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HEADER HYDROLASE 13-JAN-95 1LPO 1LPO 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH 1LPO 3
COMPND 2 HEXADECANESULFONATE 1LPO 4
SOURCE YEAST (CANDIDA RUGOSA) (FORMERLY CANDIDA CYLINDRACEA) 1LPO 5
AUTHOR P.G.GROCHULSKI,M.C.CYGLER 1LPO 6
REVDAT 1 20-APR-95 1LPO 0 1LPO 7
JRNL AUTH P.GROCHULSKI,F.BOUTHILLIER,R.J.KAZLAUSKAS, 1LPO 8
JRNL AUTH 2 A.N.SERREGI,J.D.SCHRAG,E.ZIOMEK,M.CYGLER 1LPO 9
JRNL TITL ANALOGS OF REACTION INTERMEDIATES IDENTIFY A 1LPO 10
JRNL TITL 2 UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA 1LPO 11
JRNL TITL 3 LIPASE 1LPO 12
JRNL REF BIOCHEMISTRY V. 33 3494 1994 1LPO 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1LPO 14
REMARK 1 1LPO 15
REMARK 1 REFERENCE 1 1LPO 16
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,M.CYGLER 1LPO 17
REMARK 1 TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE 1LPO 18
REMARK 1 REF PROTEIN SCI. V. 3 82 1994 1LPO 19
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1LPO 20
REMARK 1 REFERENCE 2 1LPO 21
REMARK 1 AUTH M.CYGLER,P.GROCHULSKI,R.J.KAZLAUSKAS,J.D.SCHRAG, 1LPO 22
REMARK 1 AUTH 2 F.BOUTHILLIER,B.RUBIN,A.N.SERREGI,A.K.GUPTA 1LPO 23
REMARK 1 TITL A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF 1LPO 24
REMARK 1 TITL 2 LIPASES 1LPO 25
REMARK 1 REF J.AM.CHEM.SOC. V. 116 3180 1994 1LPO 26
REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863 0004 1LPO 27
REMARK 1 REFERENCE 3 1LPO 28
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1LPO 29
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1LPO 30
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1LPO 31
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1LPO 32
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1LPO 33
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1LPO 34
REMARK 2 1LPO 35
REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1LPO 36
REMARK 3 1LPO 37
REMARK 3 REFINEMENT. 1LPO 38
REMARK 3 PROGRAM X-PLOR 1LPO 39
REMARK 3 AUTHORS BRUNGER 1LPO 40
REMARK 3 R VALUE 0.149 1LPO 41
REMARK 3 MEAN B VALUE 18.3 ANGSTROMS**2 1LPO 42
REMARK 3 NUMBER OF REFLECTIONS 26019 1LPO 43
REMARK 3 RESOLUTION RANGE 8. - 2.18 ANGSTROMS 1LPO 44
REMARK 3 DATA CUTOFF 4. SIGMA(F) 1LPO 45
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1LPO 46
REMARK 3 RMSD BOND ANGLES 1.75 DEGREES 1LPO 47
REMARK 3 1LPO 48
REMARK 3 DATA COLLECTION. 1LPO 49
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 26760 1LPO 50
REMARK 3 COMPLETENESS OF DATA 90.1 % 1LPO 51
REMARK 3 REJECTION CRITERIA 2. SIGMA(I) 1LPO 52
REMARK 3 1LPO 53
REMARK 3 SOLVENT CONTENT (VS) 48. % 1LPO 54
REMARK 3 1LPO 55
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LPO 56
REMARK 3 NUMBER OF PROTEIN ATOMS 4022 1LPO 57
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LPO 58
REMARK 3 NUMBER OF HETEROGEN ATOMS 63 1LPO 59
REMARK 3 NUMBER OF SOLVENT ATOMS 179 1LPO 60
REMARK 4 1LPO 61
REMARK 4 EXPERIMENTAL DETAILS 1LPO 62
REMARK 4 SINGLE CRYSTAL X-RAY DIFFRACTION 1LPO 63
REMARK 4 MONOCHROMATIC RADIATION 1LPO 64
REMARK 4 DATE OF DATA-COLLECTION (DD-MON-YY) : 02-05-93 1LPO 65
REMARK 4 WAVELENGTH OR WAVELENGTH RANGE : CUKA 1LPO 66
REMARK 4 DETECTOR TYPE/MANUFACTURER : RAXIS II 1LPO 67
REMARK 4 INTENSITY-INTEGRATION SOFTWARE : RAXIS SOFTWARE 1LPO 68
REMARK 4 DATA REDUNDANCY : 2.9 1LPO 69
REMARK 5 1LPO 70
