HEADER VIRAL PROTEIN 05-MAY-23 8OYU TITLE STABILISED BA.1 SARS-COV-2 SPIKE WITH H6 NANOBODIES IN '2 UP 1 DOWN' TITLE 2 RBD CONFORMATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN,FIBRITIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN,COLLAR PROTEIN,WHISKER COMPND 5 ANTIGEN CONTROL PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: H6 NANOBODY; COMPND 9 CHAIN: E, D; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2, ENTEROBACTERIA PHAGE T4; SOURCE 4 ORGANISM_TAXID: 2697049, 10665; SOURCE 5 GENE: S, 2, WAC; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, COMPLEX, SARS-COV-2, SPIKE, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.WECKENER,J.H.NAISMITH,R.J.OWENS JRNL AUTH K.A.S.CORNISH,M.WECKENER,J.H.NAISMITH,R.J.OWENS JRNL TITL TRIMERIC NANOBODIES POTENTLY NEUTRALIZE OMICRON VARIANTS OF JRNL TITL 2 SARS-COV-2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : UCSF CHIMERA, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7QO7 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) : 4.000 REMARK 3 NUMBER OF PARTICLES : 131621 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8OYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292129657. 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 STABILISED HEXAPRO REMARK 245 OMICRON BA.1 SPIKE TRIMER WITH REMARK 245 TWO H6 NANOBODIES; H6 NANOBODY; REMARK 245 STABILISED HEXAPRO OMICRON BA.1 REMARK 245 SPIKE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 40.50 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) : 200 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P 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 PHE A 2 REMARK 465 VAL A 3 REMARK 465 PHE A 4 REMARK 465 LEU A 5 REMARK 465 VAL A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 PRO A 9 REMARK 465 LEU A 10 REMARK 465 VAL A 11 REMARK 465 SER A 12 REMARK 465 SER A 13 REMARK 465 GLN A 14 REMARK 465 CYS A 15 REMARK 465 VAL A 16 REMARK 465 ASN A 17 REMARK 465 LEU A 18 REMARK 465 TRP A 147 REMARK 465 LEU A 246 REMARK 465 THR A 247 REMARK 465 PRO A 248 REMARK 465 GLY A 249 REMARK 465 ASP A 250 REMARK 465 SER A 251 REMARK 465 SER A 252 REMARK 465 VAL A 442 REMARK 465 SER A 443 REMARK 465 GLN A 674 REMARK 465 THR A 675 REMARK 465 LYS A 676 REMARK 465 SER A 677 REMARK 465 HIS A 678 REMARK 465 GLY A 679 REMARK 465 SER A 680 REMARK 465 ALA A 681 REMARK 465 SER A 682 REMARK 465 SER A 683 REMARK 465 VAL A 684 REMARK 465 ALA A 685 REMARK 465 GLY A 839 REMARK 465 ASP A 840 REMARK 465 ILE A 841 REMARK 465 ALA A 842 REMARK 465 ALA A 843 REMARK 465 ARG A 844 REMARK 465 PHE A 1145 REMARK 465 LYS A 1146 REMARK 465 GLU A 1147 REMARK 465 GLU A 1148 REMARK 465 LEU A 1149 REMARK 465 ASP A 1150 REMARK 465 LYS A 1151 REMARK 465 TYR A 1152 REMARK 465 PHE A 1153 REMARK 465 LYS A 1154 REMARK 465 ASN A 1155 REMARK 465 HIS A 1156 REMARK 465 THR A 1157 REMARK 465 SER A 1158 REMARK 465 PRO A 1159 REMARK 465 ASP A 1160 REMARK 465 VAL A 1161 REMARK 465 ASP A 1162 REMARK 465 LEU A 1163 REMARK 465 GLY A 1164 REMARK 465 ASP A 1165 REMARK 465 ILE A 1166 REMARK 465 SER A 1167 REMARK 465 GLY A 1168 REMARK 465 ILE A 1169 REMARK 465 ASN A 1170 REMARK 465 ALA A 1171 REMARK 465 SER A 1172 REMARK 465 VAL A 1173 REMARK 465 VAL A 1174 REMARK 465 ASN A 1175 REMARK 465 ILE A 1176 REMARK 465 GLN A 1177 REMARK 465 LYS A 1178 REMARK 465 GLU A 1179 REMARK 465 ILE A 1180 REMARK 465 ASP A 1181 REMARK 465 ARG A 1182 REMARK 465 LEU A 1183 REMARK 465 ASN A 1184 REMARK 465 GLU A 1185 REMARK 465 VAL A 1186 REMARK 465 ALA A 1187 REMARK 465 LYS A 1188 REMARK 465 ASN A 1189 REMARK 465 LEU A 1190 REMARK 465 ASN A 1191 REMARK 465 GLU A 1192 REMARK 465 SER A 1193 REMARK 465 LEU A 1194 REMARK 465 ILE A 1195 REMARK 465 ASP A 1196 REMARK 465 LEU A 1197 REMARK 465 GLN A 1198 REMARK 465 GLU A 1199 REMARK 465 LEU A 1200 REMARK 465 GLY A 1201 REMARK 465 LYS A 1202 REMARK 465 TYR A 1203 REMARK 465 GLU A 1204 REMARK 465 GLN A 1205 REMARK 465 GLY A 1206 REMARK 465 SER A 1207 REMARK 465 GLY A 1208 REMARK 465 TYR A 1209 REMARK 465 ILE A 1210 REMARK 465 PRO A 1211 REMARK 465 GLU A 1212 REMARK 465 ALA A 1213 REMARK 465 PRO A 1214 REMARK 465 ARG A 1215 REMARK 465 ASP A 1216 REMARK 465 GLY A 1217 REMARK 465 GLN A 1218 REMARK 465 ALA A 1219 REMARK 465 TYR A 1220 REMARK 465 VAL A 1221 REMARK 465 ARG A 1222 REMARK 465 LYS A 1223 REMARK 465 ASP A 1224 REMARK 465 GLY A 1225 REMARK 465 GLU A 1226 REMARK 465 TRP A 1227 REMARK 465 VAL A 1228 REMARK 465 LEU A 1229 REMARK 465 LEU A 1230 REMARK 465 SER A 1231 REMARK 465 THR A 1232 REMARK 465 PHE A 1233 REMARK 465 LEU A 1234 REMARK 465 GLY A 1235 REMARK 465 ARG A 1236 REMARK 465 SER A 1237 REMARK 465 LEU A 1238 REMARK 465 GLU A 1239 REMARK 465 VAL A 1240 REMARK 465 LEU A 1241 REMARK 465 PHE A 1242 REMARK 465 GLN A 1243 REMARK 465 GLY A 1244 REMARK 465 PRO A 1245 REMARK 465 GLY A 1246 REMARK 465 HIS A 1247 REMARK 465 HIS A 1248 REMARK 465 HIS A 1249 REMARK 465 HIS A 1250 REMARK 465 HIS A 1251 REMARK 465 HIS A 1252 REMARK 465 HIS A 1253 REMARK 465 HIS A 1254 REMARK 465 MET B 1 REMARK 465 PHE B 2 REMARK 465 VAL B 3 REMARK 465 PHE B 4 REMARK 465 LEU B 5 REMARK 465 VAL B 6 REMARK 465 LEU B 7 REMARK 465 LEU B 8 REMARK 465 PRO B 9 REMARK 465 LEU B 10 REMARK 465 VAL B 11 REMARK 465 SER B 12 REMARK 465 SER B 13 REMARK 465 GLN B 14 REMARK 465 CYS B 15 REMARK 465 VAL B 16 REMARK 465 ASN B 17 REMARK 465 LEU B 18 REMARK 465 TRP B 147 REMARK 465 LEU B 246 REMARK 465 THR B 247 REMARK 465 PRO B 248 REMARK 465 GLY B 249 REMARK 465 ASP B 250 REMARK 465 SER B 251 REMARK 465 SER B 252 REMARK 465 GLN B 674 REMARK 465 THR B 675 REMARK 465 LYS B 676 REMARK 465 SER B 677 REMARK 465 HIS B 678 REMARK 465 GLY B 679 REMARK 465 SER B 680 REMARK 465 ALA B 681 REMARK 465 SER B 682 REMARK 465 SER B 683 REMARK 465 VAL B 684 REMARK 465 ALA B 685 REMARK 465 LEU B 838 REMARK 465 GLY B 839 REMARK 465 ASP B 840 REMARK 465 ILE B 841 REMARK 465 ALA B 842 REMARK 465 ALA B 843 REMARK 465 ARG B 844 REMARK 465 ASP B 845 REMARK 465 LEU B 846 REMARK 465 ILE B 847 REMARK 465 PHE B 1145 REMARK 465 LYS B 1146 REMARK 465 GLU B 1147 REMARK 465 GLU B 1148 REMARK 465 LEU B 1149 REMARK 465 ASP B 1150 REMARK 465 LYS B 1151 REMARK 465 TYR B 1152 REMARK 465 PHE B 1153 REMARK 465 LYS B 1154 REMARK 465 ASN B 1155 REMARK 465 HIS B 1156 REMARK 465 THR B 1157 REMARK 465 SER B 1158 REMARK 465 PRO B 1159 REMARK 465 ASP B 1160 REMARK 465 VAL B 1161 REMARK 465 ASP B 1162 REMARK 465 LEU B 1163 REMARK 465 GLY B 1164 REMARK 465 