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HEADER HYDROLASE 11-JAN-95 1LPN 1LPN 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH 1LPN 3
COMPND 2 DODECANESULFONATE 1LPN 4
SOURCE YEAST (CANDIDA RUGOSA) (FORMERLY CANDIDA CYLINDRACEA) 1LPN 5
AUTHOR P.G.GROCHULSKI,M.C.CYGLER 1LPN 6
REVDAT 1 20-APR-95 1LPN 0 1LPN 7
JRNL AUTH P.GROCHULSKI,F.BOUTHILLIER,R.J.KAZLAUSKAS, 1LPN 8
JRNL AUTH 2 A.N.SERREGI,J.D.SCHRAG,E.ZIOMEK,M.CYGLER 1LPN 9
JRNL TITL ANALOGS OF REACTION INTERMEDIATES IDENTIFY A 1LPN 10
JRNL TITL 2 UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA 1LPN 11
JRNL TITL 3 LIPASE 1LPN 12
JRNL REF BIOCHEMISTRY V. 33 3494 1994 1LPN 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1LPN 14
REMARK 1 1LPN 15
REMARK 1 REFERENCE 1 1LPN 16
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,M.CYGLER 1LPN 17
REMARK 1 TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE 1LPN 18
REMARK 1 REF PROTEIN SCI. V. 3 82 1994 1LPN 19
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1LPN 20
REMARK 1 REFERENCE 2 1LPN 21
REMARK 1 AUTH M.CYGLER,P.GROCHULSKI,R.J.KAZLAUSKAS,J.D.SCHRAG, 1LPN 22
REMARK 1 AUTH 2 F.BOUTHILLIER,B.RUBIN,A.N.SERREGI,A.K.GUPTA 1LPN 23
REMARK 1 TITL A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF 1LPN 24
REMARK 1 TITL 2 LIPASES 1LPN 25
REMARK 1 REF J.AM.CHEM.SOC. V. 116 3180 1994 1LPN 26
REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863 0004 1LPN 27
REMARK 1 REFERENCE 3 1LPN 28
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1LPN 29
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1LPN 30
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1LPN 31
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1LPN 32
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1LPN 33
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1LPN 34
REMARK 2 1LPN 35
REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1LPN 36
REMARK 3 1LPN 37
REMARK 3 REFINEMENT. 1LPN 38
REMARK 3 PROGRAM X-PLOR 1LPN 39
REMARK 3 AUTHORS BRUNGER 1LPN 40
REMARK 3 R VALUE 0.151 1LPN 41
REMARK 3 MEAN B VALUE 18.6 ANGSTROMS**2 1LPN 42
REMARK 3 NUMBER OF REFLECTIONS 20219 1LPN 43
REMARK 3 RESOLUTION RANGE 8. - 2.18 ANGSTROMS 1LPN 44
REMARK 3 DATA CUTOFF 4. SIGMA(F) 1LPN 45
REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1LPN 46
REMARK 3 RMSD BOND ANGLES 1.82 DEGREES 1LPN 47
REMARK 3 1LPN 48
REMARK 3 DATA COLLECTION. 1LPN 49
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 22925 1LPN 50
REMARK 3 COMPLETENESS OF DATA 77.4 % 1LPN 51
REMARK 3 REJECTION CRITERIA 2. SIGMA(I) 1LPN 52
REMARK 3 1LPN 53
REMARK 3 SOLVENT CONTENT (VS) 48. % 1LPN 54
REMARK 3 1LPN 55
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LPN 56
REMARK 3 NUMBER OF PROTEIN ATOMS 4022 1LPN 57
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LPN 58
REMARK 3 NUMBER OF HETEROGEN ATOMS 74 1LPN 59
REMARK 3 NUMBER OF SOLVENT ATOMS 115 1LPN 60
REMARK 4 1LPN 61
REMARK 4 EXPERIMENTAL DETAILS 1LPN 62
REMARK 4 SINGLE CRYSTAL X-RAY DIFFRACTION 1LPN 63
REMARK 4 MONOCHROMATIC RADIATION 1LPN 64
REMARK 4 DATE OF DATA-COLLECTION (DD-MON-YY) : 20-05-93 1LPN 65
REMARK 4 WAVELENGTH OR WAVELENGTH RANGE : CUKA 1LPN 66
REMARK 4 DETECTOR TYPE/MANUFACTURER : RAXIS II 1LPN 67
REMARK 4 INTENSITY-INTEGRATION SOFTWARE : RAXIS SOFTWARE 1LPN 68
REMARK 4 DATA REDUNDANCY : 2.3 1LPN 69
REMARK 5 1LPN 70
