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HEADER HYDROLASE 06-JAN-95 1LPM 1LPM 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL LIPASE) COMPLEXED WITH 1LPM 3
COMPND 2 (1R)-MENTHYL HEXYL PHOSPHONATE 1LPM 4
SOURCE YEAST (CANDIDA RUGOSA) (FORMERLY CANDIDA CYLINDRACEA) 1LPM 5
AUTHOR P.G.GROCHULSKI,M.C.CYGLER 1LPM 6
REVDAT 1 20-APR-95 1LPM 0 1LPM 7
JRNL AUTH M.CYGLER,P.GROCHULSKI,R.J.KAZLAUSKAS,J.D.SCHRAG, 1LPM 8
JRNL AUTH 2 F.BOUTHILLIER,B.RUBIN,A.N.SERREGI,A.K.GUPTA 1LPM 9
JRNL TITL A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF 1LPM 10
JRNL TITL 2 LIPASES 1LPM 11
JRNL REF J.AM.CHEM.SOC. V. 116 3180 1994 1LPM 12
JRNL REFN ASTM JACSAT US ISSN 0002-7863 0004 1LPM 13
REMARK 1 1LPM 14
REMARK 1 REFERENCE 1 1LPM 15
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,M.CYGLER 1LPM 16
REMARK 1 TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE 1LPM 17
REMARK 1 REF PROTEIN SCI. V. 3 82 1994 1LPM 18
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1LPM 19
REMARK 1 REFERENCE 2 1LPM 20
REMARK 1 AUTH P.GROCHULSKI,F.BOUTHILLIER,R.J.KAZLAUSKAS, 1LPM 21
REMARK 1 AUTH 2 A.N.SERREGI,J.D.SCHRAG,E.ZIOMEK,M.CYGLER 1LPM 22
REMARK 1 TITL ANALOGS OF REACTION INTERMEDIATES IDENTIFY A 1LPM 23
REMARK 1 TITL 2 UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA 1LPM 24
REMARK 1 TITL 3 LIPASE 1LPM 25
REMARK 1 REF BIOCHEMISTRY V. 33 3494 1994 1LPM 26
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1LPM 27
REMARK 1 REFERENCE 3 1LPM 28
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1LPM 29
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1LPM 30
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1LPM 31
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1LPM 32
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1LPM 33
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1LPM 34
REMARK 2 1LPM 35
REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1LPM 36
REMARK 3 1LPM 37
REMARK 3 REFINEMENT. 1LPM 38
REMARK 3 PROGRAM X-PLOR 1LPM 39
REMARK 3 AUTHORS BRUNGER 1LPM 40
REMARK 3 R VALUE 0.139 1LPM 41
REMARK 3 MEAN B VALUE 21.1 ANGSTROMS**2 1LPM 42
REMARK 3 NUMBER OF REFLECTIONS 19378 1LPM 43
REMARK 3 RESOLUTION RANGE 8. - 2.18 ANGSTROMS 1LPM 44
REMARK 3 DATA CUTOFF 4. SIGMA(F) 1LPM 45
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1LPM 46
REMARK 3 RMSD BOND ANGLES 1.82 DEGREES 1LPM 47
REMARK 3 1LPM 48
REMARK 3 DATA COLLECTION. 1LPM 49
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 25316 1LPM 50
REMARK 3 COMPLETENESS OF DATA 84.8 % 1LPM 51
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1LPM 52
REMARK 3 1LPM 53
REMARK 3 SOLVENT CONTENT (VS) 48. % 1LPM 54
REMARK 3 1LPM 55
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LPM 56
REMARK 3 NUMBER OF PROTEIN ATOMS 4022 1LPM 57
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LPM 58
REMARK 3 NUMBER OF HETEROGEN ATOMS 63 1LPM 59
REMARK 3 NUMBER OF SOLVENT ATOMS 261 1LPM 60
REMARK 4 1LPM 61
REMARK 4 EXPERIMENTAL DETAILS 1LPM 62
REMARK 4 SINGLE CRYSTAL X-RAY DIFFRACTION 1LPM 63
REMARK 4 MONOCHROMATIC RADIATION 1LPM 64
REMARK 4 DATE OF DATA-COLLECTION (DD-MON-YY) : 29-04-93 1LPM 65
REMARK 4 WAVELENGTH OR WAVELENGTH RANGE : CUKA 1LPM 66
REMARK 4 DETECTOR TYPE/MANUFACTURER : RAXIS II 1LPM 67
REMARK 4 INTENSITY-INTEGRATION SOFTWARE : RAXIS SOFTWARE 1LPM 68
REMARK 4 DATA REDUNDANCY : 2.7 1LPM 69
REMARK 5 1LPM 70
REMARK 5 KEYWDS: CARBOXYLIC ESTERASE, CRL 1LPM 71
