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HEADER COMPLEX (HYDROLASE/TOXIN) 21-NOV-95 1MAH 1MAH 2
TITLE FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX 1MAH 3
COMPND MOL_ID: 1; 1MAH 4
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE; 1MAH 5
COMPND 3 CHAIN: A; 1MAH 6
COMPND 4 SYNONYM: MACHE; 1MAH 7
COMPND 5 EC: 3.1.1.7; 1MAH 8
COMPND 6 ENGINEERED: YES; 1MAH 9
COMPND 7 MOL_ID: 2; 1MAH 10
COMPND 8 MOLECULE: FASCICULIN 2; 1MAH 11
COMPND 9 CHAIN: F; 1MAH 12
COMPND 10 SYNONYM: TOXIN F-VII, FAS2, TOXIN TAI 1MAH 13
SOURCE MOL_ID: 1; 1MAH 14
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; 1MAH 15
SOURCE 3 ORGANISM_COMMON: MOUSE; 1MAH 16
SOURCE 4 STRAIN: BLACK6/CBA CROSS F1; 1MAH 17
SOURCE 5 ORGAN: BRAIN (CDNA); 1MAH 18
SOURCE 6 EXPRESSION_SYSTEM: HUMAN EMBRYONIC KIDNEY CELLS; 1MAH 19
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 293; 1MAH 20
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: LAMBDA-ZAP AND LAMBDA-FIX CDNA 1MAH 21
SOURCE 9 AND GENOMIC DNA; 1MAH 22
SOURCE 10 EXPRESSION_SYSTEM_GENE: MOUSE ACHE; 1MAH 23
SOURCE 11 MOL_ID: 2; 1MAH 24
SOURCE 12 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS; 1MAH 25
SOURCE 13 ORGANISM_COMMON: EASTERN GREEN MAMBA; 1MAH 26
SOURCE 14 TISSUE: VENOM 1MAH 27
KEYWDS HYDROLASE, SERINE ESTERASE, SYNAPSE, VENOM, TOXIN 1MAH 28
EXPDTA X-RAY DIFFRACTION 1MAH 29
AUTHOR Y.BOURNE,P.TAYLOR,P.MARCHOT 1MAH 30
REVDAT 1 03-APR-96 1MAH 0 1MAH 31
JRNL AUTH Y.BOURNE,P.TAYLOR,P.MARCHOT 1MAH 32
JRNL TITL ACETYLCHOLINESTERASE INHIBITION BY FASCICULIN: 1MAH 33
JRNL TITL 2 CRYSTAL STRUCTURE OF THE COMPLEX 1MAH 34
JRNL REF CELL(CAMBRIDGE,MASS.) V. 83 503 1995 1MAH 35
JRNL REFN ASTM CELLB5 US ISSN 0092-8674 0998 1MAH 36
REMARK 1 1MAH 37
REMARK 2 1MAH 38
REMARK 2 RESOLUTION. 3.2 ANGSTROMS. 1MAH 39
REMARK 3 1MAH 40
REMARK 3 REFINEMENT. 1MAH 41
REMARK 3 PROGRAM X-PLOR 3.1 1MAH 42
REMARK 3 AUTHORS BRUNGER 1MAH 43
REMARK 3 R VALUE 0.184 1MAH 44
REMARK 3 FREE R VALUE 0.294 1MAH 45
REMARK 3 FREE R VALUE TEST SET 5. % 1MAH 46
REMARK 3 MEAN B VALUE 35. ANGSTROMS**2 1MAH 47
REMARK 3 ESD FROM LUZZATI PLOT 0.2000 ANGSTROMS 1MAH 48
REMARK 3 ESTIMATED COORD. ERROR 0.2500 ANGSTROMS 1MAH 49
REMARK 3 FINAL RMS COORD. SHIFT 0.0001 ANGSTROMS 1MAH 50
REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1MAH 51
REMARK 3 RMSD BOND ANGLES 1.5 DEGREES 1MAH 52
REMARK 3 RMSD DIHEDRAL ANGLES 24.5 DEGREES 1MAH 53
REMARK 3 RMSD IMPROPER ANGLES 1.4 DEGREES 1MAH 54
REMARK 3 1MAH 55
REMARK 3 NUMBER OF REFLECTIONS 13823 1MAH 56
REMARK 3 RESOLUTION RANGE 10. - 3.2 ANGSTROMS 1MAH 57
REMARK 3 DATA CUTOFF 0. SIGMA(F) 1MAH 58
REMARK 3 COMPLETENESS FOR RANGE 85. % 1MAH 59
REMARK 3 1MAH 60
REMARK 3 DATA COLLECTION. 1MAH 61
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 14488 1MAH 62
REMARK 3 RESOLUTION RANGE 37.0 - 3.2 ANGSTROMS 1MAH 63
REMARK 3 COMPLETENESS OF DATA 85. % 1MAH 64
REMARK 3 REJECTION CRITERIA 0. SIGMA(I OR F) 1MAH 65
REMARK 3 1MAH 66
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1MAH 67
REMARK 3 NUMBER OF PROTEIN ATOMS 4577 1MAH 68
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1MAH 69
REMARK 3 NUMBER OF HETEROGEN ATOMS 14 1MAH 70
REMARK 3 NUMBER OF SOLVENT ATOMS 0 1MAH 71
REMARK 4 1MAH 72
