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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 28-JUL-92 1THG 1THG 2
COMPND LIPASE (E.C.3.1.1.3) TRIACYLGLYCEROL HYDROLASE 1THG 3
SOURCE FUNGUS (GEOTRICHUM CANDIDUM, STRAIN ATCC 34614) 1THG 4
AUTHOR J.D.SCHRAG,M.CYGLER 1THG 5
REVDAT 1 31-OCT-93 1THG 0 1THG 6
JRNL AUTH J.D.SCHRAG,M.CYGLER 1THG 7
JRNL TITL 1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE 1THG 8
JRNL TITL 2 FROM GEOTRICHUM CANDIDUM 1THG 9
JRNL REF J.MOL.BIOL. V. 230 575 1993 1THG 10
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1THG 11
REMARK 1 1THG 12
REMARK 1 REFERENCE 1 1THG 13
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1THG 14
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1THG 15
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1THG 16
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1THG 17
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1THG 18
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1THG 19
REMARK 1 REFERENCE 2 1THG 20
REMARK 1 AUTH J.D.SCHRAG,F.K.WINKLER,M.CYGLER 1THG 21
REMARK 1 TITL PANCREATIC LIPASES: EVOLUTIONARY INTERMEDIATES 1THG 22
REMARK 1 TITL 2 IN A POSITIONAL CHANGE OF CATALYTIC CARBOXYLATES? 1THG 23
REMARK 1 REF J.BIOL.CHEM. V. 267 4300 1992 1THG 24
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1THG 25
REMARK 1 REFERENCE 3 1THG 26
REMARK 1 AUTH J.D.SCHRAG,Y.LI,S.WU,M.CYGLER 1THG 27
REMARK 1 TITL SER-HIS-GLU TRIAD FORMS THE CATALYTIC SITE OF THE 1THG 28
REMARK 1 TITL 2 LIPASE FROM GEOTRICHUM CANDIDUM 1THG 29
REMARK 1 REF NATURE V. 351 761 1991 1THG 30
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1THG 31
REMARK 1 REFERENCE 4 1THG 32
REMARK 1 AUTH J.D.SCHRAG,Y.LI,S.WU,M.CYGLER 1THG 33
REMARK 1 TITL MULTIPLE CRYSTAL FORMS OF LIPASES FROM GEOTRICHUM 1THG 34
REMARK 1 TITL 2 CANDIDUM 1THG 35
REMARK 1 REF J.MOL.BIOL. V. 220 541 1991 1THG 36
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1THG 37
REMARK 1 REFERENCE 5 1THG 38
REMARK 1 AUTH F.K.WINKLER,A.D'ARCY,W.HUNZIKER 1THG 39
REMARK 1 TITL STRUCTURE OF HUMAN PANCREATIC LIPASE 1THG 40
REMARK 1 REF NATURE V. 343 771 1990 1THG 41
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1THG 42
REMARK 2 1THG 43
REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1THG 44
REMARK 3 1THG 45
REMARK 3 REFINEMENT. 1THG 46
REMARK 3 PROGRAM X-PLOR 1THG 47
REMARK 3 AUTHORS BRUNGER 1THG 48
REMARK 3 R VALUE 0.157 1THG 49
REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1THG 50
REMARK 3 RMSD BOND ANGLES 2.40 DEGREES 1THG 51
REMARK 4 1THG 52
REMARK 4 THERE ARE FOUR N-ACETYLGLUCOSAMINE RESIDUES AT THREE SITES 1THG 53
REMARK 4 INCLUDED IN THIS ENTRY: 1THG 54
REMARK 4 2 N-LINKED RESIDUES AT ASN 364 1THG 55
REMARK 4 1 N-LINKED RESIDUE AT ASN 283 1THG 56
REMARK 4 1 O-LINKED RESIDUE AT THR 4 1THG 57
REMARK 5 1THG 58
REMARK 5 HELICES FL1 AND FL2 FORM A FLAP COVERING THE ACTIVE SITE. 1THG 59
REMARK 5 THE FLAP COMPRISES RESIDUES 61 - 105. 1THG 60