REMARK 6 1LPM 72
REMARK 6 SOURCE 1LPM 73
REMARK 6 MOLECULE_NAME: O-(1R,2S,5R)-MENTHYL 1LPM 74
REMARK 6 HEXYLPHOSPHONOCHLORIDATE. AFTER REACTION WITH CRL LIPASE 1LPM 75
REMARK 6 THE MOLECULE FOUND IN THE CRYSTAL IS, (1R)-MENTHYL HEXYL 1LPM 76
REMARK 6 PHOSPHONATE COMPLEX. 1LPM 77
REMARK 7 1LPM 78
REMARK 7 CA 590 AND WATER HOH 834 ARE IN SPECIAL POSITIONS. 1LPM 79
REMARK 36 1LPM 80
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPM 81
REMARK 36 1LPM 82
REMARK 36 SUBTOPIC: BOND LENGTHS (36.1) 1LPM 83
REMARK 36 1LPM 84
REMARK 36 STANDARD TEXT: 1LPM 85
REMARK 36 1LPM 86
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPM 87
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPM 88
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPM 89
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPM 90
REMARK 36 1LPM 91
REMARK 36 STANDARD TABLE: 1LPM 92
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,A4,3X,A4,16X,F5.1) 1LPM 93
REMARK 36 1LPM 94
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPM 95
REMARK 36 1LPM 96
REMARK 36 M RES CSSEQI ATM1 ATM2 DEVIATION_IN_ANGSTROMS 1LPM 97
REMARK 36 1LPM 98
REMARK 36 0 THR 11 CB - CA 0.042 1LPM 99
REMARK 36 0 MET 61 SD - CE 0.044 1LPM 100
REMARK 36 0 MET 82 SD - CE 0.053 1LPM 101
REMARK 36 0 ILE 100 CB - CA 0.043 1LPM 102
REMARK 36 0 LYS 141 CD - CE 0.050 1LPM 103
REMARK 36 0 MET 145 SD - CE 0.048 1LPM 104
REMARK 36 0 ILE 149 CB - CA 0.048 1LPM 105
REMARK 36 0 MET 319 SD - CE 0.059 1LPM 106
REMARK 36 0 VAL 333 CB - CA 0.057 1LPM 107
REMARK 36 0 GLU 341 CG - CD 0.043 1LPM 108
REMARK 36 0 MET 503 SD - CE 0.053 1LPM 109
REMARK 36 1LPM 110
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPM 111
REMARK 36 1LPM 112
REMARK 36 SUBTOPIC: COVALENT BOND ANGLES (36.2) 1LPM 113
REMARK 36 1LPM 114
REMARK 36 STANDARD TEXT: 1LPM 115
REMARK 36 1LPM 116
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPM 117
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPM 118
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPM 119
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPM 120
REMARK 36 1LPM 121
REMARK 36 STANDARD TABLE: 1LPM 122
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(2X,A4,17X,F5.1) 1LPM 123
REMARK 36 1LPM 124
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPM 125
REMARK 36 1LPM 126
REMARK 36 M RES CSSEQI ATM1 ATM2 ATM3 1LPM 127
REMARK 36 1LPM 128
REMARK 36 0 ASN 16 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPM 129
REMARK 36 0 PHE 23 N - CA - C ANGL. DEV. = 8.3 DEGREES 1LPM 130
REMARK 36 0 GLY 25 N - CA - C ANGL. DEV. = 7.8 DEGREES 1LPM 131
REMARK 36 0 SER 59 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPM 132
REMARK 36 0 GLU 71 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPM 133
REMARK 36 0 LEU 80 CA - CB - CG ANGL. DEV. = 13.5 DEGREES 1LPM 134
REMARK 36 0 ASP 96 N - CA - C ANGL. DEV. = 11.1 DEGREES 1LPM 135
REMARK 36 0 LEU 118 CA - CB - CG ANGL. DEV. = 7.0 DEGREES 1LPM 136
REMARK 36 0 ASN 155 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPM 137
REMARK 36 0 GLY 162 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPM 138
REMARK 36 0 ASP 181 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPM 139
REMARK 36 0 ASN 192 N - CA - C ANGL. DEV. = 10.3 DEGREES 1LPM 140
REMARK 36 0 TYR 228 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPM 141
REMARK 36 0 VAL 245 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPM 142
