HEADER VIRAL PROTEIN 01-DEC-23 8V5V TITLE STRUCTURE OF A SARS-COV-2 SPIKE S2 SUBUNIT IN A PRE-FUSION, OPEN TITLE 2 CONFORMATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S2,FIBRITIN; COMPND 3 CHAIN: G, E, F; COMPND 4 SYNONYM: COLLAR PROTEIN,WHISKER ANTIGEN CONTROL PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: VARIABLE DOMAIN OF THE LIGHT CHAIN FROM THE HUMAN ANTIBODY COMPND 9 6C10; COMPND 10 CHAIN: d, g, e; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: VARIABLE DOMAIN OF THE HEAVY CHAIN FROM THE HUMAN ANTIBODY COMPND 14 6C10; COMPND 15 CHAIN: f, c, b; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2, TEQUATROVIRUS T4; SOURCE 4 ORGANISM_TAXID: 2697049, 10665; SOURCE 5 GENE: S, 2, WAC; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS SARS-COV-2, SPIKE, S2, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR E.OLMEDILLAS,R.DIAZ,K.HASTIE,E.OLLMANN-SAPHIRE REVDAT 1 18-DEC-24 8V5V 0 JRNL AUTH E.OLMEDILLAS,R.DIAZ,K.HASTIE,E.OLLMANN-SAPHIRE JRNL TITL STRUCTURE OF A SARS-COV-2 SPIKE S2 SUBUNIT IN A PRE-FUSION, JRNL TITL 2 OPEN CONFORMATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, EPU, WARP, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX, COOT REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6XKL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT REMARK 3 OVERALL ANISOTROPIC B VALUE : 150.000 REMARK 3 REMARK 3 FITTING PROCEDURE : COOT MODEL BUILDING AND REFINAMENT 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) : 2.930 REMARK 3 NUMBER OF PARTICLES : 408064 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 8V5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1000279562. 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 : STRUCTURE OF A SARS-COV-2 SPIKE REMARK 245 S2 SUBUNIT IN A PRE-FUSION, REMARK 245 OPEN CONFORMATION IN COMPLEX REMARK 245 WITH THE 6C10 FAB; FAB FRAGMENT REMARK 245 OF THE 6C10 HUMAN MONOCLONAL REMARK 245 ANTIBODY; STRUCTURE OF A SARS- REMARK 245 COV-2 SPIKE S2 SUBUNIT IN A PRE- REMARK 245 FUSION, OPEN CONFORMATION REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : 6 SECONDS BLOTTING TIME AT REMARK 245 FORCE 0 REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 12444 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) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 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 : 75000 REMARK 245 CALIBRATED MAGNIFICATION : 75757 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, E, F, d, g, f, c, e, b, A, REMARK 350 AND CHAINS: B, C 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 SER G 691 REMARK 465 ILE G 692 REMARK 465 ILE G 693 REMARK 465 ALA G 694 REMARK 465 TYR G 695 REMARK 465 THR G 696 REMARK 465 MET G 697 REMARK 465 SER G 698 REMARK 465 LEU G 699 REMARK 465 GLY G 700 REMARK 465 ALA G 701 REMARK 465 GLU G 702 REMARK 465 ASN G 703 REMARK 465 SER G 704 REMARK 465 VAL G 705 REMARK 465 GLU G 1150 REMARK 465 GLU G 1151 REMARK 465 LEU G 1152 REMARK 465 ASP G 1153 REMARK 465 LYS G 1154 REMARK 465 TYR G 1155 REMARK 465 PHE G 1156 REMARK 465 LYS G 1157 REMARK 465 ASN G 1158 REMARK 465 HIS G 1159 REMARK 465 THR G 1160 REMARK 465 SER G 1161 REMARK 465 PRO G 1162 REMARK 465 ASP G 1163 REMARK 465 VAL G 1164 REMARK 465 ASP G 1165 REMARK 465 LEU G 1166 REMARK 465 GLY G 1167 REMARK 465 ASP G 1168 REMARK 465 ILE G 1169 REMARK 465 SER G 1170 REMARK 465 GLY G 1171 REMARK 465 ILE G 1172 REMARK 465 ASN G 1173 REMARK 465 ALA G 1174 REMARK 465 SER G 1175 REMARK 465 VAL G 1176 REMARK 465 VAL G 1177 REMARK 465 ASN G 1178 REMARK 465 ILE G 1179 REMARK 465 GLN G 1180 REMARK 465 LYS G 1181 REMARK 465 GLU G 1182 REMARK 465 ILE G 1183 REMARK 465 ASP G 1184 REMARK 465 ARG G 1185 REMARK 465 LEU G 1186 REMARK 465 ASN G 1187 REMARK 465 GLU G 1188 REMARK 465 VAL G 1189 REMARK 465 ALA G 1190 REMARK 465 LYS G 1191 REMARK 465 ASN G 1192 REMARK 465 LEU G 1193 REMARK 465 ASN G 1194 REMARK 465 GLU G 1195 REMARK 465 SER G 1196 REMARK 465 LEU G 1197 REMARK 465 ILE G 1198 REMARK 465 ASP G 1199 REMARK 465 LEU G 1200 REMARK 465 GLN G 1201 REMARK 465 GLU G 1202 REMARK 465 LEU G 1203 REMARK 465 GLY G 1204 REMARK 465 LYS G 1205 REMARK 465 TYR G 1206 REMARK 465 GLU G 1207 REMARK 465 GLN G 1208 REMARK 465 TYR G 1209 REMARK 465 ILE G 1210 REMARK 465 LYS G 1211 REMARK 465 GLY G 1212 REMARK 465 SER G 1213 REMARK 465 GLY G 1214 REMARK 465 TYR G 1215 REMARK 465 ILE G 1216 REMARK 465 PRO G 1217 REMARK 465 GLU G 1218 REMARK 465 ALA G 1219 REMARK 465 PRO G 1220 REMARK 465 ARG G 1221 REMARK 465 ASP G 1222 REMARK 465 GLY G 1223 REMARK 465 GLN G 1224 REMARK 465 ALA G 1225 REMARK 465 TYR G 1226 REMARK 465 VAL G 1227 REMARK 465 ARG G 1228 REMARK 465 LYS G 1229 REMARK 465 ASP G 1230 REMARK 465 GLY G 1231 REMARK 465 GLU G 1232 REMARK 465 TRP G 1233 REMARK 465 VAL G 1234 REMARK 465 LEU G 1235 REMARK 465 LEU G 1236 REMARK 465 SER G 1237 REMARK 465 THR G 1238 REMARK 465 PHE G 1239 REMARK 465 LEU G 1240 REMARK 465 LEU G 1241 REMARK 465 GLU G 1242 REMARK 465 VAL G 1243 REMARK 465 LEU G 1244 REMARK 465 PHE G 1245 REMARK 465 GLN G 1246 REMARK 465 GLY G 1247 REMARK 465 PRO G 1248 REMARK 465 ALA G 1249 REMARK 465 GLY G 1250 REMARK 465 TRP G 1251 REMARK 465 SER G 1252 REMARK 465 HIS G 1253 REMARK 465 PRO G 1254 REMARK 465 GLN G 1255 REMARK 465 PHE G 1256 REMARK 465 GLU G 1257 REMARK 465 LYS G 1258 REMARK 465 GLY G 1259 REMARK 465 GLY G 1260 REMARK 465 GLY G 1261 REMARK 465 SER G 1262 REMARK 465 GLY G 1263 REMARK 465 GLY G 1264 REMARK 465 GLY G 1265 REMARK 465 SER G 1266 REMARK 465 GLY G 1267 REMARK 465 GLY G 1268 REMARK 465 GLY G 1269 REMARK 465 SER G 1270 REMARK 465 TRP G 1271 REMARK 465 SER G 1272 REMARK 465 HIS G 1273 REMARK 465 PRO G 1274 REMARK 465 GLN G 1275 REMARK 465 PHE G 1276 REMARK 465 GLU G 1277 REMARK 465 LYS G 1278 REMARK 465 SER E 691 REMARK 465 ILE E 692 REMARK 465 ILE E 693 REMARK 465 ALA E 694 REMARK 465 TYR E 695 REMARK 465 THR E 696 REMARK 465 MET E 697 