REMARK 4 DISORDERED REGIONS INCLUDE MACHE PRO A 492 - PRO A 498, 1MAH 73
REMARK 4 FAS2 LYS F 51. MACHE ARG A 13, ARG A 45, ARG A 165, 1MAH 74
REMARK 4 ARG A 253, ARG A 364, ARG A 470, ARG A 491, AND ARG A 493 1MAH 75
REMARK 4 ARE TRUNCATED TO CB. 1MAH 76
REMARK 5 1MAH 77
REMARK 5 SITE 1MAH 78
REMARK 5 SITE_IDENTIFIER: CAT 1MAH 79
REMARK 5 LOCATED AT THE BOTTOM OF A NARROW GORGE. 1MAH 80
REMARK 5 SITE_IDENTIFIER: PER 1MAH 81
REMARK 5 BINDING SITE FOR FAS2 LOOP II. 1MAH 82
REMARK 6 1MAH 83
REMARK 6 SYMMETRY 1MAH 84
REMARK 6 THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED 1MAH 85
REMARK 6 BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE. 1MAH 86
REMARK 6 1MAH 87
REMARK 6 APPLIED TO RESIDUES: A 4 .. 61 1MAH 88
REMARK 6 GENERATE A DIMER OF THE MACHE-FAS2 COMPLEX ACROSS A 1MAH 89
REMARK 6 TWO-FOLD CRYSTALLOGRAPHIC AXIS 1MAH 90
REMARK 6 1MAH 91
REMARK 6 SYMMETRY1 1 -1.000000 0.000000 0.000000 75.46878 1MAH 92
REMARK 6 SYMMETRY2 1 0.000000 1.000000 0.000000 -0.07648 1MAH 93
REMARK 6 SYMMETRY3 1 0.000000 0.000000 -1.000000 278.07110 1MAH 94
REMARK 7 1MAH 95
REMARK 7 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE 1MAH 96
REMARK 7 TRACKING NUMBER: T7538, DATE REVISED: 27-DEC-95 1MAH 97
REMARK 18 1MAH 98
REMARK 18 EXPERIMENTAL DETAILS. 1MAH 99
REMARK 18 DATE OF DATA COLLECTION : 25-JUL-95 1MAH 100
REMARK 18 SOURCE : NSLS - X12C 1MAH 101
REMARK 18 MONOCHROMATIC (Y/N) : Y 1MAH 102
REMARK 18 LAUE (Y/N) : N 1MAH 103
REMARK 18 WAVELENGTH OR RANGE (A) : 1.0 OR 1.5 1MAH 104
REMARK 18 DETECTOR TYPE : IMAGE PLATE 1MAH 105
REMARK 18 DETECTOR MANUFACTURER : MARRESEARCH 1MAH 106
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : DENZO/SCALEPACK 1MAH 107
REMARK 18 DATA REDUNDANCY : 4.-5. 1MAH 108
REMARK 18 MERGING R VALUE (INTENSITY) : 0.089 1MAH 109
REMARK 18 1MAH 110
REMARK 18 REMARK: DATA SETS FROM FOUR CRYSTALS HAVE BEEN MERGED 1MAH 111
REMARK 19 1MAH 112
REMARK 19 SOLVENT CONTENT (VS) : 60. % 1MAH 113
REMARK 999 1MAH 114
REMARK 999 SEQUENCE 1MAH 115
REMARK 999 REFERENCE 1MAH 116
REMARK 999 REFERENCE: RACHINSKY ET AL. (1990) NEURON, 5:317-327. 1MAH 117
REMARK 999 ENZYME CONTAINS THE ALTERNATIVE SPLICE OF EXON 5, IS 1MAH 118
REMARK 999 TRUNCATED AT CODON POSITION 549; THIS YIELDS AN ENZYME 1MAH 119
REMARK 999 TRUNCATED 7 RESIDUES SHORTLY THE TISSUE DERMED 1MAH 120
REMARK 999 GLYCOPHOSPHOLIPID CONTAINING FORM OF THE ENZYME. 1MAH 121
REMARK 999 1MAH 122
REMARK 999 FOR CHAIN "A" - 3 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1MAH 123
DBREF 1MAH A 4 543 SWS P21836 ACES_MOUSE 35 574 1MAH 124
DBREF 1MAH F 1 61 SWS P01403 TXF7_DENAN 1 61 1MAH 125
SEQADV 1MAH A SWS P21836 PRO 289 GAP IN PDB ENTRY 1MAH 126
SEQADV 1MAH A SWS P21836 PRO 290 GAP IN PDB ENTRY 1MAH 127
SEQADV 1MAH A SWS P21836 GLY 291 GAP IN PDB ENTRY 1MAH 128
SEQADV 1MAH A SWS P21836 GLY 292 GAP IN PDB ENTRY 1MAH 129
SEQADV 1MAH A SWS P21836 ALA 293 GAP IN PDB ENTRY 1MAH 130
SEQADV 1MAH A SWS P21836 GLY 294 GAP IN PDB ENTRY 1MAH 131
SEQADV 1MAH A SWS P21836 GLY 295 GAP IN PDB ENTRY 1MAH 132
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG 1MAH 133
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY 1MAH 134
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU 1MAH 135