REMARK 5 KEYWDS: CARBOXYLIC ESTERASE, CRL 1LPN 71
REMARK 6 1LPN 72
REMARK 6 SOURCE 1LPN 73
REMARK 6 MOLECULE_NAME: DODECANESULFONYL CHLORIDE. AFTER REACTION 1LPN 74
REMARK 6 WITH CRL LIPASE THE MOLECULE FOUND IN THE CRYSTAL IS 1LPN 75
REMARK 6 DODECANESULFONATE COMPLEX. 1LPN 76
REMARK 7 1LPN 77
REMARK 7 CA 590 IS IN A SPECIAL POSITION. 1LPN 78
REMARK 36 1LPN 79
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPN 80
REMARK 36 1LPN 81
REMARK 36 SUBTOPIC: BOND LENGTHS (36.1) 1LPN 82
REMARK 36 1LPN 83
REMARK 36 STANDARD TEXT: 1LPN 84
REMARK 36 1LPN 85
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPN 86
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPN 87
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPN 88
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPN 89
REMARK 36 1LPN 90
REMARK 36 STANDARD TABLE: 1LPN 91
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,A4,3X,A4,16X,F5.1) 1LPN 92
REMARK 36 1LPN 93
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPN 94
REMARK 36 1LPN 95
REMARK 36 M RES CSSEQI ATM1 ATM2 DEVIATION_IN_ANGSTROMS 1LPN 96
REMARK 36 1LPN 97
REMARK 36 0 MET 61 SD - CE 0.050 1LPN 98
REMARK 36 0 MET 117 SD - CE 0.053 1LPN 99
REMARK 36 0 MET 138 SD - CE 0.046 1LPN 100
REMARK 36 0 ILE 149 CB - CA 0.045 1LPN 101
REMARK 36 0 MET 186 SD - CE 0.049 1LPN 102
REMARK 36 0 TRP 188 CB - CG 0.043 1LPN 103
REMARK 36 0 MET 319 SD - CE 0.051 1LPN 104
REMARK 36 0 PRO 529 CB - CG 0.071 1LPN 105
REMARK 36 1LPN 106
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPN 107
REMARK 36 1LPN 108
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPN 109
REMARK 36 1LPN 110
REMARK 36 SUBTOPIC: COVALENT BOND ANGLES (36.2) 1LPN 111
REMARK 36 1LPN 112
REMARK 36 STANDARD TEXT: 1LPN 113
REMARK 36 1LPN 114
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPN 115
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPN 116
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPN 117
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPN 118
REMARK 36 1LPN 119
REMARK 36 STANDARD TABLE: 1LPN 120
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(2X,A4,17X,F5.1) 1LPN 121
REMARK 36 1LPN 122
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPN 123
REMARK 36 1LPN 124
REMARK 36 M RES CSSEQI ATM1 ATM2 ATM3 1LPN 125
REMARK 36 1LPN 126
REMARK 36 0 PHE 23 N - CA - C ANGL. DEV. = 9.6 DEGREES 1LPN 127
REMARK 36 0 GLY 25 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPN 128
REMARK 36 0 SER 45 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 129
REMARK 36 0 THR 54 N - CA - C ANGL. DEV. = 7.8 DEGREES 1LPN 130
REMARK 36 0 SER 59 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPN 131
REMARK 36 0 ASN 64 N - CA - C ANGL. DEV. = 8.3 DEGREES 1LPN 132
REMARK 36 0 ASP 96 N - CA - C ANGL. DEV. = 9.7 DEGREES 1LPN 133
REMARK 36 0 PRO 115 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPN 134
REMARK 36 0 LEU 118 CA - CB - CG ANGL. DEV. = 8.2 DEGREES 1LPN 135
REMARK 36 0 GLU 126 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 136
REMARK 36 0 ASN 192 N - CA - C ANGL. DEV. = 9.8 DEGREES 1LPN 137
REMARK 36 0 THR 204 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPN 138
REMARK 36 0 TYR 228 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPN 139
REMARK 36 0 ASP 273 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPN 140
REMARK 36 0 THR 293 N - CA - C ANGL. DEV. = 12.4 DEGREES 1LPN 141
