| content |
HEADER HYDROLASE (CARBOXYLIC ESTERASE) 11-JUL-95 1LBS 1LBS 2
TITLE LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1LBS 3
COMPND MOL_ID: 1; 1LBS 4
COMPND 2 MOLECULE: LIPASE B; 1LBS 5
COMPND 3 CHAIN: NULL; 1LBS 6
COMPND 4 SYNONYM: TRIACYLGLYCEROL HYDROLASE; 1LBS 7
COMPND 5 EC: 3.1.1.3; 1LBS 8
COMPND 6 HETEROGEN: PHOSPHONATE INHIBITOR; 1LBS 9
COMPND 7 HETEROGEN: N-ACETYL-D-GLUCOSAMINE 1LBS 10
SOURCE MOL_ID: 1; 1LBS 11
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA; 1LBS 12
SOURCE 3 ORGANISM_COMMON: YEAST 1LBS 13
EXPDTA X-RAY DIFFRACTION 1LBS 14
AUTHOR J.UPPENBERG,T.A.JONES 1LBS 15
REVDAT 1 15-OCT-95 1LBS 0 1LBS 16
JRNL AUTH J.UPPENBERG,N.OEHRNER,M.NORIN,K.HULT,G.J.KLEYWEGT, 1LBS 17
JRNL AUTH 2 S.PATKAR,V.WAAGEN,T.ANTHONSEN,T.A.JONES 1LBS 18
JRNL TITL CRYSTALLOGRAPHIC AND MOLECULAR MODELLING STUDIES OF 1LBS 19
JRNL TITL 2 LIPASE B FROM CANDIDA ANTARCTICA REVEAL A 1LBS 20
JRNL TITL 3 STEREOSPECIFICITY POCKET FOR SECONDARY ALCOHOLS 1LBS 21
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1LBS 22
JRNL REFN 0353 1LBS 23
REMARK 1 1LBS 24
REMARK 1 REFERENCE 1 1LBS 25
REMARK 1 AUTH J.UPPENBERG,S.PATKAR,T.BERGFORS,T.A.JONES 1LBS 26
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF 1LBS 27
REMARK 1 TITL 2 LIPASE B FROM CANDIDA ANTARCTICA 1LBS 28
REMARK 1 REF J.MOL.BIOL. V. 235 790 1994 1LBS 29
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1LBS 30
REMARK 1 REFERENCE 2 1LBS 31
REMARK 1 AUTH J.UPPENBERG,M.T.HANSEN,S.PATKAR,T.A.JONES 1LBS 32
REMARK 1 TITL THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND 1LBS 33
REMARK 1 TITL 2 REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM 1LBS 34
REMARK 1 TITL 3 CANDIDA ANTARCTICA 1LBS 35
REMARK 1 REF STRUCTURE (LONDON) V. 2 293 1994 1LBS 36
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 2005 1LBS 37
REMARK 2 1LBS 38
REMARK 2 RESOLUTION. 2.6 ANGSTROMS. 1LBS 39
REMARK 3 1LBS 40
REMARK 3 REFINEMENT. 1LBS 41
REMARK 3 PROGRAM X-PLOR 3.1 1LBS 42
REMARK 3 AUTHORS BRUNGER 1LBS 43
REMARK 3 R VALUE 0.193 1LBS 44
REMARK 3 FREE R VALUE 0.255 1LBS 45
REMARK 3 MEAN B VALUE 17.6 ANGSTROMS**2 1LBS 46
REMARK 3 RMSD BOND DISTANCES 0.019 ANGSTROMS 1LBS 47
REMARK 3 RMSD BOND ANGLES 2.1 DEGREES 1LBS 48
REMARK 3 RMSD DIHEDRAL ANGLES 25.0 DEGREES 1LBS 49
REMARK 3 RMSD IMPROPER ANGLES 1.9 DEGREES 1LBS 50
REMARK 3 1LBS 51
REMARK 3 NUMBER OF REFLECTIONS 15621 1LBS 52
REMARK 3 RESOLUTION RANGE 7.5 - 2.6 ANGSTROMS 1LBS 53
REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1LBS 54
REMARK 3 COMPLETENESS FOR RANGE 82.5 % 1LBS 55
REMARK 3 1LBS 56
