HEADER VIRAL PROTEIN 03-JUN-23 8JLX TITLE CCHFV ENVELOPE PROTEIN GC IN COMPLEX WITH GC13 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN C,CCHFV GC FUSION LOOPS; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GC,75 KDA PROTEIN,GLYCOPROTEIN G1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MOUSE ANTIBODY GC13 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MOUSE ANTIBODY GC13 LIGHT CHAIN; COMPND 11 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CRIMEAN-CONGO HEMORRHAGIC FEVER SOURCE 3 ORTHONAIROVIRUS; SOURCE 4 ORGANISM_TAXID: 1980519; SOURCE 5 GENE: GP; SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER S2 CELLS; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_TAXID: 10090 KEYWDS CCHFV, GLYCOPROTEIN C, ANTIBODY, BUNYAVIRUS, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.CHONG,S.CAO REVDAT 1 24-JAN-24 8JLX 0 JRNL AUTH T.CHONG,S.CAO JRNL TITL INTERACTIONS BETWEEN CCHFV ENVELOPE PROTEIN GC AND JRNL TITL 2 NEUTRALIZING MONOCLONAL ANTIBODY GC13 JRNL REF PLOS PATHOG. 2024 JRNL REFN ESSN 1553-7374 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 387809 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 8JLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1300037848. 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 : CCHFV ENVELOPE PROTEIN GC-GC13 REMARK 245 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : JEOL CRYO ARM 300 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 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) : 4000.00 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L 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 1049 REMARK 465 LYS A 1050 REMARK 465 ASN A 1051 REMARK 465 LEU A 1052 REMARK 465 LEU A 1053 REMARK 465 ASN A 1054 REMARK 465 SER A 1055 REMARK 465 THR A 1056 REMARK 465 SER A 1057 REMARK 465 LEU A 1058 REMARK 465 GLU A 1059 REMARK 465 THR A 1060 REMARK 465 SER A 1061 REMARK 465 LEU A 1062 REMARK 465 SER A 1063 REMARK 465 ILE A 1064 REMARK 465 GLU A 1065 REMARK 465 ALA A 1066 REMARK 465 PRO A 1067 REMARK 465 TRP A 1068 REMARK 465 GLY A 1069 REMARK 465 ALA A 1070 REMARK 465 ILE A 1071 REMARK 465 ASN A 1072 REMARK 465 VAL A 1073 REMARK 465 GLN A 1074 REMARK 465 SER A 1075 REMARK 465 THR A 1076 REMARK 465 TYR A 1077 REMARK 465 LYS A 1078 REMARK 465 PRO A 1079 REMARK 465 THR A 1080 REMARK 465 VAL A 1081 REMARK 465 SER A 1082 REMARK 465 THR A 1083 REMARK 465 ALA A 1084 REMARK 465 ASN A 1085 REMARK 465 ILE A 1086 REMARK 465 ALA A 1087 REMARK 465 LEU A 1088 REMARK 465 SER A 1089 REMARK 