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HEADER HYDROLASE 01-FEB-22 7R0A
TITLE STRUCTURE OF SARIN PHOSPHONYLATED ACETYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
TITLE 3 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: SARIN PHOSPHONYLATION 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_LINE: HEK293F;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, COMPLEX, SARIN PHOSPHONYLATED, REACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM
REVDAT 1 27-APR-22 7R0A 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. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 48485
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.970
REMARK 3 FREE R VALUE TEST SET COUNT : 956
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 45.9716 - 5.3538 1.00 7109 137 0.1597 0.1874
REMARK 3 2 5.3538 - 4.2504 1.00 6845 138 0.1368 0.1605
REMARK 3 3 4.2504 - 3.7134 1.00 6767 122 0.1510 0.2464
REMARK 3 4 3.7134 - 3.3740 1.00 6747 148 0.1782 0.2210
REMARK 3 5 3.3740 - 3.1322 1.00 6743 115 0.2130 0.2632
REMARK 3 6 3.1322 - 2.9476 1.00 6681 157 0.2182 0.3154
REMARK 3 7 2.9476 - 2.8000 1.00 6637 139 0.2383 0.2727
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.17
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 9058
REMARK 3 ANGLE : 1.145 12386
REMARK 3 CHIRALITY : 0.047 1339
REMARK 3 PLANARITY : 0.007 1627
REMARK 3 DIHEDRAL : 16.020 3330
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0071 12.6067 41.4258
REMARK 3 T TENSOR
REMARK 3 T11: 0.4932 T22: 0.3545
REMARK 3 T33: 0.2868 T12: -0.0476
REMARK 3 T13: -0.0411 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 2.7015 L22: 1.7033
REMARK 3 L33: 4.0591 L12: -1.1566
REMARK 3 L13: -0.3910 L23: -0.8404
REMARK 3 S TENSOR
REMARK 3 S11: -0.1500 S12: -0.4767 S13: 0.0458
REMARK 3 S21: 0.3673 S22: 0.2077 S23: 0.0386
REMARK 3 S31: -0.1674 S32: -0.0150 S33: -0.1023
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1613 10.3778 23.7765
REMARK 3 T TENSOR
REMARK 3 T11: 0.3025 T22: 0.2289
REMARK 3 T33: 0.2233 T12: 0.0005
REMARK 3 T13: -0.0397 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 1.9450 L22: 1.4375
REMARK 3 L33: 3.4725 L12: -0.0942
REMARK 3 L13: -0.3111 L23: -0.2910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0268 S12: -0.2566 S13: -0.0877
REMARK 3 S21: 0.1217 S22: 0.0075 S23: -0.0192
REMARK 3 S31: 0.2234 S32: 0.0503 S33: 0.0297
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5902 17.1170 11.8184
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.4379
REMARK 3 T33: 0.3157 T12: 0.0512
REMARK 3 T13: 0.0413 T23: 0.1011
REMARK 3 L TENSOR
REMARK 3 L11: 3.3101 L22: 2.2117
REMARK 3 L33: 5.6325 L12: 1.5830
REMARK 3 L13: 3.7466 L23: 0.5561
REMARK 3 S TENSOR
REMARK 3 S11: -0.2047 S12: 0.3950 S13: 0.0520
REMARK 3 S21: 0.0600 S22: -0.0123 S23: -0.2140
REMARK 3 S31: -0.2624 S32: 0.8807 S33: 0.2084
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0338 -1.9950 11.4151
REMARK 3 T TENSOR
REMARK 3 T11: 0.5622 T22: 0.3298
REMARK 3 T33: 0.2933 T12: -0.0487
REMARK 3 T13: 0.0196 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 8.8705 L22: 2.9901
REMARK 3 L33: 2.3342 L12: 0.5130
REMARK 3 L13: -0.6352 L23: 0.9470
REMARK 3 S TENSOR
REMARK 3 S11: -0.2937 S12: 0.1857 S13: -1.2072
