| content |
HEADER HYDROLASE (CARBOXYLIC ESTERASE) 05-JAN-95 1LPS 1LPS 2
COMPND LIPASE (E.C.3.1.1.3) COMPLEXED WITH (1S)-MENTHYL HEXYL 1LPS 3
COMPND 2 PHOSPHONATE 1LPS 4
SOURCE YEAST (CANDIDA RUGOSA) (FORMERLY CANDIDA CYLINDRACEA) 1LPS 5
AUTHOR P.G.GROCHULSKI,M.C.CYGLER 1LPS 6
REVDAT 2 08-MAR-95 1LPSA 1 REMARK 1LPSA 1
REVDAT 1 14-FEB-95 1LPS 0 1LPS 7
JRNL AUTH M.CYGLER,P.GROCHULSKI,R.KAZLAUSKAS,J.D.SCHRAG, 1LPS 8
JRNL AUTH 2 F.BOUTHILLIER,B.RUBIN,A.N.SERREGI,A.K.GUPTA 1LPS 9
JRNL TITL A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF 1LPS 10
JRNL TITL 2 LIPASES 1LPS 11
JRNL REF J.AM.CHEM.SOC. V. 116 3180 1994 1LPS 12
JRNL REFN ASTM JACSAT US ISSN 0002-7863 0004 1LPS 13
REMARK 1 1LPS 14
REMARK 1 REFERENCE 1 1LPS 15
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,M.CYGLER 1LPS 16
REMARK 1 TITL TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE 1LPS 17
REMARK 1 REF PROTEIN SCI. V. 3 82 1994 1LPS 18
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 1LPS 19
REMARK 1 REFERENCE 2 1LPS 20
REMARK 1 AUTH P.GROCHULSKI,F.BOUTHILLIER,R.KAZLAUSKAS, 1LPS 21
REMARK 1 AUTH 2 A.N.SERREGI,J.D.SCHRAG,E.ZIOMEK,M.CYGLER 1LPS 22
REMARK 1 TITL ANALOGS OF REACTION INTERMEDIATES IDENTIFY A 1LPS 23
REMARK 1 TITL 2 UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA 1LPS 24
REMARK 1 TITL 3 LIPASE 1LPS 25
REMARK 1 REF BIOCHEMISTRY V. 33 3494 1994 1LPS 26
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1LPS 27
REMARK 1 REFERENCE 3 1LPS 28
REMARK 1 AUTH P.GROCHULSKI,Y.LI,J.D.SCHRAG,F.BOUTHILLIER,P.SMITH, 1LPSA 2
REMARK 1 AUTH 2 D.HARRISON,B.RUBIN,M.CYGLER 1LPSA 3
REMARK 1 TITL INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN OPEN 1LPS 30
REMARK 1 TITL 2 STRUCTURE OF CANDIDA RUGOSA LIPASE 1LPS 31
REMARK 1 REF J.BIOL.CHEM. V. 268 12843 1993 1LPS 32
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1LPS 33
REMARK 2 1LPS 34
REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1LPS 35
REMARK 3 1LPS 36
REMARK 3 REFINEMENT. 1LPS 37
REMARK 3 PROGRAM X-PLOR 1LPS 38
REMARK 3 AUTHORS BRUNGER 1LPS 39
REMARK 3 R VALUE 0.138 1LPS 40
REMARK 3 MEAN B VALUE 17.2 ANGSTROMS**2 1LPS 41
REMARK 3 NUMBER OF REFLECTIONS 18430 1LPS 42
REMARK 3 RESOLUTION RANGE 8. - 2.18 ANGSTROMS 1LPS 43
REMARK 3 DATA CUTOFF 4. SIGMA(F) 1LPS 44
REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1LPS 45
REMARK 3 RMSD BOND ANGLES 1.8 DEGREES 1LPS 46
REMARK 3 1LPS 47
REMARK 3 DATA COLLECTION. 1LPS 48
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 23942 1LPS 49
REMARK 3 COMPLETENESS OF DATA 80.4 % 1LPS 50
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1LPS 51
REMARK 3 1LPS 52
REMARK 3 SOLVENT CONTENT (VS) 48. % 1LPS 53
REMARK 3 1LPS 54
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1LPS 55
REMARK 3 NUMBER OF PROTEIN ATOMS 4022 1LPS 56
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1LPS 57