REMARK 5 KEYWDS: CARBOXYLIC ESTERASE, CRL 1LPO 71
REMARK 6 1LPO 72
REMARK 6 SOURCE 1LPO 73
REMARK 6 INHIBITED BY HEXADECANESULFONYL CHLORIDE (1:4). 1LPO 74
REMARK 6 MOLECULE_NAME: HEXADECANESULFONYL CHLORIDE. AFTER 1LPO 75
REMARK 6 REACTION WITH CRL LIPASE THE MOLECULE FOUND IN THE 1LPO 76
REMARK 6 CRYSTAL IS HEXADECANESULFONATE COMPLEX. 1LPO 77
REMARK 7 1LPO 78
REMARK 7 CA 590 AND WATER HOH 729 ARE IN SPECIAL POSITIONS. 1LPO 79
REMARK 36 1LPO 80
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPO 81
REMARK 36 1LPO 82
REMARK 36 SUBTOPIC: BOND LENGTHS (36.1) 1LPO 83
REMARK 36 1LPO 84
REMARK 36 STANDARD TEXT: 1LPO 85
REMARK 36 1LPO 86
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPO 87
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPO 88
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPO 89
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPO 90
REMARK 36 1LPO 91
REMARK 36 STANDARD TABLE: 1LPO 92
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,A4,3X,A4,16X,F5.1) 1LPO 93
REMARK 36 1LPO 94
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPO 95
REMARK 36 1LPO 96
REMARK 36 M RES CSSEQI ATM1 ATM2 DEVIATION_IN_ANGSTROMS 1LPO 97
REMARK 36 1LPO 98
REMARK 36 0 PRO 58 CB - CG 0.041 1LPO 99
REMARK 36 0 MET 61 SD - CE 0.060 1LPO 100
REMARK 36 0 VAL 154 CB - CA 0.046 1LPO 101
REMARK 36 0 GLU 172 CB - CG 0.041 1LPO 102
REMARK 36 0 MET 186 SD - CE 0.064 1LPO 103
REMARK 36 0 SER 209 CB - OG 0.044 1LPO 104
REMARK 36 0 MET 244 SD - CE 0.078 1LPO 105
REMARK 36 0 MET 319 SD - CE 0.044 1LPO 106
REMARK 36 0 VAL 454 CB - CA 0.043 1LPO 107
REMARK 36 0 MET 503 SD - CE 0.051 1LPO 108
REMARK 36 0 PRO 529 CB - CG 0.044 1LPO 109
REMARK 36 1LPO 110
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPO 111
REMARK 36 1LPO 112
REMARK 36 SUBTOPIC: COVALENT BOND ANGLES (36.2) 1LPO 113
REMARK 36 1LPO 114
REMARK 36 STANDARD TEXT: 1LPO 115
REMARK 36 1LPO 116
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPO 117
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPO 118
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPO 119
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPO 120
REMARK 36 1LPO 121
REMARK 36 STANDARD TABLE: 1LPO 122
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(2X,A4,17X,F5.1) 1LPO 123
REMARK 36 1LPO 124
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPO 125
REMARK 36 1LPO 126
REMARK 36 M RES CSSEQI ATM1 ATM2 ATM3 1LPO 127
REMARK 36 1LPO 128
REMARK 36 0 PHE 23 N - CA - C ANGL. DEV. = 9.3 DEGREES 1LPO 129
REMARK 36 0 SER 45 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPO 130
REMARK 36 0 THR 54 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPO 131
REMARK 36 0 SER 59 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPO 132
REMARK 36 0 ASP 96 N - CA - C ANGL. DEV. = 9.6 DEGREES 1LPO 133
REMARK 36 0 LEU 118 CA - CB - CG ANGL. DEV. = 6.6 DEGREES 1LPO 134
REMARK 36 0 ILE 120 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPO 135
REMARK 36 0 ASN 155 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPO 136
REMARK 36 0 ASN 192 N - CA - C ANGL. DEV. = 10.0 DEGREES 1LPO 137
REMARK 36 0 ILE 193 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPO 138
REMARK 36 0 TYR 228 N - CA - C ANGL. DEV. = 8.2 DEGREES 1LPO 139
REMARK 36 0 GLY 230 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPO 140
REMARK 36 0 ASP 273 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPO 141
