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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 28-FEB-94 1TCB 1TCB 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1TCB 3
SOURCE YEAST (CANDIDA ANTARCTICA, FORM B) 1TCB 4
AUTHOR J.UPPENBERG,T.A.JONES 1TCB 5
REVDAT 1 31-MAY-94 1TCB 0 1TCB 6
JRNL AUTH J.UPPENBERG,M.T.HANSEN,S.PATKAR,T.A.JONES 1TCB 7
JRNL TITL THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND 1TCB 8
JRNL TITL 2 REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM 1TCB 9
JRNL TITL 3 CANDIDA ANTARCTICA 1TCB 10
JRNL REF STRUCTURE V. 2 293 1994 1TCB 11
JRNL REFN ASTM UK ISSN 0969-2126 2005 1TCB 12
REMARK 1 1TCB 13
REMARK 1 REFERENCE 1 1TCB 14
REMARK 1 AUTH J.UPPENBERG,S.PATKAR,T.BERGFORS,T.A.JONES 1TCB 15
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF 1TCB 16
REMARK 1 TITL 2 LIPASE B FROM CANDIDA ANTARCTICA 1TCB 17
REMARK 1 REF J.MOL.BIOL. V. 235 790 1994 1TCB 18
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1TCB 19
REMARK 2 1TCB 20
REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1TCB 21
REMARK 3 1TCB 22
REMARK 3 REFINEMENT. 1TCB 23
REMARK 3 PROGRAM X-PLOR 1TCB 24
REMARK 3 AUTHORS BRUNGER 1TCB 25
REMARK 3 R VALUE 0.187 1TCB 26
REMARK 3 RMSD BOND DISTANCES 0.006 ANGSTROMS 1TCB 27
REMARK 3 RMSD BOND ANGLES 0.9 DEGREES 1TCB 28
REMARK 3 1TCB 29
REMARK 3 NUMBER OF REFLECTIONS 31323 1TCB 30
REMARK 3 RESOLUTION RANGE 7.5 - 2.1 ANGSTROMS 1TCB 31
REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1TCB 32
REMARK 3 PERCENT COMPLETION 86. 1TCB 33
REMARK 3 1TCB 34
REMARK 3 NUMBER OF PROTEIN ATOMS 4648 1TCB 35
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1TCB 36
REMARK 3 NUMBER OF SOLVENT ATOMS 470 1TCB 37
REMARK 4 1TCB 38
REMARK 4 THE PUTATIVE CATALYTIC SITES CONSIST OF A SERINE TRIAD AND 1TCB 39
REMARK 4 HAVE THE SITE IDENTIFIERS CTA AND CTB IN THIS FORM. 1TCB 40
REMARK 5 1TCB 41
REMARK 5 THIS ENTRY IS ONE OF THREE ENTRIES ASSOCIATED WITH THE JRNL 1TCB 42
REMARK 5 REFERENCE ABOVE, WHICH DESCRIBES THREE DIFFERENT STRUCTURES 1TCB 43
REMARK 5 IN TWO CRYSTAL FORMS. THE OTHER STRUCTURES CAN BE FOUND IN 1TCB 44
REMARK 5 PROTEIN DATA BANK ENTRIES 1TCA AND 1TCC. 1TCB 45
REMARK 6 1TCB 46
REMARK 6 THIS IS THE LOW PH STRUCTURE OF THE MONOCLINIC CRYSTAL; 1TCB 47
REMARK 6 FORM WITH TWO MOLECULES IN THE ASYMMETRIC UNIT. THE 1TCB 48
REMARK 6 MOLECULES ARE CALLED A AND B. THE RMS DEVIATIONS ARE 0.18 1TCB 49
REMARK 6 ANGSTROMS FOR C-ALPHAS AND 0.31 ANGSTROMS FOR ALL ATOMS. 1TCB 50
REMARK 7 1TCB 51
REMARK 7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1TCB 52
REMARK 7 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO 1TCB 53
REMARK 7 CHAIN A. 1TCB 54
REMARK 8 1TCB 55
REMARK 8 THERE IS ESSENTIALLY NO ELECTRON DENSITY FOR THE FOLLOWING 1TCB 56
REMARK 8 SIDE CHAIN ATOMS: 1TCB 57
REMARK 8 1TCB 58
REMARK 8 MOLECULE A: 1TCB 59
REMARK 8 1TCB 60
