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HEADER MEMBRANE PROTEIN 01-AUG-23 8K9R
TITLE CRYO EM STRUCTURE OF THE PRODUCTS-BOUND PGAP1(BST1)-H443N FROM
TITLE 2 CHAETOMIUM THERMOPHILUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GPI INOSITOL-DEACYLASE,MCHERRY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: RESIDUES 1-1186 IS GPI INOSITOL-DEACYLASE (UNIPROT ID
COMPND 8 G0S652) WITH A H443N MUTATION. RESIDUES 1187-1200 IS THE LINKER WITH
COMPND 9 A 3 C PROTEASE DIGESTION SITE. RESIDUES 1201-1435 IS A FUSED MCHERRY
COMPND 10 PROTEIN (UNIPROT ID A0A366VY15 WITH THE FOLLOWING FOUR MUTATIONS THAT
COMPND 11 EXTEND ITS FLUORESCENCE LIFETIME: W148S, I166V, Q168Y AND I202R).
COMPND 12 RESIDUES 1436-1447 IS THE LINKER WITH A HIS TAG.;
COMPND 13 MOL_ID: 2;
COMPND 14 MOLECULE: GREEN FLUORESCENT PROTEIN,COMPLEMENT DECAY-ACCELERATING
COMPND 15 FACTOR;
COMPND 16 CHAIN: B;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: RESIDUES 1-6 IS A LINKER. RESIDUES 7-231 IS A
COMPND 19 THERMOSTABLE GREEN FLUORESCENT PROTEIN (PDB ENTRY 4TZA, RESIDUE 5-
COMPND 20 229). RESIDUES 232-263 IS A LINKER WITH AN EXPRESSION TAG. RESIDUES
COMPND 21 264-272 IS HUMAN CD55 (UNIPROT ID P08174, RESIDUE P345-T353).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS
SOURCE 3 144.50 / IMI 039719), PSYCHROMONAS SP. B3M02;
SOURCE 4 ORGANISM_COMMON: THERMOCHAETOIDES THERMOPHILA;
SOURCE 5 ORGANISM_TAXID: 759272, 2267226;
SOURCE 6 GENE: CTHT_0034210, DS885_16260;
SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT, HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 32630, 9606;
SOURCE 14 GENE: CD55, CR, DAF;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 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, TGP,
KEYWDS 4 THERMOSTABLE GREEN FLUORESCENCE PROTEIN, TRANSMEMBRANE ENZYME, TRIAD
KEYWDS 5 ENZYME.
EXPDTA ELECTRON MICROSCOPY
AUTHOR T.LI,J.HONG,Q.QU,D.LI
REVDAT 1 20-DEC-23 8K9R 0
JRNL AUTH T.LI,J.HONG,Q.QU,D.LI
JRNL TITL CRYOEM STRUCTURE OF GLE1-PRODH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, CRYOSPARC,
REMARK 3 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) : 2.680
REMARK 3 NUMBER OF PARTICLES : 179980
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 8K9R 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_1300034301.
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 : COMPLEX OF THE GPI INOSITOL
REMARK 245 -DEACYLASE WITH A CHIMERA GPI-
REMARK 245 ANCHORED PROTEIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 10.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
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 : FEI FALCON IV (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
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) : 5000.00
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 MET A 980
REMARK 465 ILE A 981
REMARK 465 THR A 982
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 LYS A 1195
REMARK 465 LEU A 1196
REMARK 465 GLU A 1197
REMARK 465 PHE A 1198
REMARK 465 VAL A 1199
REMARK 465 SER A 1200
REMARK 465 LYS A 1201
REMARK 465 GLY A 1202
REMARK 465 GLU A 1203
REMARK 465 GLU A 1204
REMARK 465 ASP A 1205
REMARK 465 ASN A 1206
REMARK 465 MET A 1207
REMARK 465 ALA A 1208
REMARK 465 ILE A 1209
REMARK 465 ILE A 1210
REMARK 465 LYS A 1211
REMARK 465 GLU A 1212
REMARK 465 PHE A 1213
REMARK 465 MET A 1214
REMARK 465 ARG A 1215
REMARK 465 PHE A 1216
REMARK 465 LYS A 1217
REMARK 465 VAL A 1218
REMARK 465 HIS A 1219
REMARK 465 MET A 1220
REMARK 465 GLU A 1221
REMARK 465 GLY A 1222
REMARK 465 SER A 1223
REMARK 465 VAL A 1224
REMARK 465 ASN A 1225
REMARK 465 GLY A 1226
REMARK 465 HIS A 1227
REMARK 465 GLU A 1228
REMARK 465 PHE A 1229
REMARK 465 GLU A 1230
REMARK 465 ILE A 1231
REMARK 465 GLU A 1232
REMARK 465 GLY A 1233
REMARK 465 GLU A 1234
REMARK 465 GLY A 1235
REMARK 465 GLU A 1236
REMARK 465 GLY A 1237
REMARK 465 ARG A 1238
