| content |
HEADER HYDROLASE(CARBOXYLIC ESTERASE) 19-AUG-94 1LPB 1LPB 2
COMPND LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND INHIBITED 1LPB 3
COMPND 2 BY UNDECANE PHOSPHONATE METHYL ESTER (TWO CONFORMATIONS) 1LPB 4
SOURCE LIPASE: HUMAN (HOMO SAPIENS) PANCREAS; COLIPASE: PIG 1LPB 5
SOURCE 2 (SUS SCROFA) PANCREAS 1LPB 6
AUTHOR M.-P.EGLOFF,H.VAN TILBEURGH,C.CAMBILLAU 1LPB 7
REVDAT 1 01-NOV-94 1LPB 0 1LPB 8
JRNL AUTH M.-P.EGLOFF,F.MARGUET,G.BUONO,R.VERGER,C.CAMBILLAU, 1LPB 9
JRNL AUTH 2 H.VAN TILBEURGH 1LPB 10
JRNL TITL THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE 1LPB 11
JRNL TITL 2 PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A 1LPB 12
JRNL TITL 3 C11 ALKYL PHOSPHONATE 1LPB 13
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1LPB 14
JRNL REFN 0353 1LPB 15
REMARK 1 1LPB 16
REMARK 1 REFERENCE 1 1LPB 17
REMARK 1 AUTH H.VAN TILBEURGH,M.-P.EGLOFF,C.MARTINEZ,N.RUGANI, 1LPB 18
REMARK 1 AUTH 2 R.VERGER,C.CAMBILLAU 1LPB 19
REMARK 1 TITL INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE 1LPB 20
REMARK 1 TITL 2 COMPLEX BY MIXED MICELLES REVEALED BY X-RAY 1LPB 21
REMARK 1 TITL 3 CRYSTALLOGRAPHY 1LPB 22
REMARK 1 REF NATURE V. 362 814 1993 1LPB 23
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1LPB 24
REMARK 1 REFERENCE 2 1LPB 25
REMARK 1 AUTH H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU 1LPB 26
REMARK 1 TITL STRUCTURE OF THE PANCREATIC LIPASE-PROCOLIPASE 1LPB 27
REMARK 1 TITL 2 COMPLEX 1LPB 28
REMARK 1 REF NATURE V. 359 159 1992 1LPB 29
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1LPB 30
REMARK 2 1LPB 31
REMARK 2 RESOLUTION. 2.46 ANGSTROMS. 1LPB 32
REMARK 3 1LPB 33
REMARK 3 REFINEMENT. 1LPB 34
REMARK 3 PROGRAM X-PLOR 1LPB 35
REMARK 3 AUTHORS BRUNGER 1LPB 36
REMARK 3 R VALUE 0.183 1LPB 37
REMARK 3 FREE R VALUE 0.285 1LPB 38
REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1LPB 39
REMARK 3 RMSD BOND ANGLES 1.96 DEGREES 1LPB 40
REMARK 3 1LPB 41
REMARK 3 RESOLUTION RANGE 6. - 2.46 ANGSTROMS 1LPB 42
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1LPB 43
REMARK 4 1LPB 44
REMARK 4 THE COLIPASE AND LIPASE MOLECULES HAVE BEEN ASSIGNED CHAIN 1LPB 45
REMARK 4 IDENTIFIERS *A* AND *B*, RESPECTIVELY. 1LPB 46
REMARK 5 1LPB 47
REMARK 5 CROSS REFERENCE TO SEQUENCE DATABASE 1LPB 48
REMARK 5 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPB 49
REMARK 5 COL2_PIG A 1LPB 50
REMARK 5 LIPP_HUMAN B 1LPB 51
REMARK 5 1LPB 52
REMARK 5 THE FOLLOWING RESIDUES ARE MISSING FROM THE N-TERMINUS OF 1LPB 53
REMARK 5 CHAIN A. THE SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1LPB 54
REMARK 5 VAL 1 1LPB 55
REMARK 5 PRO 2 1LPB 56
REMARK 5 ASP 3 1LPB 57
REMARK 5 PRO 4 1LPB 58
REMARK 5 ARG 5 1LPB 59
REMARK 5 1LPB 60
REMARK 5 RESIDUES OF CHAIN A MISSING THE C-TERMINUS 1LPB 61
REMARK 5 SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1LPB 62
REMARK 5 GLY 91 1LPB 63
REMARK 5 ARG 92 1LPB 64
REMARK 5 SER 93 1LPB 65
REMARK 5 ASP 94 1LPB 66
REMARK 5 SER 95 1LPB 67
REMARK 5 1LPB 68
REMARK 5 RESIDUE 37 FOR CHAIN A IS REPORTED AS LEU IN DATA BASE 1LPB 69
REMARK 5 BUT HAS BEEN CORRECTED LATER TO SER ON THE BASIS OF MASS 1LPB 70
REMARK 5 SPECTROSCOPY. 1LPB 71
REMARK 5 1LPB 72
REMARK 5 N-TERMINAL RESIDUES 1 - 5 AND C-TERMINAL RESIDUES 91 - 95 1LPB 73
REMARK 5 ARE NOT INCLUDED SINCE THEY WERE NOT VISIBLE IN THE 1LPB 74
REMARK 5 ELECTRON DENSITY. 1LPB 75
REMARK 6 1LPB 76
REMARK 6 USE OF PARTIAL OCCUPANCY FOR THE INHIBITOR (REFINED 1LPB 77
REMARK 6 OCCUPANCY) AND FOR BETA-OCTYLGLUCOSIDE MOLECULES. 1LPB 78
SEQRES 1 A 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU 1LPB 79
SEQRES 2 A 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN 1LPB 80
SEQRES 3 A 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU SER ARG CYS 1LPB 81
SEQRES 4 A 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE 1LPB 82
SEQRES 5 A 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG 1LPB 83
SEQRES 6 A 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER 1LPB 84
SEQRES 7 A 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY 1LPB 85
SEQRES 8 A 95 ARG SER ASP SER 1LPB 86
SEQRES 1 B 449 LYS GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP 1LPB 87
SEQRES 2 B 449 ASP SER PRO TRP SER GLY ILE THR GLU ARG PRO LEU HIS 1LPB 88
SEQRES 3 B 449 ILE LEU PRO TRP SER PRO LYS ASP VAL ASN THR ARG PHE 1LPB 89
SEQRES 4 B 449 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN GLU 1LPB 90
SEQRES 5 B 449 VAL ALA ALA ASP SER SER SER ILE SER GLY SER ASN PHE 1LPB 91
SEQRES 6 B 449 LYS THR ASN ARG LYS THR ARG PHE ILE ILE HIS GLY PHE 1LPB 92
SEQRES 7 B 449 ILE ASP LYS GLY GLU GLU ASN TRP LEU ALA ASN VAL CYS 1LPB 93
SEQRES 8 B 449 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS 1LPB 94
SEQRES 9 B 449 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN 1LPB 95
SEQRES 10 B 449 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA 1LPB 96
SEQRES 11 B 449 TYR PHE VAL GLU PHE LEU GLN SER ALA PHE GLY TYR SER 1LPB 97
SEQRES 12 B 449 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY ALA 1LPB 98
SEQRES 13 B 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR 1LPB 99
SEQRES 14 B 449 ILE GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS 1LPB 100
SEQRES 15 B 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER 1LPB 101
SEQRES 16 B 449 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP GLY ALA 1LPB 102
