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HEADER MEMBRANE PROTEIN 01-AUG-23 8K9Q
TITLE CRYO-EM STRUCTURE OF THE GPI INOSITOL-DEACYLASE (PGAP1/BST1) FROM
TITLE 2 CHAETOMIUM THERMOPHILUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GPI INOSITOL-DEACYLASE,FUSED THERMOSTABLE GREEN FLUORESCENT
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.1.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE PROTEIN IS A FUSION PROTEIN WITH EXPRESSION TAG.
COMPND 8 RESIDUES 1187-1196 IS THE LINKER WITH A 3 C PROTEASE DIGESTION SITE.
COMPND 9 RESIDUES 1197-1427 IS A FUSED THERMOSTABLE GREEN FLUORESCENT PROTEIN
COMPND 10 (PDB ENTRY 4TZA, RESIDUE 5-229). RESIDUES 1428-1469 IS THE LINKER A
COMPND 11 STREP II TAG AND A HIS TAG.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS
SOURCE 3 144.50 / IMI 039719), SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_COMMON: THERMOCHAETOIDES THERMOPHILA;
SOURCE 5 ORGANISM_TAXID: 759272, 32630;
SOURCE 6 GENE: CTHT_0034210;
SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS BST1, GLYCOSYLPHOSPHATIDYLINOSITOL, GPI ANCHORING, GPI-AP, GPI-AP
KEYWDS 2 REMODELASE, INTEGRAL MEMBRANE ENZYME, LIPASE, LIPID REMODELING,
KEYWDS 3 MEMBRANE ENZYME, MEMBRANE PROTEIN, NANODISC, PGAP1, TRANSMEMBRANE
KEYWDS 4 ENZYME, TRIAD ENZYME
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.HONG,T.LI,Q.QU,D.LI
REVDAT 1 20-DEC-23 8K9Q 0
JRNL AUTH D.LI,Q.QU,J.HONG
JRNL TITL STRUCTURAL INSIGHTS INTO REMODELING OF
JRNL TITL 2 GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED PROTEINS BY PGAP1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CTFFIND, CRYOSPARC,
REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.840
REMARK 3 NUMBER OF PARTICLES : 407921
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8K9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1300030358.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : GPI INOSITOL-DEACYLASE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 7.50
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR 4.5S BEFORE PLUNGING
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 ALA A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 ASP A 10
REMARK 465 ASP A 11
REMARK 465 ASP A 12
REMARK 465 ASP A 13
REMARK 465 ALA A 14
REMARK 465 PRO A 15
REMARK 465 PRO A 16
REMARK 465 ILE A 17
REMARK 465 ARG A 18
REMARK 465 VAL A 19
REMARK 465 PRO A 20
REMARK 465 ARG A 21
REMARK 465 VAL A 22
REMARK 465 ASN A 23
REMARK 465 GLN A 24
REMARK 465 CYS A 25
REMARK 465 ALA A 26
REMARK 465 THR A 27
REMARK 465 SER A 28
REMARK 465 ARG A 29
REMARK 465 THR A 30
REMARK 465 LYS A 31
REMARK 465 ASP A 32
REMARK 465 SER A 33
REMARK 465 GLN A 34
REMARK 465 SER A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 GLN A 38
REMARK 465 SER A 39
REMARK 465 ALA A 40
REMARK 465 SER A 41
REMARK 465 LYS A 42
REMARK 465 LEU A 43
REMARK 465 ASP A 44
REMARK 465 ARG A 45
REMARK 465 ARG A 46
REMARK 465 ARG A 47
REMARK 465 SER A 48
REMARK 465 ALA A 49
REMARK 465 ASP A 50
REMARK 465 ARG A 51
REMARK 465 ARG A 52
REMARK 465 PRO A 53
REMARK 465 SER A 54
REMARK 465 PHE A 55
REMARK 465 SER A 56
REMARK 465 ALA A 57
REMARK 465 ASN A 58
REMARK 465 ARG A 59
REMARK 465 ARG A 60
REMARK 465 SER A 61