REMARK 465 PRO A 1239
REMARK 465 TYR A 1240
REMARK 465 GLU A 1241
REMARK 465 GLY A 1242
REMARK 465 THR A 1243
REMARK 465 GLN A 1244
REMARK 465 THR A 1245
REMARK 465 ALA A 1246
REMARK 465 LYS A 1247
REMARK 465 LEU A 1248
REMARK 465 LYS A 1249
REMARK 465 VAL A 1250
REMARK 465 THR A 1251
REMARK 465 LYS A 1252
REMARK 465 GLY A 1253
REMARK 465 GLY A 1254
REMARK 465 PRO A 1255
REMARK 465 LEU A 1256
REMARK 465 PRO A 1257
REMARK 465 PHE A 1258
REMARK 465 ALA A 1259
REMARK 465 TRP A 1260
REMARK 465 ASP A 1261
REMARK 465 ILE A 1262
REMARK 465 LEU A 1263
REMARK 465 SER A 1264
REMARK 465 PRO A 1265
REMARK 465 GLN A 1266
REMARK 465 PHE A 1267
REMARK 465 MET A 1268
REMARK 465 TYR A 1269
REMARK 465 GLY A 1270
REMARK 465 SER A 1271
REMARK 465 LYS A 1272
REMARK 465 ALA A 1273
REMARK 465 TYR A 1274
REMARK 465 VAL A 1275
REMARK 465 LYS A 1276
REMARK 465 HIS A 1277
REMARK 465 PRO A 1278
REMARK 465 ALA A 1279
REMARK 465 ASP A 1280
REMARK 465 ILE A 1281
REMARK 465 PRO A 1282
REMARK 465 ASP A 1283
REMARK 465 TYR A 1284
REMARK 465 LEU A 1285
REMARK 465 LYS A 1286
REMARK 465 LEU A 1287
REMARK 465 SER A 1288
REMARK 465 PHE A 1289
REMARK 465 PRO A 1290
REMARK 465 GLU A 1291
REMARK 465 GLY A 1292
REMARK 465 PHE A 1293
REMARK 465 LYS A 1294
REMARK 465 TRP A 1295
REMARK 465 GLU A 1296
REMARK 465 ARG A 1297
REMARK 465 VAL A 1298
REMARK 465 MET A 1299
REMARK 465 ASN A 1300
REMARK 465 PHE A 1301
REMARK 465 GLU A 1302
REMARK 465 ASP A 1303
REMARK 465 GLY A 1304
REMARK 465 GLY A 1305
REMARK 465 VAL A 1306
REMARK 465 VAL A 1307
REMARK 465 THR A 1308
REMARK 465 VAL A 1309
REMARK 465 THR A 1310
REMARK 465 GLN A 1311
REMARK 465 ASP A 1312
REMARK 465 SER A 1313
REMARK 465 SER A 1314
REMARK 465 LEU A 1315
REMARK 465 GLN A 1316
REMARK 465 ASP A 1317
REMARK 465 GLY A 1318
REMARK 465 GLU A 1319
REMARK 465 PHE A 1320
REMARK 465 ILE A 1321
REMARK 465 TYR A 1322
REMARK 465 LYS A 1323
REMARK 465 VAL A 1324
REMARK 465 LYS A 1325
REMARK 465 LEU A 1326
REMARK 465 ARG A 1327
REMARK 465 GLY A 1328
REMARK 465 THR A 1329
REMARK 465 ASN A 1330
REMARK 465 PHE A 1331
REMARK 465 PRO A 1332
REMARK 465 SER A 1333
REMARK 465 ASP A 1334
REMARK 465 GLY A 1335
REMARK 465 PRO A 1336
REMARK 465 VAL A 1337
REMARK 465 MET A 1338
REMARK 465 GLN A 1339
REMARK 465 LYS A 1340
REMARK 465 LYS A 1341
REMARK 465 THR A 1342
REMARK 465 MET A 1343
REMARK 465 GLY A 1344
REMARK 465 SER A 1345
REMARK 465 GLU A 1346
REMARK 465 ALA A 1347
REMARK 465 SER A 1348
REMARK 465 SER A 1349
REMARK 465 GLU A 1350
REMARK 465 ARG A 1351
REMARK 465 MET A 1352
REMARK 465 TYR A 1353
REMARK 465 PRO A 1354
REMARK 465 GLU A 1355
REMARK 465 ASP A 1356
REMARK 465 GLY A 1357
REMARK 465 ALA A 1358
REMARK 465 LEU A 1359
REMARK 465 LYS A 1360
REMARK 465 GLY A 1361
REMARK 465 GLU A 1362
REMARK 465 VAL A 1363
REMARK 465 LYS A 1364
REMARK 465 TYR A 1365
REMARK 465 ARG A 1366
REMARK 465 LEU A 1367
REMARK 465 LYS A 1368
REMARK 465 LEU A 1369
REMARK 465 LYS A 1370
REMARK 465 ASP A 1371
REMARK 465 GLY A 1372
REMARK 465 GLY A 1373
REMARK 465 HIS A 1374
REMARK 465 TYR A 1375
REMARK 465 ASP A 1376
REMARK 465 ALA A 1377
REMARK 465 GLU A 1378
REMARK 465 VAL A 1379
REMARK 465 LYS A 1380
REMARK 465 THR A 1381
REMARK 465 THR A 1382
REMARK 465 TYR A 1383
REMARK 465 LYS A 1384
REMARK 465 ALA A 1385
REMARK 465 LYS A 1386
REMARK 465 LYS A 1387
REMARK 465 PRO A 1388
REMARK 465 VAL A 1389
REMARK 465 GLN A 1390
REMARK 465 LEU A 1391
REMARK 465 PRO A 1392
REMARK 465 GLY A 1393
REMARK 465 ALA A 1394
REMARK 465 TYR A 1395
REMARK 465 ASN A 1396
REMARK 465 VAL A 1397
REMARK 465 ASN A 1398
REMARK 465 ARG A 1399
REMARK 465 LYS A 1400
REMARK 465 LEU A 1401
REMARK 465 ASP A 1402
REMARK 465 ILE A 1403
REMARK 465 THR A 1404
REMARK 465 SER A 1405
REMARK 465 HIS A 1406
REMARK 465 ASN A 1407
REMARK 465 GLU A 1408
REMARK 465 ASP A 1409
REMARK 465 TYR A 1410
REMARK 465 THR A 1411
REMARK 465 ILE A 1412
REMARK 465 VAL A 1413