REMARK 3 NUMBER OF HETEROGEN ATOMS 63 1LPS 58
REMARK 3 NUMBER OF SOLVENT ATOMS 155 1LPS 59
REMARK 4 1LPS 60
REMARK 4 EXPERIMENTAL DETAILS 1LPS 61
REMARK 4 SINGLE CRYSTAL X-RAY DIFFRACTION 1LPS 62
REMARK 4 MONOCHROMATIC RADIATION 1LPS 63
REMARK 4 DATE OF DATA-COLLECTION (DD-MON-YY) : 12-05-93 1LPS 64
REMARK 4 WAVELENGTH OR WAVELENGTH RANGE : CUKA 1LPS 65
REMARK 4 DETECTOR TYPE/MANUFACTURER : RAXIS II 1LPS 66
REMARK 4 INTENSITY-INTEGRATION SOFTWARE : RAXIS SOFTWARE 1LPS 67
REMARK 4 DATA REDUNDANCY : 2.8 1LPS 68
REMARK 4 MERGING R-FACTOR (INTENSITY) : 8% 1LPS 69
REMARK 5 1LPS 70
REMARK 5 KEYWDS: CARBOXYLIC ESTERASE, CRL 1LPS 71
REMARK 6 1LPS 72
REMARK 6 CALCIUM CA 590 AND WATER HOH 756 ARE IN SPECIAL POSITIONS. 1LPS 73
REMARK 7 1LPS 74
REMARK 7 THE STARTING MATERIAL FOR THE INHIBITOR WAS 1LPS 75
REMARK 7 O-(1S,2R,5S)-MENTHYL HEXYLPHOSPHONOCHLORIDATE. BY THE 1LPS 76
REMARK 7 REACTION DESCRIBED IN THE JRNL REFERENCE ABOVE, THIS WAS 1LPS 77
REMARK 7 TURNED INTO (1S)-MENTHYL HEXYLPHOSPHONOCHLORIDATE, CALLED 1LPS 78
REMARK 7 1S-CRL. THE 1S-CRL COMPLEX WAS PREPARED BY DISSOLVING 1LPS 79
REMARK 7 1S-CRL INACTIVATOR IN MPD AND ADDING AN AQUEOUS SOULUTION 1LPS 80
REMARK 7 OF CRL. CRYSTALLIZATION PROCEEDED AS DESCRIBED IN THE JRNL 1LPS 81
REMARK 7 REFERENCE ABOVE. 1LPS 82
REMARK 8 1LPSA 4
REMARK 8 CORRECTION. CORRECT AUTHOR LIST FOR REFERENCE 3. 1LPSA 5
REMARK 8 08-MAR-95. 1LPSA 6
REMARK 36 1LPS 83
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPS 84
REMARK 36 1LPS 85
REMARK 36 SUBTOPIC: BOND LENGTHS (36.1) 1LPS 86
REMARK 36 1LPS 87
REMARK 36 STANDARD TEXT: 1LPS 88
REMARK 36 1LPS 89
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPS 90
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPS 91
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPS 92
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPS 93
REMARK 36 1LPS 94
REMARK 36 STANDARD TABLE: 1LPS 95
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,A4,3X,A4,16X,F5.1) 1LPS 96
REMARK 36 1LPS 97
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPS 98
REMARK 36 1LPS 99
REMARK 36 M RES CSSEQI ATM1 ATM2 DEVIATION_IN_ANGSTROMS 1LPS 100
REMARK 36 1LPS 101
REMARK 36 0 MET 61 SD - CE 0.052 1LPS 102
REMARK 36 0 MET 82 SD - CE 0.051 1LPS 103
REMARK 36 0 MET 138 SD - CE 0.063 1LPS 104
REMARK 36 0 ASN 155 CB - CG 0.045 1LPS 105
REMARK 36 0 MET 186 SD - CE 0.072 1LPS 106
REMARK 36 0 MET 244 SD - CE 0.067 1LPS 107
REMARK 36 0 MET 319 SD - CE 0.056 1LPS 108
REMARK 36 0 PRO 529 CB - CG 0.048 1LPS 109
REMARK 36 1LPS 110
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPS 111
REMARK 36 1LPS 112
REMARK 36 SUBTOPIC: COVALENT BOND ANGLES (36.2) 1LPS 113
REMARK 36 1LPS 114
REMARK 36 STANDARD TEXT: 1LPS 115
REMARK 36 1LPS 116
REMARK 36 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES 1LPS 117