465 TRP A 1090 REMARK 465 SER A 1091 REMARK 465 SER A 1092 REMARK 465 VAL A 1093 REMARK 465 GLU A 1094 REMARK 465 HIS A 1095 REMARK 465 ARG A 1096 REMARK 465 GLY A 1097 REMARK 465 ASN A 1098 REMARK 465 LYS A 1099 REMARK 465 ILE A 1100 REMARK 465 LEU A 1101 REMARK 465 VAL A 1102 REMARK 465 SER A 1103 REMARK 465 GLY A 1104 REMARK 465 ARG A 1105 REMARK 465 SER A 1106 REMARK 465 GLU A 1107 REMARK 465 SER A 1108 REMARK 465 ILE A 1109 REMARK 465 MET A 1110 REMARK 465 LYS A 1111 REMARK 465 LEU A 1112 REMARK 465 GLU A 1113 REMARK 465 GLU A 1114 REMARK 465 ARG A 1115 REMARK 465 THR A 1116 REMARK 465 GLY A 1117 REMARK 465 ILE A 1118 REMARK 465 SER A 1119 REMARK 465 TRP A 1120 REMARK 465 ASP A 1121 REMARK 465 LEU A 1122 REMARK 465 GLY A 1123 REMARK 465 VAL A 1124 REMARK 465 GLU A 1125 REMARK 465 ASP A 1126 REMARK 465 ALA A 1127 REMARK 465 SER A 1128 REMARK 465 GLU A 1129 REMARK 465 SER A 1130 REMARK 465 LYS A 1131 REMARK 465 LEU A 1132 REMARK 465 LEU A 1133 REMARK 465 THR A 1134 REMARK 465 VAL A 1135 REMARK 465 SER A 1136 REMARK 465 VAL A 1137 REMARK 465 MET A 1138 REMARK 465 ASP A 1139 REMARK 465 LEU A 1140 REMARK 465 SER A 1141 REMARK 465 GLN A 1142 REMARK 465 MET A 1143 REMARK 465 TYR A 1144 REMARK 465 SER A 1145 REMARK 465 PRO A 1146 REMARK 465 VAL A 1147 REMARK 465 PHE A 1148 REMARK 465 GLU A 1149 REMARK 465 TYR A 1150 REMARK 465 LEU A 1151 REMARK 465 SER A 1152 REMARK 465 GLY A 1153 REMARK 465 ASP A 1154 REMARK 465 ARG A 1155 REMARK 465 GLN A 1156 REMARK 465 GLY A 1209 REMARK 465 LEU A 1210 REMARK 465 ASP A 1211 REMARK 465 VAL A 1212 REMARK 465 LYS A 1213 REMARK 465 ASP A 1214 REMARK 465 LEU A 1215 REMARK 465 PHE A 1216 REMARK 465 THR A 1217 REMARK 465 ASP A 1218 REMARK 465 TYR A 1219 REMARK 465 MET A 1220 REMARK 465 PHE A 1221 REMARK 465 VAL A 1222 REMARK 465 LYS A 1223 REMARK 465 TRP A 1224 REMARK 465 LYS A 1225 REMARK 465 VAL A 1226 REMARK 465 GLU A 1227 REMARK 465 TYR A 1228 REMARK 465 ILE A 1229 REMARK 465 LYS A 1230 REMARK 465 THR A 1231 REMARK 465 GLU A 1232 REMARK 465 ALA A 1233 REMARK 465 ILE A 1234 REMARK 465 VAL A 1235 REMARK 465 CYS A 1236 REMARK 465 VAL A 1237 REMARK 465 GLU A 1238 REMARK 465 LEU A 1239 REMARK 465 THR A 1240 REMARK 465 SER A 1241 REMARK 465 GLN A 1242 REMARK 465 GLU A 1243 REMARK 465 ARG A 1244 REMARK 465 GLN A 1245 REMARK 465 CYS A 1246 REMARK 465 SER A 1247 REMARK 465 LEU A 1248 REMARK 465 ILE A 1249 REMARK 465 GLU A 1250 REMARK 465 ALA A 1251 REMARK 465 GLY A 1252 REMARK 465 THR A 1253 REMARK 465 ARG A 1254 REMARK 465 PHE A 1255 REMARK 465 ASN A 