REMARK 465 SER E 698 REMARK 465 LEU E 699 REMARK 465 GLY E 700 REMARK 465 ALA E 701 REMARK 465 GLU E 702 REMARK 465 ASN E 703 REMARK 465 SER E 704 REMARK 465 VAL E 705 REMARK 465 GLU E 1150 REMARK 465 GLU E 1151 REMARK 465 LEU E 1152 REMARK 465 ASP E 1153 REMARK 465 LYS E 1154 REMARK 465 TYR E 1155 REMARK 465 PHE E 1156 REMARK 465 LYS E 1157 REMARK 465 ASN E 1158 REMARK 465 HIS E 1159 REMARK 465 THR E 1160 REMARK 465 SER E 1161 REMARK 465 PRO E 1162 REMARK 465 ASP E 1163 REMARK 465 VAL E 1164 REMARK 465 ASP E 1165 REMARK 465 LEU E 1166 REMARK 465 GLY E 1167 REMARK 465 ASP E 1168 REMARK 465 ILE E 1169 REMARK 465 SER E 1170 REMARK 465 GLY E 1171 REMARK 465 ILE E 1172 REMARK 465 ASN E 1173 REMARK 465 ALA E 1174 REMARK 465 SER E 1175 REMARK 465 VAL E 1176 REMARK 465 VAL E 1177 REMARK 465 ASN E 1178 REMARK 465 ILE E 1179 REMARK 465 GLN E 1180 REMARK 465 LYS E 1181 REMARK 465 GLU E 1182 REMARK 465 ILE E 1183 REMARK 465 ASP E 1184 REMARK 465 ARG E 1185 REMARK 465 LEU E 1186 REMARK 465 ASN E 1187 REMARK 465 GLU E 1188 REMARK 465 VAL E 1189 REMARK 465 ALA E 1190 REMARK 465 LYS E 1191 REMARK 465 ASN E 1192 REMARK 465 LEU E 1193 REMARK 465 ASN E 1194 REMARK 465 GLU E 1195 REMARK 465 SER E 1196 REMARK 465 LEU E 1197 REMARK 465 ILE E 1198 REMARK 465 ASP E 1199 REMARK 465 LEU E 1200 REMARK 465 GLN E 1201 REMARK 465 GLU E 1202 REMARK 465 LEU E 1203 REMARK 465 GLY E 1204 REMARK 465 LYS E 1205 REMARK 465 TYR E 1206 REMARK 465 GLU E 1207 REMARK 465 GLN E 1208 REMARK 465 TYR E 1209 REMARK 465 ILE E 1210 REMARK 465 LYS E 1211 REMARK 465 GLY E 1212 REMARK 465 SER E 1213 REMARK 465 GLY E 1214 REMARK 465 TYR E 1215 REMARK 465 ILE E 1216 REMARK 465 PRO E 1217 REMARK 465 GLU E 1218 REMARK 465 ALA E 1219 REMARK 465 PRO E 1220 REMARK 465 ARG E 1221 REMARK 465 ASP E 1222 REMARK 465 GLY E 1223 REMARK 465 GLN E 1224 REMARK 465 ALA E 1225 REMARK 465 TYR E 1226 REMARK 465 VAL E 1227 REMARK 465 ARG E 1228 REMARK 465 LYS E 1229 REMARK 465 ASP E 1230 REMARK 465 GLY E 1231 REMARK 465 GLU E 1232 REMARK 465 TRP E 1233 REMARK 465 VAL E 1234 REMARK 465 LEU E 1235 REMARK 465 LEU E 1236 REMARK 465 SER E 1237 REMARK 465 THR E 1238 REMARK 465 PHE E 1239 REMARK 465 LEU E 1240 REMARK 465 LEU E 1241 REMARK 465 GLU E 1242 REMARK 465 VAL E 1243 REMARK 465 LEU E 1244 REMARK 465 PHE E 1245 REMARK 465 GLN E 1246 REMARK 465 GLY E 1247 REMARK 465 PRO E 1248 REMARK 465 ALA E 1249 REMARK 465 GLY E 1250 REMARK 465 TRP E 1251 REMARK 465 SER E 1252 REMARK 465 HIS E 1253 REMARK 465 PRO E 1254 REMARK 465 GLN E 1255 REMARK 465 PHE E 1256 REMARK 465 GLU E 1257 REMARK 465 LYS E 1258 REMARK 465 GLY E 1259 REMARK 465 GLY E 1260 REMARK 465 GLY E 1261 REMARK 465 SER E 1262 REMARK 465 GLY E 1263 REMARK 465 GLY E 1264 REMARK 465 GLY E 1265 REMARK 465 SER E 1266 REMARK 465 GLY E 1267 REMARK 465 GLY E 1268 REMARK 465 GLY E 1269 REMARK 465 SER E 1270 REMARK 465 TRP E 1271 REMARK 465 SER E 1272 REMARK 465 HIS E 1273 REMARK 465 PRO E 1274 REMARK 465 GLN E 1275 REMARK 465 PHE E 1276 REMARK 465 GLU E 1277 REMARK 465 LYS E 1278 REMARK 465 SER F 691 REMARK 465 ILE F 692 REMARK 465 ILE F 693 REMARK 465 ALA F 694 REMARK 465 TYR F 695 REMARK 465 THR F 696 REMARK 465 MET F 697 REMARK 465 SER F 698 REMARK 465 LEU F 699 REMARK 465 GLY F 700 REMARK 465 ALA F 701 REMARK 465 GLU F 702 REMARK 465 ASN F 703 REMARK 465 SER F 704 REMARK 465 VAL F 705 REMARK 465 GLU F 1150 REMARK 465 GLU F 1151 REMARK 465 LEU F 1152 REMARK 465 ASP F 1153 REMARK 465 LYS F 1154 REMARK 465 TYR F 1155 REMARK 465 PHE F 1156 REMARK 465 LYS F 1157 REMARK 465 ASN F 1158 REMARK 465 HIS F 1159 REMARK 465 THR F 1160 REMARK 465 SER F 1161 REMARK 465 PRO F 1162 REMARK 465 ASP F 1163 REMARK 465 VAL F 1164 REMARK 465 ASP F 1165 REMARK 465 LEU F 1166 REMARK 465 GLY F 1167 REMARK 465 ASP F 1168 REMARK 465 ILE F 1169 REMARK 465 SER F 1170 REMARK 465 GLY F 1171 REMARK 465 ILE F 1172 REMARK 465 ASN F 1173 REMARK 465 ALA F 1174 REMARK 465 SER F 1175 REMARK 465 VAL F 1176 REMARK 465 VAL F 1177 REMARK 465 ASN F 1178 REMARK 465 ILE F 1179 REMARK 465 GLN F 1180 REMARK 465 LYS F 1181 REMARK 465 GLU F 1182 REMARK 465 ILE F 1183 REMARK 465 ASP F 1184 REMARK 465 ARG F 1185 REMARK 465 LEU F 1186 REMARK 465 ASN F 1187 REMARK 465 GLU F 1188 REMARK 465 VAL F 1189 REMARK 465 ALA F 1190 REMARK 465 LYS F 1191 REMARK 465 ASN F 1192 REMARK 465 LEU F 1193 REMARK 465 ASN F 1194 REMARK 465 GLU F 1195 REMARK 465 SER F 1196 REMARK 465 LEU F 1197 REMARK 465 ILE F 1198 REMARK 465 ASP F 1199 REMARK 465 LEU F 1200 REMARK 465 GLN F 1201 REMARK 465 GLU F 1202 REMARK 465 LEU F 1203 REMARK 465 GLY F 1204 REMARK 465 LYS F 1205 REMARK 465 TYR F 1206 REMARK 465 GLU F 1207 REMARK 465 GLN F 1208 REMARK 465 TYR F 1209 REMARK 465 ILE F 1210 REMARK 465 LYS F 1211 REMARK 465 GLY F 1212 REMARK 465 SER F 1213 REMARK 465 GLY F 1214 REMARK 465 TYR F 1215 REMARK 465 ILE F 1216 REMARK 465 PRO F 1217 REMARK 465 GLU F 1218 REMARK 465 ALA F 1219 REMARK 465 PRO F 1220 REMARK 465 ARG F 1221 REMARK 465 ASP F 1222 REMARK 465 GLY F 1223 REMARK 465 GLN F 1224 REMARK 465 ALA F 1225 REMARK 465 TYR F 1226 REMARK 465 VAL F 1227 REMARK 465 ARG F 1228 REMARK 465 LYS F 1229 REMARK 465 ASP F 1230 REMARK 465 GLY F 1231 REMARK 465 GLU F 1232 REMARK 465 TRP F 1233 REMARK 465 VAL F 1234 REMARK 465 LEU F 1235 REMARK 465 LEU F 1236 REMARK 465 SER F 1237 REMARK 465 THR F 1238 REMARK 465 PHE F 1239 REMARK 465 LEU F 1240 REMARK 465 LEU F 1241 REMARK 465 GLU F 1242 REMARK 465 VAL F 1243 REMARK 465 LEU F 1244 REMARK 465 PHE F 1245 REMARK 465 GLN F 1246 REMARK 465 GLY F 1247 REMARK 465 PRO F 1248 REMARK 465 ALA F 1249 REMARK 465 GLY F 1250 REMARK 465 TRP F 1251 REMARK 465 SER F 1252 REMARK 465 HIS F 1253 REMARK 465 PRO F 1254 REMARK 465 GLN F 1255 REMARK 465 PHE F 1256 REMARK 465 GLU F 1257 REMARK 465 LYS F 1258 REMARK 465 GLY F 1259 REMARK 465 GLY F 1260 REMARK 465 GLY F 1261 REMARK 465 SER F 1262 REMARK 465 GLY F 1263 REMARK 465 GLY F 1264 REMARK 465 GLY