REMARK 36 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE 1LPS 118
REMARK 36 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN 1LPS 119
REMARK 36 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPS 120
REMARK 36 1LPS 121
REMARK 36 STANDARD TABLE: 1LPS 122
REMARK 36 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(2X,A4,17X,F5.1) 1LPS 123
REMARK 36 1LPS 124
REMARK 36 EXPECTED VALUES: ENGH AND HUBER, 1991 1LPS 125
REMARK 36 1LPS 126
REMARK 36 M RES CSSEQI ATM1 ATM2 ATM3 1LPS 127
REMARK 36 1LPS 128
REMARK 36 0 ASN 16 N - CA - C ANGL. DEV. = 8.1 DEGREES 1LPS 129
REMARK 36 0 PHE 23 N - CA - C ANGL. DEV. = 9.0 DEGREES 1LPS 130
REMARK 36 0 SER 59 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPS 131
REMARK 36 0 LEU 80 CA - CB - CG ANGL. DEV. = 11.4 DEGREES 1LPS 132
REMARK 36 0 ASP 96 N - CA - C ANGL. DEV. = 8.7 DEGREES 1LPS 133
REMARK 36 0 LEU 118 CA - CB - CG ANGL. DEV. = 6.4 DEGREES 1LPS 134
REMARK 36 0 ILE 120 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPS 135
REMARK 36 0 SER 131 N - CA - C ANGL. DEV. = 6.8 DEGREES 1LPS 136
REMARK 36 0 ASN 155 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPS 137
REMARK 36 0 ASN 192 N - CA - C ANGL. DEV. = 10.3 DEGREES 1LPS 138
REMARK 36 0 TYR 228 N - CA - C ANGL. DEV. = 8.3 DEGREES 1LPS 139
REMARK 36 0 ILE 253 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPS 140
REMARK 36 0 ASN 256 N - CA - C ANGL. DEV. = 6.5 DEGREES 1LPS 141
REMARK 36 0 ASP 273 N - CA - C ANGL. DEV. = 7.0 DEGREES 1LPS 142
REMARK 36 0 THR 293 N - CA - C ANGL. DEV. = 11.7 DEGREES 1LPS 143
REMARK 36 0 PRO 294 N - CA - C ANGL. DEV. = 7.9 DEGREES 1LPS 144
REMARK 36 0 PHE 296 N - CA - C ANGL. DEV. = 7.0 DEGREES 1LPS 145
REMARK 36 0 LEU 307 CA - CB - CG ANGL. DEV. = 7.0 DEGREES 1LPS 146
REMARK 36 0 ILE 315 N - CA - C ANGL. DEV. = 17.4 DEGREES 1LPS 147
REMARK 36 0 THR 316 N - CA - C ANGL. DEV. = 10.0 DEGREES 1LPS 148
REMARK 36 0 ASP 318 N - CA - C ANGL. DEV. = 7.1 DEGREES 1LPS 149
REMARK 36 0 PRO 332 N - CA - C ANGL. DEV. = 7.0 DEGREES 1LPS 150
REMARK 36 0 ILE 334 N - CA - C ANGL. DEV. = 9.7 DEGREES 1LPS 151
REMARK 36 0 GLN 338 N - CA - C ANGL. DEV. = 10.8 DEGREES 1LPS 152
REMARK 36 0 GLY 342 N - CA - C ANGL. DEV. = 8.6 DEGREES 1LPS 153
REMARK 36 0 VAL 352 N - CA - C ANGL. DEV. = 9.3 DEGREES 1LPS 154
REMARK 36 0 GLY 388 N - CA - C ANGL. DEV. = 6.9 DEGREES 1LPS 155
REMARK 36 0 PRO 390 C-1 - N - CA ANGL. DEV. = 9.8 DEGREES 1LPS 156
REMARK 36 0 THR 400 N - CA - C ANGL. DEV. = 7.2 DEGREES 1LPS 157
REMARK 36 0 PHE 415 N - CA - C ANGL. DEV. = 7.3 DEGREES 1LPS 158
REMARK 36 0 THR 416 N - CA - C ANGL. DEV. = 10.2 DEGREES 1LPS 159
REMARK 36 0 LEU 445 N - CA - C ANGL. DEV. = 7.4 DEGREES 1LPS 160
REMARK 36 0 THR 447 N - CA - C ANGL. DEV. = 6.7 DEGREES 1LPS 161
REMARK 36 0 PHE 448 N - CA - C ANGL. DEV. = 9.8 DEGREES 1LPS 162
REMARK 36 0 ASP 457 N - CA - C ANGL. DEV. = 8.0 DEGREES 1LPS 163
REMARK 36 0 TYR 458 N - CA - C ANGL. DEV. = 8.9 DEGREES 1LPS 164
REMARK 36 0 LEU 460 CA - CB - CG ANGL. DEV. = 9.5 DEGREES 1LPS 165
REMARK 36 0 LEU 502 CA - CB - CG ANGL. DEV. = 8.4 DEGREES 1LPS 166
REMARK 36 0 MET 503 N - CA - C ANGL. DEV. = 10.9 DEGREES 1LPS 167
REMARK 36 0 LEU 525 N - CA - C ANGL. DEV. = 6.6 DEGREES 1LPS 168
REMARK 36 0 LEU 525 CA - CB - CG ANGL. DEV. = 12.1 DEGREES 1LPS 169
REMARK 36 0 PHE 526 N - CA - C ANGL. DEV. = 10.1 DEGREES 1LPS 170
REMARK 36 0 ASN 528 N - CA - C ANGL. DEV. = 7.7 DEGREES 1LPS 171
REMARK 36 0 PRO 530 N - CA - C ANGL. DEV. = 6.4 DEGREES 1LPS 172
REMARK 36 1LPS 173
REMARK 36 TOPIC: STEREOCHEMISTRY 1LPS 174
REMARK 36 1LPS 175
REMARK 36 SUBTOPIC: TORSION ANGLES (36.4) 1LPS 176
REMARK 36 1LPS 177
REMARK 36 STANDARD TEXT: 1LPS 178
REMARK 36 1LPS 179
REMARK 36 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: 1LPS 180
REMARK 36 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; 1LPS 181
REMARK 36 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). 1LPS 182
REMARK 36 1LPS 183
REMARK 36 STANDARD TABLE: 1LPS 184
REMARK 36 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) 1LPS 185
REMARK 36 1LPS 186
REMARK 36 M RES CSSEQI PSI PHI 1LPS 187
REMARK 36 1LPS 188
REMARK 36 0 ILE 18 73.27 -66.05 1LPS 189
REMARK 36 0 PHE 38 59.43 -4.68 1LPS 190
REMARK 36 0 THR 68 177.78 160.96 1LPS 191
REMARK 36 0 SER 159 63.43 -146.64 1LPS 192
REMARK 36 0 SER 209 61.95 -115.41 1LPS 193
REMARK 36 0 ALA 243 -129.69 -124.47 1LPS 194
REMARK 36 0 SER 301 52.90 -126.76 1LPS 195
REMARK 36 0 VAL 444 67.07 -52.29 1LPS 196
REMARK 36 0 SER 450 101.29 -22.65 1LPS 197
REMARK 999 1LPS 198
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1LPS 199
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1LPS 200
REMARK 999 LIP1_CANRU 1LPS 201
REMARK 999 1LPS 202
REMARK 999 THE FOLLOWING RESIDUES ARE MISSING FROM THE N-TERMINUS 1LPS 203
REMARK 999 SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1LPS 204
REMARK 999 MET 1 1LPS 205
REMARK 999 GLU 2 1LPS 206
REMARK 999 LEU 3 1LPS 207
REMARK 999 ALA 4 1LPS 208
REMARK 999 LEU 5 1LPS 209
REMARK 999 ALA 6 1LPS 210
REMARK 999 LEU 7 1LPS 211
REMARK 999 SER 8 1LPS 212
REMARK 999 LEU 9 1LPS 213
REMARK 999 ILE 10 1LPS 214
REMARK 999 ALA 11 1LPS 215
REMARK 999 SER 12 1LPS 216
REMARK 999 VAL 13 1LPS 217
REMARK 999 ALA 14 1LPS 218
REMARK 999 ALA 15 1LPS 219
SEQRES 1 549 MET GLU LEU ALA LEU ALA LEU SER LEU ILE ALA SER VAL 1LPS 220
SEQRES 2 549 ALA ALA ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR 1LPS 221
SEQRES 3 549 ILE THR GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU 1LPS 222
SEQRES 4 549 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG 1LPS 223
SEQRES 5 549 PHE LYS ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY 1LPS 224