REMARK 3 DATA COLLECTION. 1LBS 57
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 26271 1LBS 58
REMARK 3 RESOLUTION RANGE 50.0 - 2.6 ANGSTROMS 1LBS 59
REMARK 3 COMPLETENESS OF DATA 83. % 1LBS 60
REMARK 3 REJECTION CRITERIA 0.0 SIGMA(I OR F) 1LBS 61
REMARK 3 1LBS 62
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LBS 63
REMARK 3 NUMBER OF PROTEIN ATOMS 2324 1LBS 64
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LBS 65
REMARK 3 NUMBER OF HETEROGEN ATOMS 39 1LBS 66
REMARK 3 NUMBER OF SOLVENT ATOMS 92 1LBS 67
REMARK 4 1LBS 68
REMARK 4 THIS STRUCTURE WAS BUILT USING DATA COLLECTED ON ONE 1LBS 69
REMARK 4 CRYSTAL. THE CRYSTAL SUFFERED FROM MEROHEDRAL TWINNING, 1LBS 70
REMARK 4 WHERE TWO TWIN COMPONENTS CONTRIBUTE TO DIFFERENT DEGREES 1LBS 71
REMARK 4 TO THE DIFFRACTION INTENSITIES. THE DATA SET WAS MODIFIED 1LBS 72
REMARK 4 TO REMOVE THE CONTRIBUTION FROM THE MINOR TWIN COMPONENT, 1LBS 73
REMARK 4 BEFORE THE REFINEMENT. THE MODIFICATION IS CARRIED OUT BY 1LBS 74
REMARK 4 REMOVAL OF SOME REFLECTIONS AND BY INTENSITY CORRECTIONS 1LBS 75
REMARK 4 OF OTHERS. THE DEPOSITED STRUCTURE FACTORS HAVE BEEN 1LBS 76
REMARK 4 MODIFIED. 1LBS 77
REMARK 5 1LBS 78
REMARK 5 SITE 1LBS 79
REMARK 5 SITE_IDENTIFIER: CT 1LBS 80
REMARK 5 CATALYTIC TRIAD. 1LBS 81
REMARK 6 1LBS 82
REMARK 6 MTRIX 1LBS 83
REMARK 6 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW 1LBS 84
REMARK 6 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE 1LBS 85
REMARK 6 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE 1LBS 86
REMARK 6 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL 1LBS 87
REMARK 6 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED 1LBS 88
REMARK 6 SECOND. 1LBS 89
REMARK 6 1LBS 90
REMARK 6 APPLIED TO TRANSFORMED TO 1LBS 91
REMARK 6 MTRIX RESIDUES RESIDUES RMSD 1LBS 92
REMARK 6 M1 A 1 .. A 317 ? 1 .. ? 317 1LBS 93
REMARK 6 M2 A 1 .. A 317 ? 1 .. ? 317 1LBS 94
REMARK 6 M3 A 1 .. A 317 ? 1 .. ? 317 1LBS 95
REMARK 6 M4 A 1 .. A 317 ? 1 .. ? 317 1LBS 96
REMARK 6 M5 A 1 .. A 317 ? 1 .. ? 317 1LBS 97
REMARK 18 1LBS 98
REMARK 18 EXPERIMENTAL DETAILS. 1LBS 99
REMARK 18 DATE OF DATA COLLECTION : 20-MAY-91 1LBS 100
REMARK 18 MONOCHROMATIC (Y/N) : Y 1LBS 101
REMARK 18 LAUE (Y/N) : N 1LBS 102
REMARK 18 WAVELENGTH OR RANGE (A) : 1.54 1LBS 103
REMARK 18 DETECTOR TYPE : MARK III 1LBS 104
REMARK 18 DETECTOR MANUFACTURER : SAN DIEGO MULTIWIRE 1LBS 105
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : MADNES 1LBS 106
REMARK 18 DATA REDUNDANCY : 2.1 1LBS 107
REMARK 18 MERGING R VALUE (INTENSITY) : 0.050 1LBS 108
REMARK 19 1LBS 109