REMARK 8 LYS 32: CG, CD, CE, NZ 1TCB 61
REMARK 8 ARG 242: NE, CZ, NH1, NH2 1TCB 62
REMARK 8 ILE 255: CD1 1TCB 63
REMARK 8 GLU 269: CG, CD, OE1, OE2 1TCB 64
REMARK 8 ARG 309: NH1 1TCB 65
REMARK 8 1TCB 66
REMARK 8 MOLECULE B: 1TCB 67
REMARK 8 1TCB 68
REMARK 8 LYS 32: NZ 1TCB 69
REMARK 8 GLU 269: CB, CG, CD, OE1, OE2 1TCB 70
REMARK 8 LYS 290: CA, CB, CG, CD, CE, NZ 1TCB 71
REMARK 8 ARG 309: NE, CZ, NH1, NH2 1TCB 72
REMARK 9 1TCB 73
REMARK 9 THE SEQUENCE HAS NOT BEEN REPORTED. IT WAS DERIVED FROM 1TCB 74
REMARK 9 THE DNA SEQUENCE OF J.UPPENBERG ET AL., 1994, LISTED IN 1TCB 75
REMARK 9 THE JRNL REFERENCE ABOVE. 1TCB 76
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS 1TCB 77
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER 1TCB 78
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY 1TCB 79
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP 1TCB 80
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP 1TCB 81
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL 1TCB 82
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR 1TCB 83
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP 1TCB 84
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE 1TCB 85
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA 1TCB 86
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO 1TCB 87
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN 1TCB 88
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN 1TCB 89
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU 1TCB 90
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER 1TCB 91
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS 1TCB 92
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL 1TCB 93
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR 1TCB 94
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN 1TCB 95
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO 1TCB 96
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA 1TCB 97
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL 1TCB 98
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO 1TCB 99
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER 1TCB 100
SEQRES 25 A 317 GLY ILE VAL THR PRO 1TCB 101
SEQRES 1 B 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS 1TCB 102
SEQRES 2 B 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER 1TCB 103
SEQRES 3 B 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY 1TCB 104
SEQRES 4 B 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP 1TCB 105
SEQRES 5 B 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP 1TCB 106
SEQRES 6 B 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL 1TCB 107
SEQRES 7 B 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR 1TCB 108
SEQRES 8 B 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP 1TCB 109
SEQRES 9 B 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE 1TCB 110
