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HEADER HYDROLASE 17-JAN-95 1LPP 1LPP 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH 1LPP 3
COMPND 2 HEXADECANESULFONATE 1LPP 4
SOURCE YEAST (CANDIDA RUGOSA) (FORMERLY CANDIDA CYLINDRACEA) 1LPP 5
AUTHOR P.G.GROCHULSKI,M.C.CYGLER 1LPP 6
REVDAT 1 20-APR-95 1LPP 0 1LPP 7
JRNL AUTH P.GROCHULSKI,F.BOUTHILLIER,R.J.KAZLAUSKAS, 1LPP 8
JRNL AUTH 2 A.N.SERREGI,J.D.SCHRAG,E.ZIOMEK,M.CYGLER 1LPP 9
JRNL TITL ANALOGS OF REACTION INTERMEDIATES IDENTIFY A 1LPP 10
JRNL TITL 2 UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA 1LPP 11
JRNL TITL 3 LIPASE 1LPP 12
JRNL REF BIOCHEMISTRY V. 33 3494 1994 1LPP 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1LPP 14
REMARK 1 1LPP 15
REMARK 1 REFERENCE 1 1LPP 16
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,M.CYGLER 1LPP 17
REMARK 1 TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE 1LPP 18
REMARK 1 REF PROTEIN SCI. V. 3 82 1994 1LPP 19
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1LPP 20
REMARK 1 REFERENCE 2 1LPP 21
REMARK 1 AUTH M.CYGLER,P.GROCHULSKI,R.J.KAZLAUSKAS,J.D.SCHRAG, 1LPP 22
REMARK 1 AUTH 2 F.BOUTHILLIER,B.RUBIN,A.N.SERREGI,A.K.GUPTA 1LPP 23
REMARK 1 TITL A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF 1LPP 24
REMARK 1 TITL 2 LIPASES 1LPP 25
REMARK 1 REF J.AM.CHEM.SOC. V. 116 3180 1994 1LPP 26
REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863 0004 1LPP 27
REMARK 1 REFERENCE 3 1LPP 28
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1LPP 29
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1LPP 30
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1LPP 31
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1LPP 32
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1LPP 33
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1LPP 34
REMARK 2 1LPP 35
REMARK 2 RESOLUTION. 2.05 ANGSTROMS. 1LPP 36
REMARK 3 1LPP 37
REMARK 3 REFINEMENT. 1LPP 38
REMARK 3 PROGRAM X-PLOR 1LPP 39
REMARK 3 AUTHORS BRUNGER 1LPP 40
REMARK 3 R VALUE 0.137 1LPP 41
REMARK 3 MEAN B VALUE 21.2 ANGSTROMS**2 1LPP 42
REMARK 3 NUMBER OF REFLECTIONS 26019 1LPP 43
REMARK 3 RESOLUTION RANGE 8. - 2.18 ANGSTROMS 1LPP 44
REMARK 3 DATA CUTOFF 4. SIGMA(F) 1LPP 45
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1LPP 46
REMARK 3 RMSD BOND ANGLES 1.86 DEGREES 1LPP 47
REMARK 3 1LPP 48
REMARK 3 DATA COLLECTION. 1LPP 49
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 30889 1LPP 50
REMARK 3 COMPLETENESS OF DATA 86.7 % 1LPP 51
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1LPP 52
REMARK 3 1LPP 53
REMARK 3 SOLVENT CONTENT (VS) 48. % 1LPP 54
REMARK 3 1LPP 55
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LPP 56
REMARK 3 NUMBER OF PROTEIN ATOMS 4022 1LPP 57
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LPP 58
REMARK 3 NUMBER OF HETEROGEN ATOMS 82 1LPP 59
REMARK 3 NUMBER OF SOLVENT ATOMS 296 1LPP 60
REMARK 4 1LPP 61
REMARK 4 EXPERIMENTAL DETAILS 1LPP 62
REMARK 4 SINGLE CRYSTAL X-RAY DIFFRACTION 1LPP 63
REMARK 4 MONOCHROMATIC RADIATION 1LPP 64
REMARK 4 DATE OF DATA-COLLECTION (DD-MON-YY) : 04-05-93 1LPP 65
REMARK 4 WAVELENGTH OR WAVELENGTH RANGE : CUKA 1LPP 66
REMARK 4 DETECTOR TYPE/MANUFACTURER : RAXIS II 1LPP 67
REMARK 4 INTENSITY-INTEGRATION SOFTWARE : RAXIS SOFTWARE 1LPP 68
REMARK 4 DATA REDUNDANCY : 2.7 1LPP 69
REMARK 5 1LPP 70
REMARK 5 COMPND 1LPP 71