REMARK 19 SOLVENT CONTENT (VS) : 49. % 1LBS 110
REMARK 999 1LBS 111
REMARK 999 SEQUENCE DATABASE 1LBS 112
REMARK 999 GENE BANK: CALIPASB 1LBS 113
SEQRES 1 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS 1LBS 114
SEQRES 2 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER 1LBS 115
SEQRES 3 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY 1LBS 116
SEQRES 4 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP 1LBS 117
SEQRES 5 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP 1LBS 118
SEQRES 6 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL 1LBS 119
SEQRES 7 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR 1LBS 120
SEQRES 8 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP 1LBS 121
SEQRES 9 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE 1LBS 122
SEQRES 10 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA 1LBS 123
SEQRES 11 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO 1LBS 124
SEQRES 12 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN 1LBS 125
SEQRES 13 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN 1LBS 126
SEQRES 14 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU 1LBS 127
SEQRES 15 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER 1LBS 128
SEQRES 16 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS 1LBS 129
SEQRES 17 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL 1LBS 130
SEQRES 18 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR 1LBS 131
SEQRES 19 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN 1LBS 132
SEQRES 20 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO 1LBS 133
SEQRES 21 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA 1LBS 134
SEQRES 22 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL 1LBS 135
SEQRES 23 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO 1LBS 136
SEQRES 24 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER 1LBS 137
SEQRES 25 317 GLY ILE VAL THR PRO 1LBS 138
FTNOTE 1 1LBS 139
FTNOTE 1 CIS PROLINE - PRO 70 1LBS 140
FTNOTE 2 1LBS 141
FTNOTE 2 CIS PROLINE - PRO 192 1LBS 142
HET NAG 401 14 N-ACETYL-D-GLUCOSAMINE 1LBS 143
HET NAG 402 14 N-ACETYL-D-GLUCOSAMINE 1LBS 144
HET HEE 900 11 N-HEXYLPHOSPHONATE ETHYL ESTER 1LBS 145
FORMUL 2 NAG 2(C8 H15 N1 O6) 1LBS 146
FORMUL 3 HEE C8 H18 O2 P1 1LBS 147
FORMUL 4 HOH *92(H2 O1) 1LBS 148
HELIX 1 A1 LYS 13 ALA 18 1 1LBS 149
HELIX 2 A2 GLY 44 THR 57 1 1LBS 150
HELIX 3 A3 THR 76 GLY 93 1 1LBS 151
HELIX 4 A4 GLN 106 PHE 117 1 1LBS 152
HELIX 5 A5 GLY 142 ALA 146 1 1LBS 153
HELIX 6 A6 PRO 152 GLN 156 1 1LBS 154
