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HEADER HYDROLASE 23-APR-12 4ARB
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-C5685 AT 2.25 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 4ARB 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. 2.25 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) : 2.250
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.806
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.33
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.89
REMARK 3 NUMBER OF REFLECTIONS : 95904
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1722
REMARK 3 R VALUE (WORKING SET) : 0.1715
REMARK 3 FREE R VALUE : 0.2091
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1893
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 28.8081 - 5.4117 0.99 7053 137 0.1742 0.2016
REMARK 3 2 5.4117 - 4.3000 1.00 6819 133 0.1288 0.1495
REMARK 3 3 4.3000 - 3.7578 1.00 6779 131 0.1354 0.1770
REMARK 3 4 3.7578 - 3.4148 1.00 6713 148 0.1627 0.1970
REMARK 3 5 3.4148 - 3.1704 1.00 6729 115 0.1804 0.2124
REMARK 3 6 3.1704 - 2.9837 1.00 6685 153 0.1752 0.2106
REMARK 3 7 2.9837 - 2.8344 1.00 6704 133 0.1808 0.2343
REMARK 3 8 2.8344 - 2.7111 1.00 6650 138 0.2025 0.2370
REMARK 3 9 2.7111 - 2.6068 1.00 6664 150 0.2006 0.2734
REMARK 3 10 2.6068 - 2.5169 1.00 6676 138 0.2015 0.2633
REMARK 3 11 2.5169 - 2.4382 1.00 6652 119 0.2191 0.2571
REMARK 3 12 2.4382 - 2.3686 1.00 6642 133 0.2287 0.2770
REMARK 3 13 2.3686 - 2.3063 1.00 6643 134 0.2439 0.2971
REMARK 3 14 2.3063 - 2.2500 1.00 6602 131 0.2599 0.3242
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.342
REMARK 3 B_SOL : 70.323
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.30
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.3384
REMARK 3 B22 (A**2) : 2.5156
REMARK 3 B33 (A**2) : -3.8539
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 : 0.008 8776
REMARK 3 ANGLE : 1.090 11969
REMARK 3 CHIRALITY : 0.078 1284
REMARK 3 PLANARITY : 0.005 1571
REMARK 3 DIHEDRAL : 16.664 3166
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2088 11.2991 28.9999
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.2397
REMARK 3 T33: 0.2736 T12: 0.0076
REMARK 3 T13: -0.0112 T23: 0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.2391 L22: 0.1750
REMARK 3 L33: 1.0047 L12: 0.0017
REMARK 3 L13: -0.0694 L23: -0.0483
REMARK 3 S TENSOR
REMARK 3 S11: -0.0438 S12: -0.0881 S13: 0.0254
REMARK 3 S21: 0.0719 S22: 0.0221 S23: -0.0443
REMARK 3 S31: 0.0516 S32: 0.0421 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 229:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5221 9.9315 10.2869
REMARK 3 T TENSOR
REMARK 3 T11: 0.2642 T22: 0.2348
REMARK 3 T33: 0.3165 T12: 0.0414
REMARK 3 T13: 0.0194 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.0184 L22: 0.0643
REMARK 3 L33: 1.2735 L12: 0.2585
REMARK 3 L13: -0.1056 L23: -0.4797
REMARK 3 S TENSOR
REMARK 3 S11: -0.0891 S12: 0.2130 S13: -0.0890
REMARK 3 S21: -0.0831 S22: -0.0196 S23: -0.0817
REMARK 3 S31: 0.2389 S32: 0.2579 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7065 17.4241 6.4363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2307 T22: 0.2595
REMARK 3 T33: 0.2875 T12: -0.0206
REMARK 3 T13: -0.0072 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.4685 L22: 0.3454
REMARK 3 L33: 1.8033 L12: -0.0506
REMARK 3 L13: 0.2512 L23: -0.2481
REMARK 3 S TENSOR
REMARK 3 S11: -0.0321 S12: 0.0905 S13: 0.0152
REMARK 3 S21: -0.0809 S22: 0.0074 S23: 0.0865
REMARK 3 S31: 0.0158 S32: -0.2667 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9359 1.3383 13.5125
REMARK 3 T TENSOR
REMARK 3 T11: 0.3952 T22: 0.5363
REMARK 3 T33: 0.4444 T12: -0.1935
REMARK 3 T13: -0.0118 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 0.1025 L22: 0.1980
REMARK 3 L33: 0.1138 L12: -0.1197
REMARK 3 L13: 0.1317 L23: -0.0917
REMARK 3 S TENSOR
REMARK 3 S11: -0.0452 S12: 0.1980 S13: -0.1113
REMARK 3 S21: -0.1038 S22: 0.0938 S23: 0.5021
REMARK 3 S31: 0.6675 S32: -0.8945 S33: 0.0004