REMARK 5 INHIBITED BY HEXADECANESULFONYL CHLORIDE (1:120). 1LPP 72
REMARK 6 1LPP 73
REMARK 6 SOURCE 1LPP 74
REMARK 6 MOLECULE_NAME: HEXADECANESULFONYL CHLORIDE. AFTER 1LPP 75
REMARK 6 REACTION WITH CRL LIPASE THE MOLECULE FOUND IN THE 1LPP 76
REMARK 6 CRYSTAL IS HEXADECANESULFONATE COMPLEX. 1LPP 77
REMARK 7 1LPP 78
REMARK 7 CA 590 AND HOH 779 ARE IN SPECIAL POSITIONS. 1LPP 79
REMARK 36 1LPP 80
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPP 81
REMARK 36 1LPP 82
REMARK 36 SUBTOPIC: BOND LENGTHS (36.1) 1LPP 83
REMARK 36 1LPP 84
REMARK 36 STANDARD TEXT: 1LPP 85
REMARK 36 1LPP 86
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPP 87
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPP 88
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPP 89
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPP 90
REMARK 36 1LPP 91
REMARK 36 STANDARD TABLE: 1LPP 92
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,A4,3X,A4,16X,F5.1) 1LPP 93
REMARK 36 1LPP 94
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPP 95
REMARK 36 1LPP 96
REMARK 36 M RES CSSEQI ATM1 ATM2 DEVIATION_IN_ANGSTROMS 1LPP 97
REMARK 36 1LPP 98
REMARK 36 0 MET 61 SD - CE 0.059 1LPP 99
REMARK 36 0 MET 82 SD - CE 0.059 1LPP 100
REMARK 36 0 MET 145 SD - CE 0.038 1LPP 101
REMARK 36 0 ILE 149 CB - CA 0.045 1LPP 102
REMARK 36 0 ALA 236 CB - CA 0.040 1LPP 103
REMARK 36 0 MET 244 SD - CE 0.045 1LPP 104
REMARK 36 0 ARG 279 CB - CG 0.039 1LPP 105
REMARK 36 0 THR 293 CB - CA 0.040 1LPP 106
REMARK 36 0 MET 319 SD - CE 0.043 1LPP 107
REMARK 36 0 LYS 327 CG - CD 0.038 1LPP 108
REMARK 36 1LPP 109
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPP 110
REMARK 36 1LPP 111
REMARK 36 SUBTOPIC: COVALENT BOND ANGLES (36.2) 1LPP 112
REMARK 36 1LPP 113
REMARK 36 STANDARD TEXT: 1LPP 114
REMARK 36 1LPP 115
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPP 116
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPP 117
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPP 118
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPP 119
REMARK 36 1LPP 120
REMARK 36 STANDARD TABLE: 1LPP 121
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(2X,A4,17X,F5.1) 1LPP 122
REMARK 36 1LPP 123
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPP 124
REMARK 36 1LPP 125
REMARK 36 M RES CSSEQI ATM1 ATM2 ATM3 1LPP 126
REMARK 36 1LPP 127
REMARK 36 0 GLU 21 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPP 128
REMARK 36 0 PHE 23 N - CA - C ANGL. DEV. = 8.6 DEGREES 1LPP 129
REMARK 36 0 GLY 25 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPP 130
REMARK 36 0 SER 45 N - CA - C ANGL. DEV. = 7.9 DEGREES 1LPP 131
REMARK 36 0 SER 59 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPP 132
REMARK 36 0 LEU 80 CA - CB - CG ANGL. DEV. = 6.3 DEGREES 1LPP 133
REMARK 36 0 ASP 96 N - CA - C ANGL. DEV. = 10.7 DEGREES 1LPP 134
REMARK 36 0 MET 117 N - CA - C ANGL. DEV. = 6.2 DEGREES 1LPP 135
REMARK 36 0 PHE 121 N - CA - C ANGL. DEV. = 7.0 DEGREES 1LPP 136
REMARK 36 0 ASN 155 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPP 137
REMARK 36 0 LEU 164 N - CA - C ANGL. DEV. = 6.3 DEGREES 1LPP 138
REMARK 36 0 ASN 192 N - CA - C ANGL. DEV. = 10.0 DEGREES 1LPP 139
REMARK 36 0 ILE 193 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPP 140
REMARK 36 0 ASP 273 N - CA - C ANGL. DEV. = 7.3 DEGREES 1LPP 141
REMARK 36 0 THR 293 N - CA - C ANGL. DEV. = 11.7 DEGREES 1LPP 142
