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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 27-JAN-93 1HPL 1HPL 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1HPL 3
SOURCE HORSE (EQUUS CABALLUS) PANCREAS 1HPL 4
AUTHOR Y.BOURNE,C.CAMBILLAU 1HPL 5
REVDAT 1 31-MAY-94 1HPL 0 1HPL 6
JRNL AUTH Y.BOURNE,C.MARTINEZ,B.KERFELEC,D.LOMBARDO,C.CHAPUS, 1HPL 7
JRNL AUTH 2 C.CAMBILLAU 1HPL 8
JRNL TITL HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE 1HPL 9
JRNL TITL 2 AT 2.3 ANGSTROMS RESOLUTION 1HPL 10
JRNL REF TO BE PUBLISHED 1HPL 11
JRNL REFN 0353 1HPL 12
REMARK 1 1HPL 13
REMARK 1 REFERENCE 1 1HPL 14
REMARK 1 AUTH D.LOMBARDO,C.CHAPUS,Y.BOURNE,C.CAMBILLAU 1HPL 15
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDY OF 1HPL 16
REMARK 1 TITL 2 HORSE PANCREATIC LIPASE 1HPL 17
REMARK 1 REF J.MOL.BIOL. V. 205 259 1989 1HPL 18
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1HPL 19
REMARK 2 1HPL 20
REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 1HPL 21
REMARK 3 1HPL 22
REMARK 3 REFINEMENT. 1HPL 23
REMARK 3 PROGRAM X-PLOR 1HPL 24
REMARK 3 AUTHORS BRUNGER 1HPL 25
REMARK 3 R VALUE 0.159 1HPL 26
REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS 1HPL 27
REMARK 3 RMSD BOND ANGLES 3.1 DEGREES 1HPL 28
REMARK 3 1HPL 29
REMARK 3 RESOLUTION RANGE 6. - 2.3 ANGSTROMS 1HPL 30
REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 1HPL 31
REMARK 4 1HPL 32
REMARK 4 TWO MOLECULES ARE PRESENT IN THE ASYMMETRIC UNIT. THEY 1HPL 33
REMARK 4 ARE DENOTED BY CHAIN IDENTIFIERS *A* AND *B*. THE TWO 1HPL 34
REMARK 4 MOLECULES ARE RELATED BY A NON-CRYSTALLOGRAPHIC TWO-FOLD 1HPL 35
REMARK 4 AXIS PARALLEL TO THE CRYSTALLOGRAPHIC B AXIS. THE 1HPL 36
REMARK 4 TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1HPL 37
REMARK 4 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO 1HPL 38
REMARK 4 CHAIN A. 1HPL 39
REMARK 5 1HPL 40
REMARK 5 SITES *ACT* AND *BCT*, PRESENTED ON *SITE* RECORDS BELOW, 1HPL 41
REMARK 5 ARE THE ACTIVE SITES. 1HPL 42
REMARK 6 1HPL 43
REMARK 6 CROSS REFERENCE TO SEQUENCE DATABASE 1HPL 44
REMARK 6 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1HPL 45
REMARK 6 LIPP_HORSE A 1HPL 46
REMARK 6 LIPP_HORSE B 1HPL 47
REMARK 7 1HPL 48
REMARK 7 RESIDUES OF CHAIN A MISSING FROM THE ATOM LIST. 1HPL 49