1256 REMARK 465 LEU A 1257 REMARK 465 GLY A 1258 REMARK 465 PRO A 1259 REMARK 465 VAL A 1260 REMARK 465 THR A 1261 REMARK 465 ILE A 1262 REMARK 465 THR A 1263 REMARK 465 LEU A 1264 REMARK 465 SER A 1265 REMARK 465 GLU A 1266 REMARK 465 PRO A 1267 REMARK 465 ARG A 1268 REMARK 465 ASN A 1269 REMARK 465 ILE A 1270 REMARK 465 GLN A 1271 REMARK 465 GLN A 1272 REMARK 465 LYS A 1273 REMARK 465 LEU A 1274 REMARK 465 PRO A 1275 REMARK 465 PRO A 1276 REMARK 465 GLU A 1277 REMARK 465 ILE A 1278 REMARK 465 ILE A 1279 REMARK 465 THR A 1280 REMARK 465 LEU A 1281 REMARK 465 HIS A 1282 REMARK 465 PRO A 1283 REMARK 465 ARG A 1284 REMARK 465 ILE A 1285 REMARK 465 GLU A 1286 REMARK 465 GLU A 1287 REMARK 465 GLY A 1288 REMARK 465 PHE A 1289 REMARK 465 PHE A 1290 REMARK 465 ASP A 1291 REMARK 465 LEU A 1292 REMARK 465 MET A 1293 REMARK 465 HIS A 1294 REMARK 465 VAL A 1295 REMARK 465 GLN A 1296 REMARK 465 LYS A 1297 REMARK 465 VAL A 1298 REMARK 465 LEU A 1299 REMARK 465 SER A 1300 REMARK 465 ALA A 1301 REMARK 465 SER A 1302 REMARK 465 THR A 1303 REMARK 465 VAL A 1304 REMARK 465 CYS A 1305 REMARK 465 LYS A 1306 REMARK 465 LEU A 1307 REMARK 465 GLN A 1308 REMARK 465 SER A 1309 REMARK 465 CYS A 1310 REMARK 465 THR A 1311 REMARK 465 HIS A 1312 REMARK 465 GLY A 1313 REMARK 465 VAL A 1314 REMARK 465 PRO A 1315 REMARK 465 GLY A 1316 REMARK 465 ASP A 1317 REMARK 465 LEU A 1318 REMARK 465 GLN A 1319 REMARK 465 VAL A 1320 REMARK 465 TYR A 1321 REMARK 465 HIS A 1322 REMARK 465 ILE A 1323 REMARK 465 GLY A 1324 REMARK 465 ASN A 1325 REMARK 465 LEU A 1326 REMARK 465 LEU A 1327 REMARK 465 LYS A 1328 REMARK 465 GLY A 1329 REMARK 465 ASP A 1330 REMARK 465 LYS A 1331 REMARK 465 VAL A 1332 REMARK 465 ASN A 1333 REMARK 465 GLY A 1334 REMARK 465 HIS A 1335 REMARK 465 LEU A 1336 REMARK 465 ILE A 1337 REMARK 465 HIS A 1338 REMARK 465 LYS A 1339 REMARK 465 ILE A 1340 REMARK 465 GLU A 1341 REMARK 465 PRO A 1342 REMARK 465 HIS A 1343 REMARK 465 PHE A 1344 REMARK 465 ASN A 1345 REMARK 465 THR A 1346 REMARK 465 SER A 1347 REMARK 465 TRP A 1348 REMARK 465 MET A 1349 REMARK 465 SER A 1350 REMARK 465 TRP A 1351 REMARK 465 ASP A 1352 REMARK 465 GLY A 1353 REMARK 465 CYS A 1354 REMARK 465 GLY A 1372 REMARK 465 VAL A 1373 REMARK 465 THR A 1374 REMARK 465 GLN A 1375 REMARK 465 HIS A 1376 REMARK 465 ASN A 1377 REMARK 465 HIS A 1378 REMARK 465 ALA A 1379 REMARK 465 SER A 1380 REMARK 465 PHE A 1381 REMARK 465 VAL A 1382 REMARK 465 ASN A 1383 REMARK 465 LEU A 1384 REMARK 465 LEU A 1385 REMARK 465 ASN A 1386 REMARK 465 ILE A 1387 REMARK 