REMARK 6 1THG 61
REMARK 6 RESIDUE 1 IS PYROGLUTAMATE. 1THG 62
REMARK 7 1THG 63
REMARK 7 SITE *ACT*, PRESENTED ON *SITE* RECORDS BELOW, IS THE 1THG 64
REMARK 7 ACTIVE SITE. 1THG 65
SEQRES 1 544 PCA ALA PRO THR ALA VAL LEU ASN GLY ASN GLU VAL ILE 1THG 66
SEQRES 2 544 SER GLY VAL LEU GLU GLY LYS VAL ASP THR PHE LYS GLY 1THG 67
SEQRES 3 544 ILE PRO PHE ALA ASP PRO PRO LEU ASN ASP LEU ARG PHE 1THG 68
SEQRES 4 544 LYS HIS PRO GLN PRO PHE THR GLY SER TYR GLN GLY LEU 1THG 69
SEQRES 5 544 LYS ALA ASN ASP PHE SER PRO ALA CYS MET GLN LEU ASP 1THG 70
SEQRES 6 544 PRO GLY ASN SER LEU THR LEU LEU ASP LYS ALA LEU GLY 1THG 71
SEQRES 7 544 LEU ALA LYS VAL ILE PRO GLU GLU PHE ARG GLY PRO LEU 1THG 72
SEQRES 8 544 TYR ASP MET ALA LYS GLY THR VAL SER MET ASN GLU ASP 1THG 73
SEQRES 9 544 CYS LEU TYR LEU ASN VAL PHE ARG PRO ALA GLY THR LYS 1THG 74
SEQRES 10 544 PRO ASP ALA LYS LEU PRO VAL MET VAL TRP ILE TYR GLY 1THG 75
SEQRES 11 544 GLY ALA PHE VAL TYR GLY SER SER ALA ALA TYR PRO GLY 1THG 76
SEQRES 12 544 ASN SER TYR VAL LYS GLU SER ILE ASN MET GLY GLN PRO 1THG 77
SEQRES 13 544 VAL VAL PHE VAL SER ILE ASN TYR ARG THR GLY PRO PHE 1THG 78
SEQRES 14 544 GLY PHE LEU GLY GLY ASP ALA ILE THR ALA GLU GLY ASN 1THG 79
SEQRES 15 544 THR ASN ALA GLY LEU HIS ASP GLN ARG LYS GLY LEU GLU 1THG 80
SEQRES 16 544 TRP VAL SER ASP ASN ILE ALA ASN PHE GLY GLY ASP PRO 1THG 81
SEQRES 17 544 ASP LYS VAL MET ILE PHE GLY GLU SER ALA GLY ALA MET 1THG 82
SEQRES 18 544 SER VAL ALA HIS GLN LEU ILE ALA TYR GLY GLY ASP ASN 1THG 83
SEQRES 19 544 THR TYR ASN GLY LYS LYS LEU PHE HIS SER ALA ILE LEU 1THG 84
SEQRES 20 544 GLN SER GLY GLY PRO LEU PRO TYR HIS ASP SER SER SER 1THG 85
SEQRES 21 544 VAL GLY PRO ASP ILE SER TYR ASN ARG PHE ALA GLN TYR 1THG 86
SEQRES 22 544 ALA GLY CYS ASP THR SER ALA SER ALA ASN ASP THR LEU 1THG 87
SEQRES 23 544 GLU CYS LEU ARG SER LYS SER SER SER VAL LEU HIS ASP 1THG 88
SEQRES 24 544 ALA GLN ASN SER TYR ASP LEU LYS ASP LEU PHE GLY LEU 1THG 89
SEQRES 25 544 LEU PRO GLN PHE LEU GLY PHE GLY PRO ARG PRO ASP GLY 1THG 90
SEQRES 26 544 ASN ILE ILE PRO ASP ALA ALA TYR GLU LEU PHE ARG SER 1THG 91
SEQRES 27 544 GLY ARG TYR ALA LYS VAL PRO TYR ILE SER GLY ASN GLN 1THG 92
SEQRES 28 544 GLU ASP GLU GLY THR ALA PHE ALA PRO VAL ALA LEU ASN 1THG 93
SEQRES 29 544 ALA THR THR THR PRO HIS VAL LYS LYS TRP LEU GLN TYR 1THG 94
SEQRES 30 544 ILE PHE TYR ASP ALA SER GLU ALA SER ILE ASP ARG VAL 1THG 95
SEQRES 31 544 LEU SER LEU TYR PRO GLN THR LEU SER VAL GLY SER PRO 1THG 96
SEQRES 32 544 PHE ARG THR GLY ILE LEU ASN ALA LEU THR PRO GLN PHE 1THG 97
SEQRES 33 544 LYS ARG VAL ALA ALA ILE LEU SER ASP MET LEU PHE GLN 1THG 98
SEQRES 34 544 SER PRO ARG ARG VAL MET LEU SER ALA THR LYS ASP VAL 1THG 99
SEQRES 35 544 ASN ARG TRP THR TYR LEU SER THR HIS LEU HIS ASN LEU 1THG 100
SEQRES 36 544 VAL PRO PHE LEU GLY THR PHE HIS GLY ASN GLU LEU ILE 1THG 101
SEQRES 37 544 PHE GLN PHE ASN VAL ASN ILE GLY PRO ALA ASN SER TYR 1THG 102