REMARK 465 GLU A 1414
REMARK 465 GLN A 1415
REMARK 465 TYR A 1416
REMARK 465 GLU A 1417
REMARK 465 ARG A 1418
REMARK 465 ALA A 1419
REMARK 465 GLU A 1420
REMARK 465 GLY A 1421
REMARK 465 ARG A 1422
REMARK 465 HIS A 1423
REMARK 465 SER A 1424
REMARK 465 THR A 1425
REMARK 465 GLY A 1426
REMARK 465 GLY A 1427
REMARK 465 MET A 1428
REMARK 465 ASP A 1429
REMARK 465 GLU A 1430
REMARK 465 LEU A 1431
REMARK 465 TYR A 1432
REMARK 465 LYS A 1433
REMARK 465 SER A 1434
REMARK 465 ALA A 1435
REMARK 465 HIS A 1436
REMARK 465 HIS A 1437
REMARK 465 HIS A 1438
REMARK 465 HIS A 1439
REMARK 465 HIS A 1440
REMARK 465 HIS A 1441
REMARK 465 HIS A 1442
REMARK 465 HIS A 1443
REMARK 465 HIS A 1444
REMARK 465 HIS A 1445
REMARK 465 GLY B -267
REMARK 465 GLY B -266
REMARK 465 SER B -265
REMARK 465 GLY B -264
REMARK 465 GLY B -263
REMARK 465 SER B -262
REMARK 465 ALA B -261
REMARK 465 SER B -260
REMARK 465 VAL B -259
REMARK 465 ILE B -258
REMARK 465 LYS B -257
REMARK 465 PRO B -256
REMARK 465 GLU B -255
REMARK 465 MET B -254
REMARK 465 LYS B -253
REMARK 465 ILE B -252
REMARK 465 LYS B -251
REMARK 465 LEU B -250
REMARK 465 ARG B -249
REMARK 465 MET B -248
REMARK 465 GLU B -247
REMARK 465 GLY B -246
REMARK 465 ALA B -245
REMARK 465 VAL B -244
REMARK 465 ASN B -243
REMARK 465 GLY B -242
REMARK 465 HIS B -241
REMARK 465 LYS B -240
REMARK 465 PHE B -239
REMARK 465 VAL B -238
REMARK 465 ILE B -237
REMARK 465 GLU B -236
REMARK 465 GLY B -235
REMARK 465 GLU B -234
REMARK 465 GLY B -233
REMARK 465 ILE B -232
REMARK 465 GLY B -231
REMARK 465 LYS B -230
REMARK 465 PRO B -229
REMARK 465 TYR B -228
REMARK 465 GLU B -227
REMARK 465 GLY B -226
REMARK 465 THR B -225
REMARK 465 GLN B -224
REMARK 465 THR B -223
REMARK 465 LEU B -222
REMARK 465 ASP B -221
REMARK 465 LEU B -220
REMARK 465 THR B -219
REMARK 465 VAL B -218
REMARK 465 GLU B -217
REMARK 465 GLU B -216
REMARK 465 GLY B -215
REMARK 465 ALA B -214
REMARK 465 PRO B -213
REMARK 465 LEU B -212
REMARK 465 PRO B -211
REMARK 465 PHE B -210
REMARK 465 SER B -209
REMARK 465 TYR B -208
REMARK 465 ASP B -207
REMARK 465 ILE B -206
REMARK 465 LEU B -205
REMARK 465 THR B -204
REMARK 465 PRO B -203
REMARK 465 ALA B -202
REMARK 465 PHE B -201
REMARK 465 GLN B -200
REMARK 465 TYR B -199
REMARK 465 GLY B -198
REMARK 465 ASN B -197
REMARK 465 ARG B -196
REMARK 465 ALA B -195
REMARK 465 PHE B -194
REMARK 465 THR B -193
REMARK 465 LYS B -192
REMARK 465 TYR B -191
REMARK 465 PRO B -190
REMARK 465 GLU B -189
REMARK 465 ASP B -188
REMARK 465 ILE B -187
REMARK 465 PRO B -186
REMARK 465 ASP B -185
REMARK 465 TYR B -184
REMARK 465 PHE B -183
REMARK 465 LYS B -182
REMARK 465 GLN B -181
REMARK 465 ALA B -180
REMARK 465 PHE B -179
REMARK 465 PRO B -178
REMARK 465 GLU B -177
REMARK 465 GLY B -176
REMARK 465 TYR B -175
REMARK 465 SER B -174
REMARK 465 TRP B -173
REMARK 465 GLU B -172
REMARK 465 ARG B -171
REMARK 465 SER B -170
REMARK 465 MET B -169
REMARK 465 THR B -168
REMARK 465 TYR B -167
REMARK 465 GLU B -166
REMARK 465 ASP B -165
REMARK 465 GLN B -164
REMARK 465 GLY B -163
REMARK 465 ILE B -162
REMARK 465 CYS B -161
REMARK 465 ILE B -160
REMARK 465 ALA B -159
REMARK 465 THR B -158
REMARK 465 SER B -157
REMARK 465 ASP B -156
REMARK 465 ILE B -155
REMARK 465 THR B -154
REMARK 465 MET B -153
REMARK 465 GLU B -152
REMARK 465 GLY B -151
REMARK 465 ASP B -150
REMARK 465 CYS B -149
REMARK 465 PHE B -148
REMARK 465 PHE B -147
REMARK 465 TYR B -146
REMARK 465 GLU B -145
REMARK 465 ILE B -144
REMARK 465 ARG B -143
REMARK 465 PHE B -142
REMARK 465 ASP B -141
REMARK 465 GLY B -140
REMARK 465 THR B -139
REMARK 465 ASN B -138
REMARK 465 PHE B -137
REMARK 465 PRO B -136
REMARK 465 PRO B -135
REMARK 465 ASN B -134
REMARK 465 GLY B -133
REMARK 465 PRO B -132
REMARK 465 VAL B -131
REMARK 465 MET B -130
REMARK 465 GLN B -129
REMARK 465 LYS B -128
REMARK 465 LYS B -127
REMARK 465 THR B -126
REMARK 465 LEU B -125