REMARK 36 0 THR 293 N - CA - C ANGL. DEV. = 12.6 DEGREES 1LPO 142
REMARK 36 0 PRO 294 N - CA - C ANGL. DEV. = 8.4 DEGREES 1LPO 143
REMARK 36 0 GLY 295 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPO 144
REMARK 36 0 PHE 296 N - CA - C ANGL. DEV. = 7.7 DEGREES 1LPO 145
REMARK 36 0 LEU 302 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPO 146
REMARK 36 0 ARG 303 N - CA - C ANGL. DEV. = 11.7 DEGREES 1LPO 147
REMARK 36 0 LEU 304 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPO 148
REMARK 36 0 LEU 307 CA - CB - CG ANGL. DEV. = 7.2 DEGREES 1LPO 149
REMARK 36 0 ILE 315 N - CA - C ANGL. DEV. = 15.6 DEGREES 1LPO 150
REMARK 36 0 THR 316 N - CA - C ANGL. DEV. = 8.9 DEGREES 1LPO 151
REMARK 36 0 ASP 318 N - CA - C ANGL. DEV. = 7.3 DEGREES 1LPO 152
REMARK 36 0 MET 319 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPO 153
REMARK 36 0 ILE 334 N - CA - C ANGL. DEV. = 10.5 DEGREES 1LPO 154
REMARK 36 0 GLN 338 N - CA - C ANGL. DEV. = 10.7 DEGREES 1LPO 155
REMARK 36 0 GLY 342 N - CA - C ANGL. DEV. = 9.9 DEGREES 1LPO 156
REMARK 36 0 VAL 352 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPO 157
REMARK 36 0 THR 379 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPO 158
REMARK 36 0 GLY 388 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPO 159
REMARK 36 0 PRO 390 C-1 - N - CA ANGL. DEV. = 9.9 DEGREES 1LPO 160
REMARK 36 0 LEU 399 CA - CB - CG ANGL. DEV. = 7.8 DEGREES 1LPO 161
REMARK 36 0 THR 400 N - CA - C ANGL. DEV. = 8.0 DEGREES 1LPO 162
REMARK 36 0 PHE 415 N - CA - C ANGL. DEV. = 7.3 DEGREES 1LPO 163
REMARK 36 0 THR 416 N - CA - C ANGL. DEV. = 11.3 DEGREES 1LPO 164
REMARK 36 0 LEU 445 N - CA - C ANGL. DEV. = 8.4 DEGREES 1LPO 165
REMARK 36 0 THR 447 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPO 166
REMARK 36 0 PHE 448 N - CA - C ANGL. DEV. = 9.8 DEGREES 1LPO 167
REMARK 36 0 SER 450 N - CA - C ANGL. DEV. = 7.5 DEGREES 1LPO 168
REMARK 36 0 ASP 457 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPO 169
REMARK 36 0 TYR 458 N - CA - C ANGL. DEV. = 8.7 DEGREES 1LPO 170
REMARK 36 0 LEU 460 CA - CB - CG ANGL. DEV. = 7.3 DEGREES 1LPO 171
REMARK 36 0 LEU 485 N - CA - C ANGL. DEV. = 7.3 DEGREES 1LPO 172
REMARK 36 0 LEU 486 CA - CB - CG ANGL. DEV. = 6.9 DEGREES 1LPO 173
REMARK 36 0 LEU 502 CA - CB - CG ANGL. DEV. = 7.9 DEGREES 1LPO 174
REMARK 36 0 MET 503 N - CA - C ANGL. DEV. = 10.4 DEGREES 1LPO 175
REMARK 36 0 MET 504 CB - CG - SD ANGL. DEV. = 6.5 DEGREES 1LPO 176
REMARK 36 0 LEU 525 CA - CB - CG ANGL. DEV. = 10.6 DEGREES 1LPO 177
REMARK 36 0 PHE 526 N - CA - C ANGL. DEV. = 10.4 DEGREES 1LPO 178
REMARK 36 0 ASN 528 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPO 179
REMARK 36 0 PRO 530 N - CA - C ANGL. DEV. = 8.0 DEGREES 1LPO 180
REMARK 36 1LPO 181
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPO 182
REMARK 36 1LPO 183
REMARK 36 SUBTOPIC: TORSION ANGLES (36.4) 1LPO 184
REMARK 36 1LPO 185
REMARK 36 STANDARD TEXT: 1LPO 186
REMARK 36 1LPO 187
REMARK 36 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: 1LPO 188
REMARK 36 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; 1LPO 189
REMARK 36 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPO 190
REMARK 36 1LPO 191
REMARK 36 STANDARD TABLE: 1LPO 192
REMARK 36 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) 1LPO 193
REMARK 36 1LPO 194
