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HEADER HYDROLASE (SERINE ESTERASE) 13-FEB-96 1AMN 1AMN 2
TITLE TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH 1AMN 3
TITLE 2 M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE 1AMN 4
COMPND MOL_ID: 1; 1AMN 5
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE; 1AMN 6
COMPND 3 CHAIN: NULL; 1AMN 7
COMPND 4 EC: 3.1.1.7 1AMN 8
SOURCE MOL_ID: 1; 1AMN 9
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA; 1AMN 10
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY; 1AMN 11
SOURCE 4 ORGAN: ELECTRIC ORGAN 1AMN 12
KEYWDS HYDROLASE, SERINE ESTERASE, SYNAPSE, MEMBRANE, NERVE, 1AMN 13
KEYWDS 2 MUSCLE, SIGNAL, NEUROTRANSMITTER DEGRADATION, 1AMN 14
KEYWDS 3 GLYCOPROTEIN, GPI-ANCHOR, ALTERNATIVE SPLICING 1AMN 15
EXPDTA X-RAY DIFFRACTION, SINGLE CRYSTAL 1AMN 16
AUTHOR M.HAREL,I.SILMAN,J.L.SUSSMAN 1AMN 17
REVDAT 1 03-APR-96 1AMN 0 1AMN 18
JRNL AUTH M.HAREL,D.M.QUINN,H.K.NAIR,I.SILMAN,J.L.SUSSMAN 1AMN 19
JRNL TITL THE X-RAY STRUCTURE OF A TRANSITION STATE ANALOG 1AMN 20
JRNL TITL 2 COMPLEX REVEALS THE MOLECULAR ORIGINS OF THE 1AMN 21
JRNL TITL 3 CATALYTIC POWER AND SUBSTRATE SPECIFICITY OF 1AMN 22
JRNL TITL 4 ACETYLCHOLINESTERASE 1AMN 23
JRNL REF TO BE PUBLISHED 1AMN 24
JRNL REFN 0353 1AMN 25
REMARK 1 1AMN 26
REMARK 1 REFERENCE 1 1AMN 27
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN, 1AMN 28
REMARK 1 AUTH 2 L.TOKER,I.SILMAN 1AMN 29
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM 1AMN 30
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC ACETYLCHOLINE 1AMN 31
REMARK 1 TITL 3 BINDING ENZYME 1AMN 32
REMARK 1 REF SCIENCE V. 283 872 1991 1AMN 33
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1AMN 34
REMARK 2 1AMN 35
REMARK 2 RESOLUTION. 2.8 ANGSTROMS. 1AMN 36
REMARK 3 1AMN 37
REMARK 3 REFINEMENT. 1AMN 38
REMARK 3 PROGRAM X-PLOR 1AMN 39
REMARK 3 AUTHORS BRUNGER 1AMN 40
REMARK 3 R VALUE 0.188 1AMN 41
REMARK 3 FREE R VALUE 0.235 1AMN 42
REMARK 3 MEAN B VALUE 22.0 ANGSTROMS**2 1AMN 43
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1AMN 44
REMARK 3 RMSD BOND ANGLES 1.72 DEGREES 1AMN 45
REMARK 3 RMSD DIHEDRAL ANGLES 24.11 DEGREES 1AMN 46
REMARK 3 1AMN 47
REMARK 3 NUMBER OF REFLECTIONS 24138 1AMN 48
REMARK 3 RESOLUTION RANGE 8.0 - 2.8 ANGSTROMS 1AMN 49
REMARK 3 DATA CUTOFF 0. SIGMA(F) 1AMN 50
REMARK 3 1AMN 51
REMARK 3 DATA COLLECTION. 1AMN 52
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 25272 1AMN 53
REMARK 3 COMPLETENESS OF DATA 98.0 % 1AMN 54
REMARK 3 1AMN 55
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1AMN 56
REMARK 3 NUMBER OF PROTEIN ATOMS 4151 1AMN 57
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1AMN 58
REMARK 3 NUMBER OF HETEROGEN ATOMS 22 1AMN 59
REMARK 3 NUMBER OF SOLVENT ATOMS 99 1AMN 60
REMARK 4 1AMN 61
REMARK 4 ACETYLCHOLINESTERASE CRYSTALS SOAKED IN 2MM SOLUTION OF 1AMN 62
REMARK 4 THE TRANSITION STATE ANALOG FOR 12 DAYS. 1AMN 63
REMARK 5 1AMN 64
REMARK 5 HET GROUP NAF IS M-(N,N,N-TRIMETHYLAMMONIO)-2,2,2- 1AMN 65
REMARK 5 TRIFLUORO-1,1-DIHYDROXYETHYLBENZENE. 1AMN 66
REMARK 6 1AMN 67
REMARK 6 THE FOLLOWING RESIDUES HAVE INCOMPLETE SIDE CHAIN ATOMS: 1AMN 68
REMARK 6 ARG 19, ASN 42, ARG 46, SER 55, GLU 89, SER 200, ASN 257, 1AMN 69
REMARK 6 GLU 260, GLU 261, GLU 299, GLU 344, GLU 365, LYS 413, LYS 1AMN 70
REMARK 6 498, GLU 508, ARG 515, ASN 533. 1AMN 71
REMARK 18 1AMN 72