REMARK 465 LYS B -124
REMARK 465 TRP B -123
REMARK 465 GLU B -122
REMARK 465 PRO B -121
REMARK 465 SER B -120
REMARK 465 THR B -119
REMARK 465 GLU B -118
REMARK 465 LYS B -117
REMARK 465 MET B -116
REMARK 465 TYR B -115
REMARK 465 VAL B -114
REMARK 465 GLU B -113
REMARK 465 ASP B -112
REMARK 465 GLY B -111
REMARK 465 VAL B -110
REMARK 465 LEU B -109
REMARK 465 LYS B -108
REMARK 465 GLY B -107
REMARK 465 ASP B -106
REMARK 465 VAL B -105
REMARK 465 GLU B -104
REMARK 465 MET B -103
REMARK 465 ALA B -102
REMARK 465 LEU B -101
REMARK 465 LEU B -100
REMARK 465 LEU B -99
REMARK 465 GLU B -98
REMARK 465 GLY B -97
REMARK 465 GLY B -96
REMARK 465 GLY B -95
REMARK 465 HIS B -94
REMARK 465 TYR B -93
REMARK 465 ARG B -92
REMARK 465 CYS B -91
REMARK 465 ASP B -90
REMARK 465 PHE B -89
REMARK 465 LYS B -88
REMARK 465 THR B -87
REMARK 465 THR B -86
REMARK 465 TYR B -85
REMARK 465 LYS B -84
REMARK 465 ALA B -83
REMARK 465 LYS B -82
REMARK 465 LYS B -81
REMARK 465 ASP B -80
REMARK 465 VAL B -79
REMARK 465 ARG B -78
REMARK 465 LEU B -77
REMARK 465 PRO B -76
REMARK 465 ASP B -75
REMARK 465 ALA B -74
REMARK 465 HIS B -73
REMARK 465 GLU B -72
REMARK 465 VAL B -71
REMARK 465 ASP B -70
REMARK 465 HIS B -69
REMARK 465 ARG B -68
REMARK 465 ILE B -67
REMARK 465 GLU B -66
REMARK 465 ILE B -65
REMARK 465 LEU B -64
REMARK 465 SER B -63
REMARK 465 HIS B -62
REMARK 465 ASP B -61
REMARK 465 LYS B -60
REMARK 465 ASP B -59
REMARK 465 TYR B -58
REMARK 465 ASN B -57
REMARK 465 LYS B -56
REMARK 465 VAL B -55
REMARK 465 ARG B -54
REMARK 465 LEU B -53
REMARK 465 TYR B -52
REMARK 465 GLU B -51
REMARK 465 HIS B -50
REMARK 465 ALA B -49
REMARK 465 GLU B -48
REMARK 465 ALA B -47
REMARK 465 ARG B -46
REMARK 465 TYR B -45
REMARK 465 SER B -44
REMARK 465 GLY B -43
REMARK 465 GLY B -42
REMARK 465 GLY B -41
REMARK 465 SER B -40
REMARK 465 GLY B -39
REMARK 465 GLY B -38
REMARK 465 GLY B -37
REMARK 465 SER B -36
REMARK 465 ALA B -35
REMARK 465 TRP B -34
REMARK 465 SER B -33
REMARK 465 HIS B -32
REMARK 465 PRO B -31
REMARK 465 GLN B -30
REMARK 465 PHE B -29
REMARK 465 GLU B -28
REMARK 465 LYS B -27
REMARK 465 GLY B -26
REMARK 465 GLY B -25
REMARK 465 GLY B -24
REMARK 465 SER B -23
REMARK 465 GLY B -22
REMARK 465 GLY B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 GLY B -18
REMARK 465 GLY B -17
REMARK 465 SER B -16
REMARK 465 ALA B -15
REMARK 465 TRP B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 PRO B -11
REMARK 465 GLN B -10
REMARK 465 PHE B -9
REMARK 465 GLU B -8
REMARK 465 LYS B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 PRO B -4
REMARK 465 ASN B -3
REMARK 465 LYS B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 509 CG1 CG2
REMARK 470 ASP A 510 CG OD1 OD2
REMARK 470 ASP A 511 CG OD1 OD2
REMARK 470 LYS A 512 CG CD CE NZ
REMARK 470 ASP A 514 CG OD1 OD2
REMARK 470 SER A 546 OG
REMARK 470 GLU A 548 CG CD OE1 OE2
REMARK 470 SER A 579 OG
REMARK 470 GLN A 580 CG CD OE1 NE2
REMARK 470 ASN A 582 CG OD1 ND2
REMARK 470 THR A 584 OG1 CG2
REMARK 470 ILE A 588 CG1 CG2 CD1
REMARK 470 SER A 590 OG
REMARK 470 GLN A 591 CG CD OE1 NE2
REMARK 470 LEU A 594 CG CD1 CD2
REMARK 470 LYS A 596 CG CD CE NZ
REMARK 470 ASN A 598 CG OD1 ND2
REMARK 470 THR A 601 OG1 CG2
REMARK 470 THR A 602 OG1 CG2
REMARK 470 GLU A 746 CG CD OE1 OE2
REMARK 470 ARG A 776 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 953 CG CD NE CZ NH1 NH2
REMARK 470 MET A 993 CG SD CE
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 ASP A 193 -166.79 -125.01
REMARK 500 ILE A 213 -56.98 -127.68
REMARK 500 SER A 327 -124.02 60.17
REMARK 500 VAL A 437 -65.27 -121.98
REMARK 500 GLN A 471 47.46 -78.74
REMARK 500 LYS A 596 -72.65 -83.14
REMARK 500 SER A 619 73.32 -100.69
REMARK 500 ARG A 702 143.50 -33.34
REMARK 500 ARG A 757 -33.09 -133.01
REMARK 500 LEU A 903 -112.52 58.29
REMARK 500 PHE A 911 30.82 -94.89
