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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 18-AUG-93 1ACJ 1ACJ 2
COMPND ACETYLCHOLINESTERASE (E.C.3.1.1.7) COMPLEXED WITH TACRINE 1ACJ 3
SOURCE (TORPEDO CALIFORNICA) 1ACJ 4
AUTHOR J.L.SUSSMAN,M.HAREL,I.SILMAN 1ACJ 5
REVDAT 1 31-AUG-94 1ACJ 0 1ACJ 6
JRNL AUTH M.HAREL,I.SCHALK,L.EHRET-SABATTIER,F.BOUET, 1ACJ 7
JRNL AUTH 2 M.GOELDNER,C.HIRTH,P.AXELSEN,I.SILMAN,J.SUSSMAN 1ACJ 8
JRNL TITL QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN 1ACJ 9
JRNL TITL 2 THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE 1ACJ 10
JRNL REF PROC.NAT.ACAD.SCI.USA V. 90 9031 1993 1ACJ 11
JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040 1ACJ 12
REMARK 1 1ACJ 13
REMARK 1 REFERENCE 1 1ACJ 14
REMARK 1 AUTH J.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN, 1ACJ 15
REMARK 1 AUTH 2 L.TOKER,I.SILMAN 1ACJ 16
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM 1ACJ 17
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC 1ACJ 18
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN 1ACJ 19
REMARK 1 REF SCIENCE V. 253 872 1991 1ACJ 20
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1ACJ 21
REMARK 2 1ACJ 22
REMARK 2 RESOLUTION. 2.8 ANGSTROMS. 1ACJ 23
REMARK 3 1ACJ 24
REMARK 3 REFINEMENT. 1ACJ 25
REMARK 3 PROGRAM X-PLOR 1ACJ 26
REMARK 3 AUTHORS BRUNGER 1ACJ 27
REMARK 3 R VALUE 0.195 1ACJ 28
REMARK 3 RMSD BOND DISTANCES 0.025 ANGSTROMS 1ACJ 29
REMARK 3 1ACJ 30
REMARK 3 NUMBER OF REFLECTIONS 23213 1ACJ 31
REMARK 3 RESOLUTION RANGE 8.0 - 2.8 ANGSTROMS 1ACJ 32
REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1ACJ 33
REMARK 3 PERCENT COMPLETION 92.3 1ACJ 34
REMARK 3 1ACJ 35
REMARK 3 NUMBER OF PROTEIN ATOMS 4094 1ACJ 36
REMARK 3 NUMBER OF SOLVENT ATOMS 82 1ACJ 37
REMARK 4 1ACJ 38
REMARK 4 TACRINE (1,2,3,4-TETRAHYDRO-9-AMINOACRIDINE), AN 1ACJ 39
REMARK 4 ALZHEIMER'S DISEASE EXPERIMENTAL DRUG, WAS SOAKED INTO 1ACJ 40
REMARK 4 NATIVE CRYSTALS. 1ACJ 41
REMARK 5 1ACJ 42
REMARK 5 THE STRUCTURE WAS REFINED STARTING FROM NATIVE COORDINATES 1ACJ 43
REMARK 5 USING X-PLOR. 82 WATER MOLECULES ARE INCLUDED. 1ACJ 44
REMARK 6 1ACJ 45
REMARK 6 RESIDUES 1 - 3, 486 - 489, AND 536 - 537 ARE NOT SEEN IN 1ACJ 46
REMARK 6 THE ELECTRON DENSITY MAP AND NO COORDINATES ARE SUPPLIED 1ACJ 47
REMARK 6 FOR THEM. 1ACJ 48
REMARK 7 1ACJ 49
REMARK 7 THE FOLLOWING RESIDUES HAVE MISSING SIDE CHAIN ATOMS: 19, 1ACJ 50
REMARK 7 26, 42, 46, 74, 88, 89, 107, 162, 163, 253, 257, 260, 261, 1ACJ 51
REMARK 7 268, 270, 284, 286, 299, 310, 325, 344, 350, 353, 365, 382, 1ACJ 52
REMARK 7 413, 434, 455, 461, 478, 484, 498, 499, 508, 511, 515, 526 1ACJ 53
REMARK 7 AND 533. 1ACJ 54
REMARK 8 1ACJ 55
REMARK 8 CROSS REFERENCE TO SEQUENCE DATABASE 1ACJ 56
REMARK 8 SWISS-PROT ENTRY NAME 1ACJ 57
REMARK 8 ACES_TORCA 1ACJ 58
SEQRES 1 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY 1ACJ 59
SEQRES 2 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS 1ACJ 60
SEQRES 3 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO 1ACJ 61
SEQRES 4 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS 1ACJ 62
SEQRES 5 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN 1ACJ 63
SEQRES 6 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE 1ACJ 64
SEQRES 7 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER 1ACJ 65
SEQRES 8 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO 1ACJ 66
SEQRES 9 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY 1ACJ 67
SEQRES 10 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR 1ACJ 68
SEQRES 11 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU 1ACJ 69
SEQRES 12 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU 1ACJ 70
SEQRES 13 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY 1ACJ 71
SEQRES 14 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP 1ACJ 72
SEQRES 15 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR 1ACJ 73