REMARK 18 EXPERIMENTAL DETAILS. 1AMN 73
REMARK 18 DATE OF DATA COLLECTION : 15-MAY-93 1AMN 74
REMARK 18 MONOCHROMATIC (Y/N) : Y 1AMN 75
REMARK 18 LAUE (Y/N) : N 1AMN 76
REMARK 18 WAVELENGTH OR RANGE (A) : 1.54 1AMN 77
REMARK 18 DETECTOR TYPE : XENTRONICS 1AMN 78
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : XDS 1AMN 79
REMARK 18 DATA REDUNDANCY : 3.08 1AMN 80
REMARK 18 MERGING R VALUE (INTENSITY) : 0.118 1AMN 81
REMARK 999 1AMN 82
REMARK 999 FOR CHAIN " " - 3 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1AMN 83
REMARK 999 1AMN 84
REMARK 999 FOR CHAIN " " - 3 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1AMN 85
DBREF 1AMN 4 534 SWS P04058 ACES_TORCA 25 555 1AMN 86
SEQADV 1AMN SWS P04058 PRO 506 GAP IN PDB ENTRY 1AMN 87
SEQADV 1AMN SWS P04058 HIS 507 GAP IN PDB ENTRY 1AMN 88
SEQADV 1AMN SWS P04058 SER 508 GAP IN PDB ENTRY 1AMN 89
SEQADV 1AMN SWS P04058 GLN 509 GAP IN PDB ENTRY 1AMN 90
SEQADV 1AMN SWS P04058 GLU 510 GAP IN PDB ENTRY 1AMN 91
SEQRES 1 532 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY 1AMN 92
SEQRES 2 532 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS 1AMN 93
SEQRES 3 532 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO 1AMN 94
SEQRES 4 532 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS 1AMN 95
SEQRES 5 532 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN 1AMN 96
SEQRES 6 532 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE 1AMN 97
SEQRES 7 532 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER 1AMN 98
SEQRES 8 532 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO 1AMN 99
SEQRES 9 532 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY 1AMN 100
SEQRES 10 532 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR 1AMN 101
SEQRES 11 532 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU 1AMN 102
SEQRES 12 532 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU 1AMN 103
SEQRES 13 532 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY 1AMN 104
SEQRES 14 532 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP 1AMN 105
SEQRES 15 532 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR 1AMN 106
SEQRES 16 532 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET 1AMN 107
SEQRES 17 532 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG 1AMN 108
SEQRES 18 532 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA 1AMN 109
SEQRES 19 532 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU 1AMN 110
SEQRES 20 532 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU 1AMN 111
SEQRES 21 532 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU 1AMN 112
SEQRES 22 532 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER 1AMN 113
SEQRES 23 532 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU 1AMN 114
SEQRES 24 532 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY 1AMN 115
SEQRES 25 532 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS 1AMN 116
SEQRES 26 532 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY 1AMN 117
SEQRES 27 532 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP 1AMN 118
SEQRES 28 532 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN 1AMN 119
SEQRES 29 532 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP 1AMN 120
SEQRES 30 532 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY 1AMN 121