SEQRES 6 549 GLN LYS PHE THR SER TYR GLY PRO SER CYS MET GLN GLN 1LPS 225
SEQRES 7 549 ASN PRO GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA 1LPS 226
SEQRES 8 549 ALA LEU ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA 1LPS 227
SEQRES 9 549 VAL SER PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL 1LPS 228
SEQRES 10 549 VAL ARG PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO 1LPS 229
SEQRES 11 549 VAL MET LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY 1LPS 230
SEQRES 12 549 GLY THR SER THR PHE PRO PRO ALA GLN MET ILE THR LYS 1LPS 231
SEQRES 13 549 SER ILE ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL 1LPS 232
SEQRES 14 549 ASN TYR ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP 1LPS 233
SEQRES 15 549 GLU ILE LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS 1LPS 234
SEQRES 16 549 ASP GLN ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE 1LPS 235
SEQRES 17 549 ALA ALA PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE 1LPS 236
SEQRES 18 549 GLY GLU SER ALA GLY SER MET SER VAL MET CYS HIS ILE 1LPS 237
SEQRES 19 549 LEU TRP ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO 1LPS 238
SEQRES 20 549 LEU PHE ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL 1LPS 239
SEQRES 21 549 PRO SER ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE 1LPS 240
SEQRES 22 549 PHE ASP LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA 1LPS 241
SEQRES 23 549 SER ASP LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP 1LPS 242
SEQRES 24 549 THR LEU GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU 1LPS 243
SEQRES 25 549 ALA TYR SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO 1LPS 244
SEQRES 26 549 ASP GLY VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL 1LPS 245
SEQRES 27 549 ARG GLU GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY 1LPS 246
SEQRES 28 549 ASP GLN ASN ASP GLU GLY THR PHE PHE GLY THR SER SER 1LPS 247
SEQRES 29 549 LEU ASN VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE 1LPS 248
SEQRES 30 549 LYS GLN SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP 1LPS 249
SEQRES 31 549 THR LEU MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY 1LPS 250
SEQRES 32 549 SER PRO PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO 1LPS 251
SEQRES 33 549 GLN PHE LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY 1LPS 252
SEQRES 34 549 PHE THR LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR 1LPS 253
SEQRES 35 549 GLY GLY THR LYS TYR SER PHE LEU SER LYS GLN LEU SER 1LPS 254
SEQRES 36 549 GLY LEU PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE 1LPS 255
SEQRES 37 549 VAL PHE GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE 1LPS 256
SEQRES 38 549 TYR ASN ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP 1LPS 257
SEQRES 39 549 PRO ASN THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR 1LPS 258
