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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 28-FEB-94 1TCC 1TCC 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1TCC 3
SOURCE YEAST (CANDIDA ANTARCTICA, FORM B) 1TCC 4
AUTHOR J.UPPENBERG,T.A.JONES 1TCC 5
REVDAT 1 31-MAY-94 1TCC 0 1TCC 6
JRNL AUTH J.UPPENBERG,M.T.HANSEN,S.PATKAR,T.A.JONES 1TCC 7
JRNL TITL THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND 1TCC 8
JRNL TITL 2 REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM 1TCC 9
JRNL TITL 3 CANDIDA ANTARCTICA 1TCC 10
JRNL REF STRUCTURE V. 2 293 1994 1TCC 11
JRNL REFN ASTM UK ISSN 0969-2126 2005 1TCC 12
REMARK 1 1TCC 13
REMARK 1 REFERENCE 1 1TCC 14
REMARK 1 AUTH J.UPPENBERG,S.PATKAR,T.BERGFORS,T.A.JONES 1TCC 15
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF 1TCC 16
REMARK 1 TITL 2 LIPASE B FROM CANDIDA ANTARCTICA 1TCC 17
REMARK 1 REF J.MOL.BIOL. V. 235 790 1994 1TCC 18
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1TCC 19
REMARK 2 1TCC 20
REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1TCC 21
REMARK 3 1TCC 22
REMARK 3 REFINEMENT. 1TCC 23
REMARK 3 PROGRAM X-PLOR 1TCC 24
REMARK 3 AUTHORS BRUNGER 1TCC 25
REMARK 3 R VALUE 0.196 1TCC 26
REMARK 3 RMSD BOND DISTANCES 0.006 ANGSTROMS 1TCC 27
REMARK 3 RMSD BOND ANGLES 1.3 DEGREES 1TCC 28
REMARK 3 1TCC 29
REMARK 3 NUMBER OF REFLECTIONS 18925 1TCC 30
REMARK 3 RESOLUTION RANGE 7.5 - 2.5 ANGSTROMS 1TCC 31
REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1TCC 32
REMARK 3 PERCENT COMPLETION 94. 1TCC 33
REMARK 3 1TCC 34
REMARK 3 NUMBER OF PROTEIN ATOMS 4648 1TCC 35
REMARK 3 NUMBER OF SOLVENT ATOMS 159 1TCC 36
REMARK 4 1TCC 37
REMARK 4 THE PUTATIVE CATALYTIC SITES CONSIST OF A SERINE TRIAD AND 1TCC 38
REMARK 4 HAVE THE IDENTIFIERS CTA AND CTB IN THIS FORM. 1TCC 39
REMARK 5 1TCC 40
REMARK 5 THIS ENTRY IS ONE OF THREE ENTRIES ASSOCIATED WITH THE JRNL 1TCC 41
REMARK 5 REFERENCE ABOVE, WHICH DESCRIBES THREE DIFFERENT STRUCTURES 1TCC 42
REMARK 5 IN TWO CRYSTAL FORMS. THE OTHER STRUCTURES CAN BE FOUND IN 1TCC 43
REMARK 5 PROTEIN DATA BANK ENTRIES 1TCA AND 1TCB. 1TCC 44
REMARK 6 1TCC 45
REMARK 6 THIS IS THE HIGH PH STRUCTURE OF THE MONOCLINIC CRYSTAL; 1TCC 46
REMARK 6 FORM WITH TWO MOLECULES IN THE ASYMMETRIC UNIT. THE 1TCC 47
REMARK 6 MOLECULES ARE CALLED A AND B. THE RMS DEVIATIONS ARE 0.23 1TCC 48
REMARK 6 ANGSTROMS FOR C-ALPHAS AND 0.33 ANGSTROMS FOR ALL ATOMS. 1TCC 49
REMARK 7 1TCC 50
REMARK 7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1TCC 51
REMARK 7 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO 1TCC 52
REMARK 7 CHAIN A. 1TCC 53
REMARK 8 1TCC 54
REMARK 8 THERE IS ESSENTIALLY NO ELECTRON DENSITY FOR THE FOLLOWING 1TCC 55
REMARK 8 SIDE CHAIN ATOMS: 1TCC 56
REMARK 8 1TCC 57
REMARK 8 MOLECULE A: 1TCC 58
REMARK 8 1TCC 59
REMARK 8 LYS 32: CD, CE, NZ 1TCC 60
REMARK 8 ARG 242: NE, CZ, NH1, NH2 1TCC 61
REMARK 8 ARG 249: CB, NE, NH2 1TCC 62