REMARK 465 GLY A 62
REMARK 465 THR A 63
REMARK 465 GLY A 64
REMARK 465 ALA A 65
REMARK 465 GLY A 66
REMARK 465 THR A 67
REMARK 465 GLY A 68
REMARK 465 THR A 69
REMARK 465 GLY A 70
REMARK 465 THR A 71
REMARK 465 GLY A 72
REMARK 465 ILE A 73
REMARK 465 ALA A 74
REMARK 465 ASN A 75
REMARK 465 TRP A 76
REMARK 465 ARG A 77
REMARK 465 PRO A 78
REMARK 465 PHE A 79
REMARK 465 ASP A 80
REMARK 465 SER A 81
REMARK 465 ARG A 82
REMARK 465 ASP A 83
REMARK 465 ALA A 84
REMARK 465 THR A 85
REMARK 465 VAL A 86
REMARK 465 GLU A 87
REMARK 465 ARG A 88
REMARK 465 ALA A 89
REMARK 465 GLY A 90
REMARK 465 SER A 91
REMARK 465 SER A 92
REMARK 465 THR A 93
REMARK 465 ALA A 94
REMARK 465 THR A 95
REMARK 465 THR A 96
REMARK 465 ALA A 97
REMARK 465 THR A 98
REMARK 465 THR A 99
REMARK 465 PRO A 100
REMARK 465 PRO A 101
REMARK 465 PRO A 102
REMARK 465 SER A 103
REMARK 465 SER A 104
REMARK 465 SER A 105
REMARK 465 LEU A 106
REMARK 465 GLY A 107
REMARK 465 LEU A 108
REMARK 465 MET A 109
REMARK 465 LEU A 110
REMARK 465 ALA A 111
REMARK 465 ALA A 112
REMARK 465 ASN A 113
REMARK 465 GLY A 114
REMARK 465 ALA A 115
REMARK 465 VAL A 116
REMARK 465 GLN A 117
REMARK 465 GLU A 118
REMARK 465 LYS A 119
REMARK 465 GLU A 120
REMARK 465 MET A 121
REMARK 465 VAL A 122
REMARK 465 MET A 123
REMARK 465 MET A 124
REMARK 465 GLY A 125
REMARK 465 LYS A 126
REMARK 465 ALA A 127
REMARK 465 GLN A 128
REMARK 465 GLU A 129
REMARK 465 HIS A 130
REMARK 465 GLY A 131
REMARK 465 PHE A 132
REMARK 465 VAL A 133
REMARK 465 GLY A 134
REMARK 465 ARG A 135
REMARK 465 ARG A 136
REMARK 465 ALA A 137
REMARK 465 PRO A 138
REMARK 465 ILE A 577
REMARK 465 PRO A 578
REMARK 465 SER A 579
REMARK 465 GLN A 580
REMARK 465 PRO A 581
REMARK 465 ASN A 582
REMARK 465 PRO A 583
REMARK 465 THR A 584
REMARK 465 GLY A 585
REMARK 465 PRO A 586
REMARK 465 ALA A 587
REMARK 465 ILE A 588
REMARK 465 PRO A 589
REMARK 465 SER A 590
REMARK 465 GLN A 591
REMARK 465 LEU A 592
REMARK 465 ASP A 593
REMARK 465 LEU A 594
REMARK 465 SER A 595
REMARK 465 LYS A 596
REMARK 465 GLY A 597
REMARK 465 ASN A 598
REMARK 465 ALA A 599
REMARK 465 GLY A 600
REMARK 465 THR A 601
REMARK 465 THR A 602
REMARK 465 ARG A 603
REMARK 465 THR A 874
REMARK 465 THR A 875
REMARK 465 LYS A 876
REMARK 465 MET A 877
REMARK 465 ALA A 878
REMARK 465 PRO A 879
REMARK 465 SER A 880
REMARK 465 SER A 881
REMARK 465 SER A 882
REMARK 465 ALA A 883
REMARK 465 GLY A 884
REMARK 465 LEU A 885
REMARK 465 TRP A 886
REMARK 465 HIS A 887
REMARK 465 TRP A 888
REMARK 465 GLY A 889
REMARK 465 GLY A 890
REMARK 465 ASN A 891
REMARK 465 THR A 892
REMARK 465 THR A 893
REMARK 465 PHE A 894
REMARK 465 TRP A 956
REMARK 465 VAL A 957
REMARK 465 ASN A 958
REMARK 465 ALA A 959
REMARK 465 GLU A 960
REMARK 465 ASP A 961
REMARK 465 ARG A 962
REMARK 465 ARG A 963
REMARK 465 ARG A 964
REMARK 465 PRO A 965
REMARK 465 SER A 966
REMARK 465 ASN A 967
REMARK 465 PRO A 968
REMARK 465 ALA A 969
REMARK 465 ILE A 970
REMARK 465 PHE A 971
REMARK 465 PRO A 972
REMARK 465 PRO A 973
REMARK 465 SER A 974
REMARK 465 SER A 975
REMARK 465 PRO A 976
REMARK 465 ARG A 977
REMARK 465 ARG A 978
REMARK 465 ARG A 979
REMARK 465 LEU A 1063
REMARK 465 THR A 1064
REMARK 465 PRO A 1065
REMARK 465 PHE A 1066