REMARK 36 M RES CSSEQI PSI PHI 1LPO 195
REMARK 36 1LPO 196
REMARK 36 0 ILE 18 71.34 -62.27 1LPO 197
REMARK 36 0 PHE 38 62.07 -2.65 1LPO 198
REMARK 36 0 THR 68 177.42 162.17 1LPO 199
REMARK 36 0 SER 159 65.72 -147.29 1LPO 200
REMARK 36 0 SER 209 53.26 -119.06 1LPO 201
REMARK 36 0 ALA 243 -127.41 -124.60 1LPO 202
REMARK 36 0 SER 301 55.20 -128.81 1LPO 203
REMARK 36 0 VAL 444 65.33 -46.26 1LPO 204
REMARK 999 1LPO 205
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1LPO 206
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPO 207
REMARK 999 LIP1_CANRU 1LPO 208
SEQRES 1 549 MET GLU LEU ALA LEU ALA LEU SER LEU ILE ALA SER VAL 1LPO 209
SEQRES 2 549 ALA ALA ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR 1LPO 210
SEQRES 3 549 ILE THR GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU 1LPO 211
SEQRES 4 549 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG 1LPO 212
SEQRES 5 549 PHE LYS ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY 1LPO 213
SEQRES 6 549 GLN LYS PHE THR SER TYR GLY PRO SER CYS MET GLN GLN 1LPO 214
SEQRES 7 549 ASN PRO GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA 1LPO 215
SEQRES 8 549 ALA LEU ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA 1LPO 216
SEQRES 9 549 VAL SER PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL 1LPO 217
SEQRES 10 549 VAL ARG PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO 1LPO 218
SEQRES 11 549 VAL MET LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY 1LPO 219
SEQRES 12 549 GLY THR SER THR PHE PRO PRO ALA GLN MET ILE THR LYS 1LPO 220
SEQRES 13 549 SER ILE ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL 1LPO 221
SEQRES 14 549 ASN TYR ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP 1LPO 222
SEQRES 15 549 GLU ILE LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS 1LPO 223
SEQRES 16 549 ASP GLN ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE 1LPO 224
SEQRES 17 549 ALA ALA PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE 1LPO 225
SEQRES 18 549 GLY GLU SER ALA GLY SER MET SER VAL MET CYS HIS ILE 1LPO 226
SEQRES 19 549 LEU TRP ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO 1LPO 227
SEQRES 20 549 LEU PHE ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL 1LPO 228
SEQRES 21 549 PRO SER ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE 1LPO 229
SEQRES 22 549 PHE ASP LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA 1LPO 230
SEQRES 23 549 SER ASP LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP 1LPO 231
SEQRES 24 549 THR LEU GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU 1LPO 232
SEQRES 25 549 ALA TYR SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO 1LPO 233
SEQRES 26 549 ASP GLY VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL 1LPO 234
SEQRES 27 549 ARG GLU GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY 1LPO 235
SEQRES 28 549 ASP GLN ASN ASP GLU GLY THR PHE PHE GLY THR SER SER 1LPO 236
SEQRES 29 549 LEU ASN VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE 1LPO 237
SEQRES 30 549 LYS GLN SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP 1LPO 238
SEQRES 31 549 THR LEU MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY 1LPO 239
SEQRES 32 549 SER PRO PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO 1LPO 240
SEQRES 33 549 GLN PHE LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY 1LPO 241