ASP B 1165 REMARK 465 ILE B 1166 REMARK 465 SER B 1167 REMARK 465 GLY B 1168 REMARK 465 ILE B 1169 REMARK 465 ASN B 1170 REMARK 465 ALA B 1171 REMARK 465 SER B 1172 REMARK 465 VAL B 1173 REMARK 465 VAL B 1174 REMARK 465 ASN B 1175 REMARK 465 ILE B 1176 REMARK 465 GLN B 1177 REMARK 465 LYS B 1178 REMARK 465 GLU B 1179 REMARK 465 ILE B 1180 REMARK 465 ASP B 1181 REMARK 465 ARG B 1182 REMARK 465 LEU B 1183 REMARK 465 ASN B 1184 REMARK 465 GLU B 1185 REMARK 465 VAL B 1186 REMARK 465 ALA B 1187 REMARK 465 LYS B 1188 REMARK 465 ASN B 1189 REMARK 465 LEU B 1190 REMARK 465 ASN B 1191 REMARK 465 GLU B 1192 REMARK 465 SER B 1193 REMARK 465 LEU B 1194 REMARK 465 ILE B 1195 REMARK 465 ASP B 1196 REMARK 465 LEU B 1197 REMARK 465 GLN B 1198 REMARK 465 GLU B 1199 REMARK 465 LEU B 1200 REMARK 465 GLY B 1201 REMARK 465 LYS B 1202 REMARK 465 TYR B 1203 REMARK 465 GLU B 1204 REMARK 465 GLN B 1205 REMARK 465 GLY B 1206 REMARK 465 SER B 1207 REMARK 465 GLY B 1208 REMARK 465 TYR B 1209 REMARK 465 ILE B 1210 REMARK 465 PRO B 1211 REMARK 465 GLU B 1212 REMARK 465 ALA B 1213 REMARK 465 PRO B 1214 REMARK 465 ARG B 1215 REMARK 465 ASP B 1216 REMARK 465 GLY B 1217 REMARK 465 GLN B 1218 REMARK 465 ALA B 1219 REMARK 465 TYR B 1220 REMARK 465 VAL B 1221 REMARK 465 ARG B 1222 REMARK 465 LYS B 1223 REMARK 465 ASP B 1224 REMARK 465 GLY B 1225 REMARK 465 GLU B 1226 REMARK 465 TRP B 1227 REMARK 465 VAL B 1228 REMARK 465 LEU B 1229 REMARK 465 LEU B 1230 REMARK 465 SER B 1231 REMARK 465 THR B 1232 REMARK 465 PHE B 1233 REMARK 465 LEU B 1234 REMARK 465 GLY B 1235 REMARK 465 ARG B 1236 REMARK 465 SER B 1237 REMARK 465 LEU B 1238 REMARK 465 GLU B 1239 REMARK 465 VAL B 1240 REMARK 465 LEU B 1241 REMARK 465 PHE B 1242 REMARK 465 GLN B 1243 REMARK 465 GLY B 1244 REMARK 465 PRO B 1245 REMARK 465 GLY B 1246 REMARK 465 HIS B 1247 REMARK 465 HIS B 1248 REMARK 465 HIS B 1249 REMARK 465 HIS B 1250 REMARK 465 HIS B 1251 REMARK 465 HIS B 1252 REMARK 465 HIS B 1253 REMARK 465 HIS B 1254 REMARK 465 MET C 1 REMARK 465 PHE C 2 REMARK 465 VAL C 3 REMARK 465 PHE C 4 REMARK 465 LEU C 5 REMARK 465 VAL C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 PRO C 9 REMARK 465 LEU C 10 REMARK 465 VAL C 11 REMARK 465 SER C 12 REMARK 465 SER C 13 REMARK 465 GLN C 14 REMARK 465 CYS C 15 REMARK 465 VAL C 16 REMARK 465 ASN C 17 REMARK 465 LEU C 18 REMARK 465 TRP C 147 REMARK 465 LEU C 246 REMARK 465 THR C 247 REMARK 465 PRO C 248 REMARK 465 GLY C 249 REMARK 465 ASP C 250 REMARK 465 SER C 251 REMARK 465 SER C 252 REMARK 465 VAL C 442 REMARK 465 SER C 443 REMARK 465 GLN C 674 REMARK 465 THR C 675 REMARK 465 LYS C 676 REMARK 465 SER C 677 REMARK 465 HIS C 678 REMARK 465 GLY C 679 REMARK 465 SER C 680 REMARK 465 ALA C 681 REMARK 465 SER C 682 REMARK 465 SER C 683 REMARK 465 VAL C 684 REMARK 465 ALA C 685 REMARK 465 GLY C 839 REMARK 465 ASP C 840 REMARK 465 ILE C 841 REMARK 465 ALA C 842 REMARK 465 ALA C 843 REMARK 465 ARG C 844 REMARK 465 PHE C 1145 REMARK 465 LYS C 1146 REMARK 465 GLU C 1147 REMARK 465 GLU C 1148 REMARK 465 LEU C 1149 REMARK 465 ASP C 1150 REMARK 465 LYS C 1151 REMARK 465 TYR C 1152 REMARK 465 PHE C 1153 REMARK 465 LYS C 1154 REMARK 465 ASN C 1155 REMARK 465 HIS C 1156 REMARK 465 THR C 1157 REMARK 465 SER C 1158 REMARK 465 PRO C 1159 REMARK 465 ASP C 1160 REMARK 465 VAL C 1161 REMARK 465 ASP C 1162 REMARK 465 LEU C 1163 REMARK 465 GLY C 1164 REMARK 465 ASP C 1165 REMARK 465 ILE C 1166 REMARK 465 SER C 1167 REMARK 465 GLY C 1168 REMARK 465 ILE C 1169 REMARK 465 ASN C 1170 REMARK 465 ALA C 1171 REMARK 465 SER C 1172 REMARK 465 VAL C 1173 REMARK 465 VAL C 1174 REMARK 465 ASN C 1175 REMARK 465 ILE C 1176 REMARK 465 GLN C 1177 REMARK 465 LYS C 1178 REMARK 465 GLU C 1179 REMARK 465 ILE C 1180 REMARK 465 ASP C 1181 REMARK 465 ARG C 1182 REMARK 465 LEU C 1183 REMARK 465 ASN C 1184 REMARK 465 GLU C 1185 REMARK 465 VAL C 1186 REMARK 465 ALA C 1187 REMARK 465 LYS C 1188 REMARK 465 ASN C 1189 REMARK 465 LEU C 1190 REMARK 465 ASN C 1191 REMARK 465 GLU C 1192 REMARK 465 SER C 1193 REMARK 465 LEU C 1194 REMARK 465 ILE C 1195 REMARK 465 ASP C 1196 REMARK 465 LEU C 1197 REMARK 465 GLN C 1198 REMARK 465 GLU C 1199 REMARK 465 LEU C 1200 REMARK 465 GLY C 1201 REMARK 465 LYS C 1202 REMARK 465 TYR C 1203 REMARK 465 GLU C 1204 REMARK 465 GLN C 1205 REMARK 465 GLY C 1206 REMARK 465 SER C 1207 REMARK 465 GLY C 1208 REMARK 465 TYR C 1209 REMARK 465 ILE C 1210 REMARK 465 PRO C 1211 REMARK 465 GLU C 1212 REMARK 465 ALA C 1213 REMARK 465 PRO C 1214 REMARK 465 ARG C 1215 REMARK 465 ASP C 1216 REMARK 465 GLY C 1217 REMARK 465 GLN C 1218 REMARK 465 ALA C 1219 REMARK 465 TYR C 1220 REMARK 465 VAL C 1221 REMARK 465 ARG C 1222 REMARK 465 LYS C 1223 REMARK 465 ASP C 1224 REMARK 465 GLY C 1225 REMARK 465 GLU C 1226 REMARK 465 TRP C 1227 REMARK 465 VAL C 1228 REMARK 465 LEU C 1229 REMARK 465 LEU C 1230 REMARK 465 SER C 1231 REMARK 465 THR C 1232 REMARK 465 PHE C 1233 REMARK 465 LEU C 1234 REMARK 465 GLY C 1235 REMARK 465 ARG C 1236 REMARK 465 SER C 1237 REMARK 465 LEU C 1238 REMARK 465 GLU C 1239 REMARK 465 VAL C 1240 REMARK 465 LEU C 1241 REMARK 465 PHE C 1242 REMARK 465 GLN C 1243 REMARK 465 GLY C 1244 REMARK 465 PRO C 1245 REMARK 465 GLY C 1246 REMARK 465 HIS C 1247 REMARK 465 HIS C 1248 REMARK 465 HIS C 1249 REMARK 465 HIS C 1250 REMARK 465 HIS C 1251 REMARK 465 HIS C 1252 REMARK 465 HIS C 1253 REMARK 465 HIS C 1254 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 LEU A 838 CG CD1 CD2 REMARK 470 ASP A 845 CG OD1 OD2 REMARK 470 LEU A 846 CG CD1 CD2 REMARK 470 ILE A 847 CG1 CG2 CD1 REMARK 470 LEU C 838 CG CD1 CD2 REMARK 470 ASP C 845 CG OD1 OD2 REMARK 470 LEU C 846 CG CD1 CD2 REMARK 470 ILE C 847 CG1 CG2 CD1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NH2 ARG B 354 O PRO C 227 2.15 REMARK 500 O GLU B 658 OH TYR B 692 2.17 REMARK 500 O GLU A 658 OH TYR A 692 2.18 REMARK 500 CG ASN A 279 C1 NAG A 1301 2.19 REMARK 500 OD1 ASP B 464 OG SER B 466 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO E 32 CB PRO E 32 CG 0.609 REMARK 500 PRO E 32 CG PRO E 32 CD -0.877 REMARK 500 PRO E 32 CD PRO E 32 N 0.157 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 25 CA - N - CD ANGL. DEV. = -11.9 DEGREES REMARK 500 PHE B 799 C - N - CA ANGL. DEV. = 15.1 DEGREES REMARK 500 PRO E 32 C - N - CD ANGL. DEV. = 14.4 DEGREES REMARK 500 PRO E 32 CA - N - CD ANGL. DEV. = -22.1 DEGREES REMARK 500 PRO E 32 N - CA - CB ANGL. DEV. = -12.5 DEGREES REMARK 500 PRO E 32 CA - CB - CG ANGL. DEV. = -20.2 DEGREES REMARK 500 PRO E 32 CB - CG - CD ANGL. DEV. = -41.3 DEGREES REMARK 500 PRO E 32 N - CD - CG ANGL. DEV. = -20.