REMARK 3 S21: 0.0442 S22: 0.1812 S23: -0.1339
REMARK 3 S31: 0.8272 S32: -0.0146 S33: 0.0578
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5218 16.8128 5.8577
REMARK 3 T TENSOR
REMARK 3 T11: 0.2085 T22: 0.3106
REMARK 3 T33: 0.2959 T12: -0.0322
REMARK 3 T13: -0.0492 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.6190 L22: 1.6297
REMARK 3 L33: 4.3401 L12: -0.1058
REMARK 3 L13: -0.1040 L23: -0.5655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: 0.0811 S13: 0.0222
REMARK 3 S21: -0.1257 S22: 0.0024 S23: 0.2125
REMARK 3 S31: -0.0273 S32: -0.3987 S33: -0.0565
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4728 1.1793 13.4614
REMARK 3 T TENSOR
REMARK 3 T11: 0.4715 T22: 0.7980
REMARK 3 T33: 0.4997 T12: -0.2983
REMARK 3 T13: 0.0011 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 4.4620 L22: 7.5417
REMARK 3 L33: 3.3629 L12: -1.5666
REMARK 3 L13: 2.8450 L23: -1.1830
REMARK 3 S TENSOR
REMARK 3 S11: -0.1834 S12: -0.2154 S13: -0.6816
REMARK 3 S21: 0.1491 S22: 0.1190 S23: 0.8750
REMARK 3 S31: 0.5191 S32: -1.6186 S33: 0.2136
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4986 6.1620 -0.4384
REMARK 3 T TENSOR
REMARK 3 T11: 0.4676 T22: 0.6074
REMARK 3 T33: 0.3611 T12: -0.0037
REMARK 3 T13: -0.2040 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.7232 L22: 2.6319
REMARK 3 L33: 7.9018 L12: -0.5888
REMARK 3 L13: -2.0706 L23: 2.7333
REMARK 3 S TENSOR
REMARK 3 S11: 0.1658 S12: 0.0316 S13: -0.2913
REMARK 3 S21: -0.3999 S22: -0.2663 S23: 0.3025
REMARK 3 S31: 0.3173 S32: -0.3955 S33: 0.1186
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6334 6.1985 -62.0470
REMARK 3 T TENSOR
REMARK 3 T11: 0.4806 T22: 0.4817
REMARK 3 T33: 0.3547 T12: 0.0293
REMARK 3 T13: -0.1102 T23: -0.1325
REMARK 3 L TENSOR
REMARK 3 L11: 5.9381 L22: 2.3941
REMARK 3 L33: 6.2324 L12: -0.9902
REMARK 3 L13: -2.4904 L23: 0.2331
REMARK 3 S TENSOR
REMARK 3 S11: 0.3851 S12: 0.6840 S13: 0.0341
REMARK 3 S21: -0.3102 S22: -0.1913 S23: 0.2455
REMARK 3 S31: 0.0391 S32: -0.8894 S33: -0.1957
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6183 -4.1959 -53.4294
REMARK 3 T TENSOR
REMARK 3 T11: 0.5800 T22: 0.5132
REMARK 3 T33: 0.3057 T12: -0.0243
REMARK 3 T13: -0.0458 T23: -0.1554
REMARK 3 L TENSOR
REMARK 3 L11: 0.8125 L22: 1.6398
REMARK 3 L33: 3.4441 L12: -0.3697
REMARK 3 L13: 0.0172 L23: -0.1125
REMARK 3 S TENSOR
REMARK 3 S11: 0.1904 S12: 0.1988 S13: -0.1332
REMARK 3 S21: -0.1800 S22: -0.2596 S23: 0.2224
REMARK 3 S31: 0.7292 S32: -0.0613 S33: 0.0461
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8844 4.2174 -50.9168
REMARK 3 T TENSOR
REMARK 3 T11: 0.4029 T22: 0.4333
REMARK 3 T33: 0.2272 T12: -0.0016
REMARK 3 T13: -0.0623 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 3.3056 L22: 2.2111
REMARK 3 L33: 3.2850 L12: 0.5034
REMARK 3 L13: 0.2949 L23: 0.4401
REMARK 3 S TENSOR
REMARK 3 S11: 0.1380 S12: 0.3575 S13: -0.0787
REMARK 3 S21: -0.4065 S22: -0.2380 S23: 0.3268
REMARK 3 S31: 0.2373 S32: -0.6013 S33: 0.1215
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4908 7.0062 -54.2203
REMARK 3 T TENSOR
REMARK 3 T11: 0.3284 T22: 0.4102
REMARK 3 T33: 0.2375 T12: 0.0135
REMARK 3 T13: -0.0529 T23: -0.1078
REMARK 3 L TENSOR
REMARK 3 L11: 6.0848 L22: 4.4532