REMARK 36 0 PRO 294 N - CA - C ANGL. DEV. = 6.3 DEGREES 1LPP 143
REMARK 36 0 GLY 295 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPP 144
REMARK 36 0 PHE 296 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPP 145
REMARK 36 0 ARG 303 N - CA - C ANGL. DEV. = 12.4 DEGREES 1LPP 146
REMARK 36 0 LEU 304 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPP 147
REMARK 36 0 LEU 307 CA - CB - CG ANGL. DEV. = 7.1 DEGREES 1LPP 148
REMARK 36 0 ILE 315 N - CA - C ANGL. DEV. = 13.3 DEGREES 1LPP 149
REMARK 36 0 THR 316 N - CA - C ANGL. DEV. = 9.3 DEGREES 1LPP 150
REMARK 36 0 ASP 318 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPP 151
REMARK 36 0 ASP 318 N - CA - CB ANGL. DEV. = 6.2 DEGREES 1LPP 152
REMARK 36 0 GLU 325 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPP 153
REMARK 36 0 ALA 329 N - CA - C ANGL. DEV. = 6.2 DEGREES 1LPP 154
REMARK 36 0 ILE 334 N - CA - C ANGL. DEV. = 10.2 DEGREES 1LPP 155
REMARK 36 0 GLN 338 N - CA - C ANGL. DEV. = 10.5 DEGREES 1LPP 156
REMARK 36 0 GLY 342 N - CA - C ANGL. DEV. = 8.8 DEGREES 1LPP 157
REMARK 36 0 VAL 352 N - CA - C ANGL. DEV. = 9.0 DEGREES 1LPP 158
REMARK 36 0 TYR 381 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPP 159
REMARK 36 0 PRO 390 C-1 - N - CA ANGL. DEV. = 10.2 DEGREES 1LPP 160
REMARK 36 0 LEU 399 CA - CB - CG ANGL. DEV. = 7.4 DEGREES 1LPP 161
REMARK 36 0 THR 400 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPP 162
REMARK 36 0 LEU 410 CA - CB - CG ANGL. DEV. = 6.9 DEGREES 1LPP 163
REMARK 36 0 PHE 415 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPP 164
REMARK 36 0 THR 416 N - CA - C ANGL. DEV. = 9.8 DEGREES 1LPP 165
REMARK 36 0 TYR 432 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPP 166
REMARK 36 0 LEU 435 N - CA - C ANGL. DEV. = 6.3 DEGREES 1LPP 167
REMARK 36 0 LEU 445 N - CA - C ANGL. DEV. = 9.9 DEGREES 1LPP 168
REMARK 36 0 PHE 448 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPP 169
REMARK 36 0 SER 450 N - CA - C ANGL. DEV. = 6.2 DEGREES 1LPP 170
REMARK 36 0 ASP 457 N - CA - C ANGL. DEV. = 6.3 DEGREES 1LPP 171
REMARK 36 0 TYR 458 N - CA - C ANGL. DEV. = 7.6 DEGREES 1LPP 172
REMARK 36 0 LEU 502 CA - CB - CG ANGL. DEV. = 8.2 DEGREES 1LPP 173
REMARK 36 0 MET 503 N - CA - C ANGL. DEV. = 9.5 DEGREES 1LPP 174
REMARK 36 0 MET 504 CB - CG - SD ANGL. DEV. = 6.6 DEGREES 1LPP 175
REMARK 36 0 ASN 506 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPP 176
REMARK 36 0 LEU 525 CA - CB - CG ANGL. DEV. = 8.8 DEGREES 1LPP 177
REMARK 36 0 PHE 526 N - CA - C ANGL. DEV. = 10.8 DEGREES 1LPP 178
REMARK 36 0 ASN 528 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPP 179
REMARK 36 0 PRO 530 N - CA - C ANGL. DEV. = 6.3 DEGREES 1LPP 180
REMARK 36 1LPP 181
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPP 182
REMARK 36 1LPP 183
REMARK 36 SUBTOPIC: TORSION ANGLES (36.4) 1LPP 184
REMARK 36 1LPP 185
REMARK 36 STANDARD TEXT: 1LPP 186
REMARK 36 1LPP 187
REMARK 36 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: 1LPP 188
REMARK 36 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; 1LPP 189
REMARK 36 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPP 190
REMARK 36 1LPP 191
REMARK 36 STANDARD TABLE: 1LPP 192
REMARK 36 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) 1LPP 193
REMARK 36 1LPP 194
REMARK 36 M RES CSSEQI PSI PHI 1LPP 195
REMARK 36 1LPP 196