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 PHE A 32 -146.20 57.91 REMARK 500 PHE A 59 61.72 60.52 REMARK 500 PHE A 77 50.08 -91.66 REMARK 500 ASP A 78 49.58 -82.42 REMARK 500 ASN A 85 -107.58 59.77 REMARK 500 ALA A 121 -116.09 53.17 REMARK 500 VAL A 125 74.28 56.01 REMARK 500 ASN A 160 145.22 68.92 REMARK 500 ASP A 193 52.80 36.58 REMARK 500 ALA A 289 -1.47 -140.78 REMARK 500 PRO A 327 48.72 -91.88 REMARK 500 ASN A 331 34.21 -140.66 REMARK 500 VAL A 480 -150.47 46.57 REMARK 500 SER A 493 65.12 60.92 REMARK 500 LYS A 526 125.38 -32.71 REMARK 500 SER A 527 41.51 -142.44 REMARK 500 THR A 528 -153.99 37.13 REMARK 500 VAL A 531 144.83 -171.26 REMARK 500 PHE A 540 98.69 -67.91 REMARK 500 SER A 602 153.27 65.95 REMARK 500 THR A 627 70.85 55.28 REMARK 500 TYR A 633 -125.19 37.26 REMARK 500 SER A 634 -168.45 -125.07 REMARK 500 ASN A 707 53.32 -91.55 REMARK 500 VAL A 726 -60.31 -124.62 REMARK 500 THR A 824 6.05 -68.00 REMARK 500 PHE A 830 -6.38 71.93 REMARK 500 TYR A 834 -1.66 67.07 REMARK 500 ALA A 969 -169.20 -79.02 REMARK 500 GLU A1089 26.82 -141.09 REMARK 500 PHE B 32 -151.75 61.49 REMARK 500 PHE B 77 52.03 -90.02 REMARK 500 ASN B 85 -111.88 55.60 REMARK 500 SER B 96 -169.28 -128.52 REMARK 500 ASN B 120 -168.11 -123.00 REMARK 500 THR B 122 40.80 -141.62 REMARK 500 ASN B 160 149.88 67.36 REMARK 500 GLN B 178 -177.02 -170.81 REMARK 500 ASN B 180 -16.91 75.87 REMARK 500 ASP B 193 49.74 35.29 REMARK 500 ILE B 206 -71.23 61.48 REMARK 500 GLU B 209 71.07 47.02 REMARK 500 ALA B 289 34.65 -141.74 REMARK 500 SER B 313 -169.70 -161.67 REMARK 500 THR B 342 -169.38 -72.33 REMARK 500 ASN B 357 72.02 55.72 REMARK 500 ALA B 369 -169.05 64.73 REMARK 500 PRO B 370 -165.11 -67.66 REMARK 500 PHE B 371 58.97 71.28 REMARK 500 PHE B 372 -163.54 -77.89 REMARK 500 REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ILE C 323 VAL C 324 -148.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 1303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-17296 RELATED DB: EMDB REMARK 900 STABILISED BA.1 SARS-COV-2 SPIKE WITH H6 NANOBODIES IN '2 UP 1 DOWN' REMARK 900 RBD CONFORMATION DBREF 8OYU A 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYU A 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYU B 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYU B 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYU C 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYU C 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYU E 2 127 PDB 8OYU 8OYU 2 127 DBREF 8OYU D 2 127 PDB 8OYU 8OYU 2 127 SEQADV 8OYU VAL A 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYU A UNP P0DTC2 HIS 69 DELETION SEQADV 8OYU A UNP P0DTC2 VAL 70 DELETION SEQADV 8OYU ILE A 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYU A UNP P0DTC2 GLY 142 DELETION SEQADV 8OYU A UNP P0DTC2 VAL 143 DELETION SEQADV 8OYU A UNP P0DTC2 TYR 144 DELETION SEQADV 8OYU ASP A 140 UNP P0DTC2 TYR 145 VARIANT SEQADV 8OYU ILE A 206 UNP P0DTC2 ASN 211 VARIANT SEQADV 8OYU VAL A 207 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYU ARG A 208 UNP P0DTC2 VAL 213 VARIANT SEQADV 8OYU GLU A 209 UNP P0DTC2 ARG 214 VARIANT SEQADV 8OYU PRO A 210 UNP P0DTC2 INSERTION SEQADV 8OYU GLU A 211 UNP P0DTC2 INSERTION SEQADV 8OYU ASP A 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYU LEU A 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYU PRO A 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYU PHE A 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYU ASN A 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYU LYS A 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYU SER A 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYU ASN A 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYU LYS A 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYU ALA A 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYU LYS A 490 UNP P0DTC2 GLN 493 VARIANT SEQADV 8OYU SER A 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYU ARG A 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYU TYR A 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYU HIS A 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYU LYS A 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYU GLY A 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYU TYR A 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYU LYS A 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYU HIS A 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYU GLY A 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYU SER A 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYU SER A 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYU LYS A 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYU TYR A 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYU PRO A 814 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8OYU LYS A 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYU PRO A 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYU PRO A 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYU PRO A 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYU HIS A 951 UNP P0DTC2 GLN 954 VARIANT SEQADV 8OYU LYS A 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYU PHE A 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYU PRO A 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYU PRO A 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYU GLY A 1206 UNP P0DTC2 LINKER SEQADV 8OYU SER A 1207 UNP P0DTC2 LINKER SEQADV 8OYU LEU A 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYU GLY A 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYU ARG A 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYU SER A 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU A 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLU A 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYU VAL A 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU A 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYU PHE A 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLN A 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY A 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYU PRO A 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY A 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS A 1254 UNP P10104 EXPRESSION TAG SEQADV 8OYU VAL B 