REMARK 3 L33: 3.5422 L12: -3.4353
REMARK 3 L13: 1.0240 L23: -0.7271
REMARK 3 S TENSOR
REMARK 3 S11: 0.3043 S12: 0.6407 S13: -0.2787
REMARK 3 S21: -0.2916 S22: -0.1377 S23: 0.0932
REMARK 3 S31: -0.0103 S32: 0.4292 S33: -0.1630
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0007 8.3706 -44.3915
REMARK 3 T TENSOR
REMARK 3 T11: 0.3874 T22: 0.4152
REMARK 3 T33: 0.1913 T12: -0.0232
REMARK 3 T13: -0.0237 T23: -0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 2.9269 L22: 2.1811
REMARK 3 L33: 3.5199 L12: -1.0095
REMARK 3 L13: 0.0068 L23: 0.5333
REMARK 3 S TENSOR
REMARK 3 S11: 0.2053 S12: 0.2095 S13: -0.0586
REMARK 3 S21: -0.1083 S22: -0.0999 S23: -0.1122
REMARK 3 S31: -0.0716 S32: 0.5344 S33: -0.0883
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3624 -9.4632 -47.4196
REMARK 3 T TENSOR
REMARK 3 T11: 0.6090 T22: 0.5666
REMARK 3 T33: 0.4337 T12: 0.1897
REMARK 3 T13: -0.1410 T23: -0.0670
REMARK 3 L TENSOR
REMARK 3 L11: 1.6817 L22: 3.5028
REMARK 3 L33: 2.5980 L12: -0.9404
REMARK 3 L13: -1.9104 L23: 2.0704
REMARK 3 S TENSOR
REMARK 3 S11: -0.2068 S12: 0.1328 S13: -0.2600
REMARK 3 S21: -0.0001 S22: 0.1093 S23: -0.1433
REMARK 3 S31: 0.9966 S32: 0.6411 S33: 0.2245
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7981 14.6824 -40.1664
REMARK 3 T TENSOR
REMARK 3 T11: 0.4483 T22: 0.4054
REMARK 3 T33: 0.3827 T12: -0.0374
REMARK 3 T13: -0.1051 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 5.8104 L22: 3.4108
REMARK 3 L33: 4.7372 L12: -3.1843
REMARK 3 L13: -2.9678 L23: 1.6090
REMARK 3 S TENSOR
REMARK 3 S11: 0.3835 S12: 0.0029 S13: 0.8781
REMARK 3 S21: -0.0973 S22: -0.2026 S23: -0.6455
REMARK 3 S31: -0.4235 S32: 0.5962 S33: -0.1547
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3746 -6.5942 -21.9612
REMARK 3 T TENSOR
REMARK 3 T11: 0.7087 T22: 0.3118
REMARK 3 T33: 0.3501 T12: -0.0053
REMARK 3 T13: -0.1023 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 5.2288 L22: 3.8526
REMARK 3 L33: 3.7984 L12: 0.2091
REMARK 3 L13: 1.0385 L23: -0.0913
REMARK 3 S TENSOR
REMARK 3 S11: 0.3380 S12: -0.0977 S13: -0.6210
REMARK 3 S21: 0.2896 S22: 0.0313 S23: 0.0503
REMARK 3 S31: 0.7232 S32: 0.0874 S33: -0.3799
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8445 4.8181 -24.4069
REMARK 3 T TENSOR
REMARK 3 T11: 0.4623 T22: 0.3274
REMARK 3 T33: 0.2165 T12: -0.0667
REMARK 3 T13: -0.0283 T23: -0.0944
REMARK 3 L TENSOR
REMARK 3 L11: 2.5636 L22: 2.8732
REMARK 3 L33: 2.5547 L12: -0.0278
REMARK 3 L13: -0.2548 L23: -1.2380
REMARK 3 S TENSOR
REMARK 3 S11: 0.2718 S12: -0.1510 S13: -0.1980
REMARK 3 S21: 0.4772 S22: -0.1714 S23: -0.0623
REMARK 3 S31: 0.0498 S32: 0.0459 S33: -0.0916
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4833 6.1514 -35.4143
REMARK 3 T TENSOR
REMARK 3 T11: 0.4125 T22: 0.4809
REMARK 3 T33: 0.3162 T12: -0.0171
REMARK 3 T13: 0.0234 T23: -0.1365
REMARK 3 L TENSOR
REMARK 3 L11: 3.1675 L22: 5.1924
REMARK 3 L33: 6.7095 L12: 0.0701
REMARK 3 L13: 1.0328 L23: -2.4458
REMARK 3 S TENSOR
REMARK 3 S11: 0.1710 S12: -0.0975 S13: -0.1606
REMARK 3 S21: 0.3007 S22: -0.0356 S23: 0.4913
REMARK 3 S31: 0.3807 S32: -1.1391 S33: -0.1585
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2533 22.0083 -28.7332
REMARK 3 T TENSOR
REMARK 3 T11: 0.5040 T22: 0.4342