F 1265 REMARK 465 SER F 1266 REMARK 465 GLY F 1267 REMARK 465 GLY F 1268 REMARK 465 GLY F 1269 REMARK 465 SER F 1270 REMARK 465 TRP F 1271 REMARK 465 SER F 1272 REMARK 465 HIS F 1273 REMARK 465 PRO F 1274 REMARK 465 GLN F 1275 REMARK 465 PHE F 1276 REMARK 465 GLU F 1277 REMARK 465 LYS F 1278 REMARK 465 ALA d 1 REMARK 465 ILE d 108 REMARK 465 ALA g 1 REMARK 465 ILE g 108 REMARK 465 ALA e 1 REMARK 465 ILE e 108 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 CYS G 749 27.06 -140.07 REMARK 500 SER G 884 -114.87 55.81 REMARK 500 ALA G 890 -114.33 55.60 REMARK 500 LEU G 945 32.41 -94.86 REMARK 500 PHE G 970 -113.60 55.16 REMARK 500 SER G1123 116.63 -160.62 REMARK 500 SER E 884 -127.82 59.86 REMARK 500 ALA E 890 -114.04 55.63 REMARK 500 LEU E 945 32.78 -94.60 REMARK 500 PHE E 970 -113.60 55.13 REMARK 500 SER E1123 116.56 -160.56 REMARK 500 SER F 884 -127.73 59.81 REMARK 500 ALA F 890 -113.73 55.61 REMARK 500 LEU F 945 32.22 -94.96 REMARK 500 PHE F 970 -113.50 55.06 REMARK 500 SER F1123 116.52 -160.65 REMARK 500 SER d 30 -132.02 61.25 REMARK 500 ALA d 84 -168.60 -160.31 REMARK 500 SER g 30 -132.26 62.19 REMARK 500 ALA g 84 -168.49 -160.32 REMARK 500 TYR f 106 -1.41 70.16 REMARK 500 TYR c 106 -0.88 70.03 REMARK 500 SER e 30 -132.29 62.23 REMARK 500 ALA e 84 -168.52 -160.31 REMARK 500 TYR b 106 -1.08 70.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42985 RELATED DB: EMDB REMARK 900 STRUCTURE OF A SARS-COV-2 SPIKE S2 SUBUNIT IN A PRE-FUSION, OPEN REMARK 900 CONFORMATION DBREF 8V5V G 691 1211 UNP P0DTC2 SPIKE_SARS2 691 1211 DBREF 8V5V G 1214 1240 UNP P10104 WAC_BPT4 458 484 DBREF 8V5V E 691 1211 UNP P0DTC2 SPIKE_SARS2 691 1211 DBREF 8V5V E 1214 1240 UNP P10104 WAC_BPT4 458 484 DBREF 8V5V F 691 1211 UNP P0DTC2 SPIKE_SARS2 691 1211 DBREF 8V5V F 1214 1240 UNP P10104 WAC_BPT4 458 484 DBREF 8V5V d 1 108 PDB 8V5V 8V5V 1 108 DBREF 8V5V g 1 108 PDB 8V5V 8V5V 1 108 DBREF 8V5V f 1 125 PDB 8V5V 8V5V 1 125 DBREF 8V5V c 1 125 PDB 8V5V 8V5V 1 125 DBREF 8V5V e 1 108 PDB 8V5V 8V5V 1 108 DBREF 8V5V b 1 125 PDB 8V5V 8V5V 1 125 SEQADV 8V5V CYS G 707 UNP P0DTC2 TYR 707 ENGINEERED MUTATION SEQADV 8V5V CYS G 788 UNP P0DTC2 ILE 788 CONFLICT SEQADV 8V5V PRO G 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8V5V CYS G 876 UNP P0DTC2 ALA 876 ENGINEERED MUTATION SEQADV 8V5V CYS G 883 UNP P0DTC2 THR 883 ENGINEERED MUTATION SEQADV 8V5V PRO G 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8V5V PRO G 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8V5V PRO G 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8V5V PRO G 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8V5V GLY G 1212 UNP P0DTC2 LINKER SEQADV 8V5V SER G 1213 UNP P0DTC2 LINKER SEQADV 8V5V LEU G 1235 UNP P10104 PHE 479 CONFLICT SEQADV 8V5V LEU G 1241 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU G 1242 UNP P10104 EXPRESSION TAG SEQADV 8V5V VAL G 1243 UNP P10104 EXPRESSION TAG SEQADV 8V5V LEU G 1244 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE G 1245 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN G 1246 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1247 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO G 1248 UNP P10104 EXPRESSION TAG SEQADV 8V5V ALA G 1249 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1250 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP G 1251 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER G 1252 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS G 1253 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO G 1254 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN G 1255 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE G 1256 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU G 1257 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS G 1258 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1259 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1260 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1261 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER G 1262 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1263 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1264 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1265 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER G 1266 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1267 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1268 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY G 1269 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER G 1270 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP G 1271 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER G 1272 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS G 1273 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO G 1274 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN G 1275 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE G 1276 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU G 1277 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS G 1278 UNP P10104 EXPRESSION TAG SEQADV 8V5V CYS E 707 UNP P0DTC2 TYR 707 ENGINEERED MUTATION SEQADV 8V5V CYS E 788 UNP P0DTC2 ILE 788 CONFLICT SEQADV 8V5V PRO E 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8V5V CYS E 876 UNP P0DTC2 ALA 876 ENGINEERED MUTATION SEQADV 8V5V CYS E 883 UNP P0DTC2 THR 883 ENGINEERED MUTATION SEQADV 8V5V PRO E 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8V5V PRO E 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8V5V PRO E 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8V5V PRO E 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8V5V GLY E 1212 UNP P0DTC2 LINKER SEQADV 8V5V SER E 1213 UNP P0DTC2 LINKER SEQADV 8V5V LEU E 1235 UNP P10104 PHE 479 CONFLICT SEQADV 8V5V LEU E 1241 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU E 1242 UNP P10104 EXPRESSION TAG SEQADV 8V5V VAL E 1243 UNP P10104 EXPRESSION TAG SEQADV 8V5V LEU E 