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HEADER HYDROLASE 24-AUG-12 4B83
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
TITLE 2 DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE
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;
COMPND 8 OTHER_DETAILS: LIGAND N-(2-DIETHYLAMINO-ETHYL)-3-METHOXY-
COMPND 9 BENZENESULFONAMIDE
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_CELL_LINE: HEK 293F;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,W.QIAN,
AUTHOR 2 F.EKSTROM,A.LINUSSON
REVDAT 1 04-SEP-13 4B83 0
JRNL AUTH C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,
JRNL AUTH 2 W.QIAN,F.EKSTROM,A.LINUSSON
JRNL TITL DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY
JRNL TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.042
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.69
REMARK 3 NUMBER OF REFLECTIONS : 80034
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1937
REMARK 3 R VALUE (WORKING SET) : 0.1931
REMARK 3 FREE R VALUE : 0.2223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1582
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 29.0445 - 5.3276 0.99 7439 146 0.1810 0.2045
REMARK 3 2 5.3276 - 4.2328 1.00 7247 145 0.1416 0.1377
REMARK 3 3 4.2328 - 3.6990 1.00 7167 141 0.1659 0.2047
REMARK 3 4 3.6990 - 3.3613 1.00 7132 137 0.2026 0.2489
REMARK 3 5 3.3613 - 3.1207 1.00 7128 144 0.2185 0.2467
REMARK 3 6 3.1207 - 2.9369 1.00 7065 153 0.2281 0.2288
REMARK 3 7 2.9369 - 2.7899 1.00 7097 143 0.2314 0.3040
REMARK 3 8 2.7899 - 2.6686 1.00 7042 142 0.2357 0.2960
REMARK 3 9 2.6686 - 2.5659 1.00 7037 160 0.2353 0.2787
REMARK 3 10 2.5659 - 2.4774 1.00 7045 132 0.2453 0.2735
REMARK 3 11 2.4774 - 2.4000 1.00 7053 139 0.2709 0.3258
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.352
REMARK 3 B_SOL : 52.824
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.33
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.7734
REMARK 3 B22 (A**2) : 13.5417
REMARK 3 B33 (A**2) : -24.3150
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 : 0.007 8845
REMARK 3 ANGLE : 1.074 12039
REMARK 3 CHIRALITY : 0.076 1282
REMARK 3 PLANARITY : 0.005 1565
REMARK 3 DIHEDRAL : 14.926 3256
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): 30.5140 15.3713 32.3561
REMARK 3 T TENSOR
REMARK 3 T11: 0.3504 T22: 0.3204
REMARK 3 T33: 0.3403 T12: 0.0137
REMARK 3 T13: -0.0227 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.0882 L22: 0.6209
REMARK 3 L33: 0.9298 L12: -0.1891
REMARK 3 L13: 0.0422 L23: -0.4553
REMARK 3 S TENSOR
REMARK 3 S11: -0.1079 S12: -0.0722 S13: 0.0888
REMARK 3 S21: 0.1630 S22: 0.0427 S23: -0.0774
REMARK 3 S31: -0.0704 S32: 0.0251 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 143:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9392 5.6878 19.8220
REMARK 3 T TENSOR
REMARK 3 T11: 0.2718 T22: 0.2013
REMARK 3 T33: 0.2767 T12: 0.0445
REMARK 3 T13: 0.0056 T23: 0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 0.0212 L22: 0.5173
REMARK 3 L33: 0.9571 L12: 0.3645
REMARK 3 L13: 0.1725 L23: -0.2813
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: 0.0619 S13: -0.0707
REMARK 3 S21: 0.0269 S22: 0.0048 S23: -0.0634
REMARK 3 S31: 0.1791 S32: 0.0484 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 256:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0350 9.2175 11.5148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2774 T22: 0.2346
REMARK 3 T33: 0.3358 T12: 0.0461
REMARK 3 T13: 0.0219 T23: 0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 0.6431 L22: -0.0548
REMARK 3 L33: 0.8776 L12: 0.1829
REMARK 3 L13: 0.0285 L23: -0.2827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: 0.1380 S13: 0.0085