SEQRES 40 549 THR SER SER SER GLN SER GLY ASN ASN LEU MET MET ILE 1LPS 259
SEQRES 41 549 ASN ALA LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG 1LPS 260
SEQRES 42 549 THR ALA GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER 1LPS 261
SEQRES 43 549 PHE PHE VAL 1LPS 262
FTNOTE 1 1LPS 263
FTNOTE 1 CIS PROLINE - PRO 390 1LPS 264
HET MPC 560 19 (1S)-MENTHYL HEXYL PHOSPHONATE 1LPS 265
HET NAG 991 14 N-ACETYL-D-GLUCOSAMINE 1LPS 266
HET NAG 992 14 N-ACETYL-D-GLUCOSAMINE 1LPS 267
HET NAG 994 14 N-ACETYL-D-GLUCOSAMINE 1LPS 268
HET CA 589 1 CALCIUM +2 COUNTER ION 1LPS 269
HET CA 590 1 CALCIUM +2 COUNTER ION 1LPS 270
FORMUL 2 MPC C16 H32 O2 P1 1LPS 271
FORMUL 3 NAG 3(C8 H15 N1 O6) 1LPS 272
FORMUL 4 CA 2(CA1 ++) 1LPS 273
FORMUL 5 HOH *155(H2 O1) 1LPS 274
HELIX 1 1 GLY 34 LEU 36 5 1LPS 275
HELIX 2 2 LEU 73 MET 82 1 1LPS 276
HELIX 3 3 LYS 85 VAL 90 1 1LPS 277
HELIX 4 4 THR 130 THR 132 5 1LPS 278
HELIX 5 5 ALA 136 ALA 144 1 1LPS 279
HELIX 6 6 SER 159 PHE 163 1 1LPS 280
HELIX 7 7 ASP 167 GLU 172 1 1LPS 281
HELIX 8 8 ALA 177 PHE 196 1 1LPS 282
HELIX 9 9 ALA 210 GLY 224 1 1LPS 283
HELIX 10 10 ILE 253 ALA 266 1 1LPS 284
HELIX 11 11 LYS 274 GLY 280 1 1LPS 285
HELIX 12 12 SER 283 ASN 292 1 1LPS 286
HELIX 13 13 MET 319 ARG 324 1 1LPS 287
HELIX 14 14 PHE 345 SER 349 5 1LPS 288
HELIX 15 15 ASP 355 SER 365 1 1LPS 289
HELIX 16 16 ASP 371 ALA 380 1 1LPS 290
HELIX 17 17 PHE 403 GLY 414 1 1LPS 291
HELIX 18 18 THR 416 HIS 425 1 1LPS 292
HELIX 19 19 ASN 451 ASP 457 1 1LPS 293
HELIX 20 20 SER 462 TYR 467 5 1LPS 294
HELIX 21 21 ASN 469 ASP 477 1 1LPS 295
HELIX 22 22 PRO 480 ALA 483 5 1LPS 296
HELIX 23 23 THR 519 PHE 526 1 1LPS 297
HELIX 24 24 PRO 529 PHE 532 5 1LPS 298
SHEET 1 A 2 THR 3 THR 5 0 1LPS 299
SHEET 2 A 2 THR 11 THR 13 -1 N ILE 12 O ALA 4 1LPS 300
SHEET 1 B10 GLU 21 PHE 23 0 1LPS 301
SHEET 2 B10 ILE 100 ARG 104 -1 N ARG 104 O GLU 21 1LPS 302
SHEET 3 B10 ILE 149 VAL 154 -1 N SER 153 O ASN 101 1LPS 303
SHEET 4 B10 PRO 115 ILE 120 1 N PRO 115 O ILE 150 1LPS 304
SHEET 5 B10 VAL 203 GLU 208 1 N THR 204 O VAL 116 1LPS 305
SHEET 6 B10 ALA 236 GLN 240 1 N ALA 236 O ILE 205 1LPS 306
SHEET 7 B10 PRO 332 GLN 338 1 N PRO 332 O GLY 237 1LPS 307
SHEET 8 B10 LYS 431 SER 436 1 N TYR 432 O VAL 333 1LPS 308
SHEET 9 B10 LEU 502 ILE 505 1 N MET 503 O SER 433 1LPS 309
SHEET 10 B10 LEU 510 GLY 513 -1 N GLY 513 O LEU 502 1LPS 310
SSBOND 1 CYS 60 CYS 97 1LPS 311
SSBOND 2 CYS 268 CYS 277 1LPS 312
CRYST1 65.100 97.700 176.100 90.00 90.00 90.00 C 2 2 21 8 1LPS 313
ORIGX1 1.000000 0.000000 0.000000 0.00000 1LPS 314
ORIGX2 0.000000 1.000000 0.000000 0.00000 1LPS 315
ORIGX3 0.000000 0.000000 1.000000 0.00000 1LPS 316
SCALE1 0.015361 0.000000 0.000000 0.00000 1LPS 317
SCALE2 0.000000 0.010235 0.000000 0.00000 1LPS 318
SCALE3 0.000000 0.000000 0.005679 0.00000 1LPS 319 |