1244 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE E 1245 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN E 1246 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1247 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO E 1248 UNP P10104 EXPRESSION TAG SEQADV 8V5V ALA E 1249 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1250 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP E 1251 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER E 1252 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS E 1253 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO E 1254 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN E 1255 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE E 1256 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU E 1257 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS E 1258 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1259 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1260 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1261 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER E 1262 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1263 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1264 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1265 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER E 1266 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1267 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1268 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY E 1269 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER E 1270 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP E 1271 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER E 1272 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS E 1273 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO E 1274 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN E 1275 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE E 1276 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU E 1277 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS E 1278 UNP P10104 EXPRESSION TAG SEQADV 8V5V CYS F 707 UNP P0DTC2 TYR 707 ENGINEERED MUTATION SEQADV 8V5V CYS F 788 UNP P0DTC2 ILE 788 CONFLICT SEQADV 8V5V PRO F 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8V5V CYS F 876 UNP P0DTC2 ALA 876 ENGINEERED MUTATION SEQADV 8V5V CYS F 883 UNP P0DTC2 THR 883 ENGINEERED MUTATION SEQADV 8V5V PRO F 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8V5V PRO F 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8V5V PRO F 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8V5V PRO F 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8V5V GLY F 1212 UNP P0DTC2 LINKER SEQADV 8V5V SER F 1213 UNP P0DTC2 LINKER SEQADV 8V5V LEU F 1235 UNP P10104 PHE 479 CONFLICT SEQADV 8V5V LEU F 1241 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU F 1242 UNP P10104 EXPRESSION TAG SEQADV 8V5V VAL F 1243 UNP P10104 EXPRESSION TAG SEQADV 8V5V LEU F 1244 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE F 1245 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN F 1246 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1247 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO F 1248 UNP P10104 EXPRESSION TAG SEQADV 8V5V ALA F 1249 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1250 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP F 1251 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER F 1252 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS F 1253 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO F 1254 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN F 1255 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE F 1256 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU F 1257 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS F 1258 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1259 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1260 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1261 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER F 1262 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1263 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1264 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1265 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER F 1266 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1267 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1268 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLY F 1269 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER F 1270 UNP P10104 EXPRESSION TAG SEQADV 8V5V TRP F 1271 UNP P10104 EXPRESSION TAG SEQADV 8V5V SER F 1272 UNP P10104 EXPRESSION TAG SEQADV 8V5V HIS F 1273 UNP P10104 EXPRESSION TAG SEQADV 8V5V PRO F 1274 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLN F 1275 UNP P10104 EXPRESSION TAG SEQADV 8V5V PHE F 1276 UNP P10104 EXPRESSION TAG SEQADV 8V5V GLU F 1277 UNP P10104 EXPRESSION TAG SEQADV 8V5V LYS F 1278 UNP P10104 EXPRESSION TAG SEQRES 1 G 588 SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SEQRES 2 G 588 SER VAL ALA CYS SER ASN ASN SER ILE ALA ILE PRO THR SEQRES 3 G 588 ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SEQRES 4 G 588 SER MET THR LYS THR SER VAL ASP CYS THR MET TYR ILE SEQRES 5 G 588 CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN SEQRES 6 G 588 TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU THR SEQRES 7 G 588 GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL SEQRES 8 G 588 PHE ALA GLN VAL LYS GLN CYS TYR LYS THR PRO PRO ILE SEQRES 9 G 588 LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO SEQRES 10 G 588 ASP PRO SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP SEQRES 11 G 588 LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE SEQRES 12 G 588 ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA SEQRES 13 G 588 ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU THR SEQRES 14 G 588 VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN SEQRES 15 G 588 TYR THR SER CYS LEU LEU ALA GLY THR ILE CYS SER GLY SEQRES 16 G 588 TRP THR PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE SEQRES 17 G 588 PRO MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL SEQRES 18 G 588 THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA SEQRES 19 G 588 ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER SEQRES 20 G 588 LEU SER SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP SEQRES 21 G 588 VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU VAL SEQRES 22 G 588 LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER VAL SEQRES 23 G 588 LEU ASN ASP ILE LEU SER ARG LEU ASP LYS PRO GLU ALA SEQRES 24 G 588 GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SEQRES 25 G 588 SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA SEQRES 26 G 588 ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS SEQRES 27 G 588 MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP SEQRES 28 G 588 PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SEQRES 29 G 588 SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR SEQRES 30 G 588 VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA SEQRES 31 G 588 ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY SEQRES 32 G 588 VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN SEQRES 33 G 588 ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN SEQRES 34 G 588 THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE SEQRES 35 G 588 VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU SEQRES 36 G 588 ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN SEQRES 37 G 588 HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY SEQRES 38 G 588 ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP SEQRES 39 G 588 ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU SEQRES 40 G 588 ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR ILE SEQRES 41 G 588 LYS GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 42 G 588 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 43 G 588 SER THR PHE LEU LEU GLU VAL LEU PHE GLN GLY PRO ALA SEQRES 44 G 588 GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER SEQRES 45 G 588 GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO GLN SEQRES 46 G 588 PHE GLU LYS SEQRES 1 E 588 SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SEQRES 2 E 588 SER VAL ALA CYS SER ASN ASN SER ILE ALA ILE PRO THR SEQRES 3 E 588 ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SEQRES 4 E 588 SER MET THR LYS THR SER VAL ASP CYS THR MET TYR ILE SEQRES 5 E 588 CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN SEQRES 6 E 588 TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU THR SEQRES 7 E 588 GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL SEQRES 8 E 588 PHE ALA GLN VAL LYS GLN CYS TYR LYS THR PRO PRO ILE SEQRES 9 E 588 LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO SEQRES 10 E 588 ASP PRO SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP SEQRES 11 E 588 LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE SEQRES 12 E 588 ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA SEQRES 13 E 588 ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU THR SEQRES 14 E 588 VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN SEQRES 15 E 588 TYR THR SER CYS LEU LEU ALA GLY THR ILE CYS SER GLY SEQRES 16 E 588 TRP THR PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE SEQRES 17 E 588 PRO MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL SEQRES 18 E 588 THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA SEQRES 19 E 588 ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER SEQRES 20 E 588 LEU SER SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP SEQRES 21 E 588 VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU VAL SEQRES 22 E 588 LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER VAL SEQRES 23 E 588 LEU ASN ASP ILE LEU SER ARG LEU ASP LYS PRO GLU ALA SEQRES 24 E 588 GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SEQRES 25 E 588 SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA SEQRES 26 E 588 ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS SEQRES 27 E 588 MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP SEQRES 28 E 588 PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SEQRES 29 E 588 SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR SEQRES 30 E 588 VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA SEQRES 31 E 588 ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY SEQRES 32 E 588 VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN SEQRES 33 E 588 ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN SEQRES 34 E 588 THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE SEQRES 35 E 588 VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU SEQRES 36 E 588 ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN SEQRES 37 E 588 HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY SEQRES 38 E 588 ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP SEQRES 39 E 588 ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU SEQRES 40 E 588 ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR ILE SEQRES 41 E 588 LYS GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 42 E 588 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 43 E 588 SER THR PHE LEU LEU GLU VAL LEU PHE GLN GLY PRO ALA SEQRES 44 E 588 GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER SEQRES 45 E 588 GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO GLN SEQRES 46 E 588 PHE GLU LYS SEQRES 1 F 588 SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SEQRES 2 F 588 SER VAL ALA CYS SER ASN ASN SER ILE ALA ILE PRO THR SEQRES 3 F 588 ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SEQRES 4 F 588 SER MET THR LYS THR SER VAL ASP CYS THR