SEQRES 10 B 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA 1TCB 111
SEQRES 11 B 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO 1TCB 112
SEQRES 12 B 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN 1TCB 113
SEQRES 13 B 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN 1TCB 114
SEQRES 14 B 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU 1TCB 115
SEQRES 15 B 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER 1TCB 116
SEQRES 16 B 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS 1TCB 117
SEQRES 17 B 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL 1TCB 118
SEQRES 18 B 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR 1TCB 119
SEQRES 19 B 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN 1TCB 120
SEQRES 20 B 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO 1TCB 121
SEQRES 21 B 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA 1TCB 122
SEQRES 22 B 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL 1TCB 123
SEQRES 23 B 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO 1TCB 124
SEQRES 24 B 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER 1TCB 125
SEQRES 25 B 317 GLY ILE VAL THR PRO 1TCB 126
FTNOTE 1 1TCB 127
FTNOTE 1 CIS PROLINE - PRO A 70 1TCB 128
FTNOTE 2 1TCB 129
FTNOTE 2 CIS PROLINE - PRO A 192 1TCB 130
FTNOTE 3 1TCB 131
FTNOTE 3 CIS PROLINE - PRO B 70 1TCB 132
FTNOTE 4 1TCB 133
FTNOTE 4 CIS PROLINE - PRO B 192 1TCB 134
HET NAG 401 14 N-ACETYL-D-GLUCOSAMINE 1TCB 135
HET NAG 402 14 N-ACETYL-D-GLUCOSAMINE 1TCB 136
HET BOG 501 20 B-OCTYLGLUCOSIDE 1TCB 137
HET BOG 502 20 B-OCTYLGLUCOSIDE 1TCB 138
FORMUL 3 NAG 2(C8 H15 N1 O6) 1TCB 139
FORMUL 4 BOG 2(C14 H28 O6) 1TCB 140
FORMUL 5 HOH *470(H2 O1) 1TCB 141
HELIX 1 A1 LYS A 13 ALA A 18 1 1TCB 142
HELIX 2 A2 GLY A 44 THR A 57 1 1TCB 143
HELIX 3 A3 THR A 76 GLY A 93 1 1TCB 144
HELIX 4 A4 GLN A 106 PHE A 117 1 1TCB 145
HELIX 5 A5 GLY A 142 ALA A 146 1 1TCB 146
HELIX 6 A6 PRO A 152 GLN A 156 1 1TCB 147
HELIX 7 A7 ALA A 162 ASN A 169 1 1TCB 148
HELIX 8 A8 ALA A 212 CYS A 216 1 1TCB 149
HELIX 9 A9 GLY A 226 ARG A 242 1 1TCB 150
HELIX 10 A10 PRO A 268 ALA A 287 1 1TCB 151
HELIX 11 TH1 PRO A 119 ILE A 121 5 1TCB 152
HELIX 12 TH2 VAL A 139 ALA A 141 5 1TCB 153
HELIX 13 TH3 SER A 250 ASP A 252 5 1TCB 154
HELIX 14 TH4 ILE A 255 ASP A 257 5 1TCB 155
HELIX 15 TH5 ARG A 302 PHE A 304 5 1TCB 156
HELIX 16 AP1 PRO A 68 PRO A 70 10 1TCB 157
HELIX 17 B1 LYS B 13 ALA B 18 1 1TCB 158
HELIX 18 B2 GLY B 44 THR B 57 1 1TCB 159
HELIX 19 B3 THR B 76 GLY B 93 1 1TCB 160
HELIX 20 B4 GLN B 106 PHE B 117 1 1TCB 161
HELIX 21 B5 GLY B 142 ALA B 146 1 1TCB 162
HELIX 22 B6 PRO B 152 GLN B 156 1 1TCB 163
HELIX 23 B7 ALA B 162 ASN B 169 1 1TCB 164
HELIX 24 B8 ALA B 212 CYS B 216 1 1TCB 165
HELIX 25 B9 GLY B 226 ARG B 242 1 1TCB 166
HELIX 26 B10 PRO B 268 ALA B 287 1 1TCB 167
HELIX 27 TB1 PRO B 119 ILE B 121 5 1TCB 168