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2854 6.3249 -1.0277
REMARK 3 T TENSOR
REMARK 3 T11: 0.3523 T22: 0.4280
REMARK 3 T33: 0.3840 T12: -0.0561
REMARK 3 T13: -0.0580 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.2836 L22: -0.0757
REMARK 3 L33: 0.5231 L12: -0.1560
REMARK 3 L13: 0.4453 L23: -0.1300
REMARK 3 S TENSOR
REMARK 3 S11: 0.1991 S12: -0.0153 S13: 0.0005
REMARK 3 S21: -0.2693 S22: -0.1343 S23: 0.2499
REMARK 3 S31: -0.0638 S32: 0.0471 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6209 6.1949 -61.7900
REMARK 3 T TENSOR
REMARK 3 T11: 0.3031 T22: 0.4555
REMARK 3 T33: 0.3374 T12: 0.0569
REMARK 3 T13: -0.0669 T23: -0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 0.2470 L22: 0.4960
REMARK 3 L33: 0.7685 L12: -0.0083
REMARK 3 L13: 0.3197 L23: 0.1435
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: 0.2933 S13: -0.0210
REMARK 3 S21: -0.2022 S22: -0.0718 S23: -0.0605
REMARK 3 S31: -0.0268 S32: -0.2764 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2144 -4.2019 -52.9520
REMARK 3 T TENSOR
REMARK 3 T11: 0.4212 T22: 0.4162
REMARK 3 T33: 0.3377 T12: -0.0010
REMARK 3 T13: -0.0408 T23: -0.0815
REMARK 3 L TENSOR
REMARK 3 L11: -0.1448 L22: 0.4353
REMARK 3 L33: 0.4277 L12: 0.0640
REMARK 3 L13: 0.1585 L23: 0.1880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: 0.2136 S13: -0.1023
REMARK 3 S21: -0.0542 S22: -0.0798 S23: 0.0205
REMARK 3 S31: 0.2582 S32: 0.0331 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 87:170)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9177 4.0898 -50.9208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2692 T22: 0.3304
REMARK 3 T33: 0.2832 T12: 0.0047
REMARK 3 T13: -0.0364 T23: -0.0659
REMARK 3 L TENSOR
REMARK 3 L11: 0.1928 L22: 0.3626
REMARK 3 L33: 1.4111 L12: 0.2255
REMARK 3 L13: 0.4407 L23: 0.2671
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: 0.1461 S13: -0.1781
REMARK 3 S21: -0.0732 S22: -0.0485 S23: 0.0562
REMARK 3 S31: 0.1067 S32: -0.1163 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 171:237)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1949 13.3797 -48.2655
REMARK 3 T TENSOR
REMARK 3 T11: 0.3195 T22: 0.3344
REMARK 3 T33: 0.3006 T12: 0.0167
REMARK 3 T13: -0.0162 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.2609 L22: 0.2579
REMARK 3 L33: 0.4760 L12: 0.0051
REMARK 3 L13: -0.3360 L23: 0.2790
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: 0.1080 S13: -0.0077
REMARK 3 S21: -0.0268 S22: 0.0297 S23: 0.0254
REMARK 3 S31: -0.1421 S32: 0.0455 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 238:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0118 -8.3606 -45.9560
REMARK 3 T TENSOR
REMARK 3 T11: 0.4050 T22: 0.4446
REMARK 3 T33: 0.3683 T12: 0.1291
REMARK 3 T13: -0.0919 T23: -0.0748
REMARK 3 L TENSOR
REMARK 3 L11: 0.2473 L22: 0.4135
REMARK 3 L33: 0.2147 L12: -0.2345
REMARK 3 L13: 0.2420 L23: -0.1041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: 0.1012 S13: -0.0585
REMARK 3 S21: 0.2057 S22: 0.0516 S23: -0.1090
REMARK 3 S31: 0.3595 S32: 0.6006 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 301:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8863 10.7038 -36.7752
REMARK 3 T TENSOR
REMARK 3 T11: 0.2984 T22: 0.2801
REMARK 3 T33: 0.3343 T12: -0.0390
REMARK 3 T13: -0.0315 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 0.6304 L22: 0.5318
REMARK 3 L33: 1.1269 L12: -0.3974
REMARK 3 L13: 0.1829 L23: 0.6252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0742 S12: 0.0264 S13: 0.0674
REMARK 3 S21: 0.0471 S22: 0.0090 S23: -0.0498
REMARK 3 S31: 0.0264 S32: 0.1718 S33: -0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 342:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6017 2.4875 -26.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.3423 T22: 0.2729
REMARK 3 T33: 0.3089 T12: -0.0500
REMARK 3 T13: -0.0111 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.4761 L22: 0.2269
REMARK 3 L33: 1.5145 L12: 0.0122
REMARK 3 L13: 0.2987 L23: 0.4391
REMARK 3 S TENSOR
REMARK 3 S11: 0.1166 S12: -0.0545 S13: -0.0072