465 GLU A 1388 REMARK 465 THR A 1389 REMARK 465 ASP A 1390 REMARK 465 TYR A 1391 REMARK 465 THR A 1392 REMARK 465 LYS A 1393 REMARK 465 ASN A 1394 REMARK 465 PHE A 1395 REMARK 465 HIS A 1396 REMARK 465 PHE A 1397 REMARK 465 HIS A 1398 REMARK 465 SER A 1399 REMARK 465 LYS A 1400 REMARK 465 ARG A 1401 REMARK 465 VAL A 1402 REMARK 465 THR A 1403 REMARK 465 ALA A 1404 REMARK 465 HIS A 1405 REMARK 465 GLY A 1406 REMARK 465 ASP A 1407 REMARK 465 THR A 1408 REMARK 465 PRO A 1409 REMARK 465 GLN A 1410 REMARK 465 LEU A 1411 REMARK 465 ASP A 1412 REMARK 465 LEU A 1413 REMARK 465 LYS A 1414 REMARK 465 ALA A 1415 REMARK 465 ARG A 1416 REMARK 465 PRO A 1417 REMARK 465 THR A 1418 REMARK 465 TYR A 1419 REMARK 465 GLY A 1420 REMARK 465 ALA A 1421 REMARK 465 GLY A 1422 REMARK 465 GLU A 1423 REMARK 465 ILE A 1424 REMARK 465 THR A 1425 REMARK 465 VAL A 1426 REMARK 465 LEU A 1427 REMARK 465 VAL A 1428 REMARK 465 GLU A 1429 REMARK 465 VAL A 1430 REMARK 465 ALA A 1431 REMARK 465 ASP A 1432 REMARK 465 MET A 1433 REMARK 465 GLU A 1434 REMARK 465 LEU A 1435 REMARK 465 HIS A 1436 REMARK 465 THR A 1437 REMARK 465 LYS A 1438 REMARK 465 LYS A 1439 REMARK 465 ILE A 1440 REMARK 465 GLU A 1441 REMARK 465 ILE A 1442 REMARK 465 SER A 1443 REMARK 465 GLY A 1444 REMARK 465 LEU A 1445 REMARK 465 LYS A 1446 REMARK 465 PHE A 1447 REMARK 465 ALA A 1448 REMARK 465 SER A 1449 REMARK 465 LEU A 1450 REMARK 465 ALA A 1451 REMARK 465 CYS A 1452 REMARK 465 THR A 1453 REMARK 465 GLY A 1454 REMARK 465 CYS A 1455 REMARK 465 TYR A 1456 REMARK 465 ALA A 1457 REMARK 465 CYS A 1458 REMARK 465 SER A 1459 REMARK 465 SER A 1460 REMARK 465 GLY A 1461 REMARK 465 ILE A 1462 REMARK 465 SER A 1463 REMARK 465 CYS A 1464 REMARK 465 LYS A 1465 REMARK 465 VAL A 1466 REMARK 465 ARG A 1467 REMARK 465 ILE A 1468 REMARK 465 HIS A 1469 REMARK 465 VAL A 1470 REMARK 465 ASP A 1471 REMARK 465 GLU A 1472 REMARK 465 PRO A 1473 REMARK 465 ASP A 1474 REMARK 465 GLU A 1475 REMARK 465 LEU A 1476 REMARK 465 THR A 1477 REMARK 465 VAL A 1478 REMARK 465 HIS A 1479 REMARK 465 VAL A 1480 REMARK 465 LYS A 1481 REMARK 465 SER A 1482 REMARK 465 ASP A 1483 REMARK 465 ASP A 1484 REMARK 465 PRO A 1485 REMARK 465 ASP A 1486 REMARK 465 VAL A 1487 REMARK 465 VAL A 1488 REMARK 465 ALA A 1489 REMARK 465 ALA A 1490 REMARK 465 SER A 1491 REMARK 465 SER A 1492 REMARK 465 SER A 1493 REMARK 465 LEU A 1494 REMARK 465 MET A 1495 REMARK 465 ALA A 1496 REMARK 465 ARG A 1497 REMARK 465 LYS A 1498 REMARK 465 LEU A 1499 REMARK 465 GLU A 1500 REMARK 465 PHE A 1501 REMARK 465 GLY A 1502 