REMARK 3 T33: 0.3370 T12: 0.0760
REMARK 3 T13: -0.0292 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 4.3200 L22: 7.2452
REMARK 3 L33: 5.0821 L12: 1.4037
REMARK 3 L13: -2.9163 L23: 0.9096
REMARK 3 S TENSOR
REMARK 3 S11: 0.3195 S12: -0.0895 S13: 0.8810
REMARK 3 S21: -0.0533 S22: -0.0957 S23: 0.4234
REMARK 3 S31: -0.2542 S32: -0.7949 S33: -0.1146
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7303 11.0259 -21.9039
REMARK 3 T TENSOR
REMARK 3 T11: 0.6865 T22: 0.4683
REMARK 3 T33: 0.2515 T12: -0.0362
REMARK 3 T13: -0.0440 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 5.9662 L22: 1.1862
REMARK 3 L33: 2.5555 L12: 0.4739
REMARK 3 L13: 3.8230 L23: 0.0630
REMARK 3 S TENSOR
REMARK 3 S11: 0.2650 S12: 0.1929 S13: -0.3256
REMARK 3 S21: -0.0157 S22: -0.1996 S23: 0.0268
REMARK 3 S31: -0.1965 S32: 0.1151 S33: -0.0687
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 7R0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-15
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 : 48643
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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 (%): 69.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-30 % (W/V) PEG750MME 0.1 M HEPES PH
REMARK 280 6.9-7.1, 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 38.92400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.90650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.48400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.90650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.92400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.48400
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 166 OG1 THR A 267 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 149 CA - CB - CG ANGL. DEV. = -10.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 47 -1.47 67.66
REMARK 500 CYS A 96 -1.94 -149.41
REMARK 500 ALA A 167 64.04 -167.28
REMARK 500 SGB A 203 -120.63 54.87
REMARK 500 ASP A 306 -72.89 -133.90
REMARK 500 ASP A 333 59.59 -119.43
REMARK 500 VAL A 407 -64.16 -123.09
REMARK 500 GLN A 508 50.38 39.11
REMARK 500 ALA A 542 23.76 -141.09
REMARK 500 PRO B 41 37.36 -77.54
REMARK 500 PHE B 47 -11.58 73.18
REMARK 500 LEU B 161 78.47 -109.18
REMARK 500 SGB B 203 -114.13 55.31
REMARK 500 CYS B 257 -141.80 -96.23
REMARK 500 ASN B 265 91.87 34.36
REMARK 500 ASP B 266 -47.25 -29.90
REMARK 500 THR B 275 49.33 -98.42
REMARK 500 PRO B 277 150.33 -49.47
REMARK 500 ASP B 306 -78.47 -127.54
REMARK 500 VAL B 407 -68.33 -124.59
REMARK 500 ALA B 542 36.58 -142.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS B 257 PRO B 258 -140.70
REMARK 500 SER B 293 ILE B 294 147.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7QYN RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R2F RELATED DB: PDB
REMARK 900 TABUN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
REMARK 900 PYRIDINIUM
REMARK 900 RELATED ID: 7R3C RELATED DB: PDB
REMARK 900 VX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R02 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH N-(3-(DIETHYLAMINO)PROPYL)-4-
REMARK 900 METHYL-3-NITROBENZAMIDE
REMARK 900 RELATED ID: 7R4E RELATED DB: PDB
REMARK 900 RVX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
