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 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