REMARK 465 THR A 1067
REMARK 465 SER A 1068
REMARK 465 GLY A 1095
REMARK 465 GLY A 1096
REMARK 465 THR A 1097
REMARK 465 GLY A 1098
REMARK 465 ASN A 1099
REMARK 465 GLY A 1100
REMARK 465 ARG A 1101
REMARK 465 ASP A 1151
REMARK 465 ASP A 1152
REMARK 465 TRP A 1153
REMARK 465 SER A 1154
REMARK 465 LEU A 1155
REMARK 465 THR A 1156
REMARK 465 GLY A 1157
REMARK 465 LEU A 1158
REMARK 465 ARG A 1159
REMARK 465 GLN A 1160
REMARK 465 LEU A 1161
REMARK 465 ILE A 1162
REMARK 465 LEU A 1163
REMARK 465 HIS A 1164
REMARK 465 ASN A 1165
REMARK 465 ARG A 1166
REMARK 465 ASN A 1167
REMARK 465 ASN A 1168
REMARK 465 ALA A 1169
REMARK 465 ASN A 1170
REMARK 465 ASN A 1171
REMARK 465 LYS A 1172
REMARK 465 SER A 1173
REMARK 465 GLU A 1174
REMARK 465 THR A 1175
REMARK 465 GLY A 1176
REMARK 465 SER A 1177
REMARK 465 ARG A 1178
REMARK 465 LYS A 1179
REMARK 465 ARG A 1180
REMARK 465 GLY A 1181
REMARK 465 LYS A 1182
REMARK 465 GLU A 1183
REMARK 465 PRO A 1184
REMARK 465 GLY A 1185
REMARK 465 THR A 1186
REMARK 465 LEU A 1187
REMARK 465 GLU A 1188
REMARK 465 VAL A 1189
REMARK 465 LEU A 1190
REMARK 465 PHE A 1191
REMARK 465 GLN A 1192
REMARK 465 GLY A 1193
REMARK 465 PRO A 1194
REMARK 465 GLY A 1195
REMARK 465 GLY A 1196
REMARK 465 SER A 1197
REMARK 465 GLY A 1198
REMARK 465 GLY A 1199
REMARK 465 SER A 1200
REMARK 465 ALA A 1201
REMARK 465 SER A 1202
REMARK 465 VAL A 1203
REMARK 465 ILE A 1204
REMARK 465 LYS A 1205
REMARK 465 PRO A 1206
REMARK 465 GLU A 1207
REMARK 465 MET A 1208
REMARK 465 LYS A 1209
REMARK 465 ILE A 1210
REMARK 465 LYS A 1211
REMARK 465 LEU A 1212
REMARK 465 ARG A 1213
REMARK 465 MET A 1214
REMARK 465 GLU A 1215
REMARK 465 GLY A 1216
REMARK 465 ALA A 1217
REMARK 465 VAL A 1218
REMARK 465 ASN A 1219
REMARK 465 GLY A 1220
REMARK 465 HIS A 1221
REMARK 465 LYS A 1222
REMARK 465 PHE A 1223
REMARK 465 VAL A 1224
REMARK 465 ILE A 1225
REMARK 465 GLU A 1226
REMARK 465 GLY A 1227
REMARK 465 GLU A 1228
REMARK 465 GLY A 1229
REMARK 465 ILE A 1230
REMARK 465 GLY A 1231
REMARK 465 LYS A 1232
REMARK 465 PRO A 1233
REMARK 465 TYR A 1234
REMARK 465 GLU A 1235
REMARK 465 GLY A 1236
REMARK 465 THR A 1237
REMARK 465 GLN A 1238
REMARK 465 THR A 1239
REMARK 465 LEU A 1240
REMARK 465 ASP A 1241
REMARK 465 LEU A 1242
REMARK 465 THR A 1243
REMARK 465 VAL A 1244
REMARK 465 GLU A 1245
REMARK 465 GLU A 1246
REMARK 465 GLY A 1247
REMARK 465 ALA A 1248
REMARK 465 PRO A 1249
REMARK 465 LEU A 1250
REMARK 465 PRO A 1251
REMARK 465 PHE A 1252
REMARK 465 SER A 1253
REMARK 465 TYR A 1254
REMARK 465 ASP A 1255
REMARK 465 ILE A 1256
REMARK 465 LEU A 1257
REMARK 465 THR A 1258
REMARK 465 PRO A 1259
REMARK 465 ALA A 1260
REMARK 465 PHE A 1261
REMARK 465 GLN A 1262
REMARK 465 TYR A 1263
REMARK 465 GLY A 1264
REMARK 465 ASN A 1265
REMARK 465 ARG A 1266
REMARK 465 ALA A 1267
REMARK 465 PHE A 1268
REMARK 465 THR A 1269
REMARK 465 LYS A 1270
REMARK 465 TYR A 1271
REMARK 465 PRO A 1272
REMARK 465 GLU A 1273
REMARK 465 ASP A 1274
REMARK 465 ILE A 1275
REMARK 465 PRO A 1276
REMARK 465 ASP A 1277
REMARK 465 TYR A 1278
REMARK 465 PHE A 1279
REMARK 465 LYS A 1280
REMARK 465 GLN A 1281
REMARK 465 ALA A 1282
REMARK 465 PHE A 1283
REMARK 465 PRO A 1284
REMARK 465 GLU A 1285
REMARK 465 GLY A 1286