REMARK 8 ILE 255: CG1, CD1 1TCC 63
REMARK 8 THR 256: CG2 1TCC 64
REMARK 8 GLU 269: CB, CG, CD, OE1, OE2 1TCC 65
REMARK 8 ARG 309: CB, NE, CZ, NH1, NH2 1TCC 66
REMARK 8 1TCC 67
REMARK 8 MOLECULE B: 1TCC 68
REMARK 8 1TCC 69
REMARK 8 LYS 32: NZ 1TCC 70
REMARK 8 142 - 149: NO CONNECTED DENSITY 1TCC 71
REMARK 8 ARG 242: CB, CG, CD, NE, CZ, NH1, NH2 1TCC 72
REMARK 8 ARG 249: NE, CZ, NH1, NH2 1TCC 73
REMARK 8 ILE 255: CD1, CG2 1TCC 74
REMARK 8 THR 256: CG2 1TCC 75
REMARK 8 GLU 269: N, CB, CG, OE2 1TCC 76
REMARK 8 LYS 290: CE, NZ 1TCC 77
REMARK 8 ARG 309: NE, CZ, NH1, NH2 1TCC 78
REMARK 9 1TCC 79
REMARK 9 THE SEQUENCE HAS NOT BEEN REPORTED. IT WAS DERIVED FROM 1TCC 80
REMARK 9 THE DNA SEQUENCE OF J.UPPENBERG ET AL., 1994, LISTED IN 1TCC 81
REMARK 9 THE JRNL REFERENCE ABOVE. 1TCC 82
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS 1TCC 83
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER 1TCC 84
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY 1TCC 85
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP 1TCC 86
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP 1TCC 87
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL 1TCC 88
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR 1TCC 89
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP 1TCC 90
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE 1TCC 91
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA 1TCC 92
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO 1TCC 93
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN 1TCC 94
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN 1TCC 95
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU 1TCC 96
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER 1TCC 97
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS 1TCC 98
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL 1TCC 99
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR 1TCC 100
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN 1TCC 101
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO 1TCC 102
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA 1TCC 103
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL 1TCC 104
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO 1TCC 105
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER 1TCC 106
SEQRES 25 A 317 GLY ILE VAL THR PRO 1TCC 107
SEQRES 1 B 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS 1TCC 108
SEQRES 2 B 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER 1TCC 109
SEQRES 3 B 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY 1TCC 110
SEQRES 4 B 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP 1TCC 111
SEQRES 5 B 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP 1TCC 112
SEQRES 6 B 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL 1TCC 113
SEQRES 7 B 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR 1TCC 114
