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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 18-AUG-93 1ACL 1ACL 2
COMPND ACETYLCHOLINESTERASE (E.C.3.1.1.7) COMPLEXED WITH 1ACL 3
COMPND 2 DECAMETHONIUM 1ACL 4
SOURCE (TORPEDO CALIFORNICA) 1ACL 5
AUTHOR J.L.SUSSMAN,M.HAREL,I.SILMAN 1ACL 6
REVDAT 1 31-AUG-94 1ACL 0 1ACL 7
JRNL AUTH M.HAREL,I.SCHALK,L.EHRET-SABATTIER,F.BOUET, 1ACL 8
JRNL AUTH 2 M.GOELDNER,C.HIRTH,P.AXELSEN,I.SILMAN,J.SUSSMAN 1ACL 9
JRNL TITL QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN 1ACL 10
JRNL TITL 2 THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE 1ACL 11
JRNL REF PROC.NAT.ACAD.SCI.USA V. 90 9031 1993 1ACL 12
JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040 1ACL 13
REMARK 1 1ACL 14
REMARK 1 REFERENCE 1 1ACL 15
REMARK 1 AUTH J.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN, 1ACL 16
REMARK 1 AUTH 2 L.TOKER,I.SILMAN 1ACL 17
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM 1ACL 18
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC 1ACL 19
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN 1ACL 20
REMARK 1 REF SCIENCE V. 253 872 1991 1ACL 21
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1ACL 22
REMARK 2 1ACL 23
REMARK 2 RESOLUTION. 2.8 ANGSTROMS. 1ACL 24
REMARK 3 1ACL 25
REMARK 3 REFINEMENT. 1ACL 26
REMARK 3 PROGRAM X-PLOR 1ACL 27
REMARK 3 AUTHORS BRUNGER 1ACL 28
REMARK 3 R VALUE 0.199 1ACL 29
REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1ACL 30
REMARK 3 1ACL 31
REMARK 3 NUMBER OF REFLECTIONS 23089 1ACL 32
REMARK 3 RESOLUTION RANGE 8.0 - 2.8 ANGSTROMS 1ACL 33
REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 1ACL 34
REMARK 3 PERCENT COMPLETION 91.2 1ACL 35
REMARK 3 1ACL 36
REMARK 3 NUMBER OF PROTEIN ATOMS 4110 1ACL 37
REMARK 3 NUMBER OF SOLVENT ATOMS 66 1ACL 38
REMARK 4 1ACL 39
REMARK 4 DECAMETHONIUM, A BISQUATERNARY INHIBITOR OF 1ACL 40
REMARK 4 ACETYLCHOLINESTERASE, WAS SOAKED INTO NATIVE CRYSTALS. 1ACL 41
REMARK 5 1ACL 42
REMARK 5 THE STRUCTURE WAS REFINED STARTING FROM NATIVE COORDINATES 1ACL 43
REMARK 5 USING X-PLOR. 1ACL 44
REMARK 6 1ACL 45
REMARK 6 RESIDUES 1 - 3, 485 - 489, AND 536 - 537 ARE NOT SEEN AND 1ACL 46
REMARK 6 NO COORDINATES ARE SUPPLIED FOR THEM. 1ACL 47
REMARK 7 1ACL 48
REMARK 7 PDB ADVISORY NOTICE: SIDE CHAIN ATOMS ARE MISSING FOR THE 1ACL 49
REMARK 7 FOLLOWING RESIDUES: 26, 42, 46, 47, 49, 88, 89, 161, 257, 1ACL 50
REMARK 7 260, 268, 270, 284, 299, 325, 344, 350, 353, 365, 382, 1ACL 51
REMARK 7 434, 455, 461, 478, 484, 498, 499, 508, 515, 526, AND 533. 1ACL 52
SEQRES 1 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY 1ACL 53
SEQRES 2 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS 1ACL 54
SEQRES 3 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO 1ACL 55
SEQRES 4 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS 1ACL 56
SEQRES 5 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN 1ACL 57
SEQRES 6 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE 1ACL 58
SEQRES 7 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER 1ACL 59
SEQRES 8 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO 1ACL 60
SEQRES 9 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY 1ACL 61
SEQRES 10 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR 1ACL 62
SEQRES 11 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU 1ACL 63
SEQRES 12 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU 1ACL 64
SEQRES 13 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY 1ACL 65
SEQRES 14 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP 1ACL 66
SEQRES 15 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR 1ACL 67
SEQRES 16 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET 1ACL 68
SEQRES 17 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG 1ACL 69