REMARK 36 0 PRO 294 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPN 142
REMARK 36 0 GLY 295 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 143
REMARK 36 0 PHE 296 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPN 144
REMARK 36 0 ARG 303 N - CA - C ANGL. DEV. = 12.1 DEGREES 1LPN 145
REMARK 36 0 LEU 304 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 146
REMARK 36 0 LEU 307 CA - CB - CG ANGL. DEV. = 8.4 DEGREES 1LPN 147
REMARK 36 0 ILE 315 N - CA - C ANGL. DEV. = 14.8 DEGREES 1LPN 148
REMARK 36 0 THR 316 N - CA - C ANGL. DEV. = 10.3 DEGREES 1LPN 149
REMARK 36 0 ASP 318 N - CA - C ANGL. DEV. = 8.4 DEGREES 1LPN 150
REMARK 36 0 PRO 332 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPN 151
REMARK 36 0 ILE 334 N - CA - C ANGL. DEV. = 8.5 DEGREES 1LPN 152
REMARK 36 0 GLN 338 N - CA - C ANGL. DEV. = 11.6 DEGREES 1LPN 153
REMARK 36 0 ASN 339 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPN 154
REMARK 36 0 GLY 342 N - CA - C ANGL. DEV. = 9.2 DEGREES 1LPN 155
REMARK 36 0 VAL 352 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPN 156
REMARK 36 0 THR 379 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPN 157
REMARK 36 0 PRO 390 C-1 - N - CA ANGL. DEV. = 10.3 DEGREES 1LPN 158
REMARK 36 0 LEU 399 CA - CB - CG ANGL. DEV. = 7.3 DEGREES 1LPN 159
REMARK 36 0 THR 400 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPN 160
REMARK 36 0 PHE 415 N - CA - C ANGL. DEV. = 8.2 DEGREES 1LPN 161
REMARK 36 0 THR 416 N - CA - C ANGL. DEV. = 10.7 DEGREES 1LPN 162
REMARK 36 0 LEU 417 CA - CB - CG ANGL. DEV. = 8.0 DEGREES 1LPN 163
REMARK 36 0 GLY 428 N - CA - C ANGL. DEV. = 7.5 DEGREES 1LPN 164
REMARK 36 0 TYR 432 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPN 165
REMARK 36 0 LYS 437 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 166
REMARK 36 0 LEU 439 CA - CB - CG ANGL. DEV. = 8.1 DEGREES 1LPN 167
REMARK 36 0 LEU 445 N - CA - C ANGL. DEV. = 9.2 DEGREES 1LPN 168
REMARK 36 0 THR 447 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPN 169
REMARK 36 0 TYR 458 N - CA - C ANGL. DEV. = 8.5 DEGREES 1LPN 170
REMARK 36 0 LEU 485 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPN 171
REMARK 36 0 SER 498 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPN 172
REMARK 36 0 LEU 502 CA - CB - CG ANGL. DEV. = 7.1 DEGREES 1LPN 173
REMARK 36 0 MET 503 N - CA - C ANGL. DEV. = 9.9 DEGREES 1LPN 174
REMARK 36 0 MET 504 CB - CG - SD ANGL. DEV. = 7.0 DEGREES 1LPN 175
REMARK 36 0 TYR 511 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPN 176
REMARK 36 0 ARG 518 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPN 177
REMARK 36 0 LEU 525 CA - CB - CG ANGL. DEV. = 11.3 DEGREES 1LPN 178
REMARK 36 0 PHE 526 N - CA - C ANGL. DEV. = 11.3 DEGREES 1LPN 179
REMARK 36 1LPN 180
REMARK 36 SUBTOPIC: TORSION ANGLES (36.4) 1LPN 181
REMARK 36 1LPN 182
REMARK 36 STANDARD TEXT: 1LPN 183
REMARK 36 1LPN 184
REMARK 36 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: 1LPN 185
REMARK 36 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; 1LPN 186
REMARK 36 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPN 187
REMARK 36 1LPN 188
REMARK 36 STANDARD TABLE: 1LPN 189
REMARK 36 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) 1LPN 190
REMARK 36 1LPN 191
REMARK 36 M RES CSSEQI PSI PHI 1LPN 192
REMARK 36 1LPN 193