HELIX 7 A7 ALA 162 ASN 169 1 1LBS 155
HELIX 8 A8 ALA 212 CYS 216 1 1LBS 156
HELIX 9 A9 GLY 226 ARG 242 1 1LBS 157
HELIX 10 A10 PRO 268 ALA 287 1 1LBS 158
HELIX 11 TH1 PRO 119 ILE 121 5 1LBS 159
HELIX 12 TH2 VAL 139 ALA 141 5 1LBS 160
HELIX 13 TH3 SER 250 ASP 252 5 1LBS 161
HELIX 14 TH4 ILE 255 ASP 257 5 1LBS 162
HELIX 15 TH5 ARG 302 PHE 304 5 1LBS 163
HELIX 16 P1 PRO 68 PRO 70 10 1LBS 164
SHEET 1 S1 7 LEU 20 CYS 22 0 1LBS 165
SHEET 2 S1 7 THR 62 ILE 66 -1 1LBS 166
SHEET 3 S1 7 PRO 33 VAL 37 1 1LBS 167
SHEET 4 S1 7 LEU 99 TRP 104 1 1LBS 168
SHEET 5 S1 7 VAL 125 PHE 131 1 1LBS 169
SHEET 6 S1 7 THR 179 TYR 183 1 1LBS 170
SHEET 7 S1 7 LYS 208 GLN 211 1 1LBS 171
SHEET 1 S2 2 ARG 309 THR 310 0 1LBS 172
SHEET 2 S2 2 GLY 313 ILE 314 -1 1LBS 173
TURN 1 T1 SER 26 SER 29 TYPE I 1LBS 174
TURN 2 T2 GLY 39 THR 42 TYPE II 1LBS 175
TURN 3 T3 ASP 134 GLY 137 TYPE I 1LBS 176
TURN 4 T4 THR 158 SER 161 TYPE II 1LBS 177
TURN 5 T5 SER 184 ASP 187 TYPE I 1LBS 178
TURN 6 T6 SER 197 ASP 200 TYPE III 1LBS 179
TURN 7 T7 LEU 204 GLY 207 TYPE II (NO GLY AT I 2) 1LBS 180
TURN 8 T8 GLY 217 PHE 220 TYPE I 1LBS 181
TURN 9 T9 ALA 263 LEU 266 TYPE I 1LBS 182
TURN 10 T10 THR 310 GLY 313 TYPE III 1LBS 183
SSBOND 1 CYS 22 CYS 64 1LBS 184
SSBOND 2 CYS 216 CYS 258 1LBS 185
SSBOND 3 CYS 293 CYS 311 1LBS 186
SITE 1 CT 3 SER 105 ASP 187 HIS 224 1LBS 187
CRYST1 229.500 95.600 86.800 90.00 90.00 90.00 C 2 24 1LBS 188
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LBS 189
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LBS 190
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LBS 191
SCALE1 0.004357 0.000000 0.000000 0.00000 1LBS 192
SCALE2 0.000000 0.010460 0.000000 0.00000 1LBS 193
SCALE3 0.000000 0.000000 0.011521 0.00000 1LBS 194
MTRIX1 1 0.999350 -0.035999 0.002023 -0.13630 1LBS 195
MTRIX2 1 -0.035984 -0.999330 -0.006758 1.70310 1LBS 196
MTRIX3 1 0.002265 0.006681 -0.999975 43.23990 1LBS 197
MTRIX1 2 -1.000000 0.000001 0.000002 152.99930 1LBS 198
MTRIX2 2 0.000001 1.000000 0.000002 0.00040 1LBS 199
MTRIX3 2 -0.000002 0.000002 -1.000000 57.86440 1LBS 200
MTRIX1 3 -0.999350 0.035991 -0.002025 153.13699 1LBS 201
MTRIX2 3 -0.035977 -0.999330 -0.006761 1.70200 1LBS 202
MTRIX3 3 -0.002267 -0.006684 0.999975 14.62500 1LBS 203
MTRIX1 4 -0.999350 0.035998 -0.002024 76.63690 1LBS 204
MTRIX2 4 -0.035983 -0.999330 -0.006760 1.70320 1LBS 205
MTRIX3 4 -0.002266 -0.006683 0.999975 -14.30800 1LBS 206
MTRIX1 5 -1.000000 -0.000001 0.000002 76.50030 1LBS 207
MTRIX2 5 -0.000001 1.000000 0.000001 0.00000 1LBS 208
MTRIX3 5 -0.000002 0.000001 -1.000000 28.93180 1LBS 209 |