REMARK 465 TYR A 1287
REMARK 465 SER A 1288
REMARK 465 TRP A 1289
REMARK 465 GLU A 1290
REMARK 465 ARG A 1291
REMARK 465 SER A 1292
REMARK 465 MET A 1293
REMARK 465 THR A 1294
REMARK 465 TYR A 1295
REMARK 465 GLU A 1296
REMARK 465 ASP A 1297
REMARK 465 GLN A 1298
REMARK 465 GLY A 1299
REMARK 465 ILE A 1300
REMARK 465 CYS A 1301
REMARK 465 ILE A 1302
REMARK 465 ALA A 1303
REMARK 465 THR A 1304
REMARK 465 SER A 1305
REMARK 465 ASP A 1306
REMARK 465 ILE A 1307
REMARK 465 THR A 1308
REMARK 465 MET A 1309
REMARK 465 GLU A 1310
REMARK 465 GLY A 1311
REMARK 465 ASP A 1312
REMARK 465 CYS A 1313
REMARK 465 PHE A 1314
REMARK 465 PHE A 1315
REMARK 465 TYR A 1316
REMARK 465 GLU A 1317
REMARK 465 ILE A 1318
REMARK 465 ARG A 1319
REMARK 465 PHE A 1320
REMARK 465 ASP A 1321
REMARK 465 GLY A 1322
REMARK 465 THR A 1323
REMARK 465 ASN A 1324
REMARK 465 PHE A 1325
REMARK 465 PRO A 1326
REMARK 465 PRO A 1327
REMARK 465 ASN A 1328
REMARK 465 GLY A 1329
REMARK 465 PRO A 1330
REMARK 465 VAL A 1331
REMARK 465 MET A 1332
REMARK 465 GLN A 1333
REMARK 465 LYS A 1334
REMARK 465 LYS A 1335
REMARK 465 THR A 1336
REMARK 465 LEU A 1337
REMARK 465 LYS A 1338
REMARK 465 TRP A 1339
REMARK 465 GLU A 1340
REMARK 465 PRO A 1341
REMARK 465 SER A 1342
REMARK 465 THR A 1343
REMARK 465 GLU A 1344
REMARK 465 LYS A 1345
REMARK 465 MET A 1346
REMARK 465 TYR A 1347
REMARK 465 VAL A 1348
REMARK 465 GLU A 1349
REMARK 465 ASP A 1350
REMARK 465 GLY A 1351
REMARK 465 VAL A 1352
REMARK 465 LEU A 1353
REMARK 465 LYS A 1354
REMARK 465 GLY A 1355
REMARK 465 ASP A 1356
REMARK 465 VAL A 1357
REMARK 465 GLU A 1358
REMARK 465 MET A 1359
REMARK 465 ALA A 1360
REMARK 465 LEU A 1361
REMARK 465 LEU A 1362
REMARK 465 LEU A 1363
REMARK 465 GLU A 1364
REMARK 465 GLY A 1365
REMARK 465 GLY A 1366
REMARK 465 GLY A 1367
REMARK 465 HIS A 1368
REMARK 465 TYR A 1369
REMARK 465 ARG A 1370
REMARK 465 CYS A 1371
REMARK 465 ASP A 1372
REMARK 465 PHE A 1373
REMARK 465 LYS A 1374
REMARK 465 THR A 1375
REMARK 465 THR A 1376
REMARK 465 TYR A 1377
REMARK 465 LYS A 1378
REMARK 465 ALA A 1379
REMARK 465 LYS A 1380
REMARK 465 LYS A 1381
REMARK 465 ASP A 1382
REMARK 465 VAL A 1383
REMARK 465 ARG A 1384
REMARK 465 LEU A 1385
REMARK 465 PRO A 1386
REMARK 465 ASP A 1387
REMARK 465 ALA A 1388
REMARK 465 HIS A 1389
REMARK 465 GLU A 1390
REMARK 465 VAL A 1391
REMARK 465 ASP A 1392
REMARK 465 HIS A 1393
REMARK 465 ARG A 1394
REMARK 465 ILE A 1395
REMARK 465 GLU A 1396
REMARK 465 ILE A 1397
REMARK 465 LEU A 1398
REMARK 465 SER A 1399
REMARK 465 HIS A 1400
REMARK 465 ASP A 1401
REMARK 465 LYS A 1402
REMARK 465 ASP A 1403
REMARK 465 TYR A 1404
REMARK 465 ASN A 1405
REMARK 465 LYS A 1406
REMARK 465 VAL A 1407
REMARK 465 ARG A 1408
REMARK 465 LEU A 1409
REMARK 465 TYR A 1410
REMARK 465 GLU A 1411
REMARK 465 HIS A 1412
REMARK 465 ALA A 1413
REMARK 465 GLU A 1414
REMARK 465 ALA A 1415
REMARK 465 ARG A 1416
REMARK 465 TYR A 1417
REMARK 465 SER A 1418
REMARK 465 GLY A 1419
REMARK 465 GLY A 1420
REMARK 465 GLY A 1421
REMARK 465 SER A 1422
REMARK 465 GLY A 1423
REMARK 465 GLY A 1424
REMARK 465 GLY A 1425
REMARK 465 SER A 1426
REMARK 465 ALA A 1427
REMARK 465 TRP A 1428
REMARK 465 SER A 1429
REMARK 465 HIS A 1430
REMARK 465 PRO A 1431