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYU B UNP P0DTC2 HIS 69 DELETION SEQADV 8OYU B UNP P0DTC2 VAL 70 DELETION SEQADV 8OYU ILE B 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYU B UNP P0DTC2 GLY 142 DELETION SEQADV 8OYU B UNP P0DTC2 VAL 143 DELETION SEQADV 8OYU B UNP P0DTC2 TYR 144 DELETION SEQADV 8OYU ASP B 140 UNP P0DTC2 TYR 145 VARIANT SEQADV 8OYU ILE B 206 UNP P0DTC2 ASN 211 VARIANT SEQADV 8OYU VAL B 207 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYU ARG B 208 UNP P0DTC2 VAL 213 VARIANT SEQADV 8OYU GLU B 209 UNP P0DTC2 ARG 214 VARIANT SEQADV 8OYU PRO B 210 UNP P0DTC2 INSERTION SEQADV 8OYU GLU B 211 UNP P0DTC2 INSERTION SEQADV 8OYU ASP B 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYU LEU B 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYU PRO B 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYU PHE B 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYU ASN B 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYU LYS B 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYU SER B 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYU ASN B 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYU LYS B 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYU ALA B 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYU LYS B 490 UNP P0DTC2 GLN 493 VARIANT SEQADV 8OYU SER B 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYU ARG B 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYU TYR B 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYU HIS B 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYU LYS B 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYU GLY B 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYU TYR B 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYU LYS B 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYU HIS B 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYU GLY B 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYU SER B 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYU SER B 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYU LYS B 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYU TYR B 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYU PRO B 814 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8OYU LYS B 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYU PRO B 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYU PRO B 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYU PRO B 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYU HIS B 951 UNP P0DTC2 GLN 954 VARIANT SEQADV 8OYU LYS B 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYU PHE B 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYU PRO B 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYU PRO B 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYU GLY B 1206 UNP P0DTC2 LINKER SEQADV 8OYU SER B 1207 UNP P0DTC2 LINKER SEQADV 8OYU LEU B 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYU GLY B 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYU ARG B 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYU SER B 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU B 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLU B 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYU VAL B 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU B 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYU PHE B 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLN B 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY B 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYU PRO B 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY B 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS B 1254 UNP P10104 EXPRESSION TAG SEQADV 8OYU VAL C 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYU C UNP P0DTC2 HIS 69 DELETION SEQADV 8OYU C UNP P0DTC2 VAL 70 DELETION SEQADV 8OYU ILE C 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYU C UNP P0DTC2 GLY 142 DELETION SEQADV 8OYU C UNP P0DTC2 VAL 143 DELETION SEQADV 8OYU C UNP P0DTC2 TYR 144 DELETION SEQADV 8OYU ASP C 140 UNP P0DTC2 TYR 145 VARIANT SEQADV 8OYU ILE C 206 UNP P0DTC2 ASN 211 VARIANT SEQADV 8OYU VAL C 207 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYU ARG C 208 UNP P0DTC2 VAL 213 VARIANT SEQADV 8OYU GLU C 209 UNP P0DTC2 ARG 214 VARIANT SEQADV 8OYU PRO C 210 UNP P0DTC2 INSERTION SEQADV 8OYU GLU C 211 UNP P0DTC2 INSERTION SEQADV 8OYU ASP C 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYU LEU C 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYU PRO C 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYU PHE C 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYU ASN C 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYU LYS C 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYU SER C 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYU ASN C 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYU LYS C 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYU ALA C 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYU LYS C 490 UNP P0DTC2 GLN 493 VARIANT SEQADV 8OYU SER C 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYU ARG C 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYU TYR C 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYU HIS C 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYU LYS C 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYU GLY C 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYU TYR C 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYU LYS C 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYU HIS C 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYU GLY C 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYU SER C 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYU SER C 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYU LYS C 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYU TYR C 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYU PRO C 814 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 8OYU LYS C 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYU PRO C 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYU PRO C 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYU PRO C 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYU HIS C 951 UNP P0DTC2 GLN 954 VARIANT SEQADV 8OYU LYS C 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYU PHE C 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYU PRO C 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYU PRO C 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYU GLY C 1206 UNP P0DTC2 LINKER SEQADV 8OYU SER C 1207 UNP P0DTC2 LINKER SEQADV 8OYU LEU C 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYU GLY C 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYU ARG C 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYU SER C 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU C 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLU C 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYU VAL C 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYU LEU C 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYU PHE C 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLN C 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY C 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYU PRO C 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYU GLY C 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYU HIS C 1254 UNP P10104 EXPRESSION TAG SEQRES 1 A 1254 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 A 1254 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 A 1254 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 A 1254 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 A 1254 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 A 1254 HIS VAL ILE SER GLY THR ASN GLY THR LYS ARG PHE ASP SEQRES 7 A 1254 ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SEQRES 8 A 1254 SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP ILE PHE SEQRES 9 A 1254 GLY THR THR LEU ASP SER LYS THR GLN SER LEU LEU ILE SEQRES 10 A 1254 VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL CYS GLU SEQRES 11 A 1254 PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP HIS LYS ASN SEQRES 12 A 1254 ASN LYS SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SEQRES 13 A 1254 SER ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO SEQRES 14 A 1254 PHE LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS SEQRES 15 A 1254 ASN LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR SEQRES 16 A 1254 PHE LYS ILE TYR SER LYS HIS THR PRO ILE ILE VAL ARG SEQRES 17 A 1254 GLU PRO GLU ASP LEU PRO GLN GLY PHE SER ALA LEU GLU SEQRES 18 A 1254 PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN ILE THR ARG SEQRES 19 A 1254 PHE GLN THR LEU LEU ALA LEU HIS ARG SER TYR LEU THR SEQRES 20 A 1254 PRO GLY ASP SER SER SER GLY TRP THR ALA GLY ALA ALA SEQRES 21 A 1254 ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG THR PHE LEU SEQRES 22 A 1254 LEU LYS TYR ASN GLU ASN GLY THR ILE THR ASP ALA VAL SEQRES 23 A 1254 ASP CYS ALA LEU ASP PRO LEU SER GLU THR LYS CYS THR SEQRES 24 A 1254 LEU LYS SER PHE THR VAL GLU LYS GLY ILE TYR GLN THR SEQRES 25 A 1254 SER ASN PHE ARG VAL GLN PRO THR GLU SER ILE VAL ARG SEQRES 26 A 1254 PHE PRO ASN ILE THR ASN LEU CYS PRO PHE ASP GLU VAL SEQRES 27 A 1254 PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN SEQRES 28 A 1254 ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL SEQRES 29 A 1254 LEU TYR ASN LEU ALA PRO PHE PHE THR PHE LYS CYS TYR SEQRES 30 A 1254 GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR SEQRES 31 A 1254 ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU SEQRES 32 A 1254 VAL ARG GLN ILE ALA PRO GLY GLN THR GLY ASN ILE ALA SEQRES 33 A 1254 ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS SEQRES 34 A 1254 VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SER LYS VAL SEQRES 35 A 1254 SER GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SEQRES 36 A 1254 SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU SEQRES 37 A 1254 ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA SEQRES 38 A 1254 GLY PHE ASN CYS TYR PHE PRO LEU LYS SER TYR SER PHE SEQRES 39 A 1254 ARG PRO THR TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL SEQRES 40 A 1254 VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR SEQRES 41 A 1254 VAL CYS GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN SEQRES 42 A 1254 LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU LYS GLY THR SEQRES 43 A 1254 GLY VAL LEU THR GLU SER ASN LYS LYS PHE LEU PRO PHE SEQRES 44 A 1254 GLN GLN PHE GLY ARG ASP ILE ALA ASP THR THR ASP ALA SEQRES 45 A 1254 VAL ARG ASP PRO GLN THR LEU GLU ILE LEU ASP ILE THR SEQRES 46 A 1254 PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR PRO GLY SEQRES 47 A 1254 THR ASN THR SER ASN GLN VAL ALA VAL LEU TYR GLN GLY SEQRES 48 A 1254 VAL ASN CYS THR GLU VAL PRO VAL ALA ILE HIS ALA ASP SEQRES 49 A 1254 GLN LEU THR PRO THR TRP ARG VAL TYR SER THR GLY SER SEQRES 50 A 1254 ASN VAL PHE GLN THR ARG ALA GLY CYS LEU ILE GLY ALA SEQRES 51 A 1254 GLU TYR VAL ASN ASN SER TYR GLU CYS ASP ILE PRO ILE SEQRES 52 A 1254 GLY ALA GLY ILE CYS ALA SER TYR GLN THR GLN THR LYS SEQRES 53 A 1254 SER HIS GLY SER ALA SER SER VAL ALA SER GLN SER ILE SEQRES 54 A 1254 ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SER VAL SEQRES 55 A 1254 ALA TYR SER ASN ASN SER ILE ALA ILE PRO THR ASN PHE SEQRES 56 A 1254 THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SER MET SEQRES 57 A 1254 THR LYS THR SER VAL ASP CYS THR MET TYR ILE CYS GLY SEQRES 58 A 1254 ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN TYR GLY SEQRES 59 A 1254 SER PHE CYS THR GLN LEU LYS ARG ALA LEU THR GLY ILE SEQRES 60 A 1254 ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL PHE ALA SEQRES 61 A 1254 GLN VAL LYS GLN ILE TYR LYS THR PRO PRO ILE LYS TYR SEQRES 62 A 1254 PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO SEQRES 63 A 1254 SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP LEU LEU SEQRES 64 A 1254 PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE ILE LYS SEQRES 65 A 1254 GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA ARG ASP SEQRES 66 A 1254 LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU THR VAL LEU SEQRES 67 A 1254 PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN TYR THR SEQRES 68 A 1254 SER ALA LEU LEU ALA GLY THR ILE THR SER GLY TRP THR SEQRES 69 A 1254 PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE PRO MET SEQRES 70 A 1254 GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN SEQRES 71 A 1254 ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA ASN GLN SEQRES 72 A 1254 PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER LEU SER SEQRES 73 A 1254 SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP VAL