REMARK 465 THR A 1503 REMARK 465 ASP A 1504 REMARK 465 SER A 1505 REMARK 465 THR A 1506 REMARK 465 PHE A 1507 REMARK 465 LYS A 1508 REMARK 465 ALA A 1509 REMARK 465 PHE A 1510 REMARK 465 SER A 1511 REMARK 465 ALA A 1512 REMARK 465 MET A 1513 REMARK 465 PRO A 1514 REMARK 465 LYS A 1515 REMARK 465 THR A 1516 REMARK 465 SER A 1517 REMARK 465 LEU A 1518 REMARK 465 CYS A 1519 REMARK 465 PHE A 1520 REMARK 465 TYR A 1521 REMARK 465 ILE A 1522 REMARK 465 VAL A 1523 REMARK 465 GLU A 1524 REMARK 465 ARG A 1525 REMARK 465 GLU A 1526 REMARK 465 HIS A 1527 REMARK 465 CYS A 1528 REMARK 465 LYS A 1529 REMARK 465 SER A 1530 REMARK 465 CYS A 1531 REMARK 465 SER A 1532 REMARK 465 GLU A 1533 REMARK 465 GLU A 1534 REMARK 465 ASP A 1535 REMARK 465 THR A 1536 REMARK 465 LYS A 1537 REMARK 465 LYS A 1538 REMARK 465 CYS A 1539 REMARK 465 VAL A 1540 REMARK 465 ASN A 1541 REMARK 465 THR A 1542 REMARK 465 LYS A 1543 REMARK 465 LEU A 1544 REMARK 465 GLU A 1545 REMARK 465 GLN A 1546 REMARK 465 PRO A 1547 REMARK 465 GLN A 1548 REMARK 465 SER A 1549 REMARK 465 ILE A 1550 REMARK 465 LEU A 1551 REMARK 465 ILE A 1552 REMARK 465 GLU A 1553 REMARK 465 HIS A 1554 REMARK 465 LYS A 1555 REMARK 465 GLY A 1556 REMARK 465 THR A 1557 REMARK 465 ILE A 1558 REMARK 465 ILE A 1559 REMARK 465 GLY A 1560 REMARK 465 LYS A 1561 REMARK 465 GLN A 1562 REMARK 465 ASN A 1563 REMARK 465 SER A 1564 REMARK 465 THR A 1565 REMARK 465 CYS A 1566 REMARK 465 THR A 1567 REMARK 465 ALA A 1568 REMARK 465 LYS A 1569 REMARK 465 ALA A 1570 REMARK 465 SER A 1571 REMARK 465 ARG A 1572 REMARK 465 GLY A 1573 REMARK 465 SER A 1574 REMARK 465 GLY A 1575 REMARK 465 GLY A 1576 REMARK 465 MET A 1577 REMARK 465 LYS A 1578 REMARK 465 GLN A 1579 REMARK 465 ILE A 1580 REMARK 465 GLU A 1581 REMARK 465 ASP A 1582 REMARK 465 LYS A 1583 REMARK 465 ILE A 1584 REMARK 465 GLU A 1585 REMARK 465 GLU A 1586 REMARK 465 ILE A 1587 REMARK 465 LEU A 1588 REMARK 465 SER A 1589 REMARK 465 LYS A 1590 REMARK 465 ILE A 1591 REMARK 465 TYR A 1592 REMARK 465 HIS A 1593 REMARK 465 ILE A 1594 REMARK 465 GLU A 1595 REMARK 465 ASN A 1596 REMARK 465 GLU A 1597 REMARK 465 ILE A 1598 REMARK 465 ALA A 1599 REMARK 465 ARG A 1600 REMARK 465 ILE A 1601 REMARK 465 LYS A 1602 REMARK 465 LYS A 1603 REMARK 465 LEU A 1604 REMARK 465 ILE A 1605 REMARK 465 GLY A 1606 REMARK 465 GLU A 1607 REMARK 465 GLY A 1608 REMARK 465 SER A 1609 REMARK 465 GLY A 1610 REMARK 465 GLY A 1611 REMARK 465 SER A 1612 REMARK 465 ARG A 1613 REMARK 465 GLY A 1614 REMARK 465 PRO A 1615 REMARK 465 PHE A 1616 REMARK 465 