REMARK 465 GLN A 1432
REMARK 465 PHE A 1433
REMARK 465 GLU A 1434
REMARK 465 LYS A 1435
REMARK 465 GLY A 1436
REMARK 465 GLY A 1437
REMARK 465 GLY A 1438
REMARK 465 SER A 1439
REMARK 465 GLY A 1440
REMARK 465 GLY A 1441
REMARK 465 GLY A 1442
REMARK 465 SER A 1443
REMARK 465 GLY A 1444
REMARK 465 GLY A 1445
REMARK 465 SER A 1446
REMARK 465 ALA A 1447
REMARK 465 TRP A 1448
REMARK 465 SER A 1449
REMARK 465 HIS A 1450
REMARK 465 PRO A 1451
REMARK 465 GLN A 1452
REMARK 465 PHE A 1453
REMARK 465 GLU A 1454
REMARK 465 LYS A 1455
REMARK 465 GLY A 1456
REMARK 465 SER A 1457
REMARK 465 HIS A 1458
REMARK 465 HIS A 1459
REMARK 465 HIS A 1460
REMARK 465 HIS A 1461
REMARK 465 HIS A 1462
REMARK 465 HIS A 1463
REMARK 465 HIS A 1464
REMARK 465 HIS A 1465
REMARK 465 HIS A 1466
REMARK 465 HIS A 1467
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 327 -125.72 54.59
REMARK 500 VAL A 437 -66.71 -131.78
REMARK 500 ARG A 757 -61.81 -141.77
REMARK 500 GLN A 858 -61.50 -130.68
REMARK 500 LEU A 903 -124.55 59.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-36995 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE GPI INOSITOL-DEACYLASE (PGAP1/BST1) FROM
REMARK 900 CHAETOMIUM THERMOPHILUM
DBREF 8K9Q A 2 1184 UNP G0S652 G0S652_CHATD 2 1184
DBREF 8K9Q A 1185 1467 PDB 8K9Q 8K9Q 1185 1467
SEQADV 8K9Q MET A -1 UNP G0S652 INITIATING METHIONINE
SEQADV 8K9Q GLY A 0 UNP G0S652 EXPRESSION TAG
SEQADV 8K9Q SER A 1 UNP G0S652 EXPRESSION TAG
SEQRES 1 A 1469 MET GLY SER ARG SER LEU SER SER ALA SER SER ASP ASP
SEQRES 2 A 1469 ASP ASP ALA PRO PRO ILE ARG VAL PRO ARG VAL ASN GLN
SEQRES 3 A 1469 CYS ALA THR SER ARG THR LYS ASP SER GLN SER PRO ALA
SEQRES 4 A 1469 GLN SER ALA SER LYS LEU ASP ARG ARG ARG SER ALA ASP
SEQRES 5 A 1469 ARG ARG PRO SER PHE SER ALA ASN ARG ARG SER GLY THR
SEQRES 6 A 1469 GLY ALA GLY THR GLY THR GLY THR GLY ILE ALA ASN TRP
SEQRES 7 A 1469 ARG PRO PHE ASP SER ARG ASP ALA THR VAL GLU ARG ALA
SEQRES 8 A 1469 GLY SER SER THR ALA THR THR ALA THR THR PRO PRO PRO
SEQRES 9 A 1469 SER SER SER LEU GLY LEU MET LEU ALA ALA ASN GLY ALA
SEQRES 10 A 1469 VAL GLN GLU LYS GLU MET VAL MET MET GLY LYS ALA GLN
SEQRES 11 A 1469 GLU HIS GLY PHE VAL GLY ARG ARG ALA PRO TRP ARG SER
SEQRES 12 A 1469 PRO TRP ALA ILE SER VAL PHE ALA PHE VAL THR SER LEU
SEQRES 13 A 1469 LEU GLY ILE GLY LEU LEU LEU ALA VAL ILE HIS SER SER
SEQRES 14 A 1469 VAL THR ARG GLN ILE ASP PRO LYS GLY CYS ARG MET SER
SEQRES 15 A 1469 TYR MET ARG PRO SER TYR ALA LYS LEU SER ASP PHE ASP
SEQRES 16 A 1469 THR GLU HIS THR ARG LEU ALA SER LYS TYR SER LEU TYR
SEQRES 17 A 1469 LEU TYR ARG GLU GLN GLY ILE ASP HIS ASP VAL LYS VAL
SEQRES 18 A 1469 ARG GLY VAL PRO VAL LEU PHE ILE PRO GLY ASN ALA GLY
SEQRES 19 A 1469 SER TYR LYS GLN VAL ARG PRO ILE ALA ALA GLU ALA ALA
SEQRES 20 A 1469 ASN TYR PHE HIS ASP VAL LEU GLN HIS ASP GLU ALA ALA
SEQRES 21 A 1469 LEU ARG ALA GLY VAL ARG SER LEU ASP PHE PHE THR VAL
SEQRES 22 A 1469 ASP PHE ASN GLU ASP ILE THR ALA PHE HIS GLY GLN THR
SEQRES 23 A 1469 LEU LEU ASP GLN ALA GLU TYR LEU ASN GLU ALA ILE ARG
SEQRES 24 A 1469 TYR ILE LEU SER LEU TYR LEU ASP PRO ARG VAL SER GLU
SEQRES 25 A 1469 ARG ASP PRO ASP LEU PRO ASP PRO THR SER VAL ILE VAL
SEQRES 26 A 1469 LEU GLY HIS SER MET GLY GLY ILE VAL ALA ARG THR MET
SEQRES 27 A 1469 LEU ILE MET PRO ASN TYR GLN HIS ASN SER ILE ASN THR
SEQRES 28 A 1469 ILE ILE THR MET SER ALA PRO HIS ALA ARG PRO PRO VAL
SEQRES 29 A 1469 SER PHE ASP GLY GLN ILE VAL GLN THR TYR LYS ASP ILE
SEQRES 30 A 1469 ASN ASN TYR TRP ARG HIS ALA TYR SER GLN LYS TRP ALA
SEQRES 31 A 1469 ASN ASP ASN PRO LEU TRP HIS VAL THR LEU VAL SER ILE
SEQRES 32 A 1469 ALA GLY GLY GLY LEU ASP THR VAL VAL PRO SER ASP TYR
SEQRES 33 A 1469 ALA SER ILE GLU SER LEU VAL PRO ASP THR HIS GLY PHE
SEQRES 34 A 1469 THR VAL PHE THR SER THR ILE PRO ASN VAL TRP THR SER
SEQRES 35 A 1469 MET ASP HIS GLN ALA ILE LEU TRP CYS ASP GLN PHE ARG
SEQRES 36 A 1469 LYS VAL ILE ILE ARG ALA LEU PHE ASP ILE VAL ASP VAL
SEQRES 37 A 1469 HIS ARG ALA SER GLN THR LYS PRO ARG ALA GLN ARG MET
SEQRES 38 A 1469 ARG VAL PHE LYS LYS TRP PHE LEU SER GLY MET GLU THR
SEQRES 39 A 1469 VAL ALA GLU LYS ILE ALA PRO THR SER ASP PRO THR THR
SEQRES 40 A 1469 LEU LEU ILE VAL ASP ASP LYS SER ASP SER ILE THR ALA
SEQRES 41 A 1469 GLU GLY GLU ARG LEU VAL LEU ARG GLU LEU GLY THR GLN
SEQRES 42 A 1469 GLY SER VAL ARG ALA HIS LEU MET PRO ILE PRO PRO PRO
SEQRES 43 A 1469 GLY SER PRO GLU LEU LYS ARG PHE THR LEU LEU THR ASP
SEQRES 44 A 1469 THR LYS LEU ASP LYS PRO GLY GLU ASN GLY LYS LEU GLU
SEQRES 45 A 1469 VAL MET PHE CYS SER VAL ILE PRO SER GLN PRO ASN PRO
SEQRES 46 A 1469 THR GLY PRO ALA ILE PRO SER GLN LEU ASP LEU SER LYS
SEQRES 47 A 1469 GLY ASN ALA GLY THR THR ARG LEU ALA CYS THR ASN VAL
SEQRES 48 A 1469 ALA PRO ASP VAL ILE THR LEU PRO ALA SER THR ARG PHE
SEQRES 49 A 1469 ALA ARG PHE PRO PHE SER VAL ARG LYS GLU ALA GLU ILE
SEQRES 50 A 1469 PRO PRO PHE SER TYR LEU GLU TYR VAL LEU ASP ASP ILE
SEQRES 51 A 1469 SER GLU HIS GLN PHE VAL ALA VAL ILE GLU LYS ALA THR
SEQRES 52 A 1469 ILE PRO THR PRO GLY PHE VAL ILE ALA GLU PHE SER ASP
SEQRES 53 A 1469 HIS SER ASN SER HIS HIS THR ARG HIS ILE GLY LEU ARG
SEQRES 54 A 1469 ASN LEU LEU THR PHE GLY ILE SER LEU ARG LEU PRO SER
SEQRES 55 A 1469 ASN ARG PRO MET MET SER GLU VAL ARG ILE PRO SER VAL
SEQRES 56 A 1469 LYS SER SER LEU LEU ALA TYR ASN LEU ARG ILE SER ALA
SEQRES 57 A 1469 LEU GLU CYS SER GLY ARG LYS ASP LEU PHE ALA PRO LEU
SEQRES 58 A 1469 VAL ARG GLN TYR LEU ALA GLU PRO TYR GLU SER LYS TYR
SEQRES 59 A 1469 PHE VAL ASN ALA ARG GLN ALA ALA VAL SER LEU HIS GLY
SEQRES 60 A 1469 VAL ALA PRO TYR VAL PRO PRO PRO MET SER ARG GLU PRO
SEQRES 61 A 1469 GLU ALA GLU GLY LEU ALA PHE GLN LEU TRP THR ASP PRO
SEQRES 62 A 1469 THR CYS ASN SER SER ILE GLN VAL ASP LEU THR VAL ASP
SEQRES 63 A 1469 VAL MET GLY SER LEU GLY LYS LEU TYR MET ARG TYR ARG
SEQRES 64 A 1469 THR VAL PHE ALA ALA PHE PRO LEU PHE ILE VAL SER LEU
SEQRES 65 A 1469 VAL LEU ARG LYS GLN PHE GLN VAL TYR ASP SER THR GLY
SEQRES 66 A 1469 SER PHE ILE THR PHE ALA GLU GLY LEU ASP LEU SER LEU
SEQRES 67 A 1469 ARG GLN SER ILE PRO VAL MET LEU ILE VAL LEU ALA ALA
SEQRES 68 A 1469 LEU THR LEU SER THR THR LYS MET ALA PRO SER SER SER
SEQRES 69 A 1469 ALA GLY LEU TRP HIS TRP GLY GLY ASN THR THR PHE THR
SEQRES 70 A 1469 ASN PHE HIS GLN ASN ASP LEU LEU ILE GLY THR GLN ASP
SEQRES 71 A 1469 PRO PHE PHE LEU PHE LEU ILE PRO LEU ILE GLY ILE ILE
SEQRES 72 A 1469 CYS VAL GLY VAL CYS THR VAL VAL ASN TYR ILE ALA LEU