REMARK 7 SER A 43 1HPL 50
REMARK 7 SER B 43 1HPL 51
SEQRES 1 A 449 ASN GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP 1HPL 52
SEQRES 2 A 449 ASP SER PRO TRP ALA GLY ILE VAL GLU ARG PRO LEU LYS 1HPL 53
SEQRES 3 A 449 ILE LEU PRO TRP SER PRO GLU LYS VAL ASN THR ARG PHE 1HPL 54
SEQRES 4 A 449 LEU LEU TYR THR ASN GLU ASN PRO ASP ASN PHE GLN GLU 1HPL 55
SEQRES 5 A 449 ILE VAL ALA ASP PRO SER THR ILE GLN SER SER ASN PHE 1HPL 56
SEQRES 6 A 449 ASN THR GLY ARG LYS THR ARG PHE ILE ILE HIS GLY PHE 1HPL 57
SEQRES 7 A 449 ILE ASP LYS GLY GLU GLU SER TRP LEU SER THR MET CYS 1HPL 58
SEQRES 8 A 449 GLN ASN MET PHE LYS VAL GLU SER VAL ASN CYS ILE CYS 1HPL 59
SEQRES 9 A 449 VAL ASP TRP LYS SER GLY SER ARG THR ALA TYR SER GLN 1HPL 60
SEQRES 10 A 449 ALA SER GLN ASN VAL ARG ILE VAL GLY ALA GLU VAL ALA 1HPL 61
SEQRES 11 A 449 TYR LEU VAL GLY VAL LEU GLN SER SER PHE ASP TYR SER 1HPL 62
SEQRES 12 A 449 PRO SER ASN VAL HIS ILE ILE GLY HIS SER LEU GLY SER 1HPL 63
SEQRES 13 A 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY ALA 1HPL 64
SEQRES 14 A 449 VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS 1HPL 65
SEQRES 15 A 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER 1HPL 66
SEQRES 16 A 449 ASP ALA GLN PHE VAL ASP VAL ILE HIS THR ASP ILE ALA 1HPL 67
SEQRES 17 A 449 PRO PHE ILE PRO ASN LEU GLY PHE GLY MET SER GLN THR 1HPL 68
SEQRES 18 A 449 ALA GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS GLU 1HPL 69
SEQRES 19 A 449 MET PRO GLY CYS GLN LYS ASN VAL LEU SER GLN ILE VAL 1HPL 70
SEQRES 20 A 449 ASP ILE ASP GLY ILE TRP GLN GLY THR ARG ASP PHE ALA 1HPL 71
SEQRES 21 A 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP 1HPL 72
SEQRES 22 A 449 SER ILE LEU ASN PRO ASP GLY PHE ALA GLY PHE SER CYS 1HPL 73
SEQRES 23 A 449 ALA SER TYR SER ASP PHE THR ALA ASN LYS CYS PHE PRO 1HPL 74
SEQRES 24 A 449 CYS SER SER GLU GLY CYS PRO GLN MET GLY HIS TYR ALA 1HPL 75
SEQRES 25 A 449 ASP ARG PHE PRO GLY ARG THR LYS GLY VAL GLY GLN LEU 1HPL 76
SEQRES 26 A 449 PHE TYR LEU ASN THR GLY ASP ALA SER ASN PHE ALA ARG 1HPL 77
SEQRES 27 A 449 TRP ARG TYR ARG VAL ASP VAL THR LEU SER GLY LYS LYS 1HPL 78
SEQRES 28 A 449 VAL THR GLY HIS VAL LEU VAL SER LEU PHE GLY ASN LYS 1HPL 79
SEQRES 29 A 449 GLY ASN SER ARG GLN TYR GLU ILE PHE GLN GLY THR LEU 1HPL 80
