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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 |