SEQRES 31 532 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO 1AMN 122
SEQRES 32 532 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN 1AMN 123
SEQRES 33 532 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN 1AMN 124
SEQRES 34 532 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR 1AMN 125
SEQRES 35 532 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU 1AMN 126
SEQRES 36 532 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG 1AMN 127
SEQRES 37 532 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN 1AMN 128
SEQRES 38 532 PRO ASN GLU SER LYS TRP PRO LEU PHE THR THR LYS GLU 1AMN 129
SEQRES 39 532 GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET LYS VAL 1AMN 130
SEQRES 40 532 HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE TRP ASN 1AMN 131
SEQRES 41 532 GLN PHE LEU PRO LYS LEU LEU ASN ALA THR ALA CYS 1AMN 132
FTNOTE 1 1AMN 133
FTNOTE 1 CIS PROLINE - PRO 104 1AMN 134
HET NAF 1 17 SEE REMARK 5 1AMN 135
HET SO4 593 5 SULFATE ION 1AMN 136
FORMUL 2 NAF C11 H15 N1 O2 F3 1AMN 137
FORMUL 3 SO4 O4 S1 2- 1AMN 138
FORMUL 4 HOH *99(H2 O1) 1AMN 139
HELIX 1 1 GLY 41 MET 43 5 1AMN 140
HELIX 2 2 SER 79 GLU 82 1 1AMN 141
HELIX 3 3 ASP 128 TYR 130 5 1AMN 142
HELIX 4 4 LYS 133 GLU 139 1 1AMN 143
HELIX 5 5 GLY 151 PHE 155 1 1AMN 144
HELIX 6 6 VAL 168 PHE 187 1 1AMN 145
HELIX 7 7 ALA 201 LEU 211 1 1AMN 146
HELIX 8 8 ARG 216 LEU 218 5 1AMN 147
HELIX 9 9 VAL 238 LEU 252 1 1AMN 148
HELIX 10 10 ASP 259 GLU 268 1 1AMN 149
HELIX 11 11 PRO 271 ASP 276 1 1AMN 150
HELIX 12 12 GLU 278 VAL 281 5 1AMN 151
HELIX 13 13 LEU 305 ASN 310 1 1AMN 152
HELIX 14 14 SER 329 GLY 335 1 1AMN 153
HELIX 15 15 ARG 349 SER 359 1 1AMN 154
HELIX 16 16 ASP 365 TYR 375 1 1AMN 155
HELIX 17 17 TRP 378 ASP 380 5 1AMN 156
HELIX 18 18 GLY 384 ASN 399 1 1AMN 157
HELIX 19 19 ILE 401 THR 412 1 1AMN 158
HELIX 20 20 GLU 434 MET 436 5 1AMN 159
HELIX 21 21 ILE 444 VAL 447 1 1AMN 160
HELIX 22 22 LEU 450 LEU 452 5 1AMN 161
HELIX 23 23 LYS 454 LEU 456 5 1AMN 162
HELIX 24 24 ALA 460 THR 479 1 1AMN 163
HELIX 25 25 VAL 518 ASN 525 1 1AMN 164
HELIX 26 26 PHE 527 LEU 531 1 1AMN 165
SHEET 1 A 2 LEU 7 THR 10 0 1AMN 166
SHEET 2 A 2 GLY 13 MET 16 -1 N VAL 15 O VAL 8 1AMN 167
SHEET 1 B11 THR 18 VAL 22 0 1AMN 168
SHEET 2 B11 SER 25 PRO 34 -1 N ALA 29 O THR 18 1AMN 169
SHEET 3 B11 TYR 96 VAL 101 -1 N VAL 101 O SER 28 1AMN 170
SHEET 4 B11 VAL 142 SER 145 -1 N SER 145 O ASN 98 1AMN 171
SHEET 5 B11 VAL 111 ILE 115 1 N MET 112 O VAL 142 1AMN 172
SHEET 6 B11 VAL 194 GLU 199 1 N THR 195 O VAL 111 1AMN 173
SHEET 7 B11 ARG 221 GLN 225 1 N ARG 221 O ILE 196 1AMN 174
SHEET 8 B11 ILE 319 ASN 324 1 N LEU 320 O ALA 222 1AMN 175
SHEET 9 B11 THR 418 PHE 423 1 N TYR 419 O ILE 319 1AMN 176
SHEET 10 B11 LYS 501 LEU 505 1 N ILE 503 O PHE 422 1AMN 177
SHEET 11 B11 VAL 512 GLN 514 -1 N HIS 513 O PHE 502 1AMN 178
SHEET 1 C 2 SER 235 SER 237 0 1AMN 179
SHEET 2 C 2 PRO 294 ILE 296 1 N PRO 294 O VAL 236 1AMN 180
SSBOND 1 CYS 67 CYS 94 1AMN 181
SSBOND 2 CYS 254 CYS 265 1AMN 182
SSBOND 3 CYS 402 CYS 521 1AMN 183
CRYST1 113.540 113.540 137.530 90.00 90.00 120.00 P 31 2 1 6 1AMN 184
ORIGX1 1.000000 0.000000 0.000000 0.00000 1AMN 185
ORIGX2 0.000000 1.000000 0.000000 0.00000 1AMN 186
ORIGX3 0.000000 0.000000 1.000000 0.00000 1AMN 187
SCALE1 0.008807 0.005085 0.000000 0.00000 1AMN 188
SCALE2 0.000000 0.010170 0.000000 0.00000 1AMN 189
SCALE3 0.000000 0.000000 0.007271 0.00000 1AMN 190 |