SEQRES 18 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA 1ACL 70
SEQRES 19 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU 1ACL 71
SEQRES 20 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU 1ACL 72
SEQRES 21 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU 1ACL 73
SEQRES 22 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER 1ACL 74
SEQRES 23 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU 1ACL 75
SEQRES 24 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY 1ACL 76
SEQRES 25 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS 1ACL 77
SEQRES 26 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY 1ACL 78
SEQRES 27 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP 1ACL 79
SEQRES 28 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN 1ACL 80
SEQRES 29 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP 1ACL 81
SEQRES 30 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY 1ACL 82
SEQRES 31 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO 1ACL 83
SEQRES 32 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN 1ACL 84
SEQRES 33 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN 1ACL 85
SEQRES 34 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR 1ACL 86
SEQRES 35 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU 1ACL 87
SEQRES 36 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG 1ACL 88
SEQRES 37 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN 1ACL 89
SEQRES 38 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU 1ACL 90
SEQRES 39 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR 1ACL 91
SEQRES 40 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET 1ACL 92
SEQRES 41 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN 1ACL 93
SEQRES 42 537 ALA THR GLU THR 1ACL 94
FTNOTE 1 1ACL 95
FTNOTE 1 CIS PROLINE - PRO 104 1ACL 96
FTNOTE 2 1ACL 97
FTNOTE 2 RESIDUE DME 999 IS BOUND NON-COVALENTLY IN THE ACTIVE SITE. 1ACL 98
HET DME 999 18 DECAMETHONIUM 1ACL 99
FORMUL 2 DME C16 H38 N2 ++ 1ACL 100
FORMUL 3 HOH *66(H2 O1) 1ACL 101
HELIX 1 H1 SER 79 ASN 85 1 1ACL 102
HELIX 2 H2 GLY 132 GLU 139 1 1ACL 103
HELIX 3 H3 VAL 168 ASN 183 1 1ACL 104
HELIX 4 H4 SER 200 LEU 211 1 1ACL 105
HELIX 5 H5 VAL 238 LEU 252 1 1ACL 106
HELIX 6 H6 ASP 259 GLU 268 1 1ACL 107
HELIX 7 H7 PRO 271 GLU 278 1 1ACL 108
HELIX 8 H8 LEU 305 SER 311 1 1ACL 109
HELIX 9 H9 SER 329 GLY 335 1 1ACL 110
HELIX 10 H10 ARG 349 VAL 360 1 1ACL 111
HELIX 11 H11 ASP 365 THR 376 1 1ACL 112
HELIX 12 H12 GLY 384 TYR 411 1 1ACL 113
HELIX 13 H13 GLU 443 PHE 448 1 1ACL 114
HELIX 14 H14 ALA 460 THR 479 1 1ACL 115
HELIX 15 H15 VAL 518 ALA 534 1 1ACL 116
SHEET 1 S112 LEU 6 THR 10 0 1ACL 117
SHEET 2 S112 GLY 13 MET 16 -1 1ACL 118
SHEET 3 S112 THR 18 PRO 21 -1 1ACL 119
SHEET 4 S112 HIS 26 PRO 34 -1 1ACL 120
SHEET 5 S112 VAL 57 ALA 60 -1 1ACL 121
SHEET 6 S112 TYR 96 PRO 102 -1 1ACL 122
SHEET 7 S112 VAL 142 SER 147 -1 1ACL 123
SHEET 8 S112 THR 109 TYR 116 1 1ACL 124
SHEET 9 S112 THR 193 GLU 199 1 1ACL 125
SHEET 10 S112 ARG 220 SER 226 1 1ACL 126
SHEET 11 S112 GLN 318 TYR 334 1 1ACL 127
SHEET 12 S112 GLY 417 PHE 423 1 1ACL 128
SHEET 1 S2 2 PHE 502 LEU 505 0 1ACL 129
SHEET 2 S2 2 MET 510 GLN 514 -1 1ACL 130
SSBOND 1 CYS 67 CYS 94 1ACL 131
SSBOND 2 CYS 254 CYS 265 1ACL 132
SSBOND 3 CYS 402 CYS 521 1ACL 133
SITE 1 DME 4 SER 200 HIS 440 GLU 327 DME 999 1ACL 134
CRYST1 113.050 113.050 137.500 90.00 90.00 120.00 P 31 2 1 6 1ACL 135
ORIGX1 1.000000 0.000000 0.000000 0.00000 1ACL 136
ORIGX2 0.000000 1.000000 0.000000 0.00000 1ACL 137
ORIGX3 0.000000 0.000000 1.000000 0.00000 1ACL 138
SCALE1 0.008846 0.005107 0.000000 0.00000 1ACL 139
SCALE2 0.000000 0.010214 0.000000 0.00000 1ACL 140
SCALE3 0.000000 0.000000 0.007273 0.00000 1ACL 141 |