REMARK 36 0 ILE 18 73.92 -59.73 1LPN 194
REMARK 36 0 PHE 38 65.34 -4.82 1LPN 195
REMARK 36 0 THR 68 176.93 166.04 1LPN 196
REMARK 36 0 SER 159 64.52 -148.27 1LPN 197
REMARK 36 0 SER 209 50.59 -110.99 1LPN 198
REMARK 36 0 ALA 243 -119.58 -126.13 1LPN 199
REMARK 36 0 SER 301 56.68 -124.40 1LPN 200
REMARK 36 0 VAL 444 68.80 -48.49 1LPN 201
REMARK 999 1LPN 202
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1LPN 203
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPN 204
REMARK 999 LIP1_CANRU 1LPN 205
SEQRES 1 549 MET GLU LEU ALA LEU ALA LEU SER LEU ILE ALA SER VAL 1LPN 206
SEQRES 2 549 ALA ALA ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR 1LPN 207
SEQRES 3 549 ILE THR GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU 1LPN 208
SEQRES 4 549 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG 1LPN 209
SEQRES 5 549 PHE LYS ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY 1LPN 210
SEQRES 6 549 GLN LYS PHE THR SER TYR GLY PRO SER CYS MET GLN GLN 1LPN 211
SEQRES 7 549 ASN PRO GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA 1LPN 212
SEQRES 8 549 ALA LEU ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA 1LPN 213
SEQRES 9 549 VAL SER PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL 1LPN 214
SEQRES 10 549 VAL ARG PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO 1LPN 215
SEQRES 11 549 VAL MET LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY 1LPN 216
SEQRES 12 549 GLY THR SER THR PHE PRO PRO ALA GLN MET ILE THR LYS 1LPN 217
SEQRES 13 549 SER ILE ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL 1LPN 218
SEQRES 14 549 ASN TYR ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP 1LPN 219
SEQRES 15 549 GLU ILE LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS 1LPN 220
SEQRES 16 549 ASP GLN ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE 1LPN 221
SEQRES 17 549 ALA ALA PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE 1LPN 222
SEQRES 18 549 GLY GLU SER ALA GLY SER MET SER VAL MET CYS HIS ILE 1LPN 223
SEQRES 19 549 LEU TRP ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO 1LPN 224
SEQRES 20 549 LEU PHE ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL 1LPN 225
SEQRES 21 549 PRO SER ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE 1LPN 226
SEQRES 22 549 PHE ASP LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA 1LPN 227
SEQRES 23 549 SER ASP LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP 1LPN 228
SEQRES 24 549 THR LEU GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU 1LPN 229
SEQRES 25 549 ALA TYR SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO 1LPN 230
SEQRES 26 549 ASP GLY VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL 1LPN 231
SEQRES 27 549 ARG GLU GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY 1LPN 232
SEQRES 28 549 ASP GLN ASN ASP GLU GLY THR PHE PHE GLY THR SER SER 1LPN 233
SEQRES 29 549 LEU ASN VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE 1LPN 234
SEQRES 30 549 LYS GLN SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP 1LPN 235
SEQRES 31 549 THR LEU MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY 1LPN 236
SEQRES 32 549 SER PRO PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO 1LPN 237
SEQRES 33 549 GLN PHE LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY 1LPN 238
SEQRES 34 549 PHE THR LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR 1LPN 239