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO 1MAH 136
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE 1MAH 137
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO 1MAH 138
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU 1MAH 139
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO 1MAH 140
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP 1MAH 141
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU 1MAH 142
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY 1MAH 143
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE 1MAH 144
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY 1MAH 145
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP 1MAH 146
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET 1MAH 147
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER 1MAH 148
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU 1MAH 149
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY 1MAH 150
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG 1MAH 151
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY 1MAH 152
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU 1MAH 153
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP 1MAH 154
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE 1MAH 155
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO 1MAH 156
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN 1MAH 157
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE 1MAH 158
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU 1MAH 159
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG 1MAH 160
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA 1MAH 161
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP 1MAH 162
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY 1MAH 163
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY 1MAH 164
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE 1MAH 165
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP 1MAH 166
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE 1MAH 167
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU 1MAH 168
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR 1MAH 169
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP 1MAH 170
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA 1MAH 171
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL 1MAH 172
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN 1MAH 173
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR 1MAH 174
SEQRES 1 F 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE 1MAH 175
SEQRES 2 F 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER 1MAH 176
SEQRES 3 F 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS 1MAH 177
SEQRES 4 F 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS 1MAH 178
SEQRES 5 F 61 CYS THR SER PRO ASP LYS CYS ASN TYR 1MAH 179
FTNOTE 1 1MAH 180
FTNOTE 1 CIS PROLINE - PRO A 106 1MAH 181
FTNOTE 2 1MAH 182
FTNOTE 2 ARG A 107 - PRO A 108 OMEGA = 243.30 1MAH 183
FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1MAH 184
FTNOTE 3 1MAH 185
FTNOTE 3 LEU A 161 - PRO A 162 OMEGA = 222.75 1MAH 186
FTNOTE 3 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1MAH 187