MET TYR ILE SEQRES 5 F 588 CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN SEQRES 6 F 588 TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU THR SEQRES 7 F 588 GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL SEQRES 8 F 588 PHE ALA GLN VAL LYS GLN CYS TYR LYS THR PRO PRO ILE SEQRES 9 F 588 LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO SEQRES 10 F 588 ASP PRO SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP SEQRES 11 F 588 LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE SEQRES 12 F 588 ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA SEQRES 13 F 588 ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU THR SEQRES 14 F 588 VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN SEQRES 15 F 588 TYR THR SER CYS LEU LEU ALA GLY THR ILE CYS SER GLY SEQRES 16 F 588 TRP THR PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE SEQRES 17 F 588 PRO MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL SEQRES 18 F 588 THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA SEQRES 19 F 588 ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER SEQRES 20 F 588 LEU SER SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP SEQRES 21 F 588 VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU VAL SEQRES 22 F 588 LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER VAL SEQRES 23 F 588 LEU ASN ASP ILE LEU SER ARG LEU ASP LYS PRO GLU ALA SEQRES 24 F 588 GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SEQRES 25 F 588 SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA SEQRES 26 F 588 ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS SEQRES 27 F 588 MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP SEQRES 28 F 588 PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SEQRES 29 F 588 SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR SEQRES 30 F 588 VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA SEQRES 31 F 588 ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY SEQRES 32 F 588 VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN SEQRES 33 F 588 ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN SEQRES 34 F 588 THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE SEQRES 35 F 588 VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU SEQRES 36 F 588 ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN SEQRES 37 F 588 HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY SEQRES 38 F 588 ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP SEQRES 39 F 588 ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU SEQRES 40 F 588 ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR ILE SEQRES 41 F 588 LYS GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 42 F 588 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 43 F 588 SER THR PHE LEU LEU GLU VAL LEU PHE GLN GLY PRO ALA SEQRES 44 F 588 GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER SEQRES 45 F 588 GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO GLN SEQRES 46 F 588 PHE GLU LYS SEQRES 1 d 108 ALA ILE ARG MET THR GLN SER PRO SER THR LEU SER VAL SEQRES 2 d 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 d 108 GLN SER VAL SER SER TYR LEU ALA TRP TYR GLN HIS LYS SEQRES 4 d 108 PRO GLY GLN ALA PRO ARG LEU LEU VAL TYR GLY ALA SER SEQRES 5 d 108 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 d 108 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 d 108 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 d 108 ASN ASN TRP PRO PRO PRO PHE THR PHE GLY PRO GLY THR SEQRES 9 d 108 LYS VAL ASP ILE SEQRES 1 g 108 ALA ILE ARG MET THR GLN SER PRO SER THR LEU SER VAL SEQRES 2 g 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 g 108 GLN SER VAL SER SER TYR LEU ALA TRP TYR GLN HIS LYS SEQRES 4 g 108 PRO GLY GLN ALA PRO ARG LEU LEU VAL TYR GLY ALA SER SEQRES 5 g 108 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 g 108 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 g 108 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 g 108 ASN ASN TRP PRO PRO PRO PHE THR PHE GLY PRO GLY THR SEQRES 9 g 108 LYS VAL ASP ILE SEQRES 1 f 125 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 f 125 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 f 125 TYR THR PHE THR GLY TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 f 125 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 f 125 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 f 125 GLY TRP VAL ILE MET THR ARG ASP THR SER ILE SER THR SEQRES 7 f 125 ALA TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 f 125 ALA VAL TYR TYR CYS ALA ARG CYS GLY ALA ARG SER TYR SEQRES 9 f 125 TYR TYR ASP SER GLY ASP TYR CYS ALA PHE ASP ILE TRP SEQRES 10 f 125 GLY GLN GLY THR VAL VAL THR VAL SEQRES 1 c 125 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 c 125 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 c 125 TYR THR PHE THR GLY TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 c 125 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 c 125 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 c 125 GLY TRP VAL ILE MET THR ARG ASP THR SER ILE SER THR SEQRES 7 c 125 ALA TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 c 125 ALA VAL TYR TYR CYS ALA ARG CYS GLY ALA ARG SER TYR SEQRES 9 c 125 TYR TYR ASP SER GLY ASP TYR CYS ALA PHE ASP ILE TRP SEQRES 10 c 125 GLY GLN GLY THR VAL VAL THR VAL SEQRES 1 e 108 ALA ILE ARG MET THR GLN SER PRO SER THR LEU SER VAL SEQRES 2 e 108 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 e 108 GLN SER VAL SER SER TYR LEU ALA TRP TYR GLN HIS LYS SEQRES 4 e 108 PRO GLY GLN ALA PRO ARG LEU LEU VAL TYR GLY ALA SER SEQRES 5 e 108 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 e 108 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 e 108 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 e 108 ASN ASN TRP PRO PRO PRO PHE THR PHE GLY PRO GLY THR SEQRES 9 e 108 LYS