SEQRES 34 549 PHE THR LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR 1LPO 242
SEQRES 35 549 GLY GLY THR LYS TYR SER PHE LEU SER LYS GLN LEU SER 1LPO 243
SEQRES 36 549 GLY LEU PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE 1LPO 244
SEQRES 37 549 VAL PHE GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE 1LPO 245
SEQRES 38 549 TYR ASN ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP 1LPO 246
SEQRES 39 549 PRO ASN THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR 1LPO 247
SEQRES 40 549 THR SER SER SER GLN SER GLY ASN ASN LEU MET MET ILE 1LPO 248
SEQRES 41 549 ASN ALA LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG 1LPO 249
SEQRES 42 549 THR ALA GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER 1LPO 250
SEQRES 43 549 PHE PHE VAL 1LPO 251
FTNOTE 1 1LPO 252
FTNOTE 1 CIS PROLINE - PRO 390 1LPO 253
HET HDS 560 19 1-HEXADECANOSULFONIC ACID 1LPO 254
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1LPO 255
HET NAG 992 14 N-ACETYL-D-GLUCOSAMINE 1LPO 256
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1LPO 257
HET CA 589 1 CALCIUM ION 1LPO 258
HET CA 590 1 CALCIUM ION 1LPO 259
FORMUL 2 HDS C16 H34 O3 S1 1LPO 260
FORMUL 3 NAG 3(C8 H15 N1 O6) 1LPO 261
FORMUL 4 CA 2(CA1 2+) 1LPO 262
FORMUL 5 HOH *179(H2 O1) 1LPO 263
HELIX 1 1 GLY 34 LEU 36 5 1LPO 264
HELIX 2 2 LEU 73 MET 82 1 1LPO 265
HELIX 3 3 LYS 85 VAL 90 1 1LPO 266
HELIX 4 4 ALA 136 ALA 144 1 1LPO 267
HELIX 5 5 SER 159 PHE 163 1 1LPO 268
HELIX 6 6 ASP 167 GLU 172 1 1LPO 269
HELIX 7 7 ALA 177 PHE 196 1 1LPO 270
HELIX 8 8 SER 209 GLY 224 5 1LPO 271
HELIX 9 9 ILE 253 ALA 266 1 1LPO 272
HELIX 10 10 LYS 274 GLY 280 1 1LPO 273
HELIX 11 11 SER 283 ASN 292 1 1LPO 274
HELIX 12 12 MET 319 ARG 324 1 1LPO 275
HELIX 13 13 THR 343 SER 349 1 1LPO 276
HELIX 14 14 ASP 355 SER 365 1 1LPO 277
HELIX 15 15 ASP 371 ALA 380 1 1LPO 278
HELIX 16 16 ILE 385 GLN 387 5 1LPO 279
HELIX 17 17 PHE 403 GLY 414 1 1LPO 280
HELIX 18 18 THR 416 HIS 425 1 1LPO 281
HELIX 19 19 ASN 451 ASP 457 1 1LPO 282
HELIX 20 20 SER 462 TYR 467 5 1LPO 283
HELIX 21 21 ASN 469 ASP 477 1 1LPO 284
HELIX 22 22 PRO 480 ALA 483 5 1LPO 285
HELIX 23 23 THR 519 PHE 526 1 1LPO 286
HELIX 24 24 PRO 529 PHE 532 5 1LPO 287
SHEET 1 A 2 THR 3 THR 5 0 1LPO 288
SHEET 2 A 2 THR 11 THR 13 -1 N ILE 12 O ALA 4 1LPO 289
SHEET 1 B10 GLU 21 PHE 23 0 1LPO 290
SHEET 2 B10 ILE 100 ARG 104 -1 N ARG 104 O GLU 21 1LPO 291
SHEET 3 B10 ILE 149 VAL 154 -1 N SER 153 O ASN 101 1LPO 292
SHEET 4 B10 PRO 115 ILE 120 1 N PRO 115 O ILE 150 1LPO 293
SHEET 5 B10 VAL 203 GLU 208 1 N THR 204 O VAL 116 1LPO 294
SHEET 6 B10 ALA 236 GLN 240 1 N ALA 236 O ILE 205 1LPO 295
SHEET 7 B10 PRO 332 GLN 338 1 N PRO 332 O GLY 237 1LPO 296
SHEET 8 B10 LYS 431 SER 436 1 N TYR 432 O VAL 333 1LPO 297
SHEET 9 B10 LEU 502 ILE 505 1 N MET 503 O SER 433 1LPO 298
SHEET 10 B10 LEU 510 GLY 513 -1 N GLY 513 O LEU 502 1LPO 299
SSBOND 1 CYS 60 CYS 97 1LPO 300
SSBOND 2 CYS 268 CYS 277 1LPO 301
CRYST1 65.000 97.600 176.300 90.00 90.00 90.00 C 2 2 21 8 1LPO 302
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPO 303
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPO 304
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPO 305
SCALE1 0.015385 0.000000 0.000000 0.00000 1LPO 306
SCALE2 0.000000 0.010246 0.000000 0.00000 1LPO 307
SCALE3 0.000000 0.000000 0.005672 0.00000 1LPO 308 |