HEADER HYDROLASE(CARBOXYLIC ESTERASE) 02-MAR-93 1CRL 1CRL 2 COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1CRL 3 SOURCE FUNGUS (CANDIDA RUGOSA) (FORMERLY CYLINDRACEA) 1CRL 4 AUTHOR P.GROCHULSKI,M.CYGLER 1CRL 5 REVDAT 1 31-JAN-94 1CRL 0 1CRL 6 JRNL AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1CRL 7 JRNL AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1CRL 8 JRNL TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 1CRL 9 JRNL TITL 2 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE 1CRL 10 JRNL REF J.BIOL.CHEM. V. 268 12843 1993 1CRL 11 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 071 1CRL 12 REMARK 1 1CRL 13 REMARK 1 REFERENCE 1 1CRL 14 REMARK 1 AUTH Y.KAWAGUCHI,H.HONDA,J.TANIGUCHI-MORIMURA,S.IWASAKI 1CRL 15 REMARK 1 TITL THE CODON CUG IS READ AS SERINE IN AN ASPOROGENIC 1CRL 16 REMARK 1 TITL 2 YEAST CANDIDA CYLINDRACEA 1CRL 17 REMARK 1 REF NATURE V. 341 164 1989 1CRL 18 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1CRL 19 REMARK 2 1CRL 20 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. 1CRL 21 REMARK 3 1CRL 22 REMARK 3 REFINEMENT. 1CRL 23 REMARK 3 PROGRAM X-PLOR 1CRL 24 REMARK 3 AUTHORS BRUNGER 1CRL 25 REMARK 3 R VALUE 0.134 1CRL 26 REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1CRL 27 REMARK 3 RMSD BOND ANGLES 2.64 DEGREES 1CRL 28 REMARK 4 1CRL 29 REMARK 4 THREE N-ACETYLGLUCOSAMINE RESIDUES AT TWO SITES INCLUDED: 1CRL 30 REMARK 4 TWO N-LINKED RESIDUES AT ASN 351; ONE N-LINKED RESIDUE AT 1CRL 31 REMARK 4 ASN 314. 1CRL 32 SEQRES 1 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR 1CRL 33 SEQRES 2 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE 1CRL 34 SEQRES 3 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS 1CRL 35 SEQRES 4 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY GLN LYS 1CRL 36 SEQRES 5 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO 1CRL 37 SEQRES 6 534 GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA ALA LEU 1CRL 38 SEQRES 7 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA VAL SER 1CRL 39 SEQRES 8 534 PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG 1CRL 40 SEQRES 9 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET 1CRL 41 SEQRES 10 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY GLY THR 1CRL 42 SEQRES 11 534 SER THR PHE PRO PRO ALA GLN MET ILE THR LYS SER ILE 1CRL 43 SEQRES 12 534 ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL ASN TYR 1CRL 44 SEQRES 13 534 ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP GLU ILE 1CRL 45 SEQRES 14 534 LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS ASP GLN 1CRL 46 SEQRES 15 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA ALA 1CRL 47 SEQRES 16 534 PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE GLY GLU 1CRL 48 SEQRES 17 534 SER ALA GLY SER MET SER VAL MET CYS HIS ILE LEU TRP 1CRL 49 SEQRES 18 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE 1CRL 50 SEQRES 19 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER 1CRL 51 SEQRES 20 534 ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE PHE ASP 1CRL 52 SEQRES 21 534 LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA SER ASP 1CRL 53 SEQRES 22 534 LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP THR LEU 1CRL 54 SEQRES 23 534 GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR 1CRL 55 SEQRES 24 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY 1CRL 56 SEQRES 25 534 VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL ARG GLU 1CRL 57 SEQRES 26 534 GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY ASP GLN 1CRL 58 SEQRES 27 534 ASN ASP GLU GLY THR PHE PHE GLY THR SER SER LEU ASN 1CRL 59 SEQRES 28 534 VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE LYS GLN 1CRL 60 SEQRES 29 534 SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP THR LEU 1CRL 61 SEQRES 30 534 MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY SER PRO 1CRL 62 SEQRES 31 534 PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO GLN PHE 1CRL 63 SEQRES 32 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY PHE THR 1CRL 64 SEQRES 33 534 LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR GLY GLY 1CRL 65 SEQRES 34 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU 1CRL 66 SEQRES 35 534 PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE VAL PHE 1CRL 67 SEQRES 36 534 GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE TYR ASN 1CRL 68 SEQRES 37 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN 1CRL 69 SEQRES 38 534 THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR THR SER 1CRL 70 SEQRES 39 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA 1CRL 71 SEQRES 40 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA 1CRL 72 SEQRES 41 534 GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER PHE PHE 1CRL 73 SEQRES 42 534 VAL 1CRL 74 FTNOTE 1 1CRL 75 FTNOTE 1 CIS PROLINE - PRO 390 1CRL 76 HET NAG 990 14 N-ACETYL-D-GLUCOSAMINE 1CRL 77 HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1CRL 78 HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1CRL 79 FORMUL 2 NAG 3(C8 H15 N1 O6) 1CRL 80 FORMUL 3 HOH *310(H2 O1) 1CRL 81 HELIX 1 H1 LEU 73 GLN 83 1 FLAP 1CRL 82 HELIX 2 H2 ALA 136 MET 145 1 1CRL 83 HELIX 3 H3 ASP 167 GLU 172 1 1CRL 84 HELIX 4 H4 ALA 177 ASP 191 1 1CRL 85 HELIX 5 H5 ALA 210 LEU 220 1 1CRL 86 HELIX 6 H6 ILE 253 ALA 266 1 1CRL 87 HELIX 7 H7 LYS 274 ARG 279 1 1CRL 88 HELIX 8 H8 SER 283 THR 290 1 1CRL 89 HELIX 9 H9 ASP 318 ARG 324 1 1CRL 90 HELIX 10 H10 THR 343 THR 347 1 1CRL 91 HELIX 11 H11 ASP 355 SER 365 1 1CRL 92 HELIX 12 H12 ASP 371 ALA 380 1 1CRL 93 HELIX 13 H13 PHE 403 HIS 425 1 1CRL 94 HELIX 14 H14 ASP 452 GLN 456 1 1CRL 95 HELIX 15 H15 SER 464 ALA 475 1 1CRL 96 HELIX 16 H16 THR 519 LEU 525 1 1CRL 97 SHEET 1 BN 3 PRO 2 LEU 6 0 1CRL 98 SHEET 2 BN 3 ASP 10 GLY 14 -1 N GLY 14 O PRO 2 1CRL 99 SHEET 3 BN 3 GLY 50 PHE 53 1 N PHE 53 O THR 13 1CRL 100 SHEET 1 BC 11 LEU 15 ALA 17 0 1CRL 101 SHEET 2 BC 11 ASN 20 ILE 26 -1 O ASN 20 N ALA 17 1CRL 102 SHEET 3 BC 11 ILE 100 ARG 104 -1 O ARG 104 N GLU 21 1CRL 103 SHEET 4 BC 11 ILE 150 VAL 154 1 N HIS 151 O VAL 103 1CRL 104 SHEET 5 BC 11 PRO 115 ILE 120 -1 O PRO 115 N ILE 150 1CRL 105 SHEET 6 BC 11 LYS 202 GLU 208 1 O LYS 202 N VAL 116 1CRL 106 SHEET 7 BC 11 ARG 235 GLN 240 1 N ARG 235 O VAL 203 1CRL 107 SHEET 8 BC 11 PRO 332 ASN 339 1 O PRO 332 N GLY 237 1CRL 108 SHEET 9 BC 11 THR 430 LYS 437 1 O THR 430 N VAL 333 1CRL 109 SHEET 10 BC 11 LEU 502 ASN 506 1 N MET 503 O SER 433 1CRL 110 SHEET 11 BC 11 GLY 509 GLY 513 -1 O GLY 513 N LEU 502 1CRL 111 SSBOND 1 CYS 60 CYS 97 1CRL 112 SSBOND 2 CYS 268 CYS 277 1CRL 113 SITE 1 ACT 3 SER 209 GLU 341 HIS 449 1CRL 114 CRYST1 64.900 97.500 175.600 90.00 90.00 90.00 C 2 2 21 8 1CRL 115 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CRL 116 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CRL 117 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CRL 118 SCALE1 0.015408 0.000000 0.000000 0.00000 1CRL 119 SCALE2 0.000000 0.010256 0.000000 0.00000 1CRL 120 SCALE3 0.000000 0.000000 0.005695 0.00000 1CRL 121