REMARK 3 S21: -0.0079 S22: 0.0119 S23: -0.0284
REMARK 3 S31: 0.1691 S32: 0.2361 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9126 17.4918 6.4022
REMARK 3 T TENSOR
REMARK 3 T11: 0.2709 T22: 0.2749
REMARK 3 T33: 0.3392 T12: -0.0200
REMARK 3 T13: -0.0013 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.3586 L22: 0.1749
REMARK 3 L33: 1.5274 L12: -0.1109
REMARK 3 L13: 0.5146 L23: -0.1664
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: 0.0997 S13: -0.0011
REMARK 3 S21: -0.1081 S22: -0.0044 S23: 0.0546
REMARK 3 S31: 0.0338 S32: -0.2414 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7079 1.3122 13.9330
REMARK 3 T TENSOR
REMARK 3 T11: 0.5266 T22: 0.5897
REMARK 3 T33: 0.5448 T12: -0.1847
REMARK 3 T13: 0.0031 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 0.0896 L22: 0.1913
REMARK 3 L33: 0.1822 L12: -0.1257
REMARK 3 L13: 0.1629 L23: -0.1956
REMARK 3 S TENSOR
REMARK 3 S11: -0.1931 S12: 0.2274 S13: -0.2053
REMARK 3 S21: 0.0360 S22: 0.2206 S23: 0.3257
REMARK 3 S31: 0.5216 S32: -0.9062 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6258 6.4360 -1.0784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3042 T22: 0.4207
REMARK 3 T33: 0.3341 T12: -0.0372
REMARK 3 T13: -0.0498 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.1427 L22: -0.0562
REMARK 3 L33: 0.6037 L12: -0.0107
REMARK 3 L13: 0.3453 L23: -0.0225
REMARK 3 S TENSOR
REMARK 3 S11: 0.0527 S12: -0.1029 S13: 0.0946
REMARK 3 S21: -0.2995 S22: -0.1137 S23: 0.2343
REMARK 3 S31: 0.0565 S32: 0.0858 S33: -0.0065
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6788 6.2755 -61.8803
REMARK 3 T TENSOR
REMARK 3 T11: 0.3910 T22: 0.5126
REMARK 3 T33: 0.4021 T12: 0.0724
REMARK 3 T13: -0.0790 T23: -0.1016
REMARK 3 L TENSOR
REMARK 3 L11: 0.1498 L22: 0.4826
REMARK 3 L33: 0.6522 L12: 0.0654
REMARK 3 L13: 0.1695 L23: -0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.4536 S13: -0.0278
REMARK 3 S21: -0.3975 S22: -0.1261 S23: 0.0691
REMARK 3 S31: -0.0372 S32: -0.2271 S33: -0.0001
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1549 0.3329 -61.5622
REMARK 3 T TENSOR
REMARK 3 T11: 0.4617 T22: 0.4768
REMARK 3 T33: 0.3254 T12: 0.0427
REMARK 3 T13: -0.0513 T23: -0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 0.1708 L22: 0.0941
REMARK 3 L33: 0.2390 L12: -0.2345
REMARK 3 L13: -0.1502 L23: 0.2794
REMARK 3 S TENSOR
REMARK 3 S11: 0.1084 S12: 0.1843 S13: -0.0680
REMARK 3 S21: -0.2331 S22: -0.0933 S23: -0.0308
REMARK 3 S31: 0.5073 S32: 0.0669 S33: -0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 72:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9996 1.6023 -48.4748
REMARK 3 T TENSOR
REMARK 3 T11: 0.2973 T22: 0.3152
REMARK 3 T33: 0.3107 T12: -0.0068
REMARK 3 T13: -0.0403 T23: -0.0760
REMARK 3 L TENSOR
REMARK 3 L11: -0.0280 L22: 0.1674
REMARK 3 L33: 1.2167 L12: 0.2851
REMARK 3 L13: 0.2863 L23: 0.5573
REMARK 3 S TENSOR
REMARK 3 S11: 0.0849 S12: 0.2240 S13: -0.0605
REMARK 3 S21: -0.0853 S22: -0.1558 S23: 0.0736
REMARK 3 S31: 0.2988 S32: -0.1731 S33: -0.0013
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 159:190)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3671 8.8665 -55.7789
REMARK 3 T TENSOR
REMARK 3 T11: 0.3859 T22: 0.5112
REMARK 3 T33: 0.3684 T12: 0.0256
REMARK 3 T13: -0.0128 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.2281 L22: 0.1385
REMARK 3 L33: 0.1599 L12: 0.2385
REMARK 3 L13: 0.0589 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: 0.1554 S13: 0.1923
REMARK 3 S21: -0.2409 S22: -0.0100 S23: -0.1086
REMARK 3 S31: -0.1368 S32: 0.2165 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 191:237)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9667 14.1142 -44.0985
REMARK 3 T TENSOR
