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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 19-AUG-94 1LPA 1LPA 2
COMPND LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND 1LPA 3
COMPND 2 PHOSPHOLIPID 1LPA 4
SOURCE LIPASE: HUMAN (HOMO SAPIENS) PANCREAS; COLIPASE: PIG 1LPA 5
SOURCE 2 (SUS SCROFA) PANCREAS 1LPA 6
AUTHOR H.VAN TILBEURGH,M.-P.EGLOFF,C.CAMBILLAU 1LPA 7
REVDAT 1 01-NOV-94 1LPA 0 1LPA 8
JRNL AUTH H.VAN TILBEURGH,M.-P.EGLOFF,C.MARTINEZ,N.RUGANI, 1LPA 9
JRNL AUTH 2 R.VERGER,C.CAMBILLAU 1LPA 10
JRNL TITL INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE 1LPA 11
JRNL TITL 2 COMPLEX BY MIXED MICELLES REVEALED BY X-RAY 1LPA 12
JRNL TITL 3 CRYSTALLOGRAPHY 1LPA 13
JRNL REF NATURE V. 362 814 1993 1LPA 14
JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 1LPA 15
REMARK 1 1LPA 16
REMARK 1 REFERENCE 1 1LPA 17
REMARK 1 AUTH M.-P.EGLOFF,F.MARGUET,G.BUONO,R.VERGER,C.CAMBILLAU, 1LPA 18
REMARK 1 AUTH 2 H.VAN TILBEURGH 1LPA 19
REMARK 1 TITL THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE 1LPA 20
REMARK 1 TITL 2 PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A 1LPA 21
REMARK 1 TITL 3 C11 ALKYL PHOSPHONATE 1LPA 22
REMARK 1 REF TO BE PUBLISHED REF NOW ASSIGNED AS 1LPA 23
REMARK 1 REFN 0353 1LPA 24
REMARK 1 REFERENCE 2 1LPA 25
REMARK 1 AUTH H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU 1LPA 26
REMARK 1 TITL STRUCTURE OF THE PANCREATIC LIPASE-PROCOLIPASE 1LPA 27
REMARK 1 TITL 2 COMPLEX 1LPA 28
REMARK 1 REF NATURE V. 359 159 1992 1LPA 29
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1LPA 30
REMARK 2 1LPA 31
REMARK 2 RESOLUTION. 3.04 ANGSTROMS. 1LPA 32
REMARK 3 1LPA 33
REMARK 3 REFINEMENT. 1LPA 34
REMARK 3 PROGRAM X-PLOR 1LPA 35
REMARK 3 AUTHORS BRUNGER 1LPA 36
REMARK 3 R VALUE 0.186 1LPA 37
REMARK 3 RMSD BOND DISTANCES 0.016 ANGSTROMS 1LPA 38
REMARK 3 RMSD BOND ANGLES 3.60 DEGREES 1LPA 39
REMARK 3 1LPA 40
REMARK 3 RESOLUTION RANGE 8. - 3.04 ANGSTROMS 1LPA 41
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1LPA 42
REMARK 4 1LPA 43
REMARK 4 THE COLIPASE AND LIPASE MOLECULES HAVE BEEN ASSIGNED CHAIN 1LPA 44
REMARK 4 IDENTIFIERS *A* AND *B*, RESPECTIVELY. 1LPA 45
REMARK 5 1LPA 46
REMARK 5 CROSS REFERENCE TO SEQUENCE DATABASE 1LPA 47
REMARK 5 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPA 48
REMARK 5 COL2_PIG A 1LPA 49
REMARK 5 LIPP_HUMAN B 1LPA 50
REMARK 5 1LPA 51
REMARK 5 THE FOLLOWING RESIDUES ARE MISSING FROM THE N-TERMINUS OF 1LPA 52
REMARK 5 CHAIN A. THE SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1LPA 53
REMARK 5 VAL 1 1LPA 54
REMARK 5 PRO 2 1LPA 55
REMARK 5 ASP 3 1LPA 56
REMARK 5 PRO 4 1LPA 57
REMARK 5 ARG 5 1LPA 58
REMARK 5 1LPA 59
REMARK 5 RESIDUES OF CHAIN A MISSING THE C-TERMINUS 1LPA 60
REMARK 5 SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1LPA 61
REMARK 5 GLY 91 1LPA 62
REMARK 5 ARG 92 1LPA 63
REMARK 5 SER 93 1LPA 64
REMARK 5 ASP 94 1LPA 65
REMARK 5 SER 95 1LPA 66
REMARK 5 1LPA 67
REMARK 5 N-TERMINAL RESIDUES 1 - 5 AND C-TERMINAL RESIDUES 91 - 95 1LPA 68
REMARK 5 ARE NOT INCLUDED SINCE THEY WERE NOT VISIBLE IN THE 1LPA 69
REMARK 5 ELECTRON DENSITY. 1LPA 70
SEQRES 1 A 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU 1LPA 71
SEQRES 2 A 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN 1LPA 72
SEQRES 3 A 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU LEU ARG CYS 1LPA 73
SEQRES 4 A 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE 1LPA 74
SEQRES 5 A 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG 1LPA 75
SEQRES 6 A 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER 1LPA 76
SEQRES 7 A 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY 1LPA 77
SEQRES 8 A 95 ARG SER ASP SER 1LPA 78
SEQRES 1 B 449 LYS GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP 1LPA 79
SEQRES 2 B 449 ASP SER PRO TRP SER GLY ILE THR GLU ARG PRO LEU HIS 1LPA 80
SEQRES 3 B 449 ILE LEU PRO TRP SER PRO LYS ASP VAL ASN THR ARG PHE 1LPA 81
SEQRES 4 B 449 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN GLU 1LPA 82
SEQRES 5 B 449 VAL ALA ALA ASP SER SER SER ILE SER GLY SER ASN PHE 1LPA 83
SEQRES 6 B 449 LYS THR ASN ARG LYS THR ARG PHE ILE ILE HIS GLY PHE 1LPA 84
SEQRES 7 B 449 ILE ASP LYS GLY GLU GLU ASN TRP LEU ALA ASN VAL CYS 1LPA 85
SEQRES 8 B 449 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS 1LPA 86
SEQRES 9 B 449 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN 1LPA 87
SEQRES 10 B 449 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA 1LPA 88
SEQRES 11 B 449 TYR PHE VAL GLU PHE LEU GLN SER ALA PHE GLY TYR SER 1LPA 89
SEQRES 12 B 449 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY ALA 1LPA 90
SEQRES 13 B 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR 1LPA 91
SEQRES 14 B 449 ILE GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS 1LPA 92
SEQRES 15 B 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER 1LPA 93
SEQRES 16 B 449 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP GLY ALA 1LPA 94
SEQRES 17 B 449 PRO ILE VAL PRO ASN LEU GLY PHE GLY MET SER GLN VAL 1LPA 95
SEQRES 18 B 449 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY VAL GLU 1LPA 96
SEQRES 19 B 449 MET PRO GLY CYS LYS LYS ASN ILE LEU SER GLN ILE VAL 1LPA 97
SEQRES 20 B 449 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE ALA 1LPA 98
SEQRES 21 B 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP 1LPA 99
SEQRES 22 B 449 SER ILE VAL ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS 1LPA 100
SEQRES 23 B 449 ALA SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO 1LPA 101
SEQRES 24 B 449 CYS PRO SER GLY GLY CYS PRO GLN MET GLY HIS TYR ALA 1LPA 102
SEQRES 25 B 449 ASP ARG TYR PRO GLY LYS THR ASN ASP VAL GLY GLN LYS 1LPA 103
SEQRES 26 B 449 PHE TYR LEU ASP THR GLY ASP ALA SER ASN PHE ALA ARG 1LPA 104
SEQRES 27 B 449 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS 1LPA 105
SEQRES 28 B 449 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN LYS 1LPA 106
SEQRES 29 B 449 GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY THR LEU 1LPA 107
SEQRES 30 B 449 LYS PRO ASP SER THR HIS SER ASN GLU PHE ASP SER ASP 1LPA 108
SEQRES 31 B 449 VAL ASP VAL GLY ASP LEU GLN MET VAL LYS PHE ILE TRP 1LPA 109
SEQRES 32 B 449 TYR ASN ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY 1LPA 110
SEQRES 33 B 449 ALA SER LYS ILE ILE VAL GLU THR ASN VAL GLY LYS GLN 1LPA 111
SEQRES 34 B 449 PHE ASN PHE CYS SER PRO GLU THR VAL ARG GLU GLU VAL 1LPA 112
SEQRES 35 B 449 LEU LEU THR LEU THR PRO CYS 1LPA 113
FTNOTE 1 1LPA 114
FTNOTE 1 CIS PROLINE - PRO B 16 1LPA 115
FTNOTE 2 1LPA 116
FTNOTE 2 TRP B 30 - SER B 30A OMEGA = 141.29 1LPA 117
FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1LPA 118
FTNOTE 3 1LPA 119
FTNOTE 3 SER B 30A - PRO B 31 OMEGA = 285.07 1LPA 120
FTNOTE 3 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1LPA 121
FTNOTE 4 1LPA 122
FTNOTE 4 CIS PROLINE - PRO B 211 1LPA 123
FTNOTE 5 1LPA 124
FTNOTE 5 CIS PROLINE - PRO B 298 1LPA 125
HET BNG 1 20 B-NONYLGLUCOSIDE 1LPA 126
HET CA 1 1 CALCIUM +2 COUNTER ION 1LPA 127
HET PLC 1 42 DIUNDECYL PHOSPHATIDYL CHOLINE 1LPA 128
FORMUL 3 BNG C15 H30 O6 1LPA 129
FORMUL 4 CA CA1 ++ 1LPA 130
FORMUL 5 PLC C32 H64 N1 O8 P1 1LPA 131
HELIX 1 A ASP A 31 LEU A 34 1 1LPA 132
HELIX 2 B GLY A 56 CYS A 61 1 1LPA 133
HELIX 3 J LEU A 75 THR A 80 1 1LPA 134
HELIX 4 C PHE A 84 LEU B 93 1 1LPA 135
HELIX 5 D LYS B 107 SER B 110 1 1LPA 136
HELIX 6 E TYR B 114 PHE B 139 1 1LPA 137
HELIX 7 F LEU B 153 ARG B 163 1 1LPA 138
HELIX 8 G ILE B 241 ILE B 245 1 THE TWO HELICES OF THE LID 1LPA 139
HELIX 9 H ILE B 251 ILE B 274 1 1LPA 140
HELIX 10 I TYR B 288 THR B 292 1 1LPA 141
SHEET 1 SA 2 GLU B 2 TYR B 5 0 1LPA 142
SHEET 2 SA 2 ILE A 9 ASP A 12 -1 1LPA 143
SHEET 1 SB 9 LEU A 37 LEU A 41 0 1LPA 144
SHEET 2 SB 9 SER A 50 PHE A 52 -1 1LPA 145
SHEET 3 SB 9 GLU A 70 SER A 74 -1 1LPA 146
SHEET 4 SB 9 ASN B 100 ASP B 105 1 1LPA 147
SHEET 5 SB 9 VAL B 146 HIS B 151 1 1LPA 148
SHEET 6 SB 9 ARG B 171 LEU B 175 1 1LPA 149
SHEET 7 SB 9 VAL B 199 ILE B 202 1 1LPA 150
SHEET 8 SB 9 LEU B 224 PRO B 228 1 1LPA 151
SHEET 9 SB 9 GLN B 323 LEU B 327 1 1LPA 152
SHEET 1 SC 4 TRP B 338 GLY B 348 0 1LPA 153
SHEET 2 SC 4 THR B 381 SER B 388 -1 1LPA 154
SHEET 3 SC 4 VAL B 415 THR B 424 -1 1LPA 155
SHEET 4 SC 4 GLN B 429 CYS B 433 -1 1LPA 156
SHEET 1 SD 4 VAL B 351 GLY B 361 0 1LPA 157
SHEET 2 SD 4 TYR B 369 LEU B 376 -1 1LPA 158
SHEET 3 SD 4 LEU B 395 TYR B 403 -1 1LPA 159
SHEET 4 SD 4 LEU B 444 PRO B 448 -1 1LPA 160
SHEET 1 SE 1 LEU A 67 GLU A 70 0 1LPA 161
SHEET 1 SF 1 PHE A 84 ASN A 89 0 1LPA 162
TURN 1 A GLY A 14 CYS A 17 1LPA 163
TURN 2 B SER A 20 CYS A 23 1LPA 164
TURN 3 C LYS A 42 GLU A 45 1LPA 165
TURN 4 D THR A 80 ASN A 83 1LPA 166
TURN 5 E LEU B 93 ALA B 196 1LPA 167
TURN 6 F SER B 142 ASN B 145 1LPA 168
TURN 7 G HIS B 151 GLY B 154 1LPA 169
TURN 8 H THR B 165 THR B 168 1LPA 170
TURN 9 I GLU B 179 PHE B 182 1LPA 171
TURN 10 J PRO B 186 VAL B 189 1LPA 172
TURN 11 K VAL B 210 LEU B 213 1LPA 173
TURN 12 L PHE B 227 GLY B 230 1LPA 174
TURN 13 M MET B 234 CYS B 237 1LPA 175
TURN 14 N CYS B 261 LEU B 264 1LPA 176
TURN 15 O ASN B 276 GLY B 279 1LPA 177
TURN 16 P PRO B 300 GLY B 303 1LPA 178
TURN 17 Q GLY B 316 ASN B 319 1LPA 179
TURN 18 R GLY B 361 GLY B 364 1LPA 180
TURN 19 S LYS B 377 SER B 380 1LPA 181
TURN 20 T ASN B 409 LEU B 412 1LPA 182
TURN 21 U THR B 424 GLY B 427 1LPA 183
TURN 22 V ARG B 439 VAL B 442 1LPA 184
TURN 23 W ASP A 12 GLU A 15 1LPA 185
TURN 24 X ASN A 19 GLN A 22 1LPA 186
TURN 25 Y GLU A 64 LEU A 67 1LPA 187
SSBOND 1 CYS A 17 CYS A 28 1LPA 188
SSBOND 2 CYS A 23 CYS A 39 1LPA 189
SSBOND 3 CYS A 27 CYS A 61 1LPA 190
SSBOND 4 CYS A 49 CYS A 69 1LPA 191
SSBOND 5 CYS A 63 CYS A 87 1LPA 192
SSBOND 6 CYS B 4 CYS B 10 1LPA 193
SSBOND 7 CYS B 90 CYS B 101 1LPA 194
SSBOND 8 CYS B 237 CYS B 261 1LPA 195
SSBOND 9 CYS B 285 CYS B 296 1LPA 196
SSBOND 10 CYS B 299 CYS B 304 1LPA 197
SSBOND 11 CYS B 433 CYS B 449 1LPA 198
SITE 1 CAT 3 SER B 152 ASP B 176 HIS B 263 1LPA 199
CRYST1 133.400 133.400 92.600 90.00 90.00 90.00 P 42 21 2 8 1LPA 200
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPA 201
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPA 202
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPA 203
SCALE1 0.007496 0.000000 0.000000 0.00000 1LPA 204
SCALE2 0.000000 0.007496 0.000000 0.00000 1LPA 205
SCALE3 0.000000 0.000000 0.010799 0.00000 1LPA 206 |