REMARK 500 THR A 992 -65.79 -94.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-36996 RELATED DB: EMDB
REMARK 900 CRYO EM STRUCTURE OF THE PRODUCTS-BOUND PGAP1(BST1)-H443N FROM
REMARK 900 CHAETOMIUM THERMOPHILUM
DBREF 8K9R A 2 1184 UNP G0S652 G0S652_CHATD 2 1184
DBREF1 8K9R A 1199 1433 UNP A0A366VY15_9GAMM
DBREF2 8K9R A A0A366VY15 2 236
DBREF 8K9R B -267 -5 PDB 8K9R 8K9R -267 -5
DBREF 8K9R B -4 4 UNP P08174 DAF_HUMAN 345 353
SEQADV 8K9R MET A -1 UNP G0S652 INITIATING METHIONINE
SEQADV 8K9R GLY A 0 UNP G0S652 EXPRESSION TAG
SEQADV 8K9R SER A 1 UNP G0S652 EXPRESSION TAG
SEQADV 8K9R ASN A 443 UNP G0S652 HIS 443 ENGINEERED MUTATION
SEQADV 8K9R GLY A 1185 UNP G0S652 LINKER
SEQADV 8K9R THR A 1186 UNP G0S652 LINKER
SEQADV 8K9R LEU A 1187 UNP G0S652 LINKER
SEQADV 8K9R GLU A 1188 UNP G0S652 LINKER
SEQADV 8K9R VAL A 1189 UNP G0S652 LINKER
SEQADV 8K9R LEU A 1190 UNP G0S652 LINKER
SEQADV 8K9R PHE A 1191 UNP G0S652 LINKER
SEQADV 8K9R GLN A 1192 UNP G0S652 LINKER
SEQADV 8K9R GLY A 1193 UNP G0S652 LINKER
SEQADV 8K9R PRO A 1194 UNP G0S652 LINKER
SEQADV 8K9R LYS A 1195 UNP G0S652 LINKER
SEQADV 8K9R LEU A 1196 UNP G0S652 LINKER
SEQADV 8K9R GLU A 1197 UNP G0S652 LINKER
SEQADV 8K9R PHE A 1198 UNP G0S652 LINKER
SEQADV 8K9R SER A 1345 UNP A0A366VY1 TRP 148 ENGINEERED MUTATION
SEQADV 8K9R VAL A 1363 UNP A0A366VY1 ILE 166 ENGINEERED MUTATION
SEQADV 8K9R TYR A 1365 UNP A0A366VY1 GLN 168 ENGINEERED MUTATION
SEQADV 8K9R ARG A 1399 UNP A0A366VY1 ILE 202 ENGINEERED MUTATION
SEQADV 8K9R SER A 1434 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R ALA A 1435 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1436 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1437 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1438 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1439 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1440 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1441 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1442 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1443 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1444 UNP A0A366VY1 EXPRESSION TAG
SEQADV 8K9R HIS A 1445 UNP A0A366VY1 EXPRESSION TAG
SEQRES 1 A 1447 MET GLY SER ARG SER LEU SER SER ALA SER SER ASP ASP
SEQRES 2 A 1447 ASP ASP ALA PRO PRO ILE ARG VAL PRO ARG VAL ASN GLN
SEQRES 3 A 1447 CYS ALA THR SER ARG THR LYS ASP SER GLN SER PRO ALA
SEQRES 4 A 1447 GLN SER ALA SER LYS LEU ASP ARG ARG ARG SER ALA ASP
SEQRES 5 A 1447 ARG ARG PRO SER PHE SER ALA ASN ARG ARG SER GLY THR
SEQRES 6 A 1447 GLY ALA GLY THR GLY THR GLY THR GLY ILE ALA ASN TRP
SEQRES 7 A 1447 ARG PRO PHE ASP SER ARG ASP ALA THR VAL GLU ARG ALA
SEQRES 8 A 1447 GLY SER SER THR ALA THR THR ALA THR THR PRO PRO PRO
SEQRES 9 A 1447 SER SER SER LEU GLY LEU MET LEU ALA ALA ASN GLY ALA
SEQRES 10 A 1447 VAL GLN GLU LYS GLU MET VAL MET MET GLY LYS ALA GLN
SEQRES 11 A 1447 GLU HIS GLY PHE VAL GLY ARG ARG ALA PRO TRP ARG SER
SEQRES 12 A 1447 PRO TRP ALA ILE SER VAL PHE ALA PHE VAL THR SER LEU
SEQRES 13 A 1447 LEU GLY ILE GLY LEU LEU LEU ALA VAL ILE HIS SER SER
SEQRES 14 A 1447 VAL THR ARG GLN ILE ASP PRO LYS GLY CYS ARG MET SER
SEQRES 15 A 1447 TYR MET ARG PRO SER TYR ALA LYS LEU SER ASP PHE ASP
SEQRES 16 A 1447 THR GLU HIS THR ARG LEU ALA SER LYS TYR SER LEU TYR
SEQRES 17 A 1447 LEU TYR ARG GLU GLN GLY ILE ASP HIS ASP VAL LYS VAL
SEQRES 18 A 1447 ARG GLY VAL PRO VAL LEU PHE ILE PRO GLY ASN ALA GLY
SEQRES 19 A 1447 SER TYR LYS GLN VAL ARG PRO ILE ALA ALA GLU ALA ALA
SEQRES 20 A 1447 ASN TYR PHE HIS ASP VAL LEU GLN HIS ASP GLU ALA ALA
SEQRES 21 A 1447 LEU ARG ALA GLY VAL ARG SER LEU ASP PHE PHE THR VAL
SEQRES 22 A 1447 ASP PHE ASN GLU ASP ILE THR ALA PHE HIS GLY GLN THR
SEQRES 23 A 1447 LEU LEU ASP GLN ALA GLU TYR LEU ASN GLU ALA ILE ARG
SEQRES 24 A 1447 TYR ILE LEU SER LEU TYR LEU ASP PRO ARG VAL SER GLU
SEQRES 25 A 1447 ARG ASP PRO ASP LEU PRO ASP PRO THR SER VAL ILE VAL
