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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 18-NOV-93 1TRH 1TRH 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1TRH 3
SOURCE FUNGUS (CANDIDA RUGOSA) (FORMERLY CYLINDRACEA) 1TRH 4
AUTHOR P.GROCHULSKI,M.CYGLER 1TRH 5
REVDAT 1 31-JAN-94 1TRH 0 1TRH 6
JRNL AUTH P.GROCHULSKI,M.CYGLER 1TRH 7
JRNL TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA 1TRH 8
JRNL TITL 2 LIPASE 1TRH 9
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1TRH 10
JRNL REFN 353 1TRH 11
REMARK 1 1TRH 12
REMARK 1 REFERENCE 1 1TRH 13
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1TRH 14
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1TRH 15
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1TRH 16
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1TRH 17
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1TRH 18
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1TRH 19
REMARK 1 REFERENCE 2 1TRH 20
REMARK 1 AUTH M.LOTTI,R.GRANDORI,F.FUSETTI,S.LONGHI,S.BROCCA, 1TRH 21
REMARK 1 AUTH 2 A.TRAMONTANO 1TRH 22
REMARK 1 TITL CLONING AND ANALYSIS OF CANDIDA CYLINDRACEA 1TRH 23
REMARK 1 TITL 2 LIPASE SEQUENCES 1TRH 24
REMARK 1 REF GENE V. 124 45 1993 1TRH 25
REMARK 1 REFN ASTM GENED6 NE ISSN 0378-1119 861 1TRH 26
REMARK 1 REFERENCE 3 1TRH 27
REMARK 1 AUTH Y.KAWAGUCHI,H.HONDA,J.TANIGUCHI-MORIMURA,S.IWASAKI 1TRH 28
REMARK 1 TITL THE CODON CUG IS READ AS SERINE IN AN ASPOROGENIC 1TRH 29
REMARK 1 TITL 2 YEAST CANDIDA CYLINDRACEA 1TRH 30
REMARK 1 REF NATURE V. 341 164 1989 1TRH 31
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1TRH 32
REMARK 2 1TRH 33
REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1TRH 34
REMARK 3 1TRH 35
REMARK 3 REFINEMENT. 1TRH 36
REMARK 3 PROGRAM X-PLOR 1TRH 37
REMARK 3 AUTHORS BRUNGER 1TRH 38
REMARK 3 R VALUE 0.148 1TRH 39
REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1TRH 40
REMARK 3 RMSD BOND ANGLES 2.70 DEGREES 1TRH 41
REMARK 4 1TRH 42
REMARK 4 TWO N-ACETYLGLUCOSAMINE RESIDUES AT TWO SITES INCLUDED: 1TRH 43
REMARK 4 ONE N-LINKED RESIDUE AT ASN 351; ONE N-LINKED RESIDUE AT 1TRH 44
REMARK 4 ASN 314. 1TRH 45
SEQRES 1 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR 1TRH 46
SEQRES 2 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE 1TRH 47
SEQRES 3 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS 1TRH 48
SEQRES 4 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY GLN LYS 1TRH 49
SEQRES 5 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO 1TRH 50
SEQRES 6 534 GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA ALA LEU 1TRH 51
SEQRES 7 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA VAL SER 1TRH 52
SEQRES 8 534 PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG 1TRH 53
SEQRES 9 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET 1TRH 54
SEQRES 10 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY GLY THR 1TRH 55
SEQRES 11 534 SER THR PHE PRO PRO ALA GLN MET ILE THR LYS SER ILE 1TRH 56
SEQRES 12 534 ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL ASN TYR 1TRH 57
SEQRES 13 534 ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP GLU ILE 1TRH 58
SEQRES 14 534 LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS ASP GLN 1TRH 59
SEQRES 15 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA ALA 1TRH 60
SEQRES 16 534 PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE GLY GLU 1TRH 61
SEQRES 17 534 SER ALA GLY SER MET SER VAL MET CYS HIS ILE LEU TRP 1TRH 62
SEQRES 18 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE 1TRH 63
SEQRES 19 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER 1TRH 64
SEQRES 20 534 ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE PHE ASP 1TRH 65
SEQRES 21 534 LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA SER ASP 1TRH 66