SEQRES 38 544 LEU ARG TYR PHE ILE SER PHE ALA ASN HIS HIS ASP PRO 1THG 103
SEQRES 39 544 ASN VAL GLY THR ASN LEU LEU GLN TRP ASP GLN TYR THR 1THG 104
SEQRES 40 544 ASP GLU GLY LYS GLU MET LEU GLU ILE HIS MET THR ASP 1THG 105
SEQRES 41 544 ASN VAL MET ARG THR ASP ASP TYR ARG ILE GLU GLY ILE 1THG 106
SEQRES 42 544 SER ASN PHE GLU THR ASP VAL ASN LEU TYR GLY 1THG 107
FTNOTE 1 1THG 108
FTNOTE 1 RESIDUE 403 IS A CIS PROLINE. 1THG 109
HET NAG 990 14 N-ACETYL-D-GLUCOSAMINE 1THG 110
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1THG 111
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1THG 112
HET NAG 996 14 N-ACETYL-D-GLUCOSAMINE 1THG 113
FORMUL 2 NAG 4(C8 H15 N1 O6) 1THG 114
FORMUL 3 HOH *343(H2 O1) 1THG 115
HELIX 1 FL1 PRO 66 LEU 77 1 COVERS ACTIVE SITE 1THG 116
HELIX 2 FL2 GLU 85 ALA 95 1 PRO AT 90 1THG 117
HELIX 3 HFA ASN 144 ASN 152 1 1THG 118
HELIX 4 B3A ASP 175 GLU 180 1 1THG 119
HELIX 5 HFB ALA 185 ASN 200 1 1THG 120
HELIX 6 HFC ALA 218 LEU 227 1 1THG 121
HELIX 7 B6A SER 266 ALA 274 1 1THG 122
HELIX 8 B6B ALA 282 SER 291 1 1THG 123
HELIX 9 B6C SER 294 ASP 308 1 COVERS ACTIVE SITE 1THG 124
HELIX 10 HFD ALA 332 ARG 337 1 1THG 125
HELIX 11 B7A THR 356 PRO 360 1 1THG 126
HELIX 12 B7B THR 368 ILE 378 1 1THG 127
HELIX 13 B7C GLU 384 LEU 393 1 1THG 128
HELIX 14 HFE PHE 416 ALA 438 1 BEND AT 428, PRO AT 431 1THG 129
HELIX 15 B8A LEU 467 PHE 471 1 1THG 130
HELIX 16 HFF ALA 478 HIS 491 1 DISTORTION AT 481 1THG 131
HELIX 17 BCT ILE 530 THR 538 1 1THG 132
SHEET 1 BEN 3 THR 4 LEU 7 0 1THG 133
SHEET 2 BEN 3 GLU 11 SER 14 -1 O ILE 13 N ALA 5 1THG 134
SHEET 3 BEN 3 GLY 51 ALA 54 1 N ALA 54 O SER 14 1THG 135
SHEET 1 BEC11 VAL 16 GLU 18 0 1THG 136
SHEET 2 BEC11 VAL 21 PRO 28 -1 N VAL 21 O GLU 18 1THG 137
SHEET 3 BEC11 TYR 107 PRO 113 -1 O ARG 112 N ASP 22 1THG 138
SHEET 4 BEC11 VAL 158 ILE 162 -1 N PHE 159 O PHE 111 1THG 139
SHEET 5 BEC11 PRO 123 ILE 128 1 O PRO 123 N VAL 158 1THG 140
SHEET 6 BEC11 LYS 210 GLU 216 1 O LYS 210 N VAL 124 1THG 141
SHEET 7 BEC11 SER 244 GLN 248 1 N SER 244 O VAL 211 1THG 142
SHEET 8 BEC11 PRO 345 GLN 351 1 O PRO 345 N ALA 245 1THG 143
SHEET 9 BEC11 ASN 443 SER 449 1 O ASN 443 N TYR 346 1THG 144
SHEET 10 BEC11 MET 513 ILE 516 1 O LEU 514 N LEU 448 1THG 145
SHEET 11 BEC11 ASN 521 THR 525 -1 O ARG 524 N MET 513 1THG 146
TURN 1 HRT PHE 462 ASN 465 TYPE II 1THG 147
TURN 2 NRT ASN 35 ARG 38 TYPE I 1THG 148
TURN 3 SRT SER 137 ALA 140 TYPE III 1THG 149
TURN 4 GRT ALA 362 ALA 365 TYPE I 1THG 150
TURN 5 ART ASP 353 THR 356 TYPE I 1THG 151
SSBOND 1 CYS 61 CYS 105 1THG 152
SSBOND 2 CYS 276 CYS 288 1THG 153
SITE 1 ACT 3 SER 217 GLU 354 HIS 463 1THG 154
CRYST1 59.400 84.000 56.000 90.00 100.10 90.00 P 21 2 1THG 155
ORIGX1 1.000000 0.000000 0.000000 0.00000 1THG 156
ORIGX2 0.000000 1.000000 0.000000 0.00000 1THG 157
ORIGX3 0.000000 0.000000 1.000000 0.00000 1THG 158
SCALE1 0.016835 0.000000 0.002999 0.00000 1THG 159
SCALE2 0.000000 0.011905 0.000000 0.00000 1THG 160
SCALE3 0.000000 0.000000 0.018138 0.00000 1THG 161 |