| content |
HEADER COMPLEX (SERINE ESTERASE/TOXIN) 25-OCT-95 1FSS 1FSS 2
TITLE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH 1FSS 3
TITLE 2 FASCICULIN-II 1FSS 4
COMPND MOL_ID: 1; 1FSS 5
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE; 1FSS 6
COMPND 3 CHAIN: A; 1FSS 7
COMPND 4 EC: 3.1.1.7; 1FSS 8
COMPND 5 MOL_ID: 2; 1FSS 9
COMPND 6 MOLECULE: FASCICULIN II; 1FSS 10
COMPND 7 CHAIN: B 1FSS 11
SOURCE MOL_ID: 1; 1FSS 12
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA; 1FSSA 1
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY; 1FSSA 2
SOURCE 4 VARIANT: G2 FORM; 1FSSA 3
SOURCE 5 ORGAN: ELECTRIC ORGAN; 1FSSA 4
SOURCE 6 TISSUE: ELECTROPLAQUE; 1FSSA 5
SOURCE 7 MOL_ID: 2; 1FSSA 6
SOURCE 8 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS; 1FSSA 7
SOURCE 9 ORGANISM_COMMON: EASTERN GREEN MAMBA; 1FSSA 8
SOURCE 10 TISSUE: VENOM 1FSSA 9
EXPDTA X-RAY DIFFRACTION 1FSS 20
AUTHOR M.HAREL,G.J.KLEYWEGT,I.SILMAN,J.L.SUSSMAN 1FSS 21
REVDAT 2 03-SEP-97 1FSSA 1 SOURCE 1FSSA 10
REVDAT 1 08-MAR-96 1FSS 0 1FSS 22
JRNL AUTH M.HAREL,G.J.KLEYWEGT,R.B.G.RAVELLI,I.SILMAN, 1FSS 23
JRNL AUTH 2 J.L.SUSSMAN 1FSS 24
JRNL TITL CRYSTAL STRUCTURE OF AN 1FSS 25
JRNL TITL 2 ACETYLCHOLINESTERASE-FASCICULIN COMPLEX: 1FSS 26
JRNL TITL 3 INTERACTION OF A THREE-FINGERED TOXIN FROM SNAKE 1FSS 27
JRNL TITL 4 VENOM WITH ITS TARGET 1FSS 28
JRNL REF STRUCTURE (LONDON) V. 3 1355 1995 1FSS 29
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005 1FSS 30
REMARK 1 1FSS 31
REMARK 1 REFERENCE 1 1FSS 32
REMARK 1 AUTH M.H.LE DU,P.MARCHOT,P.E.BOUGIS, 1FSS 33
REMARK 1 AUTH 2 J.C.FONTECILLA-CAMPS 1FSS 34
REMARK 1 TITL 1.9-ANGSTROMS RESOLUTION STRUCTURE OF FASCICULIN 1, 1FSS 35
REMARK 1 TITL 2 AN ANTI-ACETYLCHOLINE ESTERASE TOXIN FROM GREEN 1FSS 36
REMARK 1 TITL 3 MAMBA SNAKE VENOM 1FSS 37
REMARK 1 REF J.BIOL.CHEM. V. 267 22122 1992 1FSS 38
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1FSS 39
REMARK 1 REFERENCE 2 1FSS 40
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN, 1FSS 41
REMARK 1 AUTH 2 L.TOKER,I.SILMAN 1FSS 42
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINE ESTERASE FROM 1FSS 43
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC ACETYLCHOLINE 1FSS 44
REMARK 1 TITL 3 BINDING ENZYME 1FSS 45
REMARK 1 REF SCIENCE V. 283 872 1991 1FSS 46
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1FSS 47
REMARK 2 1FSS 48
REMARK 2 RESOLUTION. 3.0 ANGSTROMS. 1FSS 49
REMARK 3 1FSS 50
REMARK 3 REFINEMENT. 1FSS 51
REMARK 3 PROGRAM X-PLOR 1FSS 52
REMARK 3 AUTHORS BRUNGER 1FSS 53
REMARK 3 R VALUE 0.230 1FSS 54
REMARK 3 FREE R VALUE 0.31 1FSS 55
REMARK 3 MEAN B VALUE 19.6 ANGSTROMS**2 1FSS 56
REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1FSS 57
REMARK 3 RMSD BOND ANGLES 1.4 DEGREES 1FSS 58
REMARK 3 RMSD DIHEDRAL ANGLES 24.0 DEGREES 1FSS 59
REMARK 3 RMSD IMPROPER ANGLES 1.2 DEGREES 1FSS 60