REMARK 3 T11: 0.3084 T22: 0.3720
REMARK 3 T33: 0.3159 T12: 0.0216
REMARK 3 T13: -0.0190 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 0.1203 L22: 0.2426
REMARK 3 L33: 0.2367 L12: -0.2217
REMARK 3 L13: -0.0434 L23: 0.2723
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: 0.0414 S13: 0.0247
REMARK 3 S21: 0.0903 S22: -0.0062 S23: 0.0170
REMARK 3 S31: -0.1769 S32: -0.0121 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 238:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4339 -8.1447 -46.1979
REMARK 3 T TENSOR
REMARK 3 T11: 0.4629 T22: 0.5156
REMARK 3 T33: 0.3921 T12: 0.1680
REMARK 3 T13: -0.0846 T23: -0.0767
REMARK 3 L TENSOR
REMARK 3 L11: 0.2530 L22: 0.3351
REMARK 3 L33: 0.2370 L12: -0.2332
REMARK 3 L13: 0.3166 L23: -0.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0763 S12: 0.0167 S13: 0.0480
REMARK 3 S21: 0.1456 S22: 0.1572 S23: -0.0698
REMARK 3 S31: 0.4089 S32: 0.7032 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 301:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0852 10.9454 -36.8177
REMARK 3 T TENSOR
REMARK 3 T11: 0.3667 T22: 0.3652
REMARK 3 T33: 0.3917 T12: -0.0572
REMARK 3 T13: -0.0147 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.5166 L22: 0.3090
REMARK 3 L33: 0.8588 L12: -0.2779
REMARK 3 L13: -0.0005 L23: 0.4931
REMARK 3 S TENSOR
REMARK 3 S11: 0.1348 S12: 0.0392 S13: 0.0297
REMARK 3 S21: 0.1591 S22: -0.1044 S23: -0.0447
REMARK 3 S31: 0.0124 S32: 0.2991 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 342:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1444 -5.0184 -18.0758
REMARK 3 T TENSOR
REMARK 3 T11: 0.6577 T22: 0.3704
REMARK 3 T33: 0.3813 T12: -0.0312
REMARK 3 T13: -0.0633 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.4501 L22: 0.2681
REMARK 3 L33: 0.2378 L12: 0.3368
REMARK 3 L13: 0.1479 L23: 0.2937
REMARK 3 S TENSOR
REMARK 3 S11: 0.1618 S12: -0.3365 S13: 0.0765
REMARK 3 S21: 0.0909 S22: -0.0661 S23: -0.0217
REMARK 3 S31: 0.6967 S32: 0.1631 S33: 0.0001
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 407:486)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4825 8.5069 -33.4091
REMARK 3 T TENSOR
REMARK 3 T11: 0.2791 T22: 0.3417
REMARK 3 T33: 0.3745 T12: -0.0412
REMARK 3 T13: -0.0064 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.0530 L22: 0.5182
REMARK 3 L33: 1.1179 L12: 0.0406
REMARK 3 L13: -0.0627 L23: 0.5884
REMARK 3 S TENSOR
REMARK 3 S11: 0.0900 S12: -0.0389 S13: 0.0157
REMARK 3 S21: 0.1474 S22: -0.1603 S23: 0.0532
REMARK 3 S31: -0.0214 S32: -0.2438 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1337 22.5060 -28.8858
REMARK 3 T TENSOR
REMARK 3 T11: 0.4178 T22: 0.3452
REMARK 3 T33: 0.3862 T12: 0.0021
REMARK 3 T13: 0.0281 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 0.0483 L22: 0.1184
REMARK 3 L33: 0.1853 L12: -0.0703
REMARK 3 L13: -0.1147 L23: 0.1224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.3598 S13: 0.0701
REMARK 3 S21: 0.2920 S22: 0.0667 S23: 0.1847
REMARK 3 S31: -0.3250 S32: -0.3585 S33: 0.0001
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5741 11.8498 -21.5916
REMARK 3 T TENSOR
REMARK 3 T11: 0.3902 T22: 0.4943
REMARK 3 T33: 0.3012 T12: -0.0092
REMARK 3 T13: 0.0003 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: -0.0047 L22: -0.0665
REMARK 3 L33: 0.2546 L12: -0.0278
REMARK 3 L13: 0.1103 L23: -0.1150
REMARK 3 S TENSOR
REMARK 3 S11: -0.1635 S12: -0.2322 S13: -0.0195
REMARK 3 S21: 0.1935 S22: 0.1085 S23: 0.1046
REMARK 3 S31: -0.0286 S32: 0.1715 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DUE TO INSUFFICIENT ELECTRON
REMARK 3 DENSITY THE FOLLOWING RESIDUES WERE NOT MODELED CHAIN A
REMARK 3 259-263 AND 543-548, CHAIN B 1-3, 259-264 AND 543-548.
