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HEADER HYDROLASE 07-FEB-22 7R3C
TITLE VX-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: VX 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;
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 7R3C 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.336
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 77850
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.987
REMARK 3 FREE R VALUE TEST SET COUNT : 1547
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 29.0277 - 5.3275 0.95 7058 144 0.1577 0.1684
REMARK 3 2 5.3275 - 4.2328 0.96 6957 137 0.1317 0.1413
REMARK 3 3 4.2328 - 3.6990 0.97 6938 135 0.1469 0.1767
REMARK 3 4 3.6990 - 3.3613 0.98 6929 138 0.1724 0.2074
REMARK 3 5 3.3613 - 3.1207 0.98 6896 136 0.1986 0.2307
REMARK 3 6 3.1207 - 2.9369 0.98 6930 154 0.1989 0.2200
REMARK 3 7 2.9369 - 2.7900 0.98 6910 140 0.1935 0.2688
REMARK 3 8 2.7900 - 2.6686 0.99 6929 142 0.1920 0.2191
REMARK 3 9 2.6686 - 2.5659 0.99 6928 157 0.1941 0.2219
REMARK 3 10 2.5659 - 2.4774 0.99 6891 136 0.2024 0.2514
REMARK 3 11 2.4774 - 2.4000 0.99 6937 128 0.2238 0.2815
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) : 0.213
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.61
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 : 0.007 8817
REMARK 3 ANGLE : 0.917 12017
REMARK 3 CHIRALITY : 0.055 1279
REMARK 3 PLANARITY : 0.006 1568
REMARK 3 DIHEDRAL : 10.288 7074
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0259 15.2563 31.3828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3157 T22: 0.2686
REMARK 3 T33: 0.2397 T12: 0.0085
REMARK 3 T13: -0.0236 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.9330 L22: 1.3090
REMARK 3 L33: 3.4154 L12: 0.0356
REMARK 3 L13: -0.3932 L23: -0.5436
REMARK 3 S TENSOR
REMARK 3 S11: -0.1207 S12: -0.2054 S13: 0.1269
REMARK 3 S21: 0.2810 S22: 0.0357 S23: -0.0345
REMARK 3 S31: -0.1148 S32: 0.0203 S33: 0.0638
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0531 3.9821 25.5722
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.2803
REMARK 3 T33: 0.3582 T12: 0.1151
REMARK 3 T13: -0.0260 T23: 0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 2.0932 L22: 1.7520
REMARK 3 L33: 5.1019 L12: 0.7499
REMARK 3 L13: -1.0287 L23: -1.1328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1722 S12: -0.2350 S13: -0.2678
REMARK 3 S21: 0.0743 S22: -0.0534 S23: -0.3473
REMARK 3 S31: 0.6425 S32: 0.3670 S33: 0.2376
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0964 10.3808 14.1209
REMARK 3 T TENSOR
REMARK 3 T11: 0.3263 T22: 0.2659
REMARK 3 T33: 0.2515 T12: 0.0807
REMARK 3 T13: 0.0046 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 3.0616 L22: 1.4542
REMARK 3 L33: 2.9663 L12: 0.7132
REMARK 3 L13: -0.2218 L23: -0.7347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1038 S12: 0.1639 S13: -0.0647
REMARK 3 S21: -0.1367 S22: -0.0180 S23: -0.1910
REMARK 3 S31: 0.2172 S32: 0.2436 S33: 0.1596
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7775 -1.1469 11.4101
REMARK 3 T TENSOR
REMARK 3 T11: 0.5841 T22: 0.3831
REMARK 3 T33: 0.3762 T12: 0.0142
REMARK 3 T13: 0.0740 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 5.0963 L22: 2.8158
REMARK 3 L33: 2.8461 L12: -0.2611
REMARK 3 L13: 0.0927 L23: 0.8536
REMARK 3 S TENSOR
REMARK 3 S11: -0.1958 S12: 0.2186 S13: -1.0249
REMARK 3 S21: 0.0387 S22: 0.1014 S23: -0.0207
REMARK 3 S31: 0.8361 S32: 0.1260 S33: 0.0604
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6526 21.7759 -3.9043
REMARK 3 T TENSOR
REMARK 3 T11: 0.2251 T22: 0.3683
REMARK 3 T33: 0.2461 T12: -0.0317
REMARK 3 T13: -0.0228 T23: 0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 2.7083 L22: 5.3897
REMARK 3 L33: 3.3402 L12: -0.4386
REMARK 3 L13: 0.8796 L23: -1.8261
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.2662 S13: 0.1522
REMARK 3 S21: -0.1092 S22: -0.0280 S23: -0.0197
REMARK 3 S31: -0.1730 S32: -0.0086 S33: 0.0464
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7279 15.6203 10.7959
REMARK 3 T TENSOR
REMARK 3 T11: 0.2512 T22: 0.3604
REMARK 3 T33: 0.2998 T12: -0.0613
REMARK 3 T13: -0.0227 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.3344 L22: 1.1708
REMARK 3 L33: 4.1293 L12: -0.4795
REMARK 3 L13: 0.1582 L23: -0.4776
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: 0.0690 S13: -0.0129
REMARK 3 S21: -0.0776 S22: 0.0340 S23: 0.2119
REMARK 3 S31: 0.1011 S32: -0.4977 S33: 0.0573
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3073 1.4143 13.6553
REMARK 3 T TENSOR
REMARK 3 T11: 0.5481 T22: 0.5922
REMARK 3 T33: 0.4494 T12: -0.2445
REMARK 3 T13: 0.0353 T23: 0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 6.7250 L22: 2.4060
REMARK 3 L33: 5.2230 L12: -0.5293
REMARK 3 L13: 0.2938 L23: -2.9202
REMARK 3 S TENSOR
REMARK 3 S11: -0.1599 S12: -0.0202 S13: -0.6460
REMARK 3 S21: 0.3036 S22: 0.1430 S23: 0.7104
REMARK 3 S31: 0.9144 S32: -1.4885 S33: 0.0604
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9279 6.3272 -1.1315
REMARK 3 T TENSOR
REMARK 3 T11: 0.4881 T22: 0.5331
REMARK 3 T33: 0.3125 T12: 0.0014
REMARK 3 T13: -0.1185 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.8828 L22: 3.0396
REMARK 3 L33: 8.8070 L12: -0.8393
REMARK 3 L13: -3.6822 L23: 2.5352
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: -0.0271 S13: -0.1668
REMARK 3 S21: -0.3735 S22: -0.1119 S23: 0.0853
REMARK 3 S31: 0.3266 S32: 0.1587 S33: 0.0495
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7069 6.0231 -61.3326
REMARK 3 T TENSOR
REMARK 3 T11: 0.4468 T22: 0.4994
REMARK 3 T33: 0.3562 T12: 0.0497
REMARK 3 T13: -0.0995 T23: -0.1557
REMARK 3 L TENSOR
REMARK 3 L11: 5.6392 L22: 2.3385
REMARK 3 L33: 4.6927 L12: -1.1718
REMARK 3 L13: -1.5410 L23: 0.3494
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: 0.6116 S13: 0.1085
REMARK 3 S21: -0.2702 S22: -0.2030 S23: 0.3303
REMARK 3 S31: -0.2551 S32: -0.8045 S33: 0.1677
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3628 -4.2845 -52.8326
REMARK 3 T TENSOR
REMARK 3 T11: 0.4494 T22: 0.4477
REMARK 3 T33: 0.3405 T12: -0.0334
REMARK 3 T13: -0.0685 T23: -0.1182
REMARK 3 L TENSOR
REMARK 3 L11: 0.4948 L22: 1.7181
REMARK 3 L33: 6.6983 L12: -0.5262
REMARK 3 L13: 0.2128 L23: -0.5137
REMARK 3 S TENSOR
REMARK 3 S11: 0.1461 S12: 0.1155 S13: -0.1683
REMARK 3 S21: -0.1095 S22: -0.0963 S23: 0.2023
REMARK 3 S31: 0.7719 S32: -0.2168 S33: -0.0478
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2429 3.4797 -48.6220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3579 T22: 0.3758
REMARK 3 T33: 0.2320 T12: 0.0097
REMARK 3 T13: -0.0254 T23: -0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 1.9189 L22: 1.9874
REMARK 3 L33: 3.0838 L12: -0.4864
REMARK 3 L13: 0.1042 L23: 0.8123
REMARK 3 S TENSOR
REMARK 3 S11: 0.1032 S12: 0.1468 S13: -0.1109
REMARK 3 S21: -0.0276 S22: -0.0675 S23: 0.0085
REMARK 3 S31: 0.2055 S32: 0.1655 S33: -0.0309
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 298 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4844 14.1259 -40.0685
REMARK 3 T TENSOR
REMARK 3 T11: 0.3951 T22: 0.4597
REMARK 3 T33: 0.3920 T12: -0.0722
REMARK 3 T13: -0.0173 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 3.5790 L22: 1.6023
REMARK 3 L33: 4.6315 L12: -1.5963
REMARK 3 L13: -1.1965 L23: 1.6834
REMARK 3 S TENSOR
REMARK 3 S11: 0.2653 S12: 0.3228 S13: 0.5518
REMARK 3 S21: -0.0453 S22: -0.0372 S23: -0.3703
REMARK 3 S31: -0.3045 S32: 0.6247 S33: -0.2560
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3542 -6.0850 -21.9095
REMARK 3 T TENSOR
REMARK 3 T11: 0.8074 T22: 0.3445
REMARK 3 T33: 0.3626 T12: 0.0129
REMARK 3 T13: -0.0732 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 3.8805 L22: 2.3417
REMARK 3 L33: 4.7488 L12: 0.6825
REMARK 3 L13: 0.7522 L23: 0.0925
REMARK 3 S TENSOR
REMARK 3 S11: 0.3001 S12: -0.0961 S13: -0.5113
REMARK 3 S21: 0.5450 S22: 0.0167 S23: 0.0099
REMARK 3 S31: 0.9625 S32: 0.0569 S33: -0.2140
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9570 4.9182 -23.6440
REMARK 3 T TENSOR
REMARK 3 T11: 0.4585 T22: 0.3752
REMARK 3 T33: 0.2356 T12: -0.0792
REMARK 3 T13: 0.0031 T23: -0.0919
REMARK 3 L TENSOR
REMARK 3 L11: 2.0466 L22: 1.7654
REMARK 3 L33: 3.5015 L12: -0.1844
REMARK 3 L13: 0.1814 L23: -0.3789
REMARK 3 S TENSOR
REMARK 3 S11: 0.1844 S12: -0.2635 S13: -0.0885
REMARK 3 S21: 0.5123 S22: -0.1778 S23: 0.0494
REMARK 3 S31: 0.3540 S32: 0.1153 S33: 0.0106
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5174 6.8773 -35.1408
REMARK 3 T TENSOR
REMARK 3 T11: 0.3293 T22: 0.5875
REMARK 3 T33: 0.3959 T12: -0.0490
REMARK 3 T13: 0.0424 T23: -0.1538
REMARK 3 L TENSOR
REMARK 3 L11: 1.4533 L22: 3.7647
REMARK 3 L33: 4.2998 L12: 0.0810
REMARK 3 L13: 0.1142 L23: -0.6093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0209 S12: -0.1058 S13: -0.0520
REMARK 3 S21: 0.1472 S22: -0.0948 S23: 0.5124
REMARK 3 S31: 0.2604 S32: -0.9633 S33: 0.0246
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8470 22.4693 -28.6452
REMARK 3 T TENSOR
REMARK 3 T11: 0.4884 T22: 0.4280
REMARK 3 T33: 0.4005 T12: 0.0323
REMARK 3 T13: -0.0133 T23: -0.1453
REMARK 3 L TENSOR
REMARK 3 L11: 6.3238 L22: 4.5139
REMARK 3 L33: 5.3457 L12: -0.0681
REMARK 3 L13: 0.7439 L23: -2.8288
REMARK 3 S TENSOR
REMARK 3 S11: -0.0456 S12: -0.4369 S13: 0.6740
REMARK 3 S21: 0.1284 S22: 0.1043 S23: 0.4940
REMARK 3 S31: -0.6349 S32: -0.3220 S33: 0.0456
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8388 11.7232 -21.5371
REMARK 3 T TENSOR
REMARK 3 T11: 0.5499 T22: 0.4442
REMARK 3 T33: 0.2131 T12: -0.0921
REMARK 3 T13: 0.0571 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 6.5083 L22: 1.5425
REMARK 3 L33: 5.9225 L12: 0.1505
REMARK 3 L13: 5.9877 L23: -0.3125
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.3558 S13: -0.0226
REMARK 3 S21: 0.0777 S22: -0.1263 S23: -0.0433
REMARK 3 S31: 0.0021 S32: 0.5776 S33: 0.1270
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 7R3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120845.
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) : 1.0000
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 : 78034
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
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 (%): 70.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
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 39.57700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.42600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.04700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.42600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.57700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.04700
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 258
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 THR A 543
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
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 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 GLU B 4 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: 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 ND2 ASN A 350 O5 NAG A 602 2.13
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 -2.94 75.24
REMARK 500 PHE A 158 -1.09 -141.40
REMARK 500 ALA A 167 76.95 -153.57
REMARK 500 SVX A 203 -119.15 59.48
REMARK 500 ASP A 306 -83.45 -126.35
REMARK 500 VAL A 407 -62.02 -129.02
REMARK 500 PHE B 47 -0.43 70.51
REMARK 500 PRO B 55 153.14 -47.42
REMARK 500 CYS B 96 10.65 -142.21
REMARK 500 SVX B 203 -116.78 62.68
REMARK 500 ASP B 306 -80.21 -124.12
REMARK 500 ASP B 323 40.30 -84.18
REMARK 500 VAL B 407 -62.72 -125.04
REMARK 500 ARG B 525 56.29 36.60
REMARK 500 LEU B 539 -73.16 -72.80
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: 7R0A RELATED DB: PDB
REMARK 900 SARIN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
REMARK 900 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: 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: 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 7R3C A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7R3C 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 SVX 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 SVX 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 7R3C SVX A 203 SER MODIFIED RESIDUE
MODRES 7R3C SVX B 203 SER MODIFIED RESIDUE
HET SVX A 203 12
HET SVX B 203 12
HET I1X A 601 27
HET NAG A 602 14
HET NAG A 603 14
HET PG0 A 604 8
HET PG0 A 605 8
HET PG0 A 606 8
HET PG0 A 607 8
HET TOE A 608 11
HET P15 A 609 20
HET I1X B 601 27
HET PG0 B 602 8
HET PG0 B 603 8
HET PG0 B 604 8
HET TOE B 605 11
HET TOE B 606 11
HETNAM SVX O-[(R)-ETHOXY(METHYL)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 SVX 2(C6 H14 N O5 P)
FORMUL 3 I1X 2(C19 H23 N4 O4 1+)
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 6 PG0 7(C5 H12 O3)
FORMUL 10 TOE 3(C7 H16 O4)
FORMUL 11 P15 C13 H28 O7
FORMUL 18 HOH *295(H2 O)
HELIX 1 AA1 ASP A 5 GLN A 7 5 3
HELIX 2 AA2 VAL A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 GLY A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 ILE A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SVX A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 SER A 220 1 6
HELIX 11 AB2 SER A 240 GLY A 256 1 17
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASN A 464 5 9
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 SER A 541 1 8
HELIX 27 AC9 ASP B 5 GLN B 7 5 3
HELIX 28 AD1 VAL B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 GLY B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 ILE B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SVX B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 SER B 240 GLY B 256 1 17
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 ASP B 283 1 7
HELIX 40 AE4 HIS B 284 VAL B 288 5 5
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASN B 464 5 9
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 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 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 LEU A 115 O VAL A 145
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 VAL A 226 N LEU A 199
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 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O ALA B 31 N ILE B 20
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 TRP B 117 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 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 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
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
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 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.07
LINK C GLU A 202 N SVX A 203 1555 1555 1.33
LINK C SVX A 203 N ALA A 204 1555 1555 1.33
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.43
LINK ND2 ASN A 464 C1 NAG A 603 1555 1555 1.45
LINK C GLU B 202 N SVX B 203 1555 1555 1.34
LINK C SVX B 203 N ALA B 204 1555 1555 1.34
CISPEP 1 TYR A 105 PRO A 106 0 -2.16
CISPEP 2 TYR B 105 PRO B 106 0 2.22
CISPEP 3 SER B 497 PRO B 498 0 15.64
CRYST1 79.154 112.094 226.852 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 0.012634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004408 0.00000
TER 4207 ALA A 542
TER 8375 ALA B 542
MASTER 550 0 17 52 32 0 0 6 8812 2 233 84
END |