SEQRES 35 549 GLY GLY THR LYS TYR SER PHE LEU SER LYS GLN LEU SER 1LPN 240
SEQRES 36 549 GLY LEU PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE 1LPN 241
SEQRES 37 549 VAL PHE GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE 1LPN 242
SEQRES 38 549 TYR ASN ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP 1LPN 243
SEQRES 39 549 PRO ASN THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR 1LPN 244
SEQRES 40 549 THR SER SER SER GLN SER GLY ASN ASN LEU MET MET ILE 1LPN 245
SEQRES 41 549 ASN ALA LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG 1LPN 246
SEQRES 42 549 THR ALA GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER 1LPN 247
SEQRES 43 549 PHE PHE VAL 1LPN 248
FTNOTE 1 1LPN 249
FTNOTE 1 CIS PROLINE - PRO 390 1LPN 250
HET CA 589 1 CALCIUM ION 1LPN 251
HET CA 590 1 CALCIUM ION 1LPN 252
HET DSC 560 15 DODECANESULFONATE 1LPN 253
HET DSC 561 15 DODECANESULFONATE 1LPN 254
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1LPN 255
HET NAG 992 14 N-ACETYL-D-GLUCOSAMINE 1LPN 256
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1LPN 257
FORMUL 2 CA 2(CA1 2+) 1LPN 258
FORMUL 3 DSC 2(C12 H25 O2 S1) 1LPN 259
FORMUL 4 NAG 3(C8 H15 N1 O6) 1LPN 260
FORMUL 5 HOH *115(H2 O1) 1LPN 261
HELIX 1 1 GLY 34 LEU 36 5 1LPN 262
HELIX 2 2 LEU 73 MET 82 1 1LPN 263
HELIX 3 3 LYS 85 VAL 90 1 1LPN 264
HELIX 4 4 THR 130 THR 132 5 1LPN 265
HELIX 5 5 ALA 136 ALA 144 1 1LPN 266
HELIX 6 6 SER 159 PHE 163 1 1LPN 267
HELIX 7 7 ASP 167 GLU 172 1 1LPN 268
HELIX 8 8 ALA 177 PHE 196 1 1LPN 269
HELIX 9 9 SER 209 GLY 224 5 1LPN 270
HELIX 10 10 ILE 253 ALA 266 1 1LPN 271
HELIX 11 11 LYS 274 GLY 280 1 1LPN 272
HELIX 12 12 SER 283 THR 290 1 1LPN 273
HELIX 13 13 MET 319 ARG 324 1 1LPN 274
HELIX 14 14 PHE 345 SER 349 5 1LPN 275
HELIX 15 15 ASP 355 SER 365 1 1LPN 276
HELIX 16 16 ASP 371 ALA 380 1 1LPN 277
HELIX 17 17 ILE 385 GLN 387 5 1LPN 278
HELIX 18 18 PHE 403 GLY 414 1 1LPN 279
HELIX 19 19 THR 416 LEU 423 1 1LPN 280
HELIX 20 20 ASN 451 ASP 457 1 1LPN 281
HELIX 21 21 SER 462 TYR 467 5 1LPN 282
HELIX 22 22 ASN 469 ASP 477 1 1LPN 283
HELIX 23 23 PRO 480 ALA 483 5 1LPN 284
HELIX 24 24 THR 519 PHE 526 1 1LPN 285
HELIX 25 25 PRO 529 PHE 532 5 1LPN 286
SHEET 1 A 2 THR 3 THR 5 0 1LPN 287
SHEET 2 A 2 THR 11 THR 13 -1 N ILE 12 O ALA 4 1LPN 288
SHEET 1 B10 GLU 21 PHE 23 0 1LPN 289
SHEET 2 B10 ILE 100 ARG 104 -1 N ARG 104 O GLU 21 1LPN 290
SHEET 3 B10 ILE 149 VAL 154 -1 N SER 153 O ASN 101 1LPN 291
SHEET 4 B10 PRO 115 ILE 120 1 N PRO 115 O ILE 150 1LPN 292
SHEET 5 B10 VAL 203 GLU 208 1 N THR 204 O VAL 116 1LPN 293
SHEET 6 B10 ALA 236 GLN 240 1 N ALA 236 O ILE 205 1LPN 294
SHEET 7 B10 PRO 332 GLN 338 1 N PRO 332 O GLY 237 1LPN 295
SHEET 8 B10 LYS 431 SER 436 1 N TYR 432 O VAL 333 1LPN 296
SHEET 9 B10 LEU 502 ILE 505 1 N MET 503 O SER 433 1LPN 297
SHEET 10 B10 LEU 510 GLY 513 -1 N GLY 513 O LEU 502 1LPN 298
SSBOND 1 CYS 60 CYS 97 1LPN 299
SSBOND 2 CYS 268 CYS 277 1LPN 300
CRYST1 65.000 97.400 176.400 90.00 90.00 90.00 C 2 2 21 8 1LPN 301
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPN 302
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPN 303
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPN 304
SCALE1 0.015385 0.000000 0.000000 0.00000 1LPN 305
SCALE2 0.000000 0.010267 0.000000 0.00000 1LPN 306
SCALE3 0.000000 0.000000 0.005669 0.00000 1LPN 307 |