REMARK 36 0 ILE 18 71.57 -64.22 1LPP 197
REMARK 36 0 PHE 38 61.55 -0.90 1LPP 198
REMARK 36 0 THR 68 178.63 164.26 1LPP 199
REMARK 36 0 SER 159 61.60 -146.32 1LPP 200
REMARK 36 0 SER 209 49.73 -113.93 1LPP 201
REMARK 36 0 ALA 243 -123.55 -125.38 1LPP 202
REMARK 36 0 SER 301 56.60 -128.08 1LPP 203
REMARK 36 0 VAL 444 66.41 -50.97 1LPP 204
REMARK 36 0 SER 450 81.27 -9.42 1LPP 205
REMARK 999 1LPP 206
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1LPP 207
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPP 208
REMARK 999 LIP1_CANRU 1LPP 209
SEQRES 1 549 MET GLU LEU ALA LEU ALA LEU SER LEU ILE ALA SER VAL 1LPP 210
SEQRES 2 549 ALA ALA ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR 1LPP 211
SEQRES 3 549 ILE THR GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU 1LPP 212
SEQRES 4 549 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG 1LPP 213
SEQRES 5 549 PHE LYS ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY 1LPP 214
SEQRES 6 549 GLN LYS PHE THR SER TYR GLY PRO SER CYS MET GLN GLN 1LPP 215
SEQRES 7 549 ASN PRO GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA 1LPP 216
SEQRES 8 549 ALA LEU ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA 1LPP 217
SEQRES 9 549 VAL SER PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL 1LPP 218
SEQRES 10 549 VAL ARG PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO 1LPP 219
SEQRES 11 549 VAL MET LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY 1LPP 220
SEQRES 12 549 GLY THR SER THR PHE PRO PRO ALA GLN MET ILE THR LYS 1LPP 221
SEQRES 13 549 SER ILE ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL 1LPP 222
SEQRES 14 549 ASN TYR ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP 1LPP 223
SEQRES 15 549 GLU ILE LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS 1LPP 224
SEQRES 16 549 ASP GLN ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE 1LPP 225
SEQRES 17 549 ALA ALA PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE 1LPP 226
SEQRES 18 549 GLY GLU SER ALA GLY SER MET SER VAL MET CYS HIS ILE 1LPP 227
SEQRES 19 549 LEU TRP ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO 1LPP 228
SEQRES 20 549 LEU PHE ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL 1LPP 229
SEQRES 21 549 PRO SER ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE 1LPP 230
SEQRES 22 549 PHE ASP LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA 1LPP 231
SEQRES 23 549 SER ASP LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP 1LPP 232
SEQRES 24 549 THR LEU GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU 1LPP 233
SEQRES 25 549 ALA TYR SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO 1LPP 234
SEQRES 26 549 ASP GLY VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL 1LPP 235
SEQRES 27 549 ARG GLU GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY 1LPP 236
SEQRES 28 549 ASP GLN ASN ASP GLU GLY THR PHE PHE GLY THR SER SER 1LPP 237
SEQRES 29 549 LEU ASN VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE 1LPP 238
SEQRES 30 549 LYS GLN SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP 1LPP 239
SEQRES 31 549 THR LEU MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY 1LPP 240
SEQRES 32 549 SER PRO PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO 1LPP 241
SEQRES 33 549 GLN PHE LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY 1LPP 242