SEQRES 30 A 449 LYS PRO ASP ASN THR TYR SER ASN GLU PHE ASP SER ASP 1HPL 81
SEQRES 31 A 449 VAL GLU VAL GLY ASP LEU GLU LYS VAL LYS PHE ILE TRP 1HPL 82
SEQRES 32 A 449 TYR ASN ASN VAL ILE ASN LEU THR LEU PRO LYS VAL GLY 1HPL 83
SEQRES 33 A 449 ALA SER LYS ILE THR VAL GLU ARG ASN ASP GLY SER VAL 1HPL 84
SEQRES 34 A 449 PHE ASN PHE CYS SER GLU GLU THR VAL ARG GLU ASP VAL 1HPL 85
SEQRES 35 A 449 LEU LEU THR LEU THR ALA CYS 1HPL 86
SEQRES 1 B 449 ASN GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP 1HPL 87
SEQRES 2 B 449 ASP SER PRO TRP ALA GLY ILE VAL GLU ARG PRO LEU LYS 1HPL 88
SEQRES 3 B 449 ILE LEU PRO TRP SER PRO GLU LYS VAL ASN THR ARG PHE 1HPL 89
SEQRES 4 B 449 LEU LEU TYR THR ASN GLU ASN PRO ASP ASN PHE GLN GLU 1HPL 90
SEQRES 5 B 449 ILE VAL ALA ASP PRO SER THR ILE GLN SER SER ASN PHE 1HPL 91
SEQRES 6 B 449 ASN THR GLY ARG LYS THR ARG PHE ILE ILE HIS GLY PHE 1HPL 92
SEQRES 7 B 449 ILE ASP LYS GLY GLU GLU SER TRP LEU SER THR MET CYS 1HPL 93
SEQRES 8 B 449 GLN ASN MET PHE LYS VAL GLU SER VAL ASN CYS ILE CYS 1HPL 94
SEQRES 9 B 449 VAL ASP TRP LYS SER GLY SER ARG THR ALA TYR SER GLN 1HPL 95
SEQRES 10 B 449 ALA SER GLN ASN VAL ARG ILE VAL GLY ALA GLU VAL ALA 1HPL 96
SEQRES 11 B 449 TYR LEU VAL GLY VAL LEU GLN SER SER PHE ASP TYR SER 1HPL 97
SEQRES 12 B 449 PRO SER ASN VAL HIS ILE ILE GLY HIS SER LEU GLY SER 1HPL 98
SEQRES 13 B 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY ALA 1HPL 99
SEQRES 14 B 449 VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS 1HPL 100
SEQRES 15 B 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER 1HPL 101
SEQRES 16 B 449 ASP ALA GLN PHE VAL ASP VAL ILE HIS THR ASP ILE ALA 1HPL 102
SEQRES 17 B 449 PRO PHE ILE PRO ASN LEU GLY PHE GLY MET SER GLN THR 1HPL 103
SEQRES 18 B 449 ALA GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS GLU 1HPL 104
SEQRES 19 B 449 MET PRO GLY CYS GLN LYS ASN VAL LEU SER GLN ILE VAL 1HPL 105
SEQRES 20 B 449 ASP ILE ASP GLY ILE TRP GLN GLY THR ARG ASP PHE ALA 1HPL 106
SEQRES 21 B 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP 1HPL 107
SEQRES 22 B 449 SER ILE LEU ASN PRO ASP GLY PHE ALA GLY PHE SER CYS 1HPL 108
SEQRES 23 B 449 ALA SER TYR SER ASP PHE THR ALA ASN LYS CYS PHE PRO 1HPL 109