VAL SEQRES 74 A 1254 ASN HIS ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN SEQRES 75 A 1254 LEU SER SER LYS PHE GLY ALA ILE SER SER VAL LEU ASN SEQRES 76 A 1254 ASP ILE PHE SER ARG LEU ASP PRO PRO GLU ALA GLU VAL SEQRES 77 A 1254 GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU SEQRES 78 A 1254 GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU SEQRES 79 A 1254 ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS MET SER SEQRES 80 A 1254 GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS SEQRES 81 A 1254 GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SER ALA SEQRES 82 A 1254 PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SEQRES 83 A 1254 ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA ILE CYS SEQRES 84 A 1254 HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY VAL PHE SEQRES 85 A 1254 VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN ARG ASN SEQRES 86 A 1254 PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN THR PHE SEQRES 87 A 1254 VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE VAL ASN SEQRES 88 A 1254 ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER SEQRES 89 A 1254 PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SEQRES 90 A 1254 SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN SEQRES 91 A 1254 ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU SEQRES 92 A 1254 ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP SEQRES 93 A 1254 LEU GLN GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR SEQRES 94 A 1254 ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG SEQRES 95 A 1254 LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SEQRES 96 A 1254 ARG SER LEU GLU VAL LEU PHE GLN GLY PRO GLY HIS HIS SEQRES 97 A 1254 HIS HIS HIS HIS HIS HIS SEQRES 1 B 1254 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 B 1254 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 B 1254 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 B 1254 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 B 1254 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 B 1254 HIS VAL ILE SER GLY THR ASN GLY THR LYS ARG PHE ASP SEQRES 7 B 1254 ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SEQRES 8 B 1254 SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP ILE PHE SEQRES 9 B 1254 GLY THR THR LEU ASP SER LYS THR GLN SER LEU LEU ILE SEQRES 10 B 1254 VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL CYS GLU SEQRES 11 B 1254 PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP HIS LYS ASN SEQRES 12 B 1254 ASN LYS SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SEQRES 13 B 1254 SER ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO SEQRES 14 B 1254 PHE LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS SEQRES 15 B 1254 ASN LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR SEQRES 16 B 1254 PHE LYS ILE TYR SER LYS HIS THR PRO ILE ILE VAL ARG SEQRES 17 B 1254 GLU PRO GLU ASP LEU PRO GLN GLY PHE SER ALA LEU GLU SEQRES 18 B 1254 PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN ILE THR ARG SEQRES 19 B 1254 PHE GLN THR LEU LEU ALA LEU HIS ARG SER TYR LEU THR SEQRES 20 B 1254 PRO GLY ASP SER SER SER GLY TRP THR ALA GLY ALA ALA SEQRES 21 B 1254 ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG THR PHE LEU SEQRES 22 B 1254 LEU LYS TYR ASN GLU ASN GLY THR ILE THR ASP ALA VAL SEQRES 23 B 1254 ASP CYS ALA LEU ASP PRO LEU SER GLU THR LYS CYS THR SEQRES 24 B 1254 LEU LYS SER PHE THR VAL GLU LYS GLY ILE TYR GLN THR SEQRES 25 B 1254 SER ASN PHE ARG VAL GLN PRO THR GLU SER ILE VAL ARG SEQRES 26 B 1254 PHE PRO ASN ILE THR ASN LEU CYS PRO PHE ASP GLU VAL SEQRES 27 B 1254 PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN SEQRES 28 B 1254 ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL SEQRES 29 B 1254 LEU TYR ASN LEU ALA PRO PHE PHE THR PHE LYS CYS TYR SEQRES 30 B 1254 GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR SEQRES 31 B 1254 ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU SEQRES 32 B 1254 VAL ARG GLN ILE ALA PRO GLY GLN THR GLY ASN ILE ALA SEQRES 33 B 1254 ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS SEQRES 34 B 1254 VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SER LYS VAL SEQRES 35 B 1254 SER GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SEQRES 36 B 1254 SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU SEQRES 37 B 1254 ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA SEQRES 38 B 1254 GLY PHE ASN CYS TYR PHE PRO LEU LYS SER TYR SER PHE SEQRES 39 B 1254 ARG PRO THR TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL SEQRES 40 B 1254 VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR SEQRES 41 B 1254 VAL CYS GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN SEQRES 42 B 1254 LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU LYS GLY THR SEQRES 43 B 1254 GLY VAL LEU THR GLU SER ASN LYS LYS PHE LEU PRO PHE SEQRES 44 B 1254 GLN GLN PHE GLY ARG ASP ILE ALA ASP THR THR ASP ALA SEQRES 45 B 1254 VAL ARG ASP PRO GLN THR LEU GLU ILE LEU ASP ILE THR SEQRES 46 B 1254 PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR PRO GLY SEQRES 47 B 1254 THR ASN THR SER ASN GLN VAL ALA VAL LEU TYR GLN GLY SEQRES 48 B 1254 VAL ASN CYS THR GLU VAL PRO VAL ALA ILE HIS ALA ASP SEQRES 49 B 1254 GLN LEU THR PRO THR TRP ARG VAL TYR SER THR GLY SER SEQRES 50 B 1254 ASN VAL PHE GLN THR ARG ALA GLY CYS LEU ILE GLY ALA SEQRES 51 B 1254 GLU TYR VAL ASN ASN SER TYR GLU CYS ASP ILE PRO ILE SEQRES 52 B 1254 GLY ALA GLY ILE CYS ALA SER TYR GLN THR GLN THR LYS SEQRES 53 B 1254 SER HIS GLY SER ALA SER SER VAL ALA SER GLN SER ILE SEQRES 54 B 1254 ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SER VAL SEQRES 55 B 1254 ALA TYR SER ASN ASN SER ILE ALA ILE PRO THR ASN PHE SEQRES 56 B 1254 THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SER MET SEQRES 57 B 1254 THR LYS THR SER VAL ASP CYS THR MET TYR ILE CYS GLY SEQRES 58 B 1254 ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN TYR GLY SEQRES 59 B 1254 SER PHE CYS THR GLN LEU LYS ARG ALA LEU THR GLY ILE SEQRES 60 B 1254 ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL PHE ALA SEQRES 61 B 1254 GLN VAL LYS GLN ILE TYR LYS THR PRO PRO ILE LYS TYR SEQRES 62 B 1254 PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO SEQRES 63 B 1254 SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP LEU LEU SEQRES 64 B 1254 PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE ILE LYS SEQRES 65 B 1254 GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA ARG ASP SEQRES 66 B 1254 LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU THR VAL LEU SEQRES 67 B 1254 PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN TYR THR SEQRES 68 B 1254 SER ALA LEU LEU ALA GLY THR ILE THR SER GLY TRP THR SEQRES 69 B 1254 PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE PRO MET SEQRES 70 B 1254 GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN SEQRES 71 B 1254 ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA ASN GLN SEQRES 72 B 1254 PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER LEU SER SEQRES 73 B 1254 SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP VAL VAL SEQRES 74 B 1254 ASN HIS ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN SEQRES 75 B 1254 LEU SER SER LYS PHE GLY ALA ILE SER SER VAL LEU ASN SEQRES 76 B 1254 ASP ILE PHE SER ARG LEU ASP PRO PRO GLU ALA GLU VAL SEQRES 77 B 1254 GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU SEQRES 78 B 1254 GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU SEQRES 79 B 1254 ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS MET SER SEQRES 80 B 1254 GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS SEQRES 81 B 1254 GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SER ALA SEQRES 82 B 1254 PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SEQRES 83 B 1254 ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA ILE CYS SEQRES 84 B 1254 HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY VAL PHE SEQRES 85 B 1254 VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN ARG ASN SEQRES 86 B 1254 PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN THR PHE SEQRES 87 B 1254 VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE VAL ASN SEQRES 88 B 1254 ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER SEQRES 89 B 1254 PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SEQRES 90 B 1254 SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN SEQRES 91 B 1254 ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU SEQRES 92 B 1254 ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP SEQRES 93 B 1254 LEU GLN GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR SEQRES 94 B 1254 ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG SEQRES 95 B 1254 LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SEQRES 96 B 1254 ARG SER LEU GLU VAL LEU PHE GLN GLY PRO GLY HIS HIS SEQRES 97 B 1254 HIS HIS HIS HIS HIS HIS SEQRES 1 C 1254 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 C 1254 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 C 1254 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 C 1254 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 C 1254 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 C 1254 HIS VAL ILE SER GLY THR ASN GLY THR LYS ARG PHE ASP SEQRES 7 C 1254 ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SEQRES 8 C 1254 SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP ILE PHE SEQRES 9 C 1254 GLY THR THR LEU ASP SER LYS THR GLN SER LEU LEU ILE SEQRES 10 C 1254 VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL CYS GLU SEQRES 11 C 1254 PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP HIS LYS ASN SEQRES 12 C 1254 ASN LYS SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SEQRES 13 C 1254 SER ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO SEQRES 14 C 1254 PHE LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS SEQRES 15 C 1254 ASN LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR SEQRES 16 C 1254 PHE LYS ILE TYR SER LYS HIS THR PRO ILE ILE VAL ARG SEQRES 17 C 1254 GLU PRO GLU ASP LEU PRO GLN GLY PHE SER ALA LEU GLU SEQRES 18 C 1254 PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN ILE THR ARG SEQRES 19 C 1254 PHE GLN THR LEU LEU ALA LEU HIS ARG SER TYR LEU THR SEQRES 20 C 1254 PRO GLY ASP SER SER SER GLY TRP THR ALA GLY ALA ALA SEQRES 21 C 1254 ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG THR PHE LEU SEQRES 22 C 1254 LEU LYS TYR ASN GLU ASN GLY THR ILE THR ASP ALA VAL SEQRES 23 C 1254 ASP CYS ALA LEU ASP PRO LEU SER GLU THR LYS CYS THR SEQRES 24 C 1254 LEU LYS SER PHE THR VAL GLU LYS GLY ILE TYR GLN THR SEQRES 25 C 1254 SER ASN PHE ARG VAL GLN PRO THR GLU SER ILE VAL ARG SEQRES 26 C 1254 PHE PRO ASN ILE THR ASN LEU CYS PRO PHE ASP GLU VAL SEQRES 27 C 1254 PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN SEQRES 28 C 1254 ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL SEQRES 29 C 1254 LEU TYR ASN LEU ALA PRO PHE PHE THR PHE LYS CYS TYR SEQRES 30 C 1254 GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR SEQRES 31 C 1254 ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU SEQRES 32 C 1254 VAL ARG GLN ILE ALA PRO GLY GLN THR GLY ASN ILE ALA SEQRES 33 C 1254 ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS SEQRES 34 C 1254 VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SER LYS VAL SEQRES 35 C 1254 SER GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SEQRES 36 C 1254 SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU SEQRES 37 C 1254 ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA SEQRES 38 C 1254 GLY PHE ASN CYS TYR PHE PRO LEU LYS SER TYR SER PHE SEQRES 39 C 1254 ARG PRO THR TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL SEQRES 40 C 1254 VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR SEQRES 41 C 1254 VAL CYS GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN SEQRES 42 C 1254 LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU LYS GLY THR SEQRES 43 C 1254 GLY VAL LEU THR GLU SER ASN LYS LYS PHE LEU PRO PHE SEQRES 44 C 1254 GLN GLN PHE GLY ARG ASP ILE ALA ASP THR THR ASP ALA SEQRES 45 C 1254 VAL ARG ASP PRO GLN THR LEU GLU ILE LEU ASP ILE THR SEQRES 46 C 1254 PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR PRO GLY SEQRES 47 C 1254 THR ASN THR SER ASN GLN VAL ALA VAL LEU TYR GLN GLY SEQRES 48 C 1254 VAL ASN CYS THR GLU VAL PRO VAL ALA ILE HIS ALA ASP SEQRES 49 C 1254 GLN LEU THR PRO THR TRP ARG VAL TYR SER THR GLY SER SEQRES 50 C 1254 ASN VAL PHE GLN THR ARG ALA GLY CYS LEU ILE GLY ALA SEQRES 51 C 1254 GLU TYR VAL ASN ASN SER TYR GLU CYS ASP ILE PRO ILE SEQRES 52 C 1254 GLY ALA GLY ILE CYS ALA SER TYR GLN THR GLN THR LYS SEQRES 53 C 1254 SER HIS GLY SER ALA SER SER VAL ALA SER GLN SER ILE SEQRES 54 C 1254 ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SER VAL SEQRES 55 C 1254 ALA