REMARK 36 0 LEU 278 CA - CB - CG ANGL. DEV. = 7.2 DEGREES 1LPM 143
REMARK 36 0 THR 293 N - CA - C ANGL. DEV. = 11.1 DEGREES 1LPM 144
REMARK 36 0 PRO 294 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPM 145
REMARK 36 0 PHE 296 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPM 146
REMARK 36 0 ARG 303 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPM 147
REMARK 36 0 LEU 304 CA - CB - CG ANGL. DEV. = 6.5 DEGREES 1LPM 148
REMARK 36 0 LEU 307 CA - CB - CG ANGL. DEV. = 6.6 DEGREES 1LPM 149
REMARK 36 0 ILE 315 N - CA - C ANGL. DEV. = 15.9 DEGREES 1LPM 150
REMARK 36 0 THR 316 N - CA - C ANGL. DEV. = 9.4 DEGREES 1LPM 151
REMARK 36 0 PRO 332 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPM 152
REMARK 36 0 ILE 334 N - CA - C ANGL. DEV. = 11.4 DEGREES 1LPM 153
REMARK 36 0 GLN 338 N - CA - C ANGL. DEV. = 9.4 DEGREES 1LPM 154
REMARK 36 0 GLY 342 N - CA - C ANGL. DEV. = 9.9 DEGREES 1LPM 155
REMARK 36 0 VAL 352 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPM 156
REMARK 36 0 THR 379 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPM 157
REMARK 36 0 TYR 381 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPM 158
REMARK 36 0 PRO 390 C-1 - N - CA ANGL. DEV. = 10.6 DEGREES 1LPM 159
REMARK 36 0 LEU 399 CA - CB - CG ANGL. DEV. = 7.7 DEGREES 1LPM 160
REMARK 36 0 THR 400 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPM 161
REMARK 36 0 PHE 415 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPM 162
REMARK 36 0 THR 416 N - CA - C ANGL. DEV. = 11.5 DEGREES 1LPM 163
REMARK 36 0 LYS 437 N - CA - C ANGL. DEV. = 7.0 DEGREES 1LPM 164
REMARK 36 0 VAL 444 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPM 165
REMARK 36 0 LEU 445 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPM 166
REMARK 36 0 THR 447 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPM 167
REMARK 36 0 PHE 448 N - CA - C ANGL. DEV. = 9.5 DEGREES 1LPM 168
REMARK 36 0 SER 450 N - CA - C ANGL. DEV. = 7.5 DEGREES 1LPM 169
REMARK 36 0 TYR 458 N - CA - C ANGL. DEV. = 8.4 DEGREES 1LPM 170
REMARK 36 0 LEU 460 CA - CB - CG ANGL. DEV. = 8.8 DEGREES 1LPM 171
REMARK 36 0 GLY 461 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPM 172
REMARK 36 0 ASN 469 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPM 173
REMARK 36 0 ASP 477 N - CA - C ANGL. DEV. = 8.2 DEGREES 1LPM 174
REMARK 36 0 ASP 479 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPM 175
REMARK 36 0 SER 498 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPM 176
REMARK 36 0 LEU 502 CA - CB - CG ANGL. DEV. = 10.1 DEGREES 1LPM 177
REMARK 36 0 MET 503 N - CA - C ANGL. DEV. = 10.2 DEGREES 1LPM 178
REMARK 36 0 LEU 525 CA - CB - CG ANGL. DEV. = 11.5 DEGREES 1LPM 179
REMARK 36 0 PHE 526 N - CA - C ANGL. DEV. = 9.8 DEGREES 1LPM 180
REMARK 36 0 ASN 528 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPM 181
REMARK 36 1LPM 182
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPM 183
REMARK 36 1LPM 184
REMARK 36 SUBTOPIC: TORSION ANGLES (36.4) 1LPM 185
REMARK 36 1LPM 186
REMARK 36 STANDARD TEXT: 1LPM 187
REMARK 36 1LPM 188
REMARK 36 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: 1LPM 189
REMARK 36 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; 1LPM 190
REMARK 36 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPM 191
REMARK 36 1LPM 192
REMARK 36 STANDARD TABLE: 1LPM 193
REMARK 36 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) 1LPM 194