SEQRES 24 B 449 CYS SER SER GLU GLY CYS PRO GLN MET GLY HIS TYR ALA 1HPL 110
SEQRES 25 B 449 ASP ARG PHE PRO GLY ARG THR LYS GLY VAL GLY GLN LEU 1HPL 111
SEQRES 26 B 449 PHE TYR LEU ASN THR GLY ASP ALA SER ASN PHE ALA ARG 1HPL 112
SEQRES 27 B 449 TRP ARG TYR ARG VAL ASP VAL THR LEU SER GLY LYS LYS 1HPL 113
SEQRES 28 B 449 VAL THR GLY HIS VAL LEU VAL SER LEU PHE GLY ASN LYS 1HPL 114
SEQRES 29 B 449 GLY ASN SER ARG GLN TYR GLU ILE PHE GLN GLY THR LEU 1HPL 115
SEQRES 30 B 449 LYS PRO ASP ASN THR TYR SER ASN GLU PHE ASP SER ASP 1HPL 116
SEQRES 31 B 449 VAL GLU VAL GLY ASP LEU GLU LYS VAL LYS PHE ILE TRP 1HPL 117
SEQRES 32 B 449 TYR ASN ASN VAL ILE ASN LEU THR LEU PRO LYS VAL GLY 1HPL 118
SEQRES 33 B 449 ALA SER LYS ILE THR VAL GLU ARG ASN ASP GLY SER VAL 1HPL 119
SEQRES 34 B 449 PHE ASN PHE CYS SER GLU GLU THR VAL ARG GLU ASP VAL 1HPL 120
SEQRES 35 B 449 LEU LEU THR LEU THR ALA CYS 1HPL 121
FTNOTE 1 1HPL 122
FTNOTE 1 CIS PROLINE - PRO A 16 1HPL 123
FTNOTE 2 1HPL 124
FTNOTE 2 CIS PROLINE - PRO A 211 1HPL 125
FTNOTE 3 1HPL 126
FTNOTE 3 CIS PROLINE - PRO A 298 1HPL 127
FTNOTE 4 1HPL 128
FTNOTE 4 SER A 333 - ASN A 334 OMEGA =326.11 1HPL 129
FTNOTE 4 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1HPL 130
FTNOTE 5 1HPL 131
FTNOTE 5 CIS PROLINE - PRO B 16 1HPL 132
FTNOTE 6 1HPL 133
FTNOTE 6 CIS PROLINE - PRO B 211 1HPL 134
FTNOTE 7 1HPL 135
FTNOTE 7 CIS PROLINE - PRO B 298 1HPL 136
FTNOTE 8 1HPL 137
FTNOTE 8 SER B 333 - ASN B 334 OMEGA =298.62 1HPL 138
FTNOTE 8 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1HPL 139
HET CA A 960 1 CALCIUM +2 COUNTER ION 1HPL 140
HET CA B 970 1 CALCIUM +2 COUNTER ION 1HPL 141
FORMUL 3 CA 2(CA1) 1HPL 142
FORMUL 4 HOH *705(H2 O1) 1HPL 143
HELIX 1 AA PRO A 31 VAL A 34 1 1HPL 144
HELIX 2 BA PRO A 56 SER A 61 1 1HPL 145
HELIX 3 CA TRP A 85 MET A 93 1 1HPL 146
HELIX 4 DA LYS A 107 SER A 110 1 1HPL 147
HELIX 5 EA TYR A 114 PHE A 139 1 1HPL 148
HELIX 6 FA SER A 155 THR A 165 1 1HPL 149
HELIX 7 GA ILE A 248 TRP A 252 1 ONE-TURN HELIX AT ACTIVE SITE 1HPL 150
HELIX 8 HA CYS A 261 SER A 273 1 1HPL 151
HELIX 9 IA TYR A 288 THR A 292 1 1HPL 152
HELIX 10 AB PRO B 31 VAL B 34 1 1HPL 153
HELIX 11 BB PRO B 56 SER B 61 1 1HPL 154
HELIX 12 CB TRP B 85 MET B 93 1 1HPL 155
HELIX 13 DB LYS B 107 SER B 110 1 1HPL 156