SEQRES 17 B 449 PRO ILE VAL PRO ASN LEU GLY PHE GLY MET SER GLN VAL 1LPB 103
SEQRES 18 B 449 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY VAL GLU 1LPB 104
SEQRES 19 B 449 MET PRO GLY CYS LYS LYS ASN ILE LEU SER GLN ILE VAL 1LPB 105
SEQRES 20 B 449 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE ALA 1LPB 106
SEQRES 21 B 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP 1LPB 107
SEQRES 22 B 449 SER ILE VAL ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS 1LPB 108
SEQRES 23 B 449 ALA SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO 1LPB 109
SEQRES 24 B 449 CYS PRO SER GLY GLY CYS PRO GLN MET GLY HIS TYR ALA 1LPB 110
SEQRES 25 B 449 ASP ARG TYR PRO GLY LYS THR ASN ASP VAL GLY GLN LYS 1LPB 111
SEQRES 26 B 449 PHE TYR LEU ASP THR GLY ASP ALA SER ASN PHE ALA ARG 1LPB 112
SEQRES 27 B 449 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS 1LPB 113
SEQRES 28 B 449 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN LYS 1LPB 114
SEQRES 29 B 449 GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY THR LEU 1LPB 115
SEQRES 30 B 449 LYS PRO ASP SER THR HIS SER ASN GLU PHE ASP SER ASP 1LPB 116
SEQRES 31 B 449 VAL ASP VAL GLY ASP LEU GLN MET VAL LYS PHE ILE TRP 1LPB 117
SEQRES 32 B 449 TYR ASN ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY 1LPB 118
SEQRES 33 B 449 ALA SER LYS ILE ILE VAL GLU THR ASN VAL GLY LYS GLN 1LPB 119
SEQRES 34 B 449 PHE ASN PHE CYS SER PRO GLU THR VAL ARG GLU GLU VAL 1LPB 120
SEQRES 35 B 449 LEU LEU THR LEU THR PRO CYS 1LPB 121
FTNOTE 1 1LPB 122
FTNOTE 1 CIS PROLINE - PRO B 16 1LPB 123
FTNOTE 2 1LPB 124
FTNOTE 2 CIS PROLINE - PRO B 211 1LPB 125
FTNOTE 3 1LPB 126
FTNOTE 3 CIS PROLINE - PRO B 298 1LPB 127
HET MUP B 901 30 METHOXYUNDECYLPHOSPHINIC ACID 1LPB 128
HET CA 450 1 CALCIUM +2 COUNTER ION 1LPB 129
HET BOG 1 24 B-OCTYLGLUCOSIDE 1LPB 130
HET BOG 2 24 B-OCTYLGLUCOSIDE 1LPB 131
HET BOG 3 24 B-OCTYLGLUCOSIDE 1LPB 132
HET BOG 4 48 B-OCTYLGLUCOSIDE 1LPB 133
HET BOG 5 48 B-OCTYLGLUCOSIDE 1LPB 134
FORMUL 3 MUP C12 H27 O3 P1 1LPB 135
FORMUL 4 CA CA1 ++ 1LPB 136
FORMUL 5 BOG 5(C14 H28 O6) 1LPB 137
FORMUL 6 HOH *285(H2 O1) 1LPB 138
HELIX 1 A ASP A 31 LEU A 34 1 1LPB 139
HELIX 2 B GLY A 56 CYS A 61 1 1LPB 140
HELIX 3 J LEU A 75 THR A 80 1 1LPB 141
HELIX 4 C PHE A 84 LEU B 93 1 1LPB 142
HELIX 5 D LYS B 107 SER B 110 1 1LPB 143
HELIX 6 E TYR B 114 PHE B 139 1 1LPB 144
HELIX 7 F LEU B 153 ARG B 163 1 1LPB 145
HELIX 8 G ILE B 241 ILE B 245 1 THE TWO HELICES OF THE LID 1LPB 146
HELIX 9 H ILE B 251 ILE B 274 1 1LPB 147
HELIX 10 I TYR B 288 THR B 292 1 1LPB 148
SHEET 1 SA 2 GLU B 2 TYR B 5 0 1LPB 149
SHEET 2 SA 2 ILE A 9 ASP A 12 -1 1LPB 150