GLU A 1617 REMARK 465 GLY A 1618 REMARK 465 LYS A 1619 REMARK 465 PRO A 1620 REMARK 465 ILE A 1621 REMARK 465 PRO A 1622 REMARK 465 ASN A 1623 REMARK 465 PRO A 1624 REMARK 465 LEU A 1625 REMARK 465 LEU A 1626 REMARK 465 GLY A 1627 REMARK 465 LEU A 1628 REMARK 465 ASP A 1629 REMARK 465 SER A 1630 REMARK 465 THR A 1631 REMARK 465 ARG A 1632 REMARK 465 THR A 1633 REMARK 465 GLY A 1634 REMARK 465 HIS A 1635 REMARK 465 HIS A 1636 REMARK 465 HIS A 1637 REMARK 465 HIS A 1638 REMARK 465 HIS A 1639 REMARK 465 HIS A 1640 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 PRO A1195 -174.08 -69.12 REMARK 500 ASP A1364 -56.71 -121.63 REMARK 500 TRP A1365 142.05 -173.10 REMARK 500 CYS H 22 110.57 -160.69 REMARK 500 ILE H 48 -63.57 -96.42 REMARK 500 PHE H 64 36.04 -98.22 REMARK 500 ALA H 92 -168.95 -166.57 REMARK 500 THR L 51 -10.99 72.42 REMARK 500 SER L 52 -15.21 -143.00 REMARK 500 SER L 60 3.52 -68.27 REMARK 500 SER L 76 -60.66 -91.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36368 RELATED DB: EMDB REMARK 900 RELATED ID: 8JKD RELATED DB: PDB REMARK 900 RELATED ID: EMD-36407 RELATED DB: EMDB REMARK 900 CCHFV ENVELOPE PROTEIN GC IN COMPLEX WITH GC13 DBREF 8JLX A 1049 1570 UNP Q8JSZ3 GP_CCHFI 1049 1570 DBREF 8JLX A 1571 1640 PDB 8JLX 8JLX 1571 1640 DBREF 8JLX H 1 117 PDB 8JLX 8JLX 1 117 DBREF 8JLX L 1 107 PDB 8JLX 8JLX 1 107 SEQRES 1 A 592 MET LYS ASN LEU LEU ASN SER THR SER LEU GLU THR SER SEQRES 2 A 592 LEU SER ILE GLU ALA PRO TRP GLY ALA ILE ASN VAL GLN SEQRES 3 A 592 SER THR TYR LYS PRO THR VAL SER THR ALA ASN ILE ALA SEQRES 4 A 592 LEU SER TRP SER SER VAL GLU HIS ARG GLY ASN LYS ILE SEQRES 5 A 592 LEU VAL SER GLY ARG SER GLU SER ILE MET LYS LEU GLU SEQRES 6 A 592 GLU ARG THR GLY ILE SER TRP ASP LEU GLY VAL GLU ASP SEQRES 7 A 592 ALA SER GLU SER LYS LEU LEU THR VAL SER VAL MET ASP SEQRES 8 A 592 LEU SER GLN MET TYR SER PRO VAL PHE GLU TYR LEU SER SEQRES 9 A 592 GLY ASP ARG GLN VAL GLY GLU TRP PRO LYS ALA THR CYS SEQRES 10 A 592 THR GLY ASP CYS PRO GLU ARG CYS GLY CYS THR SER SER SEQRES 11 A 592 THR CYS LEU HIS LYS GLU TRP PRO HIS SER ARG ASN TRP SEQRES 12 A 592 ARG CYS ASN PRO THR TRP CYS TRP GLY VAL GLY THR GLY SEQRES 13 A 592 CYS THR CYS CYS GLY LEU ASP VAL LYS ASP LEU PHE THR SEQRES 14 A 592 ASP TYR MET PHE VAL LYS TRP LYS VAL GLU TYR ILE LYS SEQRES 15 A 592 THR GLU ALA ILE VAL CYS VAL GLU LEU THR SER GLN GLU SEQRES 16 A 592 ARG GLN CYS SER LEU ILE GLU ALA GLY THR ARG PHE ASN SEQRES 17 A 592 LEU GLY PRO VAL THR ILE THR LEU SER GLU PRO ARG ASN SEQRES 18 A 592 ILE GLN GLN LYS