SEQRES 16 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET 1ACJ 74
SEQRES 17 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG 1ACJ 75
SEQRES 18 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA 1ACJ 76
SEQRES 19 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU 1ACJ 77
SEQRES 20 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU 1ACJ 78
SEQRES 21 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU 1ACJ 79
SEQRES 22 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER 1ACJ 80
SEQRES 23 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU 1ACJ 81
SEQRES 24 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY 1ACJ 82
SEQRES 25 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS 1ACJ 83
SEQRES 26 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY 1ACJ 84
SEQRES 27 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP 1ACJ 85
SEQRES 28 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN 1ACJ 86
SEQRES 29 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP 1ACJ 87
SEQRES 30 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY 1ACJ 88
SEQRES 31 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO 1ACJ 89
SEQRES 32 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN 1ACJ 90
SEQRES 33 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN 1ACJ 91
SEQRES 34 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR 1ACJ 92
SEQRES 35 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU 1ACJ 93
SEQRES 36 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG 1ACJ 94
SEQRES 37 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN 1ACJ 95
SEQRES 38 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU 1ACJ 96
SEQRES 39 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR 1ACJ 97
SEQRES 40 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET 1ACJ 98
SEQRES 41 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN 1ACJ 99
SEQRES 42 537 ALA THR GLU THR 1ACJ 100
FTNOTE 1 1ACJ 101
FTNOTE 1 CIS PROLINE - PRO 104 1ACJ 102
FTNOTE 2 1ACJ 103
FTNOTE 2 RESIDUE THA 999 IS BOUND NON-COVALENTLY IN THE ACTIVE SITE. 1ACJ 104
HET THA 999 15 TACRINE 1ACJ 105
FORMUL 2 THA C13 H14 N2 1ACJ 106
FORMUL 3 HOH *82(H2 O1) 1ACJ 107
HELIX 1 H1 SER 79 ASN 85 1 1ACJ 108
HELIX 2 H2 GLY 132 GLU 139 1 1ACJ 109
HELIX 3 H3 VAL 168 ASN 183 1 1ACJ 110
HELIX 4 H4 SER 200 LEU 211 1 1ACJ 111
HELIX 5 H5 VAL 238 LEU 252 1 1ACJ 112
HELIX 6 H6 ASP 259 GLU 268 1 1ACJ 113
HELIX 7 H7 PRO 271 GLU 278 1 1ACJ 114
HELIX 8 H8 LEU 305 SER 311 1 1ACJ 115
HELIX 9 H9 SER 329 GLY 335 1 1ACJ 116
HELIX 10 H10 ARG 349 VAL 360 1 1ACJ 117
HELIX 11 H11 ASP 365 THR 376 1 1ACJ 118
HELIX 12 H12 GLY 384 TYR 411 1 1ACJ 119
HELIX 13 H13 GLU 443 PHE 448 1 1ACJ 120
HELIX 14 H14 ALA 460 THR 479 1 1ACJ 121
HELIX 15 H15 VAL 518 ALA 534 1 1ACJ 122
SHEET 1 S112 LEU 6 THR 10 0 1ACJ 123
SHEET 2 S112 GLY 13 MET 16 -1 1ACJ 124
SHEET 3 S112 THR 18 PRO 21 -1 1ACJ 125
SHEET 4 S112 HIS 26 PRO 34 -1 1ACJ 126
SHEET 5 S112 VAL 57 ALA 60 -1 1ACJ 127
SHEET 6 S112 TYR 96 PRO 102 -1 1ACJ 128
SHEET 7 S112 VAL 142 SER 147 -1 1ACJ 129
SHEET 8 S112 THR 109 TYR 116 1 1ACJ 130
SHEET 9 S112 THR 193 GLU 199 1 1ACJ 131
SHEET 10 S112 ARG 220 SER 226 1 1ACJ 132
SHEET 11 S112 GLN 318 TYR 334 1 1ACJ 133
SHEET 12 S112 GLY 417 PHE 423 1 1ACJ 134
SHEET 1 S2 2 PHE 502 LEU 505 0 1ACJ 135
SHEET 2 S2 2 MET 510 GLN 514 -1 1ACJ 136
SSBOND 1 CYS 67 CYS 94 1ACJ 137
SSBOND 2 CYS 254 CYS 265 1ACJ 138
SSBOND 3 CYS 402 CYS 521 1ACJ 139
SITE 1 THA 4 SER 200 HIS 440 GLU 327 THA 999 1ACJ 140
CRYST1 113.700 113.700 138.100 90.00 90.00 120.00 P 31 2 1 6 1ACJ 141
ORIGX1 1.000000 0.000000 0.000000 0.00000 1ACJ 142
ORIGX2 0.000000 1.000000 0.000000 0.00000 1ACJ 143
ORIGX3 0.000000 0.000000 1.000000 0.00000 1ACJ 144
SCALE1 0.008795 0.005078 0.000000 0.00000 1ACJ 145
SCALE2 0.000000 0.010156 0.000000 0.00000 1ACJ 146
SCALE3 0.000000 0.000000 0.007241 0.00000 1ACJ 147 |