TYR SER ASN ASN SER ILE ALA ILE PRO THR ASN PHE SEQRES 56 C 1254 THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SER MET SEQRES 57 C 1254 THR LYS THR SER VAL ASP CYS THR MET TYR ILE CYS GLY SEQRES 58 C 1254 ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN TYR GLY SEQRES 59 C 1254 SER PHE CYS THR GLN LEU LYS ARG ALA LEU THR GLY ILE SEQRES 60 C 1254 ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL PHE ALA SEQRES 61 C 1254 GLN VAL LYS GLN ILE TYR LYS THR PRO PRO ILE LYS TYR SEQRES 62 C 1254 PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO SEQRES 63 C 1254 SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP LEU LEU SEQRES 64 C 1254 PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE ILE LYS SEQRES 65 C 1254 GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA ARG ASP SEQRES 66 C 1254 LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU THR VAL LEU SEQRES 67 C 1254 PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN TYR THR SEQRES 68 C 1254 SER ALA LEU LEU ALA GLY THR ILE THR SER GLY TRP THR SEQRES 69 C 1254 PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE PRO MET SEQRES 70 C 1254 GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN SEQRES 71 C 1254 ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA ASN GLN SEQRES 72 C 1254 PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER LEU SER SEQRES 73 C 1254 SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP VAL VAL SEQRES 74 C 1254 ASN HIS ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN SEQRES 75 C 1254 LEU SER SER LYS PHE GLY ALA ILE SER SER VAL LEU ASN SEQRES 76 C 1254 ASP ILE PHE SER ARG LEU ASP PRO PRO GLU ALA GLU VAL SEQRES 77 C 1254 GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU SEQRES 78 C 1254 GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU SEQRES 79 C 1254 ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS MET SER SEQRES 80 C 1254 GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS SEQRES 81 C 1254 GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SER ALA SEQRES 82 C 1254 PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SEQRES 83 C 1254 ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA ILE CYS SEQRES 84 C 1254 HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY VAL PHE SEQRES 85 C 1254 VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN ARG ASN SEQRES 86 C 1254 PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN THR PHE SEQRES 87 C 1254 VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE VAL ASN SEQRES 88 C 1254 ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER SEQRES 89 C 1254 PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SEQRES 90 C 1254 SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN SEQRES 91 C 1254 ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU SEQRES 92 C 1254 ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP SEQRES 93 C 1254 LEU GLN GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR SEQRES 94 C 1254 ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG SEQRES 95 C 1254 LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY SEQRES 96 C 1254 ARG SER LEU GLU VAL LEU PHE GLN GLY PRO GLY HIS HIS SEQRES 97 C 1254 HIS HIS HIS HIS HIS HIS SEQRES 1 E 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 126 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3 E 126 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4 E 126 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 E 126 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6 E 126 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7 E 126 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8 E 126 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9 E 126 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10 E 126 GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 D 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 126 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3 D 126 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4 D 126 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 D 126 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6 D 126 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7 D 126 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8 D 126 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9 D 126 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10 D 126 GLN GLY THR GLN VAL THR VAL SER SER HET NAG A1301 14 HET NAG A1302 14 HET NAG A1303 14 HET NAG B1301 14 HET NAG B1302 14 HET NAG B1303 14 HET NAG B1304 14 HET NAG C1301 14 HET NAG C1302 14 HET NAG C1303 14 HET NAG C1304 14 HET NAG C1305 14 HET NAG C1306 14 HET NAG C1307 14 HET NAG C1308 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 6 NAG 37(C8 H15 N O6) HELIX 1 AA1 SER A 69 GLY A 73 5 5 HELIX 2 AA2 ASP A 291 LYS A 301 1 11 HELIX 3 AA3 PHE A 335 ASN A 340 1 6 HELIX 4 AA4 TYR A 362 LEU A 368 1 7 HELIX 5 AA5 SER A 435 SER A 440 1 6 HELIX 6 AA6 ASN A 445 LEU A 449 5 5 HELIX 7 AA7 ALA A 620 ASP A 624 5 5 HELIX 8 AA8 ASP A 734 CYS A 740 1 7 HELIX 9 AA9 SER A 743 GLN A 752 1 10 HELIX 10 AB1 CYS A 757 ALA A 780 1 24 HELIX 11 AB2 SER A 813 THR A 824 1 12 HELIX 12 AB3 LEU A 846 PHE A 852 1 7 HELIX 13 AB4 THR A 863 GLY A 882 1 20 HELIX 14 AB5 TRP A 883 GLY A 888 5 6 HELIX 15 AB6 PRO A 894 GLY A 905 1 12 HELIX 16 AB7 THR A 909 SER A 937 1 29 HELIX 17 AB8 LEU A 942 GLN A 962 1 21 HELIX 18 AB9 LEU A 963 SER A 965 5 3 HELIX 19 AC1 VAL A 973 ARG A 980 1 8 HELIX 20 AC2 ASP A 982 LEU A 1031 1 50 HELIX 21 AC3 ASP B 291 LYS B 301 1 11 HELIX 22 AC4 TYR B 362 LEU B 368 1 7 HELIX 23 AC5 GLY B 413 ASN B 419 1 7 HELIX 24 AC6 ASP B 734 CYS B 740 1 7 HELIX 25 AC7 SER B 743 GLN B 752 1 10 HELIX 26 AC8 SER B 755 ALA B 780 1 26 HELIX 27 AC9 SER B 813 THR B 824 1 12 HELIX 28 AD1 THR B 863 GLY B 882 1 20 HELIX 29 AD2 TRP B 883 ALA B 887 5 5 HELIX 30 AD3 PRO B 894 GLY B 905 1 12 HELIX 31 AD4 THR B 909 SER B 937 1 29 HELIX 32 AD5 LEU B 942 LEU B 963 1 22 HELIX 33 AD6 VAL B 973 ARG B 980 1 8 HELIX 34 AD7 ASP B 982 VAL B 1030 1 49 HELIX 35 AD8 SER C 69 GLY C 73 5 5 HELIX 36 AD9 ASP C 291 LYS C 301 1 11 HELIX 37 AE1 PHE C 335 ASN C 340 1 6 HELIX 38 AE2 TYR C 362 LEU C 368 1 7 HELIX 39 AE3 GLU C 403 ALA C 408 1 6 HELIX 40 AE4 SER C 435 SER C 440 1 6 HELIX 41 AE5 ASN C 445 LEU C 449 5 5 HELIX 42 AE6 ASN C 539 LEU C 543 5 5 HELIX 43 AE7 ALA C 620 ASP C 624 5 5 HELIX 44 AE8 ASP C 734 CYS C 740 1 7 HELIX 45 AE9 SER C 743 GLN C 752 1 10 HