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HEADER HYDROLASE 23-APR-12 4ARA
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-C5685 AT 2.5 A
TITLE 2 RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: HEK293F
KEYWDS HYDROLASE, ENATIOMERS, INHIBITOR, CHEMICAL LEAD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNGSTAFSHEDE,F.EKSTROM,
AUTHOR 2 A.LINUSSON
REVDAT 1 28-NOV-12 4ARA 0
JRNL AUTH L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNG-STAFSHEDE,
JRNL AUTH 2 F.EKSTROM,A.LINUSSON
JRNL TITL SIMILAR BUT DIFFERENT: THERMODYNAMIC AND STRUCTURAL
JRNL TITL 2 CHARACTERIZATION OF A PAIR OF ENANTIOMERS BINDING TO
JRNL TITL 3 ACETYLCHOLINESTERASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2012
JRNL REFN ESSN 1521-3773
JRNL PMID 23161758
JRNL DOI 10.1002/ANIE.201205113
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BERG,C.D.ANDERSSON,E.ARTURSSON,A.HORNBERG,A.TUNEMALM,
REMARK 1 AUTH 2 A.LINUSSON,F.EKSTROM
REMARK 1 TITL TARGETING ACETYLCHOLINESTERASE: IDENTIFICATION OF CHEMICAL
REMARK 1 TITL 2 LEADS BY HIGH THROUGHPUT SCREENING, STRUCTURE DETERMINATION
REMARK 1 TITL 3 AND MOLECULAR MODELING.
REMARK 1 REF PLOS ONE V. 6 26039 2011
REMARK 1 REFN ISSN 1932-6203
REMARK 1 PMID 22140425
REMARK 1 DOI 10.1371/JOURNAL.PONE.0026039
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.855
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.79
REMARK 3 NUMBER OF REFLECTIONS : 70252
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1834
REMARK 3 R VALUE (WORKING SET) : 0.1826
REMARK 3 FREE R VALUE : 0.2220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1416
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 28.8570 - 5.3757 0.99 7189 143 0.1885 0.2164
REMARK 3 2 5.3757 - 4.2713 1.00 6985 132 0.1405 0.1623
REMARK 3 3 4.2713 - 3.7327 1.00 6914 140 0.1496 0.1868
REMARK 3 4 3.7327 - 3.3920 1.00 6867 141 0.1836 0.2211
REMARK 3 5 3.3920 - 3.1492 1.00 6883 130 0.2051 0.2611
REMARK 3 6 3.1492 - 2.9637 1.00 6812 152 0.2038 0.2251
REMARK 3 7 2.9637 - 2.8154 1.00 6822 136 0.2017 0.2763
REMARK 3 8 2.8154 - 2.6929 1.00 6819 134 0.2188 0.2521
REMARK 3 9 2.6929 - 2.5893 1.00 6773 154 0.2283 0.2913
REMARK 3 10 2.5893 - 2.5000 1.00 6772 154 0.2516 0.3072
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.346
REMARK 3 B_SOL : 60.440
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.25
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.8219
REMARK 3 B22 (A**2) : 12.8430
REMARK 3 B33 (A**2) : -23.6649
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
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 : 0.004 8837
REMARK 3 ANGLE : 0.898 12028
REMARK 3 CHIRALITY : 0.062 1284
REMARK 3 PLANARITY : 0.005 1569
REMARK 3 DIHEDRAL : 15.764 3242
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:142)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3331 15.4227 32.1785
REMARK 3 T TENSOR
REMARK 3 T11: 0.2680 T22: 0.2377
REMARK 3 T33: 0.2733 T12: 0.0043
REMARK 3 T13: -0.0062 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.1653 L22: 0.1515
REMARK 3 L33: 1.1039 L12: -0.0646
REMARK 3 L13: -0.0023 L23: -0.0362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0523 S12: -0.0982 S13: 0.0348
REMARK 3 S21: 0.1247 S22: 0.0154 S23: -0.0733
REMARK 3 S31: -0.0659 S32: 0.0513 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 143:223)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2478 4.1202 24.0344
REMARK 3 T TENSOR
REMARK 3 T11: 0.2888 T22: 0.1961
REMARK 3 T33: 0.2787 T12: 0.0377
REMARK 3 T13: -0.0043 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 0.1483 L22: 0.5967
REMARK 3 L33: 0.8150 L12: 0.2277
REMARK 3 L13: 0.3633 L23: 0.1429
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.0490 S13: -0.0278
REMARK 3 S21: 0.1101 S22: 0.0576 S23: -0.0461
REMARK 3 S31: 0.1922 S32: 0.0234 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 224:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7919 10.9019 10.3854
REMARK 3 T TENSOR
REMARK 3 T11: 0.1622 T22: 0.1245
REMARK 3 T33: 0.2217 T12: 0.0429
REMARK 3 T13: 0.0319 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.8001 L22: 0.0000
REMARK 3 L33: 1.3220 L12: 0.3229
REMARK 3 L13: 0.2284 L23: -0.3981
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: 0.1377 S13: 0.0056
REMARK 3 S21: -0.0313 S22: 0.0118 S23: -0.0087
REMARK 3 S31: 0.1742 S32: 0.1599 S33: -0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 342:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5229 17.1741 6.3422
REMARK 3 T TENSOR
REMARK 3 T11: 0.1834 T22: 0.2424
REMARK 3 T33: 0.2619 T12: -0.0244
REMARK 3 T13: -0.0065 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.2268 L22: 0.5033
REMARK 3 L33: 1.4203 L12: -0.0797
REMARK 3 L13: 0.3579 L23: 0.1415
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: 0.1124 S13: 0.0048
REMARK 3 S21: -0.1121 S22: 0.0327 S23: 0.0835
REMARK 3 S31: 0.0444 S32: -0.2615 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8700 1.4649 13.7085
REMARK 3 T TENSOR
REMARK 3 T11: 0.3515 T22: 0.4830
REMARK 3 T33: 0.4191 T12: -0.2953
REMARK 3 T13: 0.0134 T23: 0.0765
REMARK 3 L TENSOR
REMARK 3 L11: 0.2896 L22: 0.3384
REMARK 3 L33: 0.8203 L12: -0.2812
REMARK 3 L13: -0.1398 L23: 0.0446
REMARK 3 S TENSOR
REMARK 3 S11: -0.0970 S12: 0.4955 S13: -0.1487
REMARK 3 S21: -0.0701 S22: -0.0042 S23: 0.5685
REMARK 3 S31: 0.3724 S32: -1.0654 S33: 0.0012
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6550 6.3933 -1.1430
REMARK 3 T TENSOR
REMARK 3 T11: 0.2660 T22: 0.4620
REMARK 3 T33: 0.2711 T12: -0.0665
REMARK 3 T13: -0.0476 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.0313 L22: 0.0090
REMARK 3 L33: 0.6534 L12: -0.0093
REMARK 3 L13: 0.1462 L23: -0.0442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0674 S12: -0.1576 S13: 0.0765
REMARK 3 S21: -0.3743 S22: -0.0490 S23: 0.1712
REMARK 3 S31: 0.2459 S32: 0.2076 S33: 0.0094
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6357 6.1103 -61.5447
REMARK 3 T TENSOR
REMARK 3 T11: 0.2640 T22: 0.4445
REMARK 3 T33: 0.3153 T12: 0.0732
REMARK 3 T13: -0.0824 T23: -0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 0.1856 L22: 0.7024
REMARK 3 L33: 0.9043 L12: -0.1066
REMARK 3 L13: 0.2767 L23: -0.0168
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: 0.3060 S13: 0.0863
REMARK 3 S21: -0.3115 S22: -0.1366 S23: 0.0126
REMARK 3 S31: -0.1399 S32: -0.3327 S33: -0.0008
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2890 -4.2856 -52.9246
REMARK 3 T TENSOR
REMARK 3 T11: 0.3597 T22: 0.3593
REMARK 3 T33: 0.3143 T12: -0.0442
REMARK 3 T13: -0.0313 T23: -0.0629
REMARK 3 L TENSOR
REMARK 3 L11: -0.0538 L22: 0.5770
REMARK 3 L33: 0.5359 L12: -0.0542
REMARK 3 L13: -0.1648 L23: 0.4534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0781 S12: 0.2434 S13: -0.0439
REMARK 3 S21: -0.1155 S22: -0.1693 S23: 0.0386
REMARK 3 S31: 0.5495 S32: 0.0695 S33: -0.0074
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 87:142)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3090 4.6399 -50.3098
REMARK 3 T TENSOR
REMARK 3 T11: 0.1961 T22: 0.3488
REMARK 3 T33: 0.2721 T12: 0.0221
REMARK 3 T13: -0.0882 T23: -0.0881
REMARK 3 L TENSOR
REMARK 3 L11: 0.5536 L22: 0.1622
REMARK 3 L33: 0.6006 L12: 0.3230
REMARK 3 L13: 0.2268 L23: 0.1461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: 0.1752 S13: -0.1582
REMARK 3 S21: -0.2557 S22: -0.2172 S23: 0.0825
REMARK 3 S31: 0.3045 S32: -0.4991 S33: -0.0120
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 143:190)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3105 6.7368 -54.0317
REMARK 3 T TENSOR
REMARK 3 T11: 0.3099 T22: 0.3635
REMARK 3 T33: 0.2861 T12: 0.0174
REMARK 3 T13: -0.0322 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 0.1282 L22: 0.1281
REMARK 3 L33: 0.7286 L12: 0.1347
REMARK 3 L13: -0.0386 L23: -0.0379
REMARK 3 S TENSOR
REMARK 3 S11: 0.1592 S12: 0.3240 S13: -0.1130
REMARK 3 S21: -0.2351 S22: -0.0886 S23: 0.0934
REMARK 3 S31: -0.1263 S32: 0.2206 S33: 0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 191:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1798 8.2124 -44.1651
REMARK 3 T TENSOR
REMARK 3 T11: 0.2267 T22: 0.3075
REMARK 3 T33: 0.2643 T12: 0.0043
REMARK 3 T13: -0.0305 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 0.0075 L22: 0.2716
REMARK 3 L33: 0.9570 L12: -0.1866
REMARK 3 L13: 0.0636 L23: 0.2967
REMARK 3 S TENSOR
REMARK 3 S11: 0.0677 S12: -0.0016 S13: -0.0485
REMARK 3 S21: 0.0236 S22: 0.0025 S23: -0.0339
REMARK 3 S31: -0.0771 S32: 0.2105 S33: 0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 256:297)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4756 -9.8867 -46.8130
REMARK 3 T TENSOR
REMARK 3 T11: 0.4227 T22: 0.3671
REMARK 3 T33: 0.3215 T12: 0.1473
REMARK 3 T13: -0.0921 T23: -0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 0.2412 L22: 0.2535
REMARK 3 L33: 0.1356 L12: -0.2569
REMARK 3 L13: 0.1066 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: 0.0922 S13: -0.1681
REMARK 3 S21: 0.0286 S22: -0.0414 S23: -0.0218
REMARK 3 S31: 0.3512 S32: 0.5162 S33: -0.0001
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 298:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2876 14.2963 -40.1912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1739 T22: 0.2684
REMARK 3 T33: 0.2728 T12: -0.0455
REMARK 3 T13: -0.0219 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 0.4274 L22: 0.3005
REMARK 3 L33: 0.7741 L12: -0.2992
REMARK 3 L13: 0.0964 L23: 0.2516
REMARK 3 S TENSOR
REMARK 3 S11: -0.1014 S12: 0.2486 S13: 0.1285
REMARK 3 S21: 0.0067 S22: 0.1129 S23: -0.0960
REMARK 3 S31: 0.0292 S32: 0.3509 S33: -0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 332:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8485 -6.1946 -22.0912
REMARK 3 T TENSOR
REMARK 3 T11: 0.5538 T22: 0.2004
REMARK 3 T33: 0.3377 T12: 0.0191
REMARK 3 T13: -0.0361 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.1683 L22: 0.3401
REMARK 3 L33: 0.2821 L12: 0.0680
REMARK 3 L13: -0.0702 L23: 0.0906
REMARK 3 S TENSOR
REMARK 3 S11: 0.1290 S12: -0.1209 S13: 0.0046
REMARK 3 S21: 0.2211 S22: 0.0258 S23: -0.0245
REMARK 3 S31: 0.5619 S32: 0.2245 S33: 0.0006
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 383:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7352 5.8360 -29.0308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1865 T22: 0.2232
REMARK 3 T33: 0.2259 T12: -0.0454
REMARK 3 T13: -0.0048 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 0.1448 L22: 0.6458
REMARK 3 L33: 1.4030 L12: 0.3314
REMARK 3 L13: -0.1232 L23: 0.3301
REMARK 3 S TENSOR
REMARK 3 S11: 0.1272 S12: -0.0905 S13: 0.0418
REMARK 3 S21: 0.1870 S22: -0.1625 S23: 0.0317
REMARK 3 S31: 0.0814 S32: -0.1277 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0503 22.4945 -28.6338
REMARK 3 T TENSOR
REMARK 3 T11: 0.3733 T22: 0.3490
REMARK 3 T33: 0.3594 T12: 0.0523
REMARK 3 T13: -0.0191 T23: -0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 0.1012 L22: 0.1330
REMARK 3 L33: 0.3725 L12: -0.0023
REMARK 3 L13: -0.1959 L23: 0.0712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0429 S12: -0.5460 S13: 0.2598
REMARK 3 S21: 0.0021 S22: -0.0191 S23: 0.3205
REMARK 3 S31: -0.3827 S32: -0.4171 S33: 0.0010
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3573 11.4043 -21.5981
REMARK 3 T TENSOR
REMARK 3 T11: 0.3900 T22: 0.4073
REMARK 3 T33: 0.2502 T12: -0.0125
REMARK 3 T13: -0.0043 T23: -0.0539
REMARK 3 L TENSOR
REMARK 3 L11: -0.0023 L22: -0.0104
REMARK 3 L33: 0.4414 L12: -0.0212
REMARK 3 L13: 0.0037 L23: -0.0913
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: 0.0358 S13: -0.0356
REMARK 3 S21: 0.1517 S22: -0.0224 S23: 0.1543
REMARK 3 S31: 0.0937 S32: 0.2484 S33: -0.0000
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 4ARA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-12.
REMARK 100 THE PDBE ID CODE IS EBI-52170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : RH-COATED SI MIRROR, BENT FOR
REMARK 200 VERTICAL COLLIMATION
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 28.98
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.4
REMARK 200 R MERGE FOR SHELL (I) : 0.56
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 30 % (V/V)
REMARK 280 POLYETHELENEGLYCOLEMONOMETHYLETHER, PH 7
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 39.38200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.67000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.00600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.67000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.38200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.00600
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.2 KCAL/MOL
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 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
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 ALA B 544
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
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 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 23 CG CD CE NZ
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 GLU A 268 CG CD OE1 OE2
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 107 CG CD NE CZ NH1 NH2
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: 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 285 O HOH A 2223 2.19
REMARK 500 NH1 ARG B 274 O HOH B 2037 2.19
REMARK 500 ND2 ASN B 350 O5 NAG B 1552 1.32
REMARK 500 OH7 1PE B 1546 O HOH B 2266 2.15
REMARK 500 O HOH B 2026 O HOH B 2089 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 13 O SER B 57 2555 2.16
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 -10.11 71.89
REMARK 500 ALA A 62 52.11 -119.48
REMARK 500 ALA A 167 72.36 -155.87
REMARK 500 SER A 203 -118.29 59.00
REMARK 500 PRO A 217 2.48 -67.65
REMARK 500 ASP A 306 -85.30 -133.61
REMARK 500 HIS A 387 57.31 -143.74
REMARK 500 VAL A 407 -66.15 -126.45
REMARK 500 ARG A 493 50.43 -115.59
REMARK 500 ASP A 494 91.17 -160.67
REMARK 500 SER A 541 46.35 -89.92
REMARK 500 ALA B 62 52.18 -118.38
REMARK 500 ALA B 167 70.08 -150.67
REMARK 500 SER B 203 -119.33 55.59
REMARK 500 ASP B 306 -78.00 -121.57
REMARK 500 ASN B 350 -167.19 -128.83
REMARK 500 VAL B 407 -65.39 -127.24
REMARK 500 SER B 497 125.90 65.05
REMARK 500 SER B 541 31.90 -82.58
REMARK 500 ALA B 542 -13.97 -163.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR B 337 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-
REMARK 600 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE (568):
REMARK 600 CORRESPONDING TO LIGAND C56 IN THE RACEMIC STRUCTURE 4A23
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1549 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1553 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1552 BOUND TO ASN B 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE
REMARK 900 APOFORM
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 DECIDIUM COMPLEX
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 GALLAMINE COMPLEX
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2H9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE
REMARK 900 RELATED ID: 2HA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND HLO-7
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND ORTHO-7
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED VX
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED VX AND SARIN
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN AND IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN (AGED) IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 K027
REMARK 900 RELATED ID: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 2WU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND HI-6
REMARK 900 RELATED ID: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND ORTHO-7
REMARK 900 RELATED ID: 2XUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2XUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 MTH)
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 WK)
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 WK)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 MTH)
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI INHIBITOR
REMARK 900 RELATED ID: 2XUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 SYN INHIBITOR
REMARK 900 RELATED ID: 2XUQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS
REMARK 900 RELATED ID: 4A16 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH
REMARK 900 HUPRINE DERIVATIVE
REMARK 900 RELATED ID: 4A23 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC
REMARK 900 C5685
REMARK 900 RELATED ID: 4ARB RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-
REMARK 900 C5685 AT 2.25 A RESOLUTION.
DBREF 4ARA A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4ARA B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4ARA ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4ARA THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4ARA GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4ARA ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4ARA PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4ARA ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4ARA THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4ARA GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4ARA ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4ARA PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
HET C56 A 600 50
HET PEG A1544 7
HET EDO A1545 4
HET PEG A1546 7
HET PEG A1547 7
HET EDO A1548 4
HET NAG A1549 14
HET EDO A1550 4
HET EDO A1551 4
HET EDO A1552 4
HET NAG A1553 14
HET C56 B 600 50
HET PEG B1545 7
HET 1PE B1546 16
HET PEG B1547 7
HET PEG B1548 7
HET EDO B1549 4
HET PEG B1550 7
HET PEG B1551 7
HET NAG B1552 14
HET EDO B1553 4
HET PEG B1554 7
HET CL B1555 1
HET EDO B1556 4
HETNAM C56 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-
HETNAM 2 C56 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 C56 2(C17 H26 N4 O4)