REMARK 3 DUE TO INSUFFICIENT ELECTRON DENSITY THE FOLLOWING
REMARK 3 RESIDUES WERE MODELED AS ALANINES, CHAIN A 496 AND CHAIN
REMARK 3 B 493 AND 496.
REMARK 4
REMARK 4 4B83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-12.
REMARK 100 THE PDBE ID CODE IS EBI-53845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.041
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 80333
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 29.22
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.4
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.50
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.4
REMARK 200 R MERGE FOR SHELL (I) : 0.58
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS 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 (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (W/V) PEG750MME, 0.1 M
REMARK 280 HEPES PH 7.0-7.1
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 39.79150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.89150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.92800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.89150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.79150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.92800
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: 8410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.6 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 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 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 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 493 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 258 CG CD
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: 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 PRO B 258 N - CA - CB ANGL. DEV. = 7.3 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 -6.19 76.20
REMARK 500 PHE A 158 -3.19 -141.68
REMARK 500 ALA A 167 70.35 -153.29
REMARK 500 SER A 203 -121.93 57.12
REMARK 500 ASP A 306 -82.85 -124.03
REMARK 500 VAL A 407 -59.91 -125.34
REMARK 500 ASP A 494 59.75 -159.38
REMARK 500 LEU A 518 127.70 -38.14
REMARK 500 ARG A 525 53.83 38.82
REMARK 500 PHE B 47 -4.14 72.48
REMARK 500 CYS B 96 11.92 -143.47
REMARK 500 ALA B 167 75.01 -156.81
REMARK 500 SER B 203 -120.46 52.70
REMARK 500 ASP B 306 -85.44 -117.33
REMARK 500 VAL B 407 -62.78 -125.66
REMARK 500 SER B 497 -79.41 -106.06
REMARK 500 ASN B 514 -166.66 -162.72
REMARK 500 SER B 541 8.11 -64.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 B3V A 1553
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO 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 EDO A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 A1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1545
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 B3V B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1546 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1549 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1546 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: 4ARA RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-
REMARK 900 C5685 AT 2.5 A RESOLUTION.
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.
REMARK 900 RELATED ID: 4B7Z RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B80 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B81 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH C-(4-
REMARK 900 CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B82 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B84 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B85 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-
REMARK 900 CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE
DBREF 4B83 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4B83 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4B83 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4B83 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4B83 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B83 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B83 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B83 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4B83 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4B83 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B83 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B83 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 B3V A1543 19