REMARK 3 S21: 0.1840 S22: -0.1111 S23: 0.0591
REMARK 3 S31: 0.2369 S32: -0.1260 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4034 22.5491 -28.6421
REMARK 3 T TENSOR
REMARK 3 T11: 0.3392 T22: 0.2581
REMARK 3 T33: 0.3472 T12: 0.0112
REMARK 3 T13: 0.0035 T23: -0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 0.1251 L22: 0.2306
REMARK 3 L33: 0.3656 L12: -0.0622
REMARK 3 L13: -0.2261 L23: 0.1440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0779 S12: -0.1933 S13: 0.5080
REMARK 3 S21: 0.1458 S22: -0.0633 S23: 0.3032
REMARK 3 S31: -0.2831 S32: -0.1344 S33: -0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1696 11.3791 -21.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.3579 T22: 0.4036
REMARK 3 T33: 0.2966 T12: 0.0065
REMARK 3 T13: -0.0014 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.0624 L22: 0.0994
REMARK 3 L33: 0.5935 L12: 0.0085
REMARK 3 L13: 0.2249 L23: -0.0175
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: -0.0032 S13: -0.0857
REMARK 3 S21: 0.0694 S22: -0.1010 S23: 0.1504
REMARK 3 S31: -0.0121 S32: 0.1605 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 4ARB 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-52169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-11
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 : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.039
REMARK 200 MONOCHROMATOR : RH-COATED SI MIRROR, BENT
REMARK 200 FOR 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 : 96077
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.25
REMARK 200 RESOLUTION RANGE LOW (A) : 29.10
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.7
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.7
REMARK 200 R MERGE FOR SHELL (I) : 0.48
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.70
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
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 39.46300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.53550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.89050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.53550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.46300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.89050
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: 4220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.3 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 GLN A 322 CG CD OE1 NE2
REMARK 470 ASP A 323 CG OD1 OD2
REMARK 470 ASN A 464 ND2
REMARK 470 ASP A 491 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 LYS B 478 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND1 ASN A 464 O A2G A 1547 1.80
REMARK 500 O HOH A 2042 O HOH A 2101 2.20
REMARK 500 O HOH A 2202 O HOH A 2392 2.19
REMARK 500 O HOH A 2238 O HOH A 2492 2.19
REMARK 500 O HOH B 2142 O HOH B 2287 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 -5.86 74.63
REMARK 500 PHE A 158 -7.58 -140.61
REMARK 500 ALA A 167 68.72 -156.94
REMARK 500 SER A 203 -124.47 53.42
REMARK 500 ASP A 306 -85.67 -127.94
REMARK 500 HIS A 387 59.73 -140.60
REMARK 500 VAL A 407 -60.79 -130.27
REMARK 500 ARG A 493 43.10 -109.99
REMARK 500 ASP A 494 -62.88 -132.65
REMARK 500 SER A 495 -45.86 57.84
REMARK 500 PHE B 47 -5.17 73.88
REMARK 500 ALA B 62 50.28 -116.59
REMARK 500 ALA B 167 70.66 -150.35
REMARK 500 ASN B 170 16.37 57.56
REMARK 500 SER B 203 -125.12 52.23
REMARK 500 ASP B 306 -84.69 -117.65
REMARK 500 VAL B 407 -58.18 -130.18
REMARK 500 SER B 541 41.72 -75.54
REMARK 500 ALA B 542 -11.70 -170.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-
REMARK 600 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE (568):
REMARK 600 CORRESPONDING TO LIGAND C57 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 C57 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C57 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1545 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1547 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1547 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.