SHEET 1 SB 9 SER A 37 LEU A 41 0 1LPB 151
SHEET 2 SB 9 SER A 50 PHE A 52 -1 1LPB 152
SHEET 3 SB 9 GLU A 70 SER A 74 -1 1LPB 153
SHEET 4 SB 9 ASN B 100 ASP B 105 1 1LPB 154
SHEET 5 SB 9 VAL B 146 HIS B 151 1 1LPB 155
SHEET 6 SB 9 ARG B 171 LEU B 175 1 1LPB 156
SHEET 7 SB 9 VAL B 199 ILE B 202 1 1LPB 157
SHEET 8 SB 9 LEU B 224 PRO B 228 1 1LPB 158
SHEET 9 SB 9 GLN B 323 LEU B 327 1 1LPB 159
SHEET 1 SC 4 TRP B 338 GLY B 348 0 1LPB 160
SHEET 2 SC 4 THR B 381 SER B 388 -1 1LPB 161
SHEET 3 SC 4 VAL B 415 THR B 424 -1 1LPB 162
SHEET 4 SC 4 GLN B 429 CYS B 433 -1 1LPB 163
SHEET 1 SD 4 VAL B 351 GLY B 361 0 1LPB 164
SHEET 2 SD 4 TYR B 369 LEU B 376 -1 1LPB 165
SHEET 3 SD 4 LEU B 395 TYR B 403 -1 1LPB 166
SHEET 4 SD 4 LEU B 444 PRO B 448 -1 1LPB 167
SHEET 1 SE 1 LEU A 67 GLU A 70 0 1LPB 168
SHEET 1 SF 1 PHE A 84 ASN A 89 0 1LPB 169
TURN 1 A GLY A 14 CYS A 17 1LPB 170
TURN 2 B SER A 20 CYS A 23 1LPB 171
TURN 3 C LYS A 42 GLU A 45 1LPB 172
TURN 4 D THR A 80 ASN A 83 1LPB 173
TURN 5 E LEU B 93 ALA B 196 1LPB 174
TURN 6 F SER B 142 ASN B 145 1LPB 175
TURN 7 G HIS B 151 GLY B 154 1LPB 176
TURN 8 H THR B 165 THR B 168 1LPB 177
TURN 9 I GLU B 179 PHE B 182 1LPB 178
TURN 10 J PRO B 186 VAL B 189 1LPB 179
TURN 11 K VAL B 210 LEU B 213 1LPB 180
TURN 12 L PHE B 227 GLY B 230 1LPB 181
TURN 13 M MET B 234 CYS B 237 1LPB 182
TURN 14 N CYS B 261 LEU B 264 1LPB 183
TURN 15 O ASN B 276 GLY B 279 1LPB 184
TURN 16 P PRO B 300 GLY B 303 1LPB 185
TURN 17 Q GLY B 316 ASN B 319 1LPB 186
TURN 18 R GLY B 361 GLY B 364 1LPB 187
TURN 19 S LYS B 377 SER B 380 1LPB 188
TURN 20 T ASN B 409 LEU B 412 1LPB 189
TURN 21 U THR B 424 GLY B 427 1LPB 190
TURN 22 V ARG B 439 VAL B 442 1LPB 191
TURN 23 W ASP A 12 GLU A 15 1LPB 192
TURN 24 X ASN A 19 GLN A 22 1LPB 193
TURN 25 Y GLU A 64 LEU A 67 1LPB 194
SSBOND 1 CYS A 17 CYS A 28 1LPB 195
SSBOND 2 CYS A 23 CYS A 39 1LPB 196
SSBOND 3 CYS A 27 CYS A 61 1LPB 197
SSBOND 4 CYS A 49 CYS A 69 1LPB 198
SSBOND 5 CYS A 63 CYS A 87 1LPB 199
SSBOND 6 CYS B 4 CYS B 10 1LPB 200
SSBOND 7 CYS B 90 CYS B 101 1LPB 201
SSBOND 8 CYS B 237 CYS B 261 1LPB 202
SSBOND 9 CYS B 285 CYS B 296 1LPB 203
SSBOND 10 CYS B 299 CYS B 304 1LPB 204
SSBOND 11 CYS B 433 CYS B 449 1LPB 205
SITE 1 CAT 3 SER B 152 ASP B 176 HIS B 263 1LPB 206
CRYST1 133.700 133.700 93.300 90.00 90.00 90.00 P 42 21 2 8 1LPB 207
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPB 208
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPB 209
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPB 210
SCALE1 0.007479 0.000000 0.000000 0.00000 1LPB 211
SCALE2 0.000000 0.007479 0.000000 0.00000 1LPB 212
SCALE3 0.000000 0.000000 0.010718 0.00000 1LPB 213 |