FORMUL 4 PEG 9(C4 H10 O3)
FORMUL 5 EDO 8(C2 H6 O2)
FORMUL 6 NAG 3(C8 H15 N O6)
FORMUL 7 1PE C10 H22 O6
FORMUL 8 CL CL 1-
FORMUL 9 HOH *628(H2 O)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLU A 142 1 8
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 SER A 215 1 13
HELIX 10 10 LEU A 216 ARG A 219 5 4
HELIX 11 11 SER A 240 GLY A 256 1 17
HELIX 12 12 ASN A 265 ARG A 274 1 10
HELIX 13 13 PRO A 277 HIS A 284 1 8
HELIX 14 14 GLU A 285 LEU A 289 5 5
HELIX 15 15 THR A 311 THR A 318 1 8
HELIX 16 16 GLY A 335 GLY A 342 5 8
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 ASP A 460 ASN A 464 5 5
HELIX 25 25 THR A 466 GLY A 487 1 22
HELIX 26 26 ARG A 525 ARG A 534 1 10
HELIX 27 27 ARG A 534 SER A 541 1 8
HELIX 28 28 VAL B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 GLU B 142 1 8
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 ILE B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 LEU B 214 1 12
HELIX 36 36 SER B 215 LEU B 221 5 7
HELIX 37 37 SER B 240 GLY B 256 1 17
HELIX 38 38 ASN B 265 THR B 275 1 11
HELIX 39 39 PRO B 277 ASP B 283 1 7
HELIX 40 40 HIS B 284 LEU B 289 5 6
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 GLY B 342 5 8
HELIX 43 43 SER B 355 VAL B 367 1 13
HELIX 44 44 SER B 371 THR B 383 1 13
HELIX 45 45 ASP B 390 VAL B 407 1 18
HELIX 46 46 VAL B 407 GLN B 421 1 15
HELIX 47 47 PRO B 440 GLY B 444 5 5
HELIX 48 48 GLU B 450 PHE B 455 1 6
HELIX 49 49 GLY B 456 ASP B 460 5 5
HELIX 50 50 ASP B 460 ASN B 464 5 5
HELIX 51 51 THR B 466 GLY B 487 1 22
HELIX 52 52 ARG B 525 ARG B 534 1 10
HELIX 53 53 PHE B 535 SER B 541 1 7
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A1549 1555 1555 1.47
LINK ND2 ASN A 464 C1 NAG A1553 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG B1552 1555 1555 1.47
CISPEP 1 TYR A 105 PRO A 106 0 -0.99
CISPEP 2 TYR B 105 PRO B 106 0 1.55
CISPEP 3 SER B 497 PRO B 498 0 11.72
SITE 1 AC1 13 TYR A 72 ASP A 74 TRP A 86 TYR A 124
SITE 2 AC1 13 TRP A 286 ILE A 294 PHE A 295 ARG A 296
SITE 3 AC1 13 TYR A 337 PHE A 338 TYR A 341 HOH A2236
SITE 4 AC1 13 HOH A2258
SITE 1 AC2 3 ASP A 304 SER A 309 ASP A 310
SITE 1 AC3 1 GLU A 313
SITE 1 AC4 2 ASP A 323 PEG A1547
SITE 1 AC5 5 ILE A 213 ARG A 219 PHE A 222 ASP A 323
SITE 2 AC5 5 PEG A1546
SITE 1 AC6 1 GLU A 313
SITE 1 AC7 1 ASP A 5
SITE 1 AC8 3 SER A 57 VAL A 59 HOH A2346
SITE 1 AC9 2 THR A 63 HOH A2347
SITE 1 BC1 15 TYR B 72 ASP B 74 TRP B 86 GLY B 121
SITE 2 BC1 15 GLY B 122 TYR B 124 TRP B 286 SER B 293
SITE 3 BC1 15 ILE B 294 PHE B 295 ARG B 296 TYR B 337
SITE 4 BC1 15 PHE B 338 TYR B 341 HOH B2176
SITE 1 BC2 6 THR B 112 PRO B 113 GLU B 142 GLY B 143
SITE 2 BC2 6 ALA B 144 ARG B 485
SITE 1 BC3 11 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 BC3 11 ALA B 377 LEU B 380 HIS B 381 PHE B 531
SITE 3 BC3 11 PHE B 535 HOH B2203 HOH B2266
SITE 1 BC4 2 ASP B 323 EDO B1549
SITE 1 BC5 3 HIS B 381 TYR B 382 HOH B2268
SITE 1 BC6 2 ARG B 219 PEG B1547
SITE 1 BC7 3 ARG B 11 GLU B 185 HOH B2269
SITE 1 BC8 5 LYS B 332 ASP B 333 ASP B 396 LEU B 441
SITE 2 BC8 5 TRP B 442
SITE 1 BC9 1 GLU B 313
SITE 1 CC1 1 SER B 309
SITE 1 CC2 1 SER B 240
SITE 1 CC3 1 LYS B 516
SITE 1 CC4 5 SER A 347 ASN A 350 HOH A2261 HOH A2344
SITE 2 CC4 5 HOH A2345
SITE 1 CC5 1 ASN A 464
SITE 1 CC6 3 SER B 347 ASN B 350 HOH B2270
CRYST1 78.764 112.012 227.340 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 0.012696 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004399 0.00000
TER 4174 ALA A 542
TER 8338 THR B 543
MASTER 867 0 24 53 32 0 36 6 9218 2 268 86
END |