HELIX 28 TB2 VAL B 139 ALA B 141 5 1TCB 169
HELIX 29 TB3 SER B 250 ASP B 252 5 1TCB 170
HELIX 30 TB4 ILE B 255 ASP B 257 5 1TCB 171
HELIX 31 TB5 ARG B 302 PHE B 304 5 1TCB 172
HELIX 32 BP1 PRO B 68 PRO B 70 10 1TCB 173
SHEET 1 AS1 7 LEU A 20 CYS A 22 0 1TCB 174
SHEET 2 AS1 7 THR A 62 ILE A 66 -1 1TCB 175
SHEET 3 AS1 7 PRO A 33 VAL A 37 1 1TCB 176
SHEET 4 AS1 7 LEU A 99 TRP A 104 1 1TCB 177
SHEET 5 AS1 7 VAL A 125 PHE A 131 1 1TCB 178
SHEET 6 AS1 7 THR A 179 TYR A 183 1 1TCB 179
SHEET 7 AS1 7 LYS A 208 GLN A 211 1 1TCB 180
SHEET 1 AS2 2 ARG A 309 THR A 310 0 1TCB 181
SHEET 2 AS2 2 GLY A 313 ILE A 314 -1 1TCB 182
SHEET 1 BS1 7 LEU B 20 CYS B 22 0 1TCB 183
SHEET 2 BS1 7 THR B 62 ILE B 66 -1 1TCB 184
SHEET 3 BS1 7 PRO B 33 VAL B 37 1 1TCB 185
SHEET 4 BS1 7 LEU B 99 TRP B 104 1 1TCB 186
SHEET 5 BS1 7 VAL B 125 PHE B 131 1 1TCB 187
SHEET 6 BS1 7 THR B 179 TYR B 183 1 1TCB 188
SHEET 7 BS1 7 LYS B 208 GLN B 211 1 1TCB 189
SHEET 1 BS2 2 ARG B 309 THR B 310 0 1TCB 190
SHEET 2 BS2 2 GLY B 313 ILE B 314 -1 1TCB 191
TURN 1 A1 SER A 26 SER A 29 TYPE I 1TCB 192
TURN 2 A2 GLY A 39 THR A 42 TYPE II 1TCB 193
TURN 3 A3 ASP A 134 GLY A 137 TYPE I 1TCB 194
TURN 4 A4 THR A 158 SER A 161 TYPE II 1TCB 195
TURN 5 A5 SER A 184 ASP A 187 TYPE I 1TCB 196
TURN 6 A6 SER A 197 ASP A 200 TYPE III 1TCB 197
TURN 7 A7 LEU A 204 GLY A 207 TYPE II (NO GLY AT I 2) 1TCB 198
TURN 8 A8 GLY A 217 PHE A 220 TYPE I 1TCB 199
TURN 9 A9 ALA A 263 LEU A 266 TYPE I 1TCB 200
TURN 10 A10 THR A 310 GLY A 313 TYPE III 1TCB 201
TURN 11 B1 SER B 26 SER B 29 TYPE I 1TCB 202
TURN 12 B2 GLY B 39 THR B 42 TYPE II 1TCB 203
TURN 13 B3 ASP B 134 GLY B 137 TYPE I 1TCB 204
TURN 14 B4 THR B 158 SER B 161 TYPE II 1TCB 205
TURN 15 B5 SER B 184 ASP B 187 TYPE I 1TCB 206
TURN 16 B6 SER B 197 ASP B 200 TYPE III 1TCB 207
TURN 17 B7 LEU B 204 GLY B 207 TYPE II (NO GLY AT I 2) 1TCB 208
TURN 18 B8 GLY B 217 PHE B 220 TYPE I 1TCB 209
TURN 19 B9 ALA B 263 LEU B 266 TYPE I 1TCB 210
TURN 20 B10 THR B 310 GLY B 313 TYPE III 1TCB 211
SSBOND 1 CYS A 22 CYS A 64 1TCB 212
SSBOND 2 CYS A 216 CYS A 258 1TCB 213
SSBOND 3 CYS A 293 CYS A 311 1TCB 214
SSBOND 4 CYS B 22 CYS B 64 1TCB 215
SSBOND 5 CYS B 216 CYS B 258 1TCB 216
SSBOND 6 CYS B 293 CYS B 311 1TCB 217
SITE 1 CTA 3 SER A 105 ASP A 187 HIS A 224 1TCB 218
SITE 1 CTB 3 SER B 105 ASP B 187 HIS B 224 1TCB 219
CRYST1 69.200 50.500 86.700 90.00 101.50 90.00 P 21 4 1TCB 220
ORIGX1 1.000000 0.000000 0.000000 0.00000 1TCB 221
ORIGX2 0.000000 1.000000 0.000000 0.00000 1TCB 222
ORIGX3 0.000000 0.000000 1.000000 0.00000 1TCB 223
SCALE1 0.014451 0.000000 0.002940 0.00000 1TCB 224
SCALE2 0.000000 0.019802 0.000000 0.00000 1TCB 225
SCALE3 0.000000 0.000000 0.011770 0.00000 1TCB 226
MTRIX1 1 0.273800 0.936300 0.220100 -4.06350 1 1TCB 227
MTRIX2 1 0.938300 -0.310200 0.152500 -1.01290 1 1TCB 228
MTRIX3 1 0.211100 0.164700 -0.963500 27.24890 1 1TCB 229 |