REMARK 3 1FSS 61
REMARK 3 NUMBER OF REFLECTIONS 12579 1FSS 62
REMARK 3 RESOLUTION RANGE 8.0 - 3.0 ANGSTROMS 1FSS 63
REMARK 3 DATA CUTOFF 0. SIGMA(F) 1FSS 64
REMARK 3 1FSS 65
REMARK 3 DATA COLLECTION. 1FSS 66
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 14206 1FSS 67
REMARK 3 COMPLETENESS OF DATA 97.7 % 1FSS 68
REMARK 3 1FSS 69
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1FSS 70
REMARK 3 NUMBER OF PROTEIN ATOMS 4690 1FSS 71
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1FSS 72
REMARK 3 NUMBER OF HETEROGEN ATOMS 10 1FSS 73
REMARK 3 NUMBER OF SOLVENT ATOMS 36 1FSS 74
REMARK 4 1FSS 75
REMARK 4 ACETYLCHOLINESTERASE - FASCICULIN II COMPLEX WAS 1FSS 76
REMARK 4 CRYSTALLIZED FROM A 1:1 STOICHIOMETRIC MIXTURE. 1FSS 77
REMARK 5 1FSS 78
REMARK 5 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; 1FSS 79
REMARK 5 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; 1FSS 80
REMARK 5 I=INSERTION CODE): 1FSS 81
REMARK 5 M RES CSSEQI ATOMS 1FSS 82
REMARK 5 HIS A 486 CG ND1 CE1 NE2 CD2 1FSS 83
REMARK 5 SER A 487 OG 1FSS 84
REMARK 5 GLN A 488 CG CD OE1 NE2 1FSS 85
REMARK 5 GLU A 489 CG CD OE1 OE2 1FSS 86
REMARK 5 SER A 490 OG 1FSS 87
REMARK 5 LYS A 491 CG CD CE NZ 1FSS 88
REMARK 6 1FSS 89
REMARK 6 WATER HOH 800 IS IN A SPECIAL POSITION. 1FSS 90
REMARK 18 1FSS 91
REMARK 18 EXPERIMENTAL DETAILS. 1FSS 92
REMARK 18 DATE OF DATA COLLECTION : 15-NOV-94 1FSS 93
REMARK 18 SOURCE : NSLS 1FSS 94
REMARK 18 BEAMLINE : X12C 1FSS 95
REMARK 18 MONOCHROMATIC (Y/N) : Y 1FSS 96
REMARK 18 LAUE (Y/N) : N 1FSS 97
REMARK 18 WAVELENGTH OR RANGE (A) : 1.15 1FSS 98
REMARK 18 DETECTOR TYPE : 30 CM IMAGE PLATE 1FSS 99
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1FSS 100
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : DENZO/SCALEPACK 1FSS 101
REMARK 18 DATA REDUNDANCY : 3.43 1FSS 102
REMARK 18 MERGING R VALUE (INTENSITY) : 0.105 1FSS 103
REMARK 860 1FSSA 11
REMARK 860 CORRECTION AFTER RELEASE 1FSSA 12
REMARK 860 CORRECT SOURCE FOR ACETYLCHOLINESTERASE. 03-SEP-1997. 1FSSA 13
REMARK 999 1FSS 104
REMARK 999 FOR CHAIN "A" - 3 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1FSS 105
REMARK 999 1FSS 106
REMARK 999 FOR CHAIN "A" - 2 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1FSS 107
DBREF 1FSS A 4 535 SWS P04058 ACES_TORCA 25 556 1FSS 108
DBREF 1FSS B 1 61 SWS P01403 TXF7_DENAN 1 61 1FSS 109
SEQADV 1FSS ASN B 47 SWS P01403 TYR 47 VARIANT 1FSS 110
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY 1FSS 111
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS 1FSS 112
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO 1FSS 113
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS 1FSS 114
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN 1FSS 115
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE 1FSS 116
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER 1FSS 117