SEQRES 26 A 1447 LEU GLY HIS SER MET GLY GLY ILE VAL ALA ARG THR MET
SEQRES 27 A 1447 LEU ILE MET PRO ASN TYR GLN HIS ASN SER ILE ASN THR
SEQRES 28 A 1447 ILE ILE THR MET SER ALA PRO HIS ALA ARG PRO PRO VAL
SEQRES 29 A 1447 SER PHE ASP GLY GLN ILE VAL GLN THR TYR LYS ASP ILE
SEQRES 30 A 1447 ASN ASN TYR TRP ARG HIS ALA TYR SER GLN LYS TRP ALA
SEQRES 31 A 1447 ASN ASP ASN PRO LEU TRP HIS VAL THR LEU VAL SER ILE
SEQRES 32 A 1447 ALA GLY GLY GLY LEU ASP THR VAL VAL PRO SER ASP TYR
SEQRES 33 A 1447 ALA SER ILE GLU SER LEU VAL PRO ASP THR HIS GLY PHE
SEQRES 34 A 1447 THR VAL PHE THR SER THR ILE PRO ASN VAL TRP THR SER
SEQRES 35 A 1447 MET ASP ASN GLN ALA ILE LEU TRP CYS ASP GLN PHE ARG
SEQRES 36 A 1447 LYS VAL ILE ILE ARG ALA LEU PHE ASP ILE VAL ASP VAL
SEQRES 37 A 1447 HIS ARG ALA SER GLN THR LYS PRO ARG ALA GLN ARG MET
SEQRES 38 A 1447 ARG VAL PHE LYS LYS TRP PHE LEU SER GLY MET GLU THR
SEQRES 39 A 1447 VAL ALA GLU LYS ILE ALA PRO THR SER ASP PRO THR THR
SEQRES 40 A 1447 LEU LEU ILE VAL ASP ASP LYS SER ASP SER ILE THR ALA
SEQRES 41 A 1447 GLU GLY GLU ARG LEU VAL LEU ARG GLU LEU GLY THR GLN
SEQRES 42 A 1447 GLY SER VAL ARG ALA HIS LEU MET PRO ILE PRO PRO PRO
SEQRES 43 A 1447 GLY SER PRO GLU LEU LYS ARG PHE THR LEU LEU THR ASP
SEQRES 44 A 1447 THR LYS LEU ASP LYS PRO GLY GLU ASN GLY LYS LEU GLU
SEQRES 45 A 1447 VAL MET PHE CYS SER VAL ILE PRO SER GLN PRO ASN PRO
SEQRES 46 A 1447 THR GLY PRO ALA ILE PRO SER GLN LEU ASP LEU SER LYS
SEQRES 47 A 1447 GLY ASN ALA GLY THR THR ARG LEU ALA CYS THR ASN VAL
SEQRES 48 A 1447 ALA PRO ASP VAL ILE THR LEU PRO ALA SER THR ARG PHE
SEQRES 49 A 1447 ALA ARG PHE PRO PHE SER VAL ARG LYS GLU ALA GLU ILE
SEQRES 50 A 1447 PRO PRO PHE SER TYR LEU GLU TYR VAL LEU ASP ASP ILE
SEQRES 51 A 1447 SER GLU HIS GLN PHE VAL ALA VAL ILE GLU LYS ALA THR
SEQRES 52 A 1447 ILE PRO THR PRO GLY PHE VAL ILE ALA GLU PHE SER ASP
SEQRES 53 A 1447 HIS SER ASN SER HIS HIS THR ARG HIS ILE GLY LEU ARG
SEQRES 54 A 1447 ASN LEU LEU THR PHE GLY ILE SER LEU ARG LEU PRO SER
SEQRES 55 A 1447 ASN ARG PRO MET MET SER GLU VAL ARG ILE PRO SER VAL
SEQRES 56 A 1447 LYS SER SER LEU LEU ALA TYR ASN LEU ARG ILE SER ALA
SEQRES 57 A 1447 LEU GLU CYS SER GLY ARG LYS ASP LEU PHE ALA PRO LEU
SEQRES 58 A 1447 VAL ARG GLN TYR LEU ALA GLU PRO TYR GLU SER LYS TYR
SEQRES 59 A 1447 PHE VAL ASN ALA ARG GLN ALA ALA VAL SER LEU HIS GLY
SEQRES 60 A 1447 VAL ALA PRO TYR VAL PRO PRO PRO MET SER ARG GLU PRO
SEQRES 61 A 1447 GLU ALA GLU GLY LEU ALA PHE GLN LEU TRP THR ASP PRO
SEQRES 62 A 1447 THR CYS ASN SER SER ILE GLN VAL ASP LEU THR VAL ASP
SEQRES 63 A 1447 VAL MET GLY SER LEU GLY LYS LEU TYR MET ARG TYR ARG
SEQRES 64 A 1447 THR VAL PHE ALA ALA PHE PRO LEU PHE ILE VAL SER LEU
SEQRES 65 A 1447 VAL LEU ARG LYS GLN PHE GLN VAL TYR ASP SER THR GLY
SEQRES 66 A 1447 SER PHE ILE THR PHE ALA GLU GLY LEU ASP LEU SER LEU
SEQRES 67 A 1447 ARG GLN SER ILE PRO VAL MET LEU ILE VAL LEU ALA ALA
SEQRES 68 A 1447 LEU THR LEU SER THR THR LYS MET ALA PRO SER SER SER
SEQRES 69 A 1447 ALA GLY LEU TRP HIS TRP GLY GLY ASN THR THR PHE THR
SEQRES 70 A 1447 ASN PHE HIS GLN ASN ASP LEU LEU ILE GLY THR GLN ASP
SEQRES 71 A 1447 PRO PHE PHE LEU PHE LEU ILE PRO LEU ILE GLY ILE ILE
SEQRES 72 A 1447 CYS VAL GLY VAL CYS THR VAL VAL ASN TYR ILE ALA LEU
SEQRES 73 A 1447 SER LEU THR ARG LEU ILE SER VAL VAL ILE SER PHE ILE
SEQRES 74 A 1447 GLY PHE LEU THR VAL ARG PHE GLY TRP VAL ASN ALA GLU
SEQRES 75 A 1447 ASP ARG ARG ARG PRO SER ASN PRO ALA ILE PHE PRO PRO
SEQRES 76 A 1447 SER SER PRO ARG ARG ARG MET ILE THR THR ALA VAL LEU
SEQRES 77 A 1447 LEU PHE LEU VAL SER THR MET ILE PRO TYR GLN LEU ALA
SEQRES 78 A 1447 TYR LEU VAL ALA CYS LEU VAL GLN LEU GLY THR LEU VAL
SEQRES 79 A 1447 ARG ALA GLN ARG ILE SER SER GLU LEU ARG SER PRO ALA
SEQRES 80 A 1447 ASN SER ASN PHE HIS ASN TYR VAL HIS SER ILE PHE ILE
SEQRES 81 A 1447 LEU MET LEU TRP ILE LEU PRO ILE ASN LEU PRO THR LEU