VAL ASP ILE SEQRES 1 b 125 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 b 125 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 b 125 TYR THR PHE THR GLY TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 b 125 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 b 125 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 b 125 GLY TRP VAL ILE MET THR ARG ASP THR SER ILE SER THR SEQRES 7 b 125 ALA TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 b 125 ALA VAL TYR TYR CYS ALA ARG CYS GLY ALA ARG SER TYR SEQRES 9 b 125 TYR TYR ASP SER GLY ASP TYR CYS ALA PHE ASP ILE TRP SEQRES 10 b 125 GLY GLN GLY THR VAL VAL THR VAL HET NAG A 1 14 HET NAG A 2 14 HET NAG B 1 14 HET NAG B 2 14 HET NAG C 1 14 HET NAG C 2 14 HET NAG G1301 14 HET NAG G1302 14 HET NAG G1303 14 HET NAG G1304 14 HET NAG G1305 14 HET NAG E1301 14 HET NAG E1302 14 HET NAG E1303 14 HET NAG E1304 14 HET NAG E1305 14 HET NAG F1301 14 HET NAG F1302 14 HET NAG F1303 14 HET NAG F1304 14 HET NAG F1305 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 10 NAG 21(C8 H15 N O6) HELIX 1 AA1 ASP G 737 ILE G 742 1 6 HELIX 2 AA2 CYS G 749 ALA G 783 1 35 HELIX 3 AA3 SER G 816 VAL G 826 1 11 HELIX 4 AA4 GLY G 832 GLY G 842 1 11 HELIX 5 AA5 ARG G 847 PHE G 855 1 9 HELIX 6 AA6 THR G 866 CYS G 883 1 18 HELIX 7 AA7 PRO G 897 GLY G 910 1 14 HELIX 8 AA8 THR G 912 ASN G 919 1 8 HELIX 9 AA9 ASN G 919 THR G 941 1 23 HELIX 10 AB1 LEU G 945 SER G 967 1 23 HELIX 11 AB2 VAL G 976 LEU G 984 1 9 HELIX 12 AB3 ASP G 985 VAL G 1033 1 49 HELIX 13 AB4 PRO G 1140 LYS G 1149 1 10 HELIX 14 AB5 ASP E 737 ILE E 742 1 6 HELIX 15 AB6 CYS E 749 ALA E 783 1 35 HELIX 16 AB7 SER E 816 VAL E 826 1 11 HELIX 17 AB8 GLY E 832 GLY E 842 1 11 HELIX 18 AB9 ARG E 847 PHE E 855 1 9 HELIX 19 AC1 THR E 866 CYS E 883 1 18 HELIX 20 AC2 PRO E 897 GLY E 910 1 14 HELIX 21 AC3 THR E 912 ASN E 919 1 8 HELIX 22 AC4 ASN E 919 THR E 941 1 23 HELIX 23 AC5 LEU E 945 SER E 967 1 23 HELIX 24 AC6 VAL E 976 LEU E 984 1 9 HELIX 25 AC7 ASP E 985 VAL E 1033 1 49 HELIX 26 AC8 PRO E 1140 LYS E 1149 1 10 HELIX 27 AC9 ASP F 737 ILE F 742 1 6 HELIX 28 AD1 CYS F 749 ALA F 783 1 35 HELIX 29 AD2 SER F 816 VAL F 826 1 11 HELIX 30 AD3 GLY F 832 GLY F 842 1 11 HELIX 31 AD4 ARG F 847 PHE F 855 1 9 HELIX 32 AD5 THR F 866 CYS F 883 1 18 HELIX 33 AD6 PRO F 897 GLY F 910 1 14 HELIX 34 AD7 THR F 912 ASN F 919 1 8 HELIX 35 AD8 ASN F 919 THR F 941 1 23 HELIX 36 AD9 LEU F 945 SER F 967 1 23 HELIX 37 AE1 VAL F 976 LEU F 984 1 9 HELIX 38 AE2 ASP F 985 VAL F 1033 1 49 HELIX 39 AE3 PRO F 1140 LYS F 1149 1 10 HELIX 40 AE4 GLN d 79 PHE d 83 5 5 HELIX 41 AE5 GLN g 79 PHE g 83 5 5 HELIX 42 AE6 THR f 87 THR f 91 5 5 HELIX 43 AE7 THR c 87 THR c 91 5 5 HELIX 44 AE8 GLN e 79 PHE e 83 5 5 HELIX 45 AE9 THR b 87 THR b 91 5 5 SHEET 1 AA1 4 SER G 711 ILE G 714 0 SHEET 2 AA1 4 LYS G1073 THR G1077 -1 O LYS G1073 N ILE G 714 SHEET 3 AA1 4 VAL G1094 SER G1097 -1 O SER G1097 N THR G1076 SHEET 4 AA1 4 TRP G1102 THR G1105 -1 O THR G1105 N VAL G1094 SHEET 1 AA2 3 ASN G 717 PRO G 728 0 SHEET 2 AA2 3 GLY G1059 ALA G1070 -1 O THR G1066 N SER G 721 SHEET 3 AA2 3 TYR G1047 SER G1051 -1 N MET G1050 O VAL G1065 SHEET 1 AA3 3 ASN G 717 PRO G 728 0 SHEET 2 AA3 3 GLY G1059 ALA G1070 -1 O THR G1066 N SER G 721 SHEET 3 AA3 3 GLN G1054 ALA G1056 -1 N GLN G1054 O VAL G1061 SHEET 1 AA4 2 LYS G 733 SER G 735 0 SHEET 2 AA4 2 THR G 859 LEU G 861 -1 O THR G 859 N SER G 735 SHEET 1 AA5 2 ASP G 796 PHE G 797 0 SHEET 2 AA5 2 PHE G 800 ASN G 801 -1 O PHE G 800 N PHE G 797 SHEET 1 AA6 4 THR G1120 VAL G1122 0 SHEET 2 AA6 4 ALA G1087 PRO G1090 -1 N PHE G1089 O PHE G1121 SHEET 3 AA6 4 ALA G1080 CYS G1082 -1 N ILE G1081 O HIS G1088 SHEET 4 AA6 4 ILE G1132 ASN G1134 1 O VAL G1133 N CYS G1082 SHEET 1 AA7 2 SER E 711 ILE E 714 0 SHEET 2 AA7 2 LYS E1073 THR E1076 -1 O LYS E1073 N ILE E 714 SHEET 1 AA8 3 ASN E 717 PRO E 728 0 SHEET 2 AA8 3 GLY E1059 ALA E1070 -1 O THR E1066 N SER E 721 SHEET 3 AA8 3 TYR E1047 SER E1051 -1 N MET E1050 O VAL E1065 SHEET 1 AA9 3 ASN E 717 PRO E 728 0 SHEET 2 AA9 3 GLY E1059 ALA E1070 -1 O THR E1066 N SER E 721 SHEET 3 AA9 3 GLN E1054 ALA E1056 -1 N GLN E1054 O VAL E1061 SHEET 1 AB1 2 LYS E 733 SER E 735 0 SHEET 2 AB1 2 THR E 859 LEU E 861 -1 O THR E 859 N SER E 735 SHEET 1 AB2 2 ASP E 796 PHE E 797 0 SHEET 2 AB2 2 PHE E 800 ASN E 801 -1 O PHE E 800 N PHE E 797 SHEET 1 AB3 4 THR E1120 VAL E1122 0 SHEET 2 AB3 4 ALA E1087 PRO E1090 -1 N PHE E1089 O PHE E1121 SHEET 3 AB3 4 ALA E1080 CYS E1082 -1 N ILE E1081 O HIS E1088 SHEET 4 AB3 4 ILE E1132 ASN E1134 1 O VAL E1133 N CYS E1082 SHEET 1 AB4 2 VAL E1094 SER E1097 0 SHEET 2 AB4 2 TRP E1102 THR E1105 -1 O THR E1105 N VAL E1094 SHEET 1 AB5 4 SER F 711 ILE F 714 0 SHEET 2 AB5 4 LYS F1073 THR F1077 -1 O LYS F1073 N ILE F 714 SHEET 3 AB5 4 VAL F1094 SER F1097 -1 O SER F1097 N THR F1076 SHEET 4 AB5 4 TRP F1102 THR F1105 -1 O THR F1105 N VAL F1094 SHEET 1 AB6 3 ASN F 717 PRO F 728 0 SHEET 2 AB6 3 GLY F1059 ALA F1070 -1 O THR F1066 N SER F 721 SHEET 3 AB6 3 TYR F1047 SER F1051 -1 N MET F1050 O VAL F1065 SHEET 1 AB7 3 ASN F 717 PRO F 728 0 SHEET 2 AB7 3 GLY F1059 ALA F1070 -1 O THR F1066 N SER F 721 SHEET 3 AB7 3 GLN F1054 ALA F1056 -1 N GLN F1054 O VAL F1061 SHEET 1 AB8 2 LYS F 733 SER F 735 0 SHEET 2 AB8 2 THR F 859 LEU F 861 -1 O THR F 859 N SER F 735 SHEET 1 AB9 2 ASP F 796 PHE F 797 0 SHEET 2 AB9 2 PHE F 800 ASN F 801 -1 O PHE F 800 N PHE F 797 SHEET 1 AC1 4 THR F1120 VAL F1122 0 SHEET 2 AC1 4 ALA F1087 PRO F1090 -1 N PHE F1089 O PHE F1121 SHEET 3 AC1 4 ALA F1080 CYS F1082 -1 N ILE F1081 O HIS F1088 SHEET 4 AC1 4 ILE F1132 ASN F1134 1 O VAL F1133 N CYS F1082 SHEET 1 AC2 4 MET d 4 SER d 7 0 SHEET 2 AC2 4 ALA d 19 ALA d 25 -1 O ARG d 24 N THR d 5 SHEET 3 AC2 4 GLU d 70 ILE d 75 -1 O PHE d 71 N CYS d 23 SHEET 4 AC2 4 PHE d 62 SER d 67 -1 N SER d 65 O THR d 72 SHEET 1 AC3 5 THR d 53 ARG d 54 0 SHEET 2 AC3 5 ARG d 45 TYR d 49 -1 N TYR d 49 O THR d 53 SHEET 3 AC3 5 LEU d 33 HIS d 38 -1 N TRP d 35 O VAL d 48 SHEET 4 AC3 5 VAL d 85 GLN d 90 -1 O VAL d 85 N HIS d 38 SHEET 5 AC3 5 THR d 104 LYS d 105 -1 O THR d 104 N TYR d 86 SHEET 1 AC4 4 MET g 4 SER g 7 0 SHEET 2 AC4 4 ALA g 19 ALA g 25 -1 O ARG g 24 N THR g 5 SHEET 3 AC4 4 GLU g 70 ILE g 75 -1 O PHE g 71 N CYS g 23 SHEET 4 AC4 4 PHE g 62 SER g 67 -1 N SER g 65 O THR g 72 SHEET 1 AC5 5 THR g 53 ARG g 54 0 SHEET 2 AC5 5 ARG g 45 TYR g 49 -1 N TYR g 49 O THR g 53 SHEET 3 AC5 5 LEU g 33 HIS g 38 -1 N TRP g 35 O VAL g 48 SHEET 4 AC5 5 VAL g 85 GLN g 90 -1 O VAL g 85 N HIS g 38 SHEET 5 AC5 5 THR g 104 LYS g 105 -1 O THR g 104 N TYR g 86 SHEET 1 AC6 4 GLN f 3 GLN f 6 0 SHEET 2 AC6 4 LYS f 19 SER f 25 -1 O LYS f 23 N VAL f 5 SHEET 3 AC6 4 THR f 78 LEU f 83 -1 O MET f 81 N VAL f 20 SHEET 4 AC6 4 VAL f 68 ASP f 73 -1 N ILE f 69 O GLU f 82 SHEET 1 AC7 6 GLU f 10 VAL f 11 0 SHEET 2 AC7 6 THR f 121 THR f 124 1 O VAL f 122 N GLU f 10 SHEET 3 AC7 6 VAL f 93 GLY f 100 -1 N TYR f 94 O THR f 121 SHEET 4 AC7 6 ILE f 34 GLN f 39 -1 N HIS f 35 O ALA f 97 SHEET 5 AC7 6 LEU f 45 ILE f 51 -1 O GLU f 46 N ARG f 38 SHEET 6 AC7 6 THR f 58 TYR f 60 -1 O ASN f 59 N TRP f 50 SHEET 1 AC8 4 GLU f 10 VAL f 11 0 SHEET 2 AC8 4 THR f 121 THR f 124 1 O VAL f 122 N GLU f 10 SHEET 3 AC8 4 VAL f 93 GLY f 100 -1 N TYR f 94 O THR f 121 SHEET 4 AC8 4 ALA f 113 TRP f 117 -1 O ILE f 116 N ARG f 98 SHEET 1 AC9 4 GLN c 3 GLN c 6 0 SHEET 2 AC9 4 VAL c 18 SER c 25 -1 O LYS c 23 N VAL c 5 SHEET 3 AC9 4 THR c 78 LEU c 83 -1 O MET c 81 N VAL c 20 SHEET 4 AC9 4 VAL c 68 ASP c 73 -1 N ILE c 69 O GLU c 82 SHEET 1 AD1 6 GLU c 10 VAL c 11 0 SHEET 2 AD1 6 THR c 121 THR c 124 1 O VAL c 122 N GLU c 10 SHEET 3 AD1 6 VAL c 93 GLY c 100 -1 N TYR c 94 O THR c 121 SHEET 4 AD1 6 ILE c 34 GLN c 39 -1 N HIS c 35 O ALA c 97 SHEET 5 AD1 6 LEU c 45 ILE c 51 -1 O GLU c 46 N ARG c 38 SHEET 6 AD1 6 THR c 58 TYR c 60 -1 O ASN c 59 N TRP c 50 SHEET 1 AD2 4 GLU c 10 VAL c 11 0 SHEET 2 AD2 4 THR c 121 THR c 124 1 O VAL c 122 N GLU c 10 SHEET 3 AD2 4 VAL c 93 GLY c 100 -1 N TYR c 94 O THR c 121 SHEET 4 AD2 4 ALA c 113 TRP c 117 -1 O ILE c 116 N ARG c 98 SHEET 1 AD3 4 MET e 4 SER e 7 0 SHEET 2 AD3 4 ALA e 19 ALA e 25 -1 O ARG e 24 N THR e 5 SHEET 3 AD3 4 GLU e 70 ILE e 75 -1 O PHE e 71 N CYS e 23 SHEET 4 AD3 4 PHE e 62 SER e 67 -1 N SER e 65 O THR e 72 SHEET 1 AD4 5 THR e 53 ARG e 54 0 SHEET 2 AD4 5 ARG e 45 TYR e 49 -1 N TYR e 49 O THR e 53 SHEET 3 AD4 5 LEU e 33 HIS e 38 -1 N TRP e 35 O VAL e 48 SHEET 4 AD4 5 VAL e 85 GLN e 90 -1 O VAL e 85 N HIS e 38 SHEET 5 AD4 5 THR e 104 LYS e 105 -1 O THR e 104 N TYR e 86 SHEET 1 AD5 4 GLN b 3 GLN b 6 0 SHEET 2 AD5 4 VAL b 18 SER b 25 -1 O LYS b 23 N VAL b 5 SHEET 3 AD5 4 THR b 78 LEU b 83 -1 O MET b 81 N VAL b 20 SHEET 4 AD5 4 VAL b 68 ASP b 73 -1 N THR b 71 O TYR b 80 SHEET 1 AD6 6 GLU b 10 VAL b 11 0 SHEET 2 AD6 6 THR b 121 THR b 124 1 O VAL b 122 N GLU b 10 SHEET 3 AD6 6 VAL b 93 GLY b 100 -1 N TYR b 94 O THR b 121 SHEET 4 AD6 6 ILE b 34 GLN b 39 -1 N HIS b 35 O ALA b 97 SHEET 5 AD6 6 LEU b 45 ILE b 51 -1 O GLU b 46 N ARG b 38 SHEET 6 AD6 6 THR b 58 TYR b 60 -1 O ASN b 59 N TRP b 50 SHEET 1 AD7 4 GLU b 10 VAL b 11 0 SHEET 2 AD7 4 THR b 121 THR b 124 1 O VAL b 122 N GLU b 10 SHEET 3 AD7 4 VAL b 93 GLY b 100 -1 N TYR b 94 O THR b 121 SHEET 4 AD7 4 ALA b 113 TRP b 117 -1 O ILE b 116 N ARG b 98 SSBOND 1 CYS G 707 CYS E 883 1555 1555 2.03 SSBOND 2 CYS G 738 CYS G 760 1555 1555 2.03 SSBOND 3 CYS G 743 CYS G 749 1555 1555 2.03 SSBOND 4 CYS G 788 CYS G 876 1555 1555 2.03 SSBOND 5 CYS G 840 CYS G 851 1555 1555 2.03 SSBOND 6 CYS G 1032 CYS G 1043 1555 1555 2.03 SSBOND 7 CYS G 1082 CYS G 1126 1555 1555 2.03 SSBOND 8 CYS E 707 CYS F 883 1555 1555 2.03 SSBOND 9 CYS E 738 CYS E 760 1555 1555 2.03 SSBOND 10 CYS E 743 CYS E 749 1555 1555 2.03 SSBOND 11 CYS E 788 CYS E 876 1555 1555 2.03 SSBOND 12 CYS E 840 CYS E 851 1555 1555 2.03 SSBOND 13 CYS E 1032 CYS E 1043 1555 1555 2.03 SSBOND 14 CYS E 1082 CYS E 1126 1555 1555 2.03 SSBOND 15 CYS F 738 CYS F 760 1555 1555 2.03 SSBOND 16 CYS F 743 CYS F 749 1555 1555 2.03 SSBOND 17 CYS F 788 CYS F 876 1555 1555 2.03 SSBOND 18 CYS F 840 CYS F 851 1555 1555 2.03 SSBOND 19 CYS F 1032 CYS F 1043 1555 1555 2.03 SSBOND 20 CYS F 1082 CYS F 1126 1555 1555 2.03 SSBOND 21 CYS d 23 CYS d 88 1555 1555 2.03 SSBOND 22 CYS g 23 CYS g 88 1555 1555 2.03 SSBOND 23 CYS f 22 CYS f 96 1555 1555 2.03 SSBOND 24 CYS f 99 CYS f 112 1555 1555 2.03 SSBOND 25 CYS c 22 CYS c 96 1555 1555 2.03 SSBOND 26 CYS c 99 CYS c 112 1555 1555 2.03 SSBOND 27 CYS e 23 CYS e 88 1555 1555 2.03 SSBOND 28 CYS b 22 CYS b 96 1555 1555 2.03 SSBOND 29 CYS b 99 CYS b 112 1555 1555 2.03 LINK ND2 ASN G 709 C1 NAG G1302 1555 1555 1.44 LINK ND2 ASN G 717 C1 NAG G1301 1555 1555 1.44 LINK ND2 ASN G 801 C1 NAG G1303 1555 1555 1.44 LINK ND2 ASN G1074 C1 NAG G1304 1555 1555 1.44 LINK ND2 ASN G1098 C1 NAG A 1 1555 1555 1.44 LINK ND2 ASN G1134 C1 NAG G1305 1555 1555 1.44 LINK ND2 ASN E 709 C1 NAG E1302 1555 1555 1.44 LINK ND2 ASN E 717 C1 NAG E1301 1555 1555 1.44 LINK ND2 ASN E 801 C1 NAG E1303 1555 1555 1.44 LINK ND2 ASN E1074 C1 NAG E1304 1555 1555 1.44 LINK ND2 ASN E1098 C1 NAG B 1 1555 1555 1.44 LINK ND2 ASN E1134 C1 NAG E1305 1555 1555 1.44 LINK ND2 ASN F 709 C1 NAG F1302 1555 1555 1.44 LINK ND2 ASN F 717 C1 NAG F1301 1555 1555 1.44 LINK ND2 ASN F 801 C1 NAG F1303 1555 1555 1.44 LINK ND2 ASN F1074 C1 NAG F1304 1555 1555 1.44 LINK ND2 ASN F1098 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN F1134 C1 NAG F1305 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.46 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.46 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46 CISPEP 1 SER d 7 PRO d 8 0 -4.32 CISPEP 2 TRP d 94 PRO d 95 0 1.84 CISPEP 3 SER g 7 PRO g 8 0 -4.25 CISPEP 4 TRP g 94 PRO g 95 0 1.73 CISPEP 5 SER e 7 PRO e 8 0 -4.20 CISPEP 6 TRP e 94 PRO e 95 0 1.81 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