DBREF 7R0A A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7R0A 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 SGB 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 SGB 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 7R0A SGB A 203 SER MODIFIED RESIDUE
MODRES 7R0A SGB B 203 SER MODIFIED RESIDUE
HET SGB A 203 13
HET SGB B 203 13
HET I4H A 601 15
HET NAG A 602 14
HET NAG A 603 14
HET PG0 A 604 8
HET PG0 A 605 8
HET P15 A 606 20
HET PG0 A 607 8
HET TOE A 608 11
HET I4H B 601 15
HET NAG B 602 14
HET PG0 B 603 8
HET PG0 B 604 8
HET TOE B 605 11
HET TOE B 606 11
HETNAM SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE
HETNAM I4H ~{N}-ETHYL-4-METHYL-3-NITRO-BENZAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
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 SGB 2(C7 H16 N O5 P)
FORMUL 3 I4H 2(C10 H12 N2 O3)
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 6 PG0 5(C5 H12 O3)
FORMUL 8 P15 C13 H28 O7
FORMUL 10 TOE 3(C7 H16 O4)
FORMUL 17 HOH *90(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 SGB A 203 SER A 215 1 13
HELIX 9 AA9 LEU A 216 PHE A 222 5 7
HELIX 10 AB1 SER A 240 VAL A 255 1 16
HELIX 11 AB2 ASP A 266 THR A 275 1 10
HELIX 12 AB3 PRO A 277 ASP A 283 1 7
HELIX 13 AB4 HIS A 284 LEU A 289 5 6
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 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASN A 464 5 9
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 SER A 541 1 8
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 VAL B 153 LEU B 159 1 7
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 SGB B 203 LEU B 214 1 12
HELIX 35 AD8 SER B 215 ARG B 219 5 5
HELIX 36 AD9 ALA B 241 VAL B 255 1 15
HELIX 37 AE1 ASN B 265 THR B 275 1 11
HELIX 38 AE2 PRO B 277 ASP B 283 1 7
HELIX 39 AE3 HIS B 284 LEU B 289 5 6
HELIX 40 AE4 THR B 311 ASN B 317 1 7
HELIX 41 AE5 GLY B 335 VAL B 340 1 6
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 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
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 VAL A 29 N LEU A 22
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 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
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 LYS B 23 0
SHEET 2 AA511 PRO B 28 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
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 VAL B 114
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 ALA B 225
SHEET 9 AA511 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 VAL B 520 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 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK C GLU A 202 N SGB A 203 1555 1555 1.34
LINK C SGB 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 1.46
LINK C GLU B 202 N SGB B 203 1555 1555 1.34
LINK C SGB B 203 N ALA B 204 1555 1555 1.33
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.47
CISPEP 1 TYR A 105 PRO A 106 0 -4.04
CISPEP 2 TYR B 105 PRO B 106 0 4.77
CISPEP 3 SER B 497 PRO B 498 0 8.65
CRYST1 77.848 108.968 227.813 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 0.012846 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004390 0.00000
TER 4293 THR A 543
TER 8616 THR B 543
MASTER 605 0 16 51 34 0 0 6 8629 2 210 84
END |