SEQRES 8 B 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP 1TCC 115
SEQRES 9 B 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE 1TCC 116
SEQRES 10 B 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA 1TCC 117
SEQRES 11 B 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO 1TCC 118
SEQRES 12 B 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN 1TCC 119
SEQRES 13 B 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN 1TCC 120
SEQRES 14 B 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU 1TCC 121
SEQRES 15 B 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER 1TCC 122
SEQRES 16 B 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS 1TCC 123
SEQRES 17 B 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL 1TCC 124
SEQRES 18 B 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR 1TCC 125
SEQRES 19 B 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN 1TCC 126
SEQRES 20 B 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO 1TCC 127
SEQRES 21 B 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA 1TCC 128
SEQRES 22 B 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL 1TCC 129
SEQRES 23 B 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO 1TCC 130
SEQRES 24 B 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER 1TCC 131
SEQRES 25 B 317 GLY ILE VAL THR PRO 1TCC 132
FTNOTE 1 1TCC 133
FTNOTE 1 CIS PROLINE - PRO A 70 1TCC 134
FTNOTE 2 1TCC 135
FTNOTE 2 CIS PROLINE - PRO A 192 1TCC 136
FTNOTE 3 1TCC 137
FTNOTE 3 CIS PROLINE - PRO B 70 1TCC 138
FTNOTE 4 1TCC 139
FTNOTE 4 CIS PROLINE - PRO B 192 1TCC 140
HET NAG 401 14 N-ACETYL-D-GLUCOSAMINE 1TCC 141
HET NAG 402 14 N-ACETYL-D-GLUCOSAMINE 1TCC 142
HET BOG 501 20 B-OCTYLGLUCOSIDE 1TCC 143
FORMUL 3 NAG 2(C8 H15 N1 O6) 1TCC 144
FORMUL 4 BOG C14 H28 O6 1TCC 145
FORMUL 5 HOH *159(H2 O1) 1TCC 146
HELIX 1 A1 LYS A 13 ALA A 18 1 1TCC 147
HELIX 2 A2 GLY A 44 THR A 57 1 1TCC 148
HELIX 3 A3 THR A 76 GLY A 93 1 1TCC 149
HELIX 4 A4 GLN A 106 PHE A 117 1 1TCC 150
HELIX 5 A5 GLY A 142 ALA A 146 1 1TCC 151
HELIX 6 A6 PRO A 152 GLN A 156 1 1TCC 152
HELIX 7 A7 ALA A 162 ASN A 169 1 1TCC 153
HELIX 8 A8 ALA A 212 CYS A 216 1 1TCC 154
HELIX 9 A9 GLY A 226 ARG A 242 1 1TCC 155
HELIX 10 A10 PRO A 268 ALA A 287 1 1TCC 156
HELIX 11 TH1 PRO A 119 ILE A 121 5 1TCC 157
HELIX 12 TH2 VAL A 139 ALA A 141 5 1TCC 158
HELIX 13 TH3 SER A 250 ASP A 252 5 1TCC 159
HELIX 14 TH4 ILE A 255 ASP A 257 5 1TCC 160
HELIX 15 TH5 ARG A 302 PHE A 304 5 1TCC 161
HELIX 16 AP1 PRO A 68 PRO A 70 10 1TCC 162
HELIX 17 B1 LYS B 13 ALA B 18 1 1TCC 163
HELIX 18 B2 GLY B 44 THR B 57 1 1TCC 164
HELIX 19 B3 THR B 76 GLY B 93 1 1TCC 165
HELIX 20 B4 GLN B 106 PHE B 117 1 1TCC 166
HELIX 21 B5 GLY B 142 ALA B 146 1 1TCC 167
HELIX 22 B6 PRO B 152 GLN B 156 1 1TCC 168
HELIX 23 B7 ALA B 162 ASN B 169 1 1TCC 169
HELIX 24 B8 ALA B 212 CYS B 216 1 1TCC 170
HELIX 25 B9 GLY B 226 ARG B 242 1 1TCC 171
HELIX 26 B10 PRO B 268 ALA B 287 1 1TCC 172