SEQRES 22 534 LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP THR LEU 1TRH 67
SEQRES 23 534 GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR 1TRH 68
SEQRES 24 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY 1TRH 69
SEQRES 25 534 VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL ARG GLU 1TRH 70
SEQRES 26 534 GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY ASP GLN 1TRH 71
SEQRES 27 534 ASN ASP GLU GLY THR PHE PHE GLY THR SER SER LEU ASN 1TRH 72
SEQRES 28 534 VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE LYS GLN 1TRH 73
SEQRES 29 534 SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP THR LEU 1TRH 74
SEQRES 30 534 MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY SER PRO 1TRH 75
SEQRES 31 534 PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO GLN PHE 1TRH 76
SEQRES 32 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY PHE THR 1TRH 77
SEQRES 33 534 LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR GLY GLY 1TRH 78
SEQRES 34 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU 1TRH 79
SEQRES 35 534 PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE VAL PHE 1TRH 80
SEQRES 36 534 GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE TYR ASN 1TRH 81
SEQRES 37 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN 1TRH 82
SEQRES 38 534 THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR THR SER 1TRH 83
SEQRES 39 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA 1TRH 84
SEQRES 40 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA 1TRH 85
SEQRES 41 534 GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER PHE PHE 1TRH 86
SEQRES 42 534 VAL 1TRH 87
FTNOTE 1 1TRH 88
FTNOTE 1 CIS PROLINE - PRO 92 1TRH 89
FTNOTE 2 1TRH 90
FTNOTE 2 CIS PROLINE - PRO 390 1TRH 91
HET NAG 990 14 N-ACETYL-D-GLUCOSAMINE 1TRH 92
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1TRH 93
FORMUL 2 NAG 2(C8 H15 N1 O6) 1TRH 94
FORMUL 3 HOH *301(H2 O1) 1TRH 95
HELIX 1 H1 LYS 75 SER 84 1 FLAP 1TRH 96
HELIX 2 H2 ALA 136 MET 145 1 1TRH 97
HELIX 3 H3 ASP 167 GLU 172 1 1TRH 98
HELIX 4 H4 ALA 177 ASP 191 1 1TRH 99
HELIX 5 H5 ALA 210 LEU 220 1 1TRH 100
HELIX 6 H6 ILE 253 ALA 266 1 1TRH 101
HELIX 7 H7 LYS 274 ARG 279 1 1TRH 102
HELIX 8 H8 SER 283 THR 290 1 1TRH 103
HELIX 9 H9 ASP 318 ARG 324 1 1TRH 104
HELIX 10 H10 THR 343 THR 347 1 1TRH 105
HELIX 11 H11 ASP 355 SER 365 1 1TRH 106
HELIX 12 H12 ASP 371 ALA 380 1 1TRH 107
HELIX 13 H13 PHE 403 HIS 425 1 1TRH 108
HELIX 14 H14 ASP 452 GLN 456 1 1TRH 109
HELIX 15 H15 SER 464 ALA 475 1 1TRH 110
HELIX 16 H16 THR 519 LEU 525 1 1TRH 111
SHEET 1 BN 3 PRO 2 LEU 6 0 1TRH 112
SHEET 2 BN 3 ASP 10 GLY 14 -1 N GLY 14 O PRO 2 1TRH 113
SHEET 3 BN 3 GLY 50 PHE 53 1 N PHE 53 O THR 13 1TRH 114
SHEET 1 BC 11 LEU 15 ALA 17 0 1TRH 115
SHEET 2 BC 11 ASN 20 ILE 26 -1 O ASN 20 N ALA 17 1TRH 116
SHEET 3 BC 11 ILE 100 ARG 104 -1 O ARG 104 N GLU 21 1TRH 117
SHEET 4 BC 11 ILE 150 VAL 154 1 N HIS 151 O VAL 103 1TRH 118
SHEET 5 BC 11 PRO 115 ILE 120 -1 O PRO 115 N ILE 150 1TRH 119
SHEET 6 BC 11 LYS 202 GLU 208 1 O LYS 202 N VAL 116 1TRH 120
SHEET 7 BC 11 ARG 235 GLN 240 1 N ARG 235 O VAL 203 1TRH 121
SHEET 8 BC 11 PRO 332 ASN 339 1 O PRO 332 N GLY 237 1TRH 122
SHEET 9 BC 11 THR 430 LYS 437 1 O THR 430 N VAL 333 1TRH 123
SHEET 10 BC 11 LEU 502 ASN 506 1 N MET 503 O SER 433 1TRH 124
SHEET 11 BC 11 GLY 509 GLY 513 -1 O GLY 513 N LEU 502 1TRH 125
SSBOND 1 CYS 60 CYS 97 1TRH 126
SSBOND 2 CYS 268 CYS 277 1TRH 127
SITE 1 ACT 3 SER 209 GLU 341 HIS 449 1TRH 128
CRYST1 105.000 106.700 59.800 90.00 94.80 90.00 C 2 4 1TRH 129
ORIGX1 1.000000 0.000000 0.000000 0.00000 1TRH 130
ORIGX2 0.000000 1.000000 0.000000 0.00000 1TRH 131
ORIGX3 0.000000 0.000000 1.000000 0.00000 1TRH 132
SCALE1 0.009524 0.000000 0.000800 0.00000 1TRH 133
SCALE2 0.000000 0.009372 0.000000 0.00000 1TRH 134
SCALE3 0.000000 0.000000 0.016781 0.00000 1TRH 135 |