HET EDO A1544 4
HET EDO A1545 4
HET NAG A1546 14
HET PEG A1547 7
HET PEG A1548 7
HET NAG A1549 14
HET EDO A1550 4
HET EDO A1551 4
HET EDO A1552 4
HET B3V A1553 12
HET SO4 A1554 5
HET EDO A1555 4
HET PE8 A1556 25
HET EDO B1543 4
HET B3V B1544 19
HET EDO B1545 4
HET NAG B1546 14
HET PEG B1547 7
HET EDO B1548 4
HET B3V B1549 19
HET SO4 B1550 5
HET EDO B1551 4
HET PG4 B1552 13
HET EDO B1553 4
HET EDO B2000 4
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM B3V N-[2-(DIETHYLAMINO)ETHYL]-3-METHOXY-
HETNAM 2 B3V BENZENESULFONAMIDE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 B3V 4(C13 H22 N2 O3 S)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 EDO 12(C2 H6 O2)
FORMUL 7 PEG 3(C4 H10 O3)
FORMUL 8 PE8 C16 H34 O9
FORMUL 9 NAG 3(C8 H15 N O6)
FORMUL 10 HOH *374(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 GLY A 143 1 9
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 LEU A 214 1 12
HELIX 10 10 SER A 215 PHE A 222 5 8
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 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
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 ALA A 542 1 9
HELIX 28 28 ASP B 5 GLN B 7 5 3
HELIX 29 29 VAL B 42 ARG B 46 5 5
HELIX 30 30 PHE B 80 MET B 85 1 6
HELIX 31 31 LEU B 130 ASP B 134 5 5
HELIX 32 32 GLY B 135 GLY B 143 1 9
HELIX 33 33 VAL B 153 LEU B 159 1 7
HELIX 34 34 ASN B 170 ILE B 187 1 18
HELIX 35 35 ALA B 188 PHE B 190 5 3
HELIX 36 36 SER B 203 LEU B 214 1 12
HELIX 37 37 SER B 215 PHE B 222 5 8
HELIX 38 38 ALA B 241 VAL B 255 1 15
HELIX 39 39 ASN B 265 THR B 275 1 11
HELIX 40 40 PRO B 277 ASP B 283 1 7
HELIX 41 41 HIS B 284 LEU B 289 5 6
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 VAL B 340 1 6
HELIX 44 44 SER B 355 VAL B 367 1 13
HELIX 45 45 SER B 371 THR B 383 1 13
HELIX 46 46 ASP B 390 VAL B 407 1 18
HELIX 47 47 VAL B 407 GLN B 421 1 15
HELIX 48 48 PRO B 440 GLY B 444 5 5
HELIX 49 49 GLU B 450 PHE B 455 1 6
HELIX 50 50 GLY B 456 ASP B 460 5 5
HELIX 51 51 ASP B 460 ASN B 464 5 5
HELIX 52 52 THR B 466 GLY B 487 1 22
HELIX 53 53 ARG B 525 ARG B 534 1 10
HELIX 54 54 ARG B 534 SER B 541 1 8
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
SHEET 1 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
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 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK ND2 ASN A 350 C1 NAG A1546 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A1549 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B1546 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -5.12
CISPEP 2 TYR B 105 PRO B 106 0 -0.14
CISPEP 3 CYS B 257 PRO B 258 0 0.57
CISPEP 4 SER B 497 PRO B 498 0 -8.64
SITE 1 AC1 13 TRP A 86 GLY A 120 GLY A 121 GLY A 122
SITE 2 AC1 13 TYR A 124 TRP A 286 PHE A 297 TYR A 337
SITE 3 AC1 13 PHE A 338 TYR A 341 HIS A 447 GLY A 448
SITE 4 AC1 13 HOH A2154
SITE 1 AC2 2 GLY A 163 ARG A 165
SITE 1 AC3 2 SER A 57 VAL A 59
SITE 1 AC4 1 ASP A 5
SITE 1 AC5 3 ILE A 20 THR A 63 PRO B 492
SITE 1 AC6 4 THR A 112 GLU A 142 GLY A 143 ARG A 485
SITE 1 AC7 7 ILE A 213 ARG A 219 PHE A 222 PHE A 321
SITE 2 AC7 7 GLN A 322 ASP A 323 LEU A 324
SITE 1 AC8 5 LYS A 23 ALA A 24 PRO A 25 ARG A 136
SITE 2 AC8 5 ASP A 460
SITE 1 AC9 14 ALA A 377 LEU A 380 HIS A 381 GLN A 527
SITE 2 AC9 14 PHE A 531 PHE A 535 HOH A2212 ALA B 377
SITE 3 AC9 14 LEU B 380 HIS B 381 GLN B 527 PHE B 531
SITE 4 AC9 14 PHE B 535 PG4 B1552
SITE 1 BC1 5 PRO B 113 GLU B 142 GLY B 143 ALA B 144
SITE 2 BC1 5 ARG B 485
SITE 1 BC2 9 TRP B 86 TYR B 124 TRP B 286 PHE B 297
SITE 2 BC2 9 TYR B 337 PHE B 338 TYR B 341 HIS B 447
SITE 3 BC2 9 HOH B2115
SITE 1 BC3 2 ARG B 356 GLU B 389
SITE 1 BC4 3 ARG B 11 ARG B 13 GLU B 185
SITE 1 BC5 8 ILE B 213 ARG B 219 PHE B 222 ASP B 320
SITE 2 BC5 8 PHE B 321 GLN B 322 ASP B 323 LEU B 324
SITE 1 BC6 4 LYS B 23 PRO B 25 ARG B 136 ASP B 460
SITE 1 BC7 5 GLN A 527 PE8 A1556 HIS B 381 TYR B 382
SITE 2 BC7 5 ASP B 384
SITE 1 BC8 1 THR B 486
SITE 1 BC9 1 GLN B 413
SITE 1 CC1 3 SER A 347 ASN A 350 HOH A2166
SITE 1 CC2 2 SER A 462 ASN A 464
SITE 1 CC3 2 SER B 347 ASN B 350
CRYST1 79.583 111.856 227.783 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 0.012565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004390 0.00000
TER 4197 ALA A 542
TER 8375 ALA B 542
MASTER 830 0 26 54 34 0 34 6 8975 2 243 86
END |