B 257 PRO B 258 0 7.09
CRYST1 78.956 110.997 227.549 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012665 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004395 0.00000
TER 4218 THR A 543
TER 8405 ALA B 542
MASTER 579 0 17 50 34 0 0 6 8645 2 227 84
END |