SEQRES 82 A 1447 VAL VAL TRP MET HIS ASN LEU SER VAL HIS TRP LEU THR
SEQRES 83 A 1447 PRO PHE THR SER HIS HIS ASN VAL PHE SER ILE MET PRO
SEQRES 84 A 1447 PHE ILE LEU LEU VAL GLU THR HIS THR THR GLY GLN MET
SEQRES 85 A 1447 ILE PRO ARG THR GLY GLY THR GLY ASN GLY ARG CYS CYS
SEQRES 86 A 1447 VAL LEU LEU ARG HIS ILE THR SER ILE LEU LEU LEU SER
SEQRES 87 A 1447 LEU ALA LEU TYR ALA ALA VAL TYR GLY VAL SER TYR ALA
SEQRES 88 A 1447 TYR THR LEU HIS GLN PHE VAL ASN LEU PHE ALA PHE TRP
SEQRES 89 A 1447 LEU VAL MET VAL HIS SER THR ALA ASP ASP TRP SER LEU
SEQRES 90 A 1447 THR GLY LEU ARG GLN LEU ILE LEU HIS ASN ARG ASN ASN
SEQRES 91 A 1447 ALA ASN ASN LYS SER GLU THR GLY SER ARG LYS ARG GLY
SEQRES 92 A 1447 LYS GLU PRO GLY THR LEU GLU VAL LEU PHE GLN GLY PRO
SEQRES 93 A 1447 LYS LEU GLU PHE VAL SER LYS GLY GLU GLU ASP ASN MET
SEQRES 94 A 1447 ALA ILE ILE LYS GLU PHE MET ARG PHE LYS VAL HIS MET
SEQRES 95 A 1447 GLU GLY SER VAL ASN GLY HIS GLU PHE GLU ILE GLU GLY
SEQRES 96 A 1447 GLU GLY GLU GLY ARG PRO TYR GLU GLY THR GLN THR ALA
SEQRES 97 A 1447 LYS LEU LYS VAL THR LYS GLY GLY PRO LEU PRO PHE ALA
SEQRES 98 A 1447 TRP ASP ILE LEU SER PRO GLN PHE MET TYR GLY SER LYS
SEQRES 99 A 1447 ALA TYR VAL LYS HIS PRO ALA ASP ILE PRO ASP TYR LEU
SEQRES 100 A 1447 LYS LEU SER PHE PRO GLU GLY PHE LYS TRP GLU ARG VAL
SEQRES 101 A 1447 MET ASN PHE GLU ASP GLY GLY VAL VAL THR VAL THR GLN
SEQRES 102 A 1447 ASP SER SER LEU GLN ASP GLY GLU PHE ILE TYR LYS VAL
SEQRES 103 A 1447 LYS LEU ARG GLY THR ASN PHE PRO SER ASP GLY PRO VAL
SEQRES 104 A 1447 MET GLN LYS LYS THR MET GLY SER GLU ALA SER SER GLU
SEQRES 105 A 1447 ARG MET TYR PRO GLU ASP GLY ALA LEU LYS GLY GLU VAL
SEQRES 106 A 1447 LYS TYR ARG LEU LYS LEU LYS ASP GLY GLY HIS TYR ASP
SEQRES 107 A 1447 ALA GLU VAL LYS THR THR TYR LYS ALA LYS LYS PRO VAL
SEQRES 108 A 1447 GLN LEU PRO GLY ALA TYR ASN VAL ASN ARG LYS LEU ASP
SEQRES 109 A 1447 ILE THR SER HIS ASN GLU ASP TYR THR ILE VAL GLU GLN
SEQRES 110 A 1447 TYR GLU ARG ALA GLU GLY ARG HIS SER THR GLY GLY MET
SEQRES 111 A 1447 ASP GLU LEU TYR LYS SER ALA HIS HIS HIS HIS HIS HIS
SEQRES 112 A 1447 HIS HIS HIS HIS
SEQRES 1 B 272 GLY GLY SER GLY GLY SER ALA SER VAL ILE LYS PRO GLU
SEQRES 2 B 272 MET LYS ILE LYS LEU ARG MET GLU GLY ALA VAL ASN GLY
SEQRES 3 B 272 HIS LYS PHE VAL ILE GLU GLY GLU GLY ILE GLY LYS PRO
SEQRES 4 B 272 TYR GLU GLY THR GLN THR LEU ASP LEU THR VAL GLU GLU
SEQRES 5 B 272 GLY ALA PRO LEU PRO PHE SER TYR ASP ILE LEU THR PRO
SEQRES 6 B 272 ALA PHE GLN TYR GLY ASN ARG ALA PHE THR LYS TYR PRO
SEQRES 7 B 272 GLU ASP ILE PRO ASP TYR PHE LYS GLN ALA PHE PRO GLU
SEQRES 8 B 272 GLY TYR SER TRP GLU ARG SER MET THR TYR GLU ASP GLN
SEQRES 9 B 272 GLY ILE CYS ILE ALA THR SER ASP ILE THR MET GLU GLY
SEQRES 10 B 272 ASP CYS PHE PHE TYR GLU ILE ARG PHE ASP GLY THR ASN
SEQRES 11 B 272 PHE PRO PRO ASN GLY PRO VAL MET GLN LYS LYS THR LEU
SEQRES 12 B 272 LYS TRP GLU PRO SER THR GLU LYS MET TYR VAL GLU ASP
SEQRES 13 B 272 GLY VAL LEU LYS GLY ASP VAL GLU MET ALA LEU LEU LEU
SEQRES 14 B 272 GLU GLY GLY GLY HIS TYR ARG CYS ASP PHE LYS THR THR
SEQRES 15 B 272 TYR LYS ALA LYS LYS ASP VAL ARG LEU PRO ASP ALA HIS
SEQRES 16 B 272 GLU VAL ASP HIS ARG ILE GLU ILE LEU SER HIS ASP LYS
SEQRES 17 B 272 ASP TYR ASN LYS VAL ARG LEU TYR GLU HIS ALA GLU ALA
SEQRES 18 B 272 ARG TYR SER GLY GLY GLY SER GLY GLY GLY SER ALA TRP
SEQRES 19 B 272 SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY
SEQRES 20 B 272 GLY SER GLY GLY SER ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 21 B 272 LYS GLY SER PRO ASN LYS GLY SER GLY THR THR SER
HET MAN A1501 11
HET MAN A1502 11
HET 05E A1503 18
HET PA1 A1504 11
HET L9H A1505 58
HET PLM A1506 18
HET CLR A1507 28
HET 80Y B 101 18
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM 05E 2-AZANYLETHYL [(2~{S},3~{S},4~{S},5~{S},6~{R})-6-
HETNAM 2 05E (HYDROXYMETHYL)-2,4,5-TRIS(OXIDANYL)OXAN-3-YL]