DBREF 4ARB A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4ARB B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4ARB ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4ARB THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4ARB GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4ARB ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4ARB PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4ARB ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4ARB THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4ARB GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4ARB ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4ARB 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
MODRES 4ARB ASN A 350 ASN GLYCOSYLATION SITE
MODRES 4ARB ASN B 350 ASN GLYCOSYLATION SITE
HET C57 A1543 25
HET PEG A1544 7
HET NAG A1545 14
HET PEG A1546 7
HET NAG A1547 14
HET PEG A1548 7
HET PEG A1549 7
HET C57 B1544 25
HET P6G B1545 19
HET PEG B1546 7
HET NAG B1547 14
HET PEG B1548 7
HETNAM C57 4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-
HETNAM 2 C57 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 C57 2(C17 H26 N4 O4)
FORMUL 4 PEG 6(C4 H10 O3)
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 6 P6G C12 H26 O7
FORMUL 7 HOH *989(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 SER A 215 1 13
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 THR A 275 1 11
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 SER A 541 1 8
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 SER B 220 1 6
HELIX 38 38 SER B 240 VAL B 255 1 16
HELIX 39 39 ASN B 265 ARG B 276 1 12
HELIX 40 40 PRO B 277 TRP B 286 1 10
HELIX 41 41 HIS B 287 LEU B 289 5 3
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
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
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 2.05
LINK ND2 ASN A 350 C1 NAG A1545 1555 1555 1.48
LINK ND2 ASN A 464 C1 NAG A1547 1555 1555 1.51
LINK ND2 ASN B 350 C1 NAG B1547 1555 1555 1.41
CISPEP 1 TYR A 105 PRO A 106 0 -1.33
CISPEP 2 TYR B 105 PRO B 106 0 0.77
CISPEP 3 SER B 497 PRO B 498 0 5.67
SITE 1 AC1 14 TYR A 72 ASP A 74 TRP A 86 TYR A 124
SITE 2 AC1 14 TRP A 286 SER A 293 ILE A 294 PHE A 295
SITE 3 AC1 14 ARG A 296 TYR A 337 PHE A 338 TYR A 341
SITE 4 AC1 14 HOH A2367 HOH A2368
SITE 1 AC2 3 ASP A 304 GLY A 305 SER A 309
SITE 1 AC3 3 HIS A 381 HIS A 393 HOH A2431
SITE 1 AC4 3 GLN A 413 ARG A 417 HOH A2535
SITE 1 AC5 11 TYR B 72 ASP B 74 TYR B 124 TRP B 286
SITE 2 AC5 11 SER B 293 ILE B 294 PHE B 295 ARG B 296
SITE 3 AC5 11 TYR B 337 PHE B 338 TYR B 341
SITE 1 AC6 13 ALA A 377 LEU A 380 HIS A 381 GLN A 527
SITE 2 AC6 13 PHE A 531 PHE A 535 HOH A2430 LEU B 380
SITE 3 AC6 13 HIS B 381 THR B 528 PHE B 531 HOH B2341
SITE 4 AC6 13 HOH B2447
SITE 1 AC7 3 HIS B 381 ASP B 384 HOH B2449
SITE 1 AC8 3 GLY B 305 SER B 309 HOH B2451
SITE 1 AC9 7 SER A 347 ASN A 350 HOH A2398 HOH A2399
SITE 2 AC9 7 HOH A2532 HOH A2533 HOH A2534
SITE 1 BC1 1 ASN A 464
SITE 1 BC2 6 SER B 347 ASN B 350 LEU B 353 HOH B2322
SITE 2 BC2 6 HOH B2323 HOH B2450
CRYST1 78.926 111.781 227.071 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 0.012670 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004404 0.00000
TER 4196 ALA A 542
TER 8367 THR B 543
MASTER 738 0 12 54 32 0 21 6 9507 2 168 86
END |