SEQRES 34 549 PHE THR LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR 1LPP 243
SEQRES 35 549 GLY GLY THR LYS TYR SER PHE LEU SER LYS GLN LEU SER 1LPP 244
SEQRES 36 549 GLY LEU PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE 1LPP 245
SEQRES 37 549 VAL PHE GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE 1LPP 246
SEQRES 38 549 TYR ASN ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP 1LPP 247
SEQRES 39 549 PRO ASN THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR 1LPP 248
SEQRES 40 549 THR SER SER SER GLN SER GLY ASN ASN LEU MET MET ILE 1LPP 249
SEQRES 41 549 ASN ALA LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG 1LPP 250
SEQRES 42 549 THR ALA GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER 1LPP 251
SEQRES 43 549 PHE PHE VAL 1LPP 252
FTNOTE 1 1LPP 253
FTNOTE 1 CIS PROLINE - PRO 390 1LPP 254
HET HDS 560 19 1-HEXADECANOSULFONIC ACID 1LPP 255
HET HDS 561 19 1-HEXADECANOSULFONIC ACID 1LPP 256
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1LPP 257
HET NAG 992 14 N-ACETYL-D-GLUCOSAMINE 1LPP 258
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1LPP 259
HET CA 589 1 CALCIUM ION 1LPP 260
HET CA 590 1 CALCIUM ION 1LPP 261
FORMUL 2 HDS 2(C16 H34 O3 S1) 1LPP 262
FORMUL 3 NAG 3(C8 H15 N1 O6) 1LPP 263
FORMUL 4 CA 2(CA1 2+) 1LPP 264
FORMUL 5 HOH *296(H2 O1) 1LPP 265
HELIX 1 1 GLY 34 LEU 36 5 1LPP 266
HELIX 2 2 LEU 73 MET 82 1 1LPP 267
HELIX 3 3 LYS 85 VAL 90 1 1LPP 268
HELIX 4 4 THR 130 THR 132 5 1LPP 269
HELIX 5 5 ALA 136 ALA 144 1 1LPP 270
HELIX 6 6 SER 159 PHE 163 1 1LPP 271
HELIX 7 7 ASP 167 GLU 172 1 1LPP 272
HELIX 8 8 ALA 177 PHE 196 1 1LPP 273
HELIX 9 9 SER 209 GLY 224 5 1LPP 274
HELIX 10 10 ILE 253 ALA 266 1 1LPP 275
HELIX 11 11 LYS 274 GLY 280 1 1LPP 276
HELIX 12 12 SER 283 ASN 292 1 1LPP 277
HELIX 13 13 MET 319 ARG 324 1 1LPP 278
HELIX 14 14 THR 343 SER 349 1 1LPP 279
HELIX 15 15 ASP 355 SER 365 1 1LPP 280
HELIX 16 16 ASP 371 ALA 380 1 1LPP 281
HELIX 17 17 PHE 403 GLY 414 1 1LPP 282
HELIX 18 18 THR 416 HIS 425 1 1LPP 283
HELIX 19 19 ASN 451 ASP 457 1 1LPP 284
HELIX 20 20 SER 462 TYR 467 5 1LPP 285
HELIX 21 21 ASN 469 ASP 477 1 1LPP 286
HELIX 22 22 PRO 480 ALA 483 5 1LPP 287
HELIX 23 23 THR 519 PHE 526 1 1LPP 288
HELIX 24 24 PRO 529 PHE 532 5 1LPP 289
SHEET 1 A 2 THR 3 THR 5 0 1LPP 290
SHEET 2 A 2 THR 11 THR 13 -1 N ILE 12 O ALA 4 1LPP 291
SHEET 1 B10 GLU 21 PHE 23 0 1LPP 292
SHEET 2 B10 ILE 100 ARG 104 -1 N ARG 104 O GLU 21 1LPP 293
SHEET 3 B10 ILE 149 VAL 154 -1 N SER 153 O ASN 101 1LPP 294
SHEET 4 B10 PRO 115 ILE 120 1 N PRO 115 O ILE 150 1LPP 295
SHEET 5 B10 VAL 203 GLU 208 1 N THR 204 O VAL 116 1LPP 296
SHEET 6 B10 ALA 236 GLN 240 1 N ALA 236 O ILE 205 1LPP 297
SHEET 7 B10 PRO 332 GLN 338 1 N PRO 332 O GLY 237 1LPP 298
SHEET 8 B10 LYS 431 SER 436 1 N TYR 432 O VAL 333 1LPP 299
SHEET 9 B10 LEU 502 ILE 505 1 N MET 503 O LEU 435 1LPP 300
SHEET 10 B10 LEU 510 GLY 513 -1 N GLY 513 O LEU 502 1LPP 301
SSBOND 1 CYS 60 CYS 97 1LPP 302
SSBOND 2 CYS 268 CYS 277 1LPP 303
CRYST1 65.100 97.400 176.200 90.00 90.00 90.00 C 2 2 21 8 1LPP 304
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPP 305
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPP 306
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPP 307
SCALE1 0.015361 0.000000 0.000000 0.00000 1LPP 308
SCALE2 0.000000 0.010267 0.000000 0.00000 1LPP 309
SCALE3 0.000000 0.000000 0.005675 0.00000 1LPP 310 |