HETNAM 3 05E HYDROGEN PHOSPHATE
HETNAM PA1 2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM L9H [(2~{R})-1-OCTADECOXY-3-[OXIDANYL-[(2~{R},3~{R},5~{S},
HETNAM 2 L9H 6~{R})-2,3,4,5,6-PENTAKIS(OXIDANYL)CYCLOHEXYL]OXY-
HETNAM 3 L9H PHOSPHORYL]OXY-PROPAN-2-YL] OCTADECANOATE
HETNAM PLM PALMITIC ACID
HETNAM CLR CHOLESTEROL
HETNAM 80Y 2-AZANYLETHYL [(2R,3S,4S,5S,6S)-3,4,5,6-
HETNAM 2 80Y TETRAKIS(OXIDANYL)OXAN-2-YL]METHYL HYDROGEN PHOSPHATE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN PA1 ALPAH-D-GLUCOSAMINE; 2-AMINO-2-DEOXY-ALPHA-D-GLUCOSE;
HETSYN 2 PA1 2-AMINO-2-DEOXY-D-GLUCOSE; 2-AMINO-2-DEOXY-GLUCOSE
FORMUL 3 MAN 2(C6 H12 O6)
FORMUL 5 05E C8 H18 N O9 P
FORMUL 6 PA1 C6 H13 N O5
FORMUL 7 L9H C45 H89 O12 P
FORMUL 8 PLM C16 H32 O2
FORMUL 9 CLR C27 H46 O
FORMUL 10 80Y C8 H18 N O9 P
HELIX 1 AA1 SER A 146 ARG A 170 1 25
HELIX 2 AA2 THR A 197 LYS A 202 5 6
HELIX 3 AA3 SER A 233 GLN A 236 5 4
HELIX 4 AA4 VAL A 237 VAL A 251 1 15
HELIX 5 AA5 ASP A 255 ALA A 261 1 7
HELIX 6 AA6 HIS A 281 TYR A 303 1 23
HELIX 7 AA7 SER A 327 LEU A 337 1 11
HELIX 8 AA8 ASP A 365 SER A 384 1 20
HELIX 9 AA9 TRP A 387 ASN A 391 5 5
HELIX 10 AB1 PRO A 411 SER A 416 5 6
HELIX 11 AB2 GLN A 444 CYS A 449 1 6
HELIX 12 AB3 CYS A 449 ASP A 462 1 14
HELIX 13 AB4 PRO A 474 LEU A 487 1 14
HELIX 14 AB5 ILE A 497 SER A 501 5 5
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 GLU A 777 GLU A 781 5 5
HELIX 21 AC3 ASP A 790 ASN A 794 5 5
HELIX 22 AC4 VAL A 805 LYS A 811 1 7
HELIX 23 AC5 LYS A 811 ARG A 817 1 7
HELIX 24 AC6 THR A 818 ALA A 822 5 5
HELIX 25 AC7 PHE A 823 GLY A 843 1 21
HELIX 26 AC8 THR A 847 GLN A 858 1 12
HELIX 27 AC9 GLN A 858 LEU A 872 1 15
HELIX 28 AD1 ASP A 908 LEU A 912 5 5
HELIX 29 AD2 PHE A 913 PHE A 954 1 42
HELIX 30 AD3 VAL A 985 MET A 993 1 9
HELIX 31 AD4 PRO A 995 ARG A 1022 1 28
HELIX 32 AD5 SER A 1023 HIS A 1061 1 39
HELIX 33 AD6 THR A 1067 THR A 1087 1 21
HELIX 34 AD7 CYS A 1103 GLY A 1125 1 23
HELIX 35 AD8 TYR A 1130 THR A 1149 1 20
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 SER A 265 ASP A 272 -1 O ASP A 272 N SER A 204
SHEET 4 AA1 8 GLY A 221 ILE A 227 1 N VAL A 224 O PHE A 269
SHEET 5 AA1 8 VAL A 321 HIS A 326 1 O ILE A 322 N LEU A 225
SHEET 6 AA1 8 ILE A 347 MET A 353 1 O MET A 353 N GLY A 325
SHEET 7 AA1 8 THR A 397 ALA A 402 1 O ILE A 401 N THR A 352
SHEET 8 AA1 8 GLY A 426 PHE A 430 1 O VAL A 429 N SER A 400
SHEET 1 AA2 6 ARG A 535 PRO A 540 0
SHEET 2 AA2 6 PHE A 653 GLU A 658 -1 O VAL A 656 N HIS A 537
SHEET 3 AA2 6 LEU A 569 VAL A 576 -1 N GLU A 570 O ILE A 657
SHEET 4 AA2 6 THR A 602 ASN A 608 -1 O THR A 607 N PHE A 573
SHEET 5 AA2 6 THR A 505 VAL A 509 -1 N THR A 505 O CYS A 606
SHEET 6 AA2 6 GLN A 591 LEU A 594 1 O GLN A 591 N LEU A 506
SHEET 1 AA3 5 LEU A 523 LEU A 528 0
SHEET 2 AA3 5 THR A 664 ASP A 674 -1 O THR A 664 N LEU A 528
SHEET 3 AA3 5 LYS A 550 THR A 556 -1 N LEU A 555 O ILE A 669
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 ARG A 709 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 LEU A 744 -1 N ARG A 741 O GLN A 786
SHEET 5 AA4 5 GLU A 749 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 ASP A 804 -1 O VAL A 799 N LEU A 696
SHEET 3 AA5 4 ALA A 719 ILE A 724 -1 N ALA A 719 O ASP A 804
SHEET 4 AA5 4 GLN A 758 SER A 762 -1 O VAL A 761 N TYR A 720
SSBOND 1 CYS A 177 CYS A 449 1555 1555 2.04
SSBOND 2 CYS A 574 CYS A 606 1555 1555 2.03
SSBOND 3 CYS A 729 CYS A 793 1555 1555 2.04
LINK C1 MAN A1501 O53 80Y B 101 1555 1555 1.39
LINK C1 MAN A1502 O96 05E A1503 1555 1555 1.38
LINK O2 MAN A1502 C51 80Y B 101 1555 1555 1.40
LINK C80 05E A1503 O4 PA1 A1504 1555 1555 1.40
LINK C1 PA1 A1504 O10 L9H A1505 1555 1555 1.39
LINK C SER B 4 N80 80Y B 101 1555 1555 1.33
CISPEP 1 GLU A 746 PRO A 747 0 -4.47
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 7488 ALA A1150
TER 7513 SER B 4
MASTER 923 0 8 35 28 0 0 6 7684 2 180 133
END |