LEU PRO PRO GLU ILE ILE THR LEU HIS SEQRES 19 A 592 PRO ARG ILE GLU GLU GLY PHE PHE ASP LEU MET HIS VAL SEQRES 20 A 592 GLN LYS VAL LEU SER ALA SER THR VAL CYS LYS LEU GLN SEQRES 21 A 592 SER CYS THR HIS GLY VAL PRO GLY ASP LEU GLN VAL TYR SEQRES 22 A 592 HIS ILE GLY ASN LEU LEU LYS GLY ASP LYS VAL ASN GLY SEQRES 23 A 592 HIS LEU ILE HIS LYS ILE GLU PRO HIS PHE ASN THR SER SEQRES 24 A 592 TRP MET SER TRP ASP GLY CYS ASP LEU ASP TYR TYR CYS SEQRES 25 A 592 ASN MET GLY ASP TRP PRO SER CYS THR TYR THR GLY VAL SEQRES 26 A 592 THR GLN HIS ASN HIS ALA SER PHE VAL ASN LEU LEU ASN SEQRES 27 A 592 ILE GLU THR ASP TYR THR LYS ASN PHE HIS PHE HIS SER SEQRES 28 A 592 LYS ARG VAL THR ALA HIS GLY ASP THR PRO GLN LEU ASP SEQRES 29 A 592 LEU LYS ALA ARG PRO THR TYR GLY ALA GLY GLU ILE THR SEQRES 30 A 592 VAL LEU VAL GLU VAL ALA ASP MET GLU LEU HIS THR LYS SEQRES 31 A 592 LYS ILE GLU ILE SER GLY LEU LYS PHE ALA SER LEU ALA SEQRES 32 A 592 CYS THR GLY CYS TYR ALA CYS SER SER GLY ILE SER CYS SEQRES 33 A 592 LYS VAL ARG ILE HIS VAL ASP GLU PRO ASP GLU LEU THR SEQRES 34 A 592 VAL HIS VAL LYS SER ASP ASP PRO ASP VAL VAL ALA ALA SEQRES 35 A 592 SER SER SER LEU MET ALA ARG LYS LEU GLU PHE GLY THR SEQRES 36 A 592 ASP SER THR PHE LYS ALA PHE SER ALA MET PRO LYS THR SEQRES 37 A 592 SER LEU CYS PHE TYR ILE VAL GLU ARG GLU HIS CYS LYS SEQRES 38 A 592 SER CYS SER GLU GLU ASP THR LYS LYS CYS VAL ASN THR SEQRES 39 A 592 LYS LEU GLU GLN PRO GLN SER ILE LEU ILE GLU HIS LYS SEQRES 40 A 592 GLY THR ILE ILE GLY LYS GLN ASN SER THR CYS THR ALA SEQRES 41 A 592 LYS ALA SER ARG GLY SER GLY GLY MET LYS GLN ILE GLU SEQRES 42 A 592 ASP LYS ILE GLU GLU ILE LEU SER LYS ILE TYR HIS ILE SEQRES 43 A 592 GLU ASN GLU ILE ALA ARG ILE LYS LYS LEU ILE GLY GLU SEQRES 44 A 592 GLY SER GLY GLY SER ARG GLY PRO PHE GLU GLY LYS PRO SEQRES 45 A 592 ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR ARG THR SEQRES 46 A 592 GLY HIS HIS HIS HIS HIS HIS SEQRES 1 H 117 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU VAL VAL ARG SEQRES 2 H 117 PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 H 117 TYR THR PHE THR ASP TYR ALA THR HIS TRP VAL LYS GLN SEQRES 4 H 117 SER HIS VAL LYS SER LEU GLU TRP ILE GLY VAL ILE SER SEQRES 5 H 117 THR TYR ASN GLY GLU THR ASP CYS ASN GLN LYS PHE LYS SEQRES 6 H 117 GLY LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7 H 117 ALA TYR MET GLU LEU ALA ARG LEU THR SER GLU ASP SER SEQRES 8 H 117 ALA ILE TYR TYR CYS ALA ASN GLY TYR TYR GLN ALA MET SEQRES 9 H 117 ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN THR PRO SER SER LEU SER ALA SEQRES 2 L 107 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 L 107 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ARG SEQRES 4 L 107 PRO ASP GLY THR LEU LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 L 107 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 L 107 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 L 107 SER THR LEU PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 107 GLU ILE LYS HELIX 1 AA1 GLN H 62 LYS H 65 5 4 HELIX 2 AA2 THR H 87 SER H 91 5 5 HELIX 3 AA3 GLU L 79 ILE L 83 5 5 SHEET 1 AA1 3 LYS A1162 THR A1164 0 SHEET 2 AA1 3 CYS A1205 CYS A1208 -1 O CYS A1207 N LYS A1162 SHEET 3 AA1 3 LYS A1183 PRO A1186 -1 N TRP A1185 O THR A1206 SHEET 1 AA2 2 LEU A1356 TYR A1359 0 SHEET 2 AA2 2 SER A1367 TYR A1370 -1 O SER A1367 N TYR A1359 SHEET 1 AA3 4 GLN H 3 GLN H 6 0 SHEET 2 AA3 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA3 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AA3 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA4 6 GLU H 10 VAL H 12 0 SHEET 2 AA4 6 THR H 111 VAL H 115 1 O SER H 112 N GLU H 10 SHEET 3 AA4 6 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 111 SHEET 4 AA4 6 ALA H 33 GLN H 39 -1 N ALA H 33 O GLY H 99 SHEET 5 AA4 6 LEU H 45 SER H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 AA4 6 THR H 58 CYS H 60 -1 O ASP H 59 N VAL H 50 SHEET 1 AA5 4 GLU H 10 VAL H 12 0 SHEET 2 AA5 4 THR H 111 VAL H 115 1 O SER H 112 N GLU H 10 SHEET 3 AA5 4 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 111 SHEET 4 AA5 4 MET H 104 TRP H 107 -1 O ASP H 105 N ASN H 98 SHEET 1 AA6 4 MET L 4 GLN L 6 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA6 4 PHE L 62 SER L 67 -1 N SER L 67 O ASP L 70 SHEET 1 AA7 2 SER L 10 SER L 12 0 SHEET 2 AA7 2 LYS L 103 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 1 AA8 5 ARG L 53 LEU L 54 0 SHEET 2 AA8 5 LEU L 44 TYR L 49 -1 N TYR L 49 O ARG L 53 SHEET 3 AA8 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA8 5 THR L 85 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 5 AA8 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SSBOND 1 CYS A 1165 CYS A 1198 1555 1555 2.03 SSBOND 2 CYS A 1169 CYS A 1205 1555 1555 2.03 SSBOND 3 CYS A 1173 CYS A 1207 1555 1555 2.04 SSBOND 4 CYS A 1175 CYS A 1180 1555 1555 2.04 SSBOND 5 CYS A 1193 CYS A 1360 1555 1555 2.03 SSBOND 6 CYS A 1208 CYS A 1368 1555 1555 2.03 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.04 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