SEQRES 73 A 1469 SER LEU THR ARG LEU ILE SER VAL VAL ILE SER PHE ILE
SEQRES 74 A 1469 GLY PHE LEU THR VAL ARG PHE GLY TRP VAL ASN ALA GLU
SEQRES 75 A 1469 ASP ARG ARG ARG PRO SER ASN PRO ALA ILE PHE PRO PRO
SEQRES 76 A 1469 SER SER PRO ARG ARG ARG MET ILE THR THR ALA VAL LEU
SEQRES 77 A 1469 LEU PHE LEU VAL SER THR MET ILE PRO TYR GLN LEU ALA
SEQRES 78 A 1469 TYR LEU VAL ALA CYS LEU VAL GLN LEU GLY THR LEU VAL
SEQRES 79 A 1469 ARG ALA GLN ARG ILE SER SER GLU LEU ARG SER PRO ALA
SEQRES 80 A 1469 ASN SER ASN PHE HIS ASN TYR VAL HIS SER ILE PHE ILE
SEQRES 81 A 1469 LEU MET LEU TRP ILE LEU PRO ILE ASN LEU PRO THR LEU
SEQRES 82 A 1469 VAL VAL TRP MET HIS ASN LEU SER VAL HIS TRP LEU THR
SEQRES 83 A 1469 PRO PHE THR SER HIS HIS ASN VAL PHE SER ILE MET PRO
SEQRES 84 A 1469 PHE ILE LEU LEU VAL GLU THR HIS THR THR GLY GLN MET
SEQRES 85 A 1469 ILE PRO ARG THR GLY GLY THR GLY ASN GLY ARG CYS CYS
SEQRES 86 A 1469 VAL LEU LEU ARG HIS ILE THR SER ILE LEU LEU LEU SER
SEQRES 87 A 1469 LEU ALA LEU TYR ALA ALA VAL TYR GLY VAL SER TYR ALA
SEQRES 88 A 1469 TYR THR LEU HIS GLN PHE VAL ASN LEU PHE ALA PHE TRP
SEQRES 89 A 1469 LEU VAL MET VAL HIS SER THR ALA ASP ASP TRP SER LEU
SEQRES 90 A 1469 THR GLY LEU ARG GLN LEU ILE LEU HIS ASN ARG ASN ASN
SEQRES 91 A 1469 ALA ASN ASN LYS SER GLU THR GLY SER ARG LYS ARG GLY
SEQRES 92 A 1469 LYS GLU PRO GLY THR LEU GLU VAL LEU PHE GLN GLY PRO
SEQRES 93 A 1469 GLY GLY SER GLY GLY SER ALA SER VAL ILE LYS PRO GLU
SEQRES 94 A 1469 MET LYS ILE LYS LEU ARG MET GLU GLY ALA VAL ASN GLY
SEQRES 95 A 1469 HIS LYS PHE VAL ILE GLU GLY GLU GLY ILE GLY LYS PRO
SEQRES 96 A 1469 TYR GLU GLY THR GLN THR LEU ASP LEU THR VAL GLU GLU
SEQRES 97 A 1469 GLY ALA PRO LEU PRO PHE SER TYR ASP ILE LEU THR PRO
SEQRES 98 A 1469 ALA PHE GLN TYR GLY ASN ARG ALA PHE THR LYS TYR PRO
SEQRES 99 A 1469 GLU ASP ILE PRO ASP TYR PHE LYS GLN ALA PHE PRO GLU
SEQRES 100 A 1469 GLY TYR SER TRP GLU ARG SER MET THR TYR GLU ASP GLN
SEQRES 101 A 1469 GLY ILE CYS ILE ALA THR SER ASP ILE THR MET GLU GLY
SEQRES 102 A 1469 ASP CYS PHE PHE TYR GLU ILE ARG PHE ASP GLY THR ASN
SEQRES 103 A 1469 PHE PRO PRO ASN GLY PRO VAL MET GLN LYS LYS THR LEU
SEQRES 104 A 1469 LYS TRP GLU PRO SER THR GLU LYS MET TYR VAL GLU ASP
SEQRES 105 A 1469 GLY VAL LEU LYS GLY ASP VAL GLU MET ALA LEU LEU LEU
SEQRES 106 A 1469 GLU GLY GLY GLY HIS TYR ARG CYS ASP PHE LYS THR THR
SEQRES 107 A 1469 TYR LYS ALA LYS LYS ASP VAL ARG LEU PRO ASP ALA HIS
SEQRES 108 A 1469 GLU VAL ASP HIS ARG ILE GLU ILE LEU SER HIS ASP LYS
SEQRES 109 A 1469 ASP TYR ASN LYS VAL ARG LEU TYR GLU HIS ALA GLU ALA
SEQRES 110 A 1469 ARG TYR SER GLY GLY GLY SER GLY GLY GLY SER ALA TRP
SEQRES 111 A 1469 SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY
SEQRES 112 A 1469 GLY SER GLY GLY SER ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 113 A 1469 LYS GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET Y01 A1501 35
HET Y01 A1502 35
HET Y01 A1503 35
HET D39 A1504 52
HET D39 A1505 52
HETNAM Y01 CHOLESTEROL HEMISUCCINATE
HETNAM D39 (2~{S})-2-AZANYL-3-[[(2~{R})-3-HEXADECANOYLOXY-2-
HETNAM 2 D39 [(~{Z})-OCTADEC-9-ENOYL]OXY-PROPOXY]-OXIDANYL-
HETNAM 3 D39 PHOSPHORYL]OXY-PROPANOIC ACID
FORMUL 2 Y01 3(C31 H50 O4)
FORMUL 5 D39 2(C40 H76 N O10 P)
HELIX 1 AA1 SER A 146 THR A 169 1 24
HELIX 2 AA2 SER A 233 GLN A 236 5 4
HELIX 3 AA3 VAL A 237 VAL A 251 1 15
HELIX 4 AA4 LEU A 252 HIS A 254 5 3
HELIX 5 AA5 ASP A 255 GLY A 262 1 8
HELIX 6 AA6 ILE A 277 PHE A 280 5 4
HELIX 7 AA7 HIS A 281 SER A 301 1 21
HELIX 8 AA8 MET A 328 LEU A 337 1 10
HELIX 9 AA9 ASP A 365 GLN A 385 1 21
HELIX 10 AB1 GLY A 403 ASP A 407 5 5
HELIX 11 AB2 PRO A 411 SER A 416 5 6
HELIX 12 AB3 GLN A 444 CYS A 449 1 6
HELIX 13 AB4 CYS A 449 PHE A 461 1 13
HELIX 14 AB5 PRO A 474 LEU A 487 1 14
HELIX 15 AB6 ALA A 610 VAL A 613 5 4
HELIX 16 AB7 ARG A 630 GLU A 634 5 5
HELIX 17 AB8 LEU A 645 SER A 649 1 5
HELIX 18 AB9 HIS A 675 SER A 678 1 4
HELIX 19 AC1 GLY A 685 GLY A 693 1 9
HELIX 20 AC2 ASP A 804 GLY A 810 1 7
HELIX 21 AC3 GLY A 810 TYR A 816 1 7
HELIX 22 AC4 ALA A 822 GLY A 843 1 22
HELIX 23 AC5 THR A 847 GLN A 858 1 12
HELIX 24 AC6 GLN A 858 LEU A 872 1 15
HELIX 25 AC7 HIS A 898 LEU A 902 5 5
HELIX 26 AC8 PHE A 910 LEU A 912 5 3
HELIX 27 AC9 PHE A 913 PHE A 954 1 42
HELIX 28 AD1 ILE A 981 THR A 992 1 12
HELIX 29 AD2 PRO A 995 ARG A 1022 1 28
HELIX 30 AD3 SER A 1023 TRP A 1042 1 20
HELIX 31 AD4 ILE A 1043 LEU A 1048 1 6
HELIX 32 AD5 LEU A 1048 SER A 1059 1 12
HELIX 33 AD6 HIS A 1070 SER A 1074 1 5
HELIX 34 AD7 ILE A 1075 THR A 1084 1 10
HELIX 35 AD8 CYS A 1103 TYR A 1124 1 22
HELIX 36 AD9 TYR A 1128 THR A 1131 5 4
HELIX 37 AE1 LEU A 1132 ALA A 1150 1 19
SHEET 1 AA1 8 TYR A 186 LYS A 188 0
SHEET 2 AA1 8 SER A 204 TYR A 208 -1 O LEU A 207 N ALA A 187
SHEET 3 AA1 8 LEU A 266 ASP A 272 -1 O THR A 270 N TYR A 206
SHEET 4 AA1 8 VAL A 222 ILE A 227 1 N VAL A 224 O PHE A 269
SHEET 5 AA1 8 VAL A 321 HIS A 326 1 O LEU A 324 N LEU A 225
SHEET 6 AA1 8 ILE A 347 MET A 353 1 O ILE A 351 N VAL A 323
SHEET 7 AA1 8 THR A 397 ALA A 402 1 O ILE A 401 N THR A 352
SHEET 8 AA1 8 THR A 428 PHE A 430 1 O VAL A 429 N ALA A 402
SHEET 1 AA2 5 THR A 505 LEU A 506 0
SHEET 2 AA2 5 ALA A 605 ASN A 608 -1 O CYS A 606 N THR A 505
SHEET 3 AA2 5 LEU A 569 SER A 575 -1 N SER A 575 O ALA A 605
SHEET 4 AA2 5 PHE A 653 GLU A 658 -1 O ALA A 655 N MET A 572
SHEET 5 AA2 5 ARG A 535 PRO A 540 -1 N HIS A 537 O VAL A 656
SHEET 1 AA3 5 LEU A 523 LEU A 528 0
SHEET 2 AA3 5 THR A 664 ASP A 674 -1 O ALA A 670 N LEU A 523
SHEET 3 AA3 5 LYS A 550 THR A 556 -1 N THR A 553 O GLU A 671
SHEET 4 AA3 5 PHE A 638 VAL A 644 -1 O SER A 639 N THR A 556
SHEET 5 AA3 5 ILE A 614 LEU A 616 -1 N ILE A 614 O TYR A 640
SHEET 1 AA4 5 HIS A 679 THR A 681 0
SHEET 2 AA4 5 MET A 705 ILE A 710 1 O GLU A 707 N HIS A 680
SHEET 3 AA4 5 LEU A 783 TRP A 788 -1 O LEU A 787 N SER A 706
SHEET 4 AA4 5 LEU A 739 TYR A 743 -1 N LEU A 739 O TRP A 788
SHEET 5 AA4 5 SER A 750 VAL A 754 -1 O LYS A 751 N GLN A 742
SHEET 1 AA5 4 ILE A 694 LEU A 698 0
SHEET 2 AA5 4 ILE A 797 VAL A 803 -1 O ILE A 797 N LEU A 698
SHEET 3 AA5 4 ALA A 719 ILE A 724 -1 N ASN A 721 O THR A 802
SHEET 4 AA5 4 GLN A 758 SER A 762 -1 O ALA A 759 N LEU A 722
SSBOND 1 CYS A 177 CYS A 449 1555 1555 2.01
SSBOND 2 CYS A 574 CYS A 606 1555 1555 2.01
SSBOND 3 CYS A 729 CYS A 793 1555 1555 2.05
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 7341 ALA A1150
MASTER 671 0 5 37 27 0 0 6 7549 1 215 113
END |