HELIX 14 EB TYR B 114 PHE B 139 1 1HPL 157
HELIX 15 FB SER B 155 THR B 165 1 1HPL 158
HELIX 16 GB ILE B 248 TRP B 252 1 ONE-TURN HELIX AT ACTIVE SITE 1HPL 159
HELIX 17 HB CYS B 261 SER B 273 1 1HPL 160
HELIX 18 IB TYR B 288 THR B 292 1 1HPL 161
SHEET 1 AA 2 VAL A 3 TYR A 5 0 1HPL 162
SHEET 2 AA 2 GLY A 9 PHE A 11 -1 1HPL 163
SHEET 1 BA 9 ARG A 37 THR A 42 0 1HPL 164
SHEET 2 BA 9 ASN A 45 GLU A 51 -1 1HPL 165
SHEET 3 BA 9 THR A 70 ILE A 74 -1 1HPL 166
SHEET 4 BA 9 ASN A 100 ASP A 105 1 1HPL 167
SHEET 5 BA 9 VAL A 146 HIS A 151 1 1HPL 168
SHEET 6 BA 9 ARG A 171 LEU A 175 1 1HPL 169
SHEET 7 BA 9 VAL A 199 ILE A 202 1 1HPL 170
SHEET 8 BA 9 LEU A 224 PHE A 226 1 1HPL 171
SHEET 9 BA 9 GLN A 323 PHE A 325 1 1HPL 172
SHEET 1 CA 4 TRP A 338 GLY A 348 0 1HPL 173
SHEET 2 CA 4 THR A 381 SER A 388 -1 1HPL 174
SHEET 3 CA 4 VAL A 415 GLU A 423 -1 1HPL 175
SHEET 4 CA 4 VAL A 429 CYS A 433 -1 1HPL 176
SHEET 1 DA 4 VAL A 351 GLY A 361 0 1HPL 177
SHEET 2 DA 4 TYR A 369 LEU A 376 -1 1HPL 178
SHEET 3 DA 4 LEU A 395 ASN A 406 -1 1HPL 179
SHEET 4 DA 4 LEU A 444 LEU A 446 -1 1HPL 180
SHEET 1 AB 2 VAL B 3 TYR B 5 0 1HPL 181
SHEET 2 AB 2 GLY B 9 PHE B 11 -1 1HPL 182
SHEET 1 BB 9 ARG B 37 THR B 42 0 1HPL 183
SHEET 2 BB 9 ASN B 45 GLU B 51 -1 1HPL 184
SHEET 3 BB 9 THR B 70 ILE B 74 -1 1HPL 185
SHEET 4 BB 9 ASN B 100 ASP B 105 1 1HPL 186
SHEET 5 BB 9 VAL B 146 HIS B 151 1 1HPL 187
SHEET 6 BB 9 ARG B 171 LEU B 175 1 1HPL 188
SHEET 7 BB 9 VAL B 199 ILE B 202 1 1HPL 189
SHEET 8 BB 9 LEU B 224 PHE B 226 1 1HPL 190
SHEET 9 BB 9 GLN B 323 PHE B 325 1 1HPL 191
SHEET 1 CB 4 TRP B 338 GLY B 348 0 1HPL 192
SHEET 2 CB 4 THR B 381 SER B 388 -1 1HPL 193
SHEET 3 CB 4 VAL B 415 GLU B 423 -1 1HPL 194
SHEET 4 CB 4 VAL B 429 CYS B 433 -1 1HPL 195
SHEET 1 DB 4 VAL B 351 GLY B 361 0 1HPL 196
SHEET 2 DB 4 TYR B 369 LEU B 376 -1 1HPL 197
SHEET 3 DB 4 LEU B 395 ASN B 406 -1 1HPL 198
SHEET 4 DB 4 LEU B 444 LEU B 446 -1 1HPL 199
TURN 1 AA ILE A 20 ARG A 23 1HPL 200
TURN 2 BA THR A 42 ASN A 45 1HPL 201
TURN 3 CA ASN A 65 ARG A 68 1HPL 202
TURN 4 DA ASP A 79 GLU A 82 1HPL 203
TURN 5 EA GLU A 82 TRP A 85 1HPL 204
TURN 6 FA MET A 93 VAL A 96 1HPL 205
TURN 7 GA THR A 165 ALA A 168 1HPL 206
TURN 8 HA PRO A 186 VAL A 189 1HPL 207
TURN 9 IA ASP A 192 ASP A 195 1HPL 208
TURN 10 JA MET A 234 CYS A 237 1HPL 209
TURN 11 KA ILE A 251 GLY A 254 1HPL 210
TURN 12 LA ASP A 272 LEU A 275 1HPL 211
TURN 13 MA ASN A 276 GLY A 279 1HPL 212
TURN 14 NA ASP A 290 ASN A 294 1HPL 213
TURN 15 OA SER A 300 GLY A 303 1HPL 214
TURN 16 PA GLY A 308 ALA A 311 1HPL 215
TURN 17 QA ALA A 311 PHE A 314 1HPL 216
TURN 18 RA PHE A 314 ARG A 317 1HPL 217
TURN 19 SA ARG A 424 GLY A 427 1HPL 218
TURN 20 AB ILE B 20 ARG B 23 1HPL 219
TURN 21 BB THR B 42 ASN B 45 1HPL 220
TURN 22 CB ASN B 65 ARG B 68 1HPL 221
TURN 23 DB ASP B 79 GLU B 82 1HPL 222
TURN 24 EB GLU B 82 TRP B 85 1HPL 223
TURN 25 FB MET B 93 VAL B 96 1HPL 224
TURN 26 GB THR B 165 ALA B 168 1HPL 225
TURN 27 HB PRO B 186 VAL B 189 1HPL 226
TURN 28 IB ASP B 192 ASP B 195 1HPL 227
TURN 29 JB MET B 234 CYS B 237 1HPL 228
TURN 30 KB ILE B 251 GLY B 254 1HPL 229
TURN 31 LB ASP B 272 LEU B 275 1HPL 230
TURN 32 MB ASN B 276 GLY B 279 1HPL 231
TURN 33 NB ASP B 290 ASN B 294 1HPL 232
TURN 34 OB SER B 300 GLY B 303 1HPL 233
TURN 35 PB GLY B 308 ALA B 311 1HPL 234
TURN 36 QB ALA B 311 PHE B 314 1HPL 235
TURN 37 RB PHE B 314 ARG B 317 1HPL 236
TURN 38 SB ARG B 424 GLY B 427 1HPL 237
SSBOND 1 CYS A 4 CYS A 10 1HPL 238
SSBOND 2 CYS A 90 CYS A 101 1HPL 239
SSBOND 3 CYS A 237 CYS A 261 1HPL 240
SSBOND 4 CYS A 285 CYS A 296 1HPL 241
SSBOND 5 CYS A 299 CYS A 304 1HPL 242
SSBOND 6 CYS A 433 CYS A 449 1HPL 243
SSBOND 7 CYS B 4 CYS B 10 1HPL 244
SSBOND 8 CYS B 90 CYS B 101 1HPL 245
SSBOND 9 CYS B 237 CYS B 261 1HPL 246
SSBOND 10 CYS B 285 CYS B 296 1HPL 247
SSBOND 11 CYS B 299 CYS B 304 1HPL 248
SSBOND 12 CYS B 433 CYS B 449 1HPL 249
SITE 1 ACT 3 SER A 152 ASP A 176 HIS A 263 1HPL 250
SITE 1 BCT 3 SER B 152 ASP B 176 HIS B 263 1HPL 251
CRYST1 79.800 97.200 145.300 90.00 90.00 90.00 P 21 21 21 8 1HPL 252
ORIGX1 1.000000 0.000000 0.000000 0.00000 1HPL 253
ORIGX2 0.000000 1.000000 0.000000 0.00000 1HPL 254
ORIGX3 0.000000 0.000000 1.000000 0.00000 1HPL 255
SCALE1 0.012531 0.000000 0.000000 0.00000 1HPL 256
SCALE2 0.000000 0.010288 0.000000 0.00000 1HPL 257
SCALE3 0.000000 0.000000 0.006882 0.00000 1HPL 258
MTRIX1 1 -0.999900 -0.001100 0.002900 79.35000 1 1HPL 259
MTRIX2 1 -0.001100 0.998660 -0.050000 2.02820 1 1HPL 260
MTRIX3 1 -0.002300 -0.050200 -0.998000 61.23560 1 1HPL 261 |