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO 1FSS 118
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY 1FSS 119
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR 1FSS 120
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU 1FSS 121
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU 1FSS 122
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY 1FSS 123
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP 1FSS 124
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR 1FSS 125
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET 1FSS 126
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG 1FSS 127
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA 1FSS 128
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU 1FSS 129
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU 1FSS 130
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU 1FSS 131
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER 1FSS 132
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU 1FSS 133
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY 1FSS 134
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS 1FSS 135
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY 1FSS 136
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP 1FSS 137
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN 1FSS 138
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP 1FSS 139
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY 1FSS 140
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO 1FSS 141
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN 1FSS 142
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN 1FSS 143
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR 1FSS 144
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU 1FSS 145
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG 1FSS 146
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN 1FSS 147
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU 1FSS 148
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR 1FSS 149
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET 1FSS 150
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN 1FSS 151
SEQRES 42 A 537 ALA THR ALA CYS 1FSS 152
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE 1FSS 153
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER 1FSS 154
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS 1FSS 155
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS 1FSS 156
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR 1FSS 157
FTNOTE 1 1FSS 158
FTNOTE 1 CIS PROLINE - PRO A 104 1FSS 159
FTNOTE 2 1FSS 160
FTNOTE 2 CIS PROLINE - PRO B 31 1FSS 161
FTNOTE 3 1FSS 162
FTNOTE 3 CIS PROLINE - PRO B 56 1FSS 163
HET ZN A 901 1 ZINC ION 1FSS 164
HET ZN A 902 1 ZINC ION 1FSS 165
HET NAG A 990 14 N-ACETYL-D-GLUCOSAMINE 1FSS 166