FTNOTE 4 1MAH 188
FTNOTE 4 SER A 497 - PRO A 498 OMEGA = 139.38 1MAH 189
FTNOTE 4 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1MAH 190
FTNOTE 5 1MAH 191
FTNOTE 5 CIS PROLINE - PRO F 31 1MAH 192
FTNOTE 6 1MAH 193
FTNOTE 6 CIS PROLINE - PRO F 56 1MAH 194
HET NAG 509 14 N-ACETYL-D-GLUCOSAMINE 1MAH 195
FORMUL 3 NAG C8 H15 N1 O6 1MAH 196
HELIX 1 1 GLY A 43 ARG A 45 5 1MAH 197
HELIX 2 2 GLU A 81 TRP A 86 1 1MAH 198
HELIX 3 3 ASP A 131 TYR A 133 5 1MAH 199
HELIX 4 4 GLY A 135 GLU A 142 1 1MAH 200
HELIX 5 5 GLY A 154 PHE A 158 1 1MAH 201
HELIX 6 6 VAL A 171 GLU A 185 1 1MAH 202
HELIX 7 7 ILE A 187 PHE A 190 5 1MAH 203
HELIX 8 8 ALA A 204 LEU A 214 1 1MAH 204
HELIX 9 9 LEU A 216 LEU A 221 1 1MAH 205
HELIX 10 10 ALA A 241 VAL A 255 1 1MAH 206
HELIX 11 11 THR A 267 THR A 275 1 1MAH 207
HELIX 12 12 ALA A 278 HIS A 287 1 1MAH 208
HELIX 13 13 PRO A 312 THR A 318 1 1MAH 209
HELIX 14 14 GLY A 335 TYR A 341 5 1MAH 210
HELIX 15 15 ARG A 356 GLY A 366 1 1MAH 211
HELIX 16 16 ASP A 372 TYR A 382 1 1MAH 212
HELIX 17 17 PRO A 391 ASN A 406 1 1MAH 213
HELIX 18 18 VAL A 408 ALA A 420 1 1MAH 214
HELIX 19 19 LEU A 441 MET A 443 5 1MAH 215
HELIX 20 20 ILE A 451 ILE A 454 1 1MAH 216
HELIX 21 21 LEU A 457 LEU A 459 5 1MAH 217
HELIX 22 22 THR A 467 ARG A 485 1 1MAH 218
HELIX 23 23 ALA A 526 SER A 541 1 1MAH 219
SHEET 1 A 3 LEU A 9 VAL A 12 0 1MAH 220
SHEET 2 A 3 GLY A 15 ARG A 18 -1 N LEU A 17 O VAL A 10 1MAH 221
SHEET 3 A 3 VAL A 59 ASP A 61 1 N LEU A 60 O GLN A 16 1MAH 222
SHEET 1 B 5 ILE A 20 ALA A 24 0 1MAH 223
SHEET 2 B 5 GLY A 27 PHE A 32 -1 N ALA A 31 O ILE A 20 1MAH 224
SHEET 3 B 5 ASN A 100 PRO A 104 -1 N THR A 103 O SER A 30 1MAH 225
SHEET 4 B 5 VAL A 145 SER A 148 -1 N SER A 148 O ASN A 100 1MAH 226
SHEET 5 B 5 VAL A 114 ILE A 116 1 N LEU A 115 O VAL A 145 1MAH 227
SHEET 1 C 6 THR A 198 GLU A 202 0 1MAH 228
SHEET 2 C 6 ARG A 224 GLN A 228 1 N ARG A 224 O LEU A 199 1MAH 229
SHEET 3 C 6 GLN A 325 VAL A 331 1 N GLN A 325 O ALA A 225 1MAH 230
SHEET 4 C 6 ARG A 424 PHE A 430 1 N ARG A 424 O VAL A 326 1MAH 231
SHEET 5 C 6 GLN A 509 LEU A 513 1 N VAL A 511 O ILE A 429 1MAH 232
SHEET 6 C 6 GLU A 519 ARG A 522 -1 N ARG A 521 O TYR A 510 1MAH 233
SHEET 1 D 2 MET F 2 SER F 5 0 1MAH 234
SHEET 2 D 2 ILE F 13 ASN F 16 -1 N THR F 15 O CYS F 3 1MAH 235
SHEET 1 E 3 ARG F 37 CYS F 39 0 1MAH 236
SHEET 2 E 3 CYS F 22 ARG F 27 -1 N TYR F 23 O GLY F 38 1MAH 237
SHEET 3 E 3 LEU F 48 CYS F 53 -1 N CYS F 53 O CYS F 22 1MAH 238
SSBOND 1 CYS A 69 CYS A 96 1MAH 239
SSBOND 2 CYS A 257 CYS A 272 1MAH 240
SSBOND 3 CYS A 409 CYS A 529 1MAH 241
SSBOND 4 CYS F 3 CYS F 22 1MAH 242
SSBOND 5 CYS F 17 CYS F 39 1MAH 243
SSBOND 6 CYS F 41 CYS F 52 1MAH 244
SSBOND 7 CYS F 53 CYS F 59 1MAH 245
SITE 1 CAT 4 SER A 203 GLU A 334 HIS A 447 TRP A 86 1MAH 246
SITE 1 PAS 4 TYR A 72 TYR A 124 GLN A 279 TYR A 341 1MAH 247
CRYST1 75.500 75.500 556.200 90.00 90.00 120.00 P 65 2 2 12 1MAH 248
ORIGX1 1.000000 0.000000 0.000000 0.00000 1MAH 249
ORIGX2 0.000000 1.000000 0.000000 0.00000 1MAH 250
ORIGX3 0.000000 0.000000 1.000000 0.00000 1MAH 251
SCALE1 0.013245 0.007647 0.000000 0.00000 1MAH 252
SCALE2 0.000000 0.015294 0.000000 0.00000 1MAH 253
SCALE3 0.000000 0.000000 0.001798 0.00000 1MAH 254 |