HELIX 27 TB1 PRO B 119 ILE B 121 5 1TCC 173
HELIX 28 TB2 VAL B 139 ALA B 141 5 1TCC 174
HELIX 29 TB3 SER B 250 ASP B 252 5 1TCC 175
HELIX 30 TB4 ILE B 255 ASP B 257 5 1TCC 176
HELIX 31 TB5 ARG B 302 PHE B 304 5 1TCC 177
HELIX 32 BP1 PRO B 68 PRO B 70 10 1TCC 178
SHEET 1 AS1 7 LEU A 20 CYS A 22 0 1TCC 179
SHEET 2 AS1 7 THR A 62 ILE A 66 -1 1TCC 180
SHEET 3 AS1 7 PRO A 33 VAL A 37 1 1TCC 181
SHEET 4 AS1 7 LEU A 99 TRP A 104 1 1TCC 182
SHEET 5 AS1 7 VAL A 125 PHE A 131 1 1TCC 183
SHEET 6 AS1 7 THR A 179 TYR A 183 1 1TCC 184
SHEET 7 AS1 7 LYS A 208 GLN A 211 1 1TCC 185
SHEET 1 AS2 2 ARG A 309 THR A 310 0 1TCC 186
SHEET 2 AS2 2 GLY A 313 ILE A 314 -1 1TCC 187
SHEET 1 BS1 7 LEU B 20 CYS B 22 0 1TCC 188
SHEET 2 BS1 7 THR B 62 ILE B 66 -1 1TCC 189
SHEET 3 BS1 7 PRO B 33 VAL B 37 1 1TCC 190
SHEET 4 BS1 7 LEU B 99 TRP B 104 1 1TCC 191
SHEET 5 BS1 7 VAL B 125 PHE B 131 1 1TCC 192
SHEET 6 BS1 7 THR B 179 TYR B 183 1 1TCC 193
SHEET 7 BS1 7 LYS B 208 GLN B 211 1 1TCC 194
SHEET 1 BS2 2 ARG B 309 THR B 310 0 1TCC 195
SHEET 2 BS2 2 GLY B 313 ILE B 314 -1 1TCC 196
TURN 1 A1 SER A 26 SER A 29 TYPE I 1TCC 197
TURN 2 A2 GLY A 39 THR A 42 TYPE II 1TCC 198
TURN 3 A3 ASP A 134 GLY A 137 TYPE I 1TCC 199
TURN 4 A4 THR A 158 SER A 161 TYPE II 1TCC 200
TURN 5 A5 SER A 184 ASP A 187 TYPE I 1TCC 201
TURN 6 A6 SER A 197 ASP A 200 TYPE III 1TCC 202
TURN 7 A7 LEU A 204 GLY A 207 TYPE II (NO GLY AT I 2) 1TCC 203
TURN 8 A8 GLY A 217 PHE A 220 TYPE I 1TCC 204
TURN 9 A9 ALA A 263 LEU A 266 TYPE I 1TCC 205
TURN 10 A10 THR A 310 GLY A 313 TYPE III 1TCC 206
TURN 11 B1 SER B 26 SER B 29 TYPE I 1TCC 207
TURN 12 B2 GLY B 39 THR B 42 TYPE II 1TCC 208
TURN 13 B3 ASP B 134 GLY B 137 TYPE I 1TCC 209
TURN 14 B4 THR B 158 SER B 161 TYPE II 1TCC 210
TURN 15 B5 SER B 184 ASP B 187 TYPE I 1TCC 211
TURN 16 B6 SER B 197 ASP B 200 TYPE III 1TCC 212
TURN 17 B7 LEU B 204 GLY B 207 TYPE II (NO GLY AT I 2) 1TCC 213
TURN 18 B8 GLY B 217 PHE B 220 TYPE I 1TCC 214
TURN 19 B9 ALA B 263 LEU B 266 TYPE I 1TCC 215
TURN 20 B10 THR B 310 GLY B 313 TYPE III 1TCC 216
SSBOND 1 CYS A 22 CYS A 64 1TCC 217
SSBOND 2 CYS A 216 CYS A 258 1TCC 218
SSBOND 3 CYS A 293 CYS A 311 1TCC 219
SSBOND 4 CYS B 22 CYS B 64 1TCC 220
SSBOND 5 CYS B 216 CYS B 258 1TCC 221
SSBOND 6 CYS B 293 CYS B 311 1TCC 222
SITE 1 CTA 3 SER A 105 ASP A 187 HIS A 224 1TCC 223
SITE 1 CTB 3 SER B 105 ASP B 187 HIS B 224 1TCC 224
CRYST1 67.000 50.500 86.700 90.00 100.10 90.00 P 21 4 1TCC 225
ORIGX1 1.000000 0.000000 0.000000 0.00000 1TCC 226
ORIGX2 0.000000 1.000000 0.000000 0.00000 1TCC 227
ORIGX3 0.000000 0.000000 1.000000 0.00000 1TCC 228
SCALE1 0.014925 0.000000 0.002659 0.00000 1TCC 229
SCALE2 0.000000 0.019802 0.000000 0.00000 1TCC 230
SCALE3 0.000000 0.000000 0.011716 0.00000 1TCC 231
MTRIX1 1 0.281300 0.935400 0.214100 -4.76610 1 1TCC 232
MTRIX2 1 0.938100 -0.315000 0.144100 -0.25750 1 1TCC 233
MTRIX3 1 0.202200 0.160300 -0.966100 28.25220 1 1TCC 234 |