FORMUL 3 ZN 2(ZN1 2+) 1FSS 167
FORMUL 4 NAG C8 H15 N1 O6 1FSS 168
FORMUL 5 HOH *36(H2 O1) 1FSS 169
HELIX 1 1 GLY A 41 MET A 43 5 1FSS 170
HELIX 2 2 SER A 79 TRP A 84 1 1FSS 171
HELIX 3 3 LYS A 133 THR A 138 1 1FSS 172
HELIX 4 4 GLY A 151 PHE A 155 1 1FSS 173
HELIX 5 5 ASN A 167 PHE A 187 5 1FSS 174
HELIX 6 6 ALA A 201 LEU A 211 1 1FSS 175
HELIX 7 7 PRO A 213 LEU A 218 5 1FSS 176
HELIX 8 8 GLU A 240 ARG A 250 1 1FSS 177
HELIX 9 9 ASP A 259 GLU A 268 1 1FSS 178
HELIX 10 10 PRO A 271 ASP A 276 1 1FSS 179
HELIX 11 11 TRP A 279 VAL A 281 5 1FSS 180
HELIX 12 12 LEU A 305 SER A 311 1 1FSS 181
HELIX 13 13 PHE A 330 TYR A 334 5 1FSS 182
HELIX 14 14 ARG A 349 SER A 359 1 1FSS 183
HELIX 15 15 ASP A 365 GLN A 374 1 1FSS 184
HELIX 16 16 GLY A 384 ASN A 399 1 1FSS 185
HELIX 17 17 ILE A 401 LYS A 413 1 1FSS 186
HELIX 18 18 GLU A 434 MET A 436 5 1FSS 187
HELIX 19 19 ILE A 444 VAL A 447 1 1FSS 188
HELIX 20 20 LEU A 450 LEU A 452 5 1FSS 189
HELIX 21 21 LYS A 454 LEU A 456 5 1FSS 190
HELIX 22 22 ALA A 460 THR A 479 1 1FSS 191
HELIX 23 23 VAL A 518 ASN A 525 1 1FSS 192
HELIX 24 24 PHE A 527 ALA A 534 1 1FSS 193
SHEET 1 A 3 LEU A 7 THR A 10 0 1FSS 194
SHEET 2 A 3 GLY A 13 MET A 16 -1 N VAL A 15 O VAL A 8 1FSS 195
SHEET 3 A 3 VAL A 57 ASN A 59 1 N TRP A 58 O LYS A 14 1FSS 196
SHEET 1 B11 THR A 18 VAL A 22 0 1FSS 197
SHEET 2 B11 SER A 25 PRO A 34 -1 N ALA A 29 O THR A 18 1FSS 198
SHEET 3 B11 TYR A 96 VAL A 101 -1 N VAL A 101 O SER A 28 1FSS 199
SHEET 4 B11 VAL A 142 SER A 145 -1 N SER A 145 O ASN A 98 1FSS 200
SHEET 5 B11 VAL A 111 ILE A 115 1 N MET A 112 O VAL A 142 1FSS 201
SHEET 6 B11 VAL A 194 GLU A 199 1 N THR A 195 O VAL A 111 1FSS 202
SHEET 7 B11 ARG A 221 GLN A 225 1 N ARG A 221 O ILE A 196 1FSS 203
SHEET 8 B11 ILE A 319 ASN A 324 1 N LEU A 320 O ALA A 222 1FSS 204
SHEET 9 B11 THR A 418 PHE A 423 1 N TYR A 419 O ILE A 319 1FSS 205
SHEET 10 B11 LYS A 501 LEU A 505 1 N ILE A 503 O PHE A 422 1FSS 206
SHEET 11 B11 VAL A 512 GLN A 514 -1 N HIS A 513 O PHE A 502 1FSS 207
SHEET 1 C 2 MET B 2 SER B 5 0 1FSS 208
SHEET 2 C 2 ILE B 13 ASN B 16 -1 N THR B 15 O CYS B 3 1FSS 209
SHEET 1 D 2 CYS B 22 SER B 26 0 1FSS 210
SHEET 2 D 2 VAL B 34 CYS B 39 -1 N GLY B 38 O TYR B 23 1FSS 211
SSBOND 1 CYS A 67 CYS A 94 1FSS 212
SSBOND 2 CYS A 254 CYS A 265 1FSS 213
SSBOND 3 CYS A 402 CYS A 521 1FSS 214
SSBOND 4 CYS B 3 CYS B 22 1FSS 215
SSBOND 5 CYS B 17 CYS B 39 1FSS 216
SSBOND 6 CYS B 41 CYS B 52 1FSS 217
SSBOND 7 CYS B 53 CYS B 59 1FSS 218
CRYST1 87.390 115.000 67.470 90.00 90.00 90.00 P 21 21 2 4 1FSS 219
ORIGX1 1.000000 0.000000 0.000000 0.00000 1FSS 220
ORIGX2 0.000000 1.000000 0.000000 0.00000 1FSS 221
ORIGX3 0.000000 0.000000 1.000000 0.00000 1FSS 222
SCALE1 0.011443 0.000000 0.000000 0.00000 1FSS 223
SCALE2 0.000000 0.008696 0.000000 0.00000 1FSS 224
SCALE3 0.000000 0.000000 0.014821 0.00000 1FSS 225 |