REMARK 36 1LPM 195
REMARK 36 M RES CSSEQI PSI PHI 1LPM 196
REMARK 36 1LPM 197
REMARK 36 0 ILE 18 77.14 -64.09 1LPM 198
REMARK 36 0 THR 68 176.21 161.57 1LPM 199
REMARK 36 0 SER 159 58.49 -151.59 1LPM 200
REMARK 36 0 SER 209 55.99 -110.72 1LPM 201
REMARK 36 0 ALA 243 -113.98 -122.49 1LPM 202
REMARK 36 0 SER 301 54.36 -132.48 1LPM 203
REMARK 36 0 VAL 444 63.07 -49.91 1LPM 204
REMARK 36 0 SER 450 86.17 -5.14 1LPM 205
REMARK 999 1LPM 206
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1LPM 207
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPM 208
REMARK 999 LIP1_CANRU 1LPM 209
SEQRES 1 549 MET GLU LEU ALA LEU ALA LEU SER LEU ILE ALA SER VAL 1LPM 210
SEQRES 2 549 ALA ALA ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR 1LPM 211
SEQRES 3 549 ILE THR GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU 1LPM 212
SEQRES 4 549 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG 1LPM 213
SEQRES 5 549 PHE LYS ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY 1LPM 214
SEQRES 6 549 GLN LYS PHE THR SER TYR GLY PRO SER CYS MET GLN GLN 1LPM 215
SEQRES 7 549 ASN PRO GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA 1LPM 216
SEQRES 8 549 ALA LEU ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA 1LPM 217
SEQRES 9 549 VAL SER PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL 1LPM 218
SEQRES 10 549 VAL ARG PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO 1LPM 219
SEQRES 11 549 VAL MET LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY 1LPM 220
SEQRES 12 549 GLY THR SER THR PHE PRO PRO ALA GLN MET ILE THR LYS 1LPM 221
SEQRES 13 549 SER ILE ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL 1LPM 222
SEQRES 14 549 ASN TYR ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP 1LPM 223
SEQRES 15 549 GLU ILE LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS 1LPM 224
SEQRES 16 549 ASP GLN ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE 1LPM 225
SEQRES 17 549 ALA ALA PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE 1LPM 226
SEQRES 18 549 GLY GLU SER ALA GLY SER MET SER VAL MET CYS HIS ILE 1LPM 227
SEQRES 19 549 LEU TRP ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO 1LPM 228
SEQRES 20 549 LEU PHE ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL 1LPM 229
SEQRES 21 549 PRO SER ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE 1LPM 230
SEQRES 22 549 PHE ASP LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA 1LPM 231
SEQRES 23 549 SER ASP LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP 1LPM 232
SEQRES 24 549 THR LEU GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU 1LPM 233
SEQRES 25 549 ALA TYR SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO 1LPM 234
SEQRES 26 549 ASP GLY VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL 1LPM 235
SEQRES 27 549 ARG GLU GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY 1LPM 236
SEQRES 28 549 ASP GLN ASN ASP GLU GLY THR PHE PHE GLY THR SER SER 1LPM 237
SEQRES 29 549 LEU ASN VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE 1LPM 238
SEQRES 30 549 LYS GLN SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP 1LPM 239
SEQRES 31 549 THR LEU MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY 1LPM 240
SEQRES 32 549 SER PRO PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO 1LPM 241
SEQRES 33 549 GLN PHE LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY 1LPM 242
SEQRES 34 549 PHE THR LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR 1LPM 243
SEQRES 35 549 GLY GLY THR LYS TYR SER PHE LEU SER LYS GLN LEU SER 1LPM 244
SEQRES 36 549 GLY LEU PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE 1LPM 245
SEQRES 37 549 VAL PHE GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE 1LPM 246
SEQRES 38 549 TYR ASN ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP 1LPM 247
SEQRES 39 549 PRO ASN THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR 1LPM 248
SEQRES 40 549 THR SER SER SER GLN SER GLY ASN ASN LEU MET MET ILE 1LPM 249
SEQRES 41 549 ASN ALA LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG 1LPM 250
SEQRES 42 549 THR ALA GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER 1LPM 251
SEQRES 43 549 PHE PHE VAL 1LPM 252
FTNOTE 1 1LPM 253
FTNOTE 1 CIS PROLINE - PRO 390 1LPM 254
HET MPA 560 19 (1R)-MENTHYL HEXYL PHOSPHONATE 1LPM 255
HET CA 589 1 CALCIUM ION 1LPM 256
HET CA 590 1 CALCIUM ION 1LPM 257
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1LPM 258
HET NAG 992 14 N-ACETYL-D-GLUCOSAMINE 1LPM 259
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1LPM 260
FORMUL 2 MPA C16 H32 O2 P1 1LPM 261
FORMUL 3 CA 2(CA1 2+) 1LPM 262
FORMUL 4 NAG 3(C8 H15 N1 O6) 1LPM 263
FORMUL 5 HOH *261(H2 O1) 1LPM 264
HELIX 1 1 GLY 34 LEU 36 5 1LPM 265
HELIX 2 2 LEU 73 MET 82 1 1LPM 266
HELIX 3 3 LYS 85 VAL 90 1 1LPM 267
HELIX 4 4 THR 130 THR 132 5 1LPM 268
HELIX 5 5 ALA 136 ALA 144 1 1LPM 269
HELIX 6 6 SER 159 PHE 163 1 1LPM 270
HELIX 7 7 ASP 167 GLU 172 1 1LPM 271
HELIX 8 8 ALA 177 PHE 196 1 1LPM 272
HELIX 9 9 ALA 210 GLY 224 1 1LPM 273
HELIX 10 10 ILE 253 ALA 266 1 1LPM 274
HELIX 11 11 LYS 274 GLY 280 1 1LPM 275
HELIX 12 12 SER 283 ASN 291 1 1LPM 276
HELIX 13 13 MET 319 ARG 324 1 1LPM 277
HELIX 14 14 THR 343 SER 349 1 1LPM 278
HELIX 15 15 ASP 355 SER 365 1 1LPM 279
HELIX 16 16 ASP 371 ALA 380 1 1LPM 280
HELIX 17 17 ILE 385 GLN 387 5 1LPM 281
HELIX 18 18 PHE 403 GLY 414 1 1LPM 282
HELIX 19 19 THR 416 HIS 425 1 1LPM 283
HELIX 20 20 ASN 451 ASP 457 1 1LPM 284
HELIX 21 21 SER 462 TYR 467 5 1LPM 285
HELIX 22 22 ASN 469 ASP 477 1 1LPM 286
HELIX 23 23 PRO 480 ALA 483 5 1LPM 287
HELIX 24 24 THR 519 PHE 526 1 1LPM 288
HELIX 25 25 PRO 529 PHE 532 5 1LPM 289
SHEET 1 A 2 THR 3 THR 5 0 1LPM 290
SHEET 2 A 2 THR 11 THR 13 -1 N ILE 12 O ALA 4 1LPM 291
SHEET 1 B10 GLU 21 PHE 23 0 1LPM 292
SHEET 2 B10 ILE 100 ARG 104 -1 N ARG 104 O GLU 21 1LPM 293
SHEET 3 B10 ILE 149 VAL 154 -1 N SER 153 O ASN 101 1LPM 294
SHEET 4 B10 PRO 115 ILE 120 1 N PRO 115 O ILE 150 1LPM 295
SHEET 5 B10 VAL 203 GLU 208 1 N THR 204 O VAL 116 1LPM 296
SHEET 6 B10 ALA 236 GLN 240 1 N ALA 236 O ILE 205 1LPM 297
SHEET 7 B10 PRO 332 GLN 338 1 N PRO 332 O GLY 237 1LPM 298
SHEET 8 B10 LYS 431 SER 436 1 N TYR 432 O VAL 333 1LPM 299
SHEET 9 B10 LEU 502 ILE 505 1 N MET 503 O LEU 435 1LPM 300
SHEET 10 B10 LEU 510 GLY 513 -1 N GLY 513 O LEU 502 1LPM 301
SSBOND 1 CYS 60 CYS 97 1LPM 302
SSBOND 2 CYS 268 CYS 277 1LPM 303
CRYST1 65.200 97.500 176.300 90.00 90.00 90.00 C 2 2 21 8 1LPM 304
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPM 305
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPM 306
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPM 307
SCALE1 0.015337 0.000000 0.000000 0.00000 1LPM 308
SCALE2 0.000000 0.010256 0.000000 0.00000 1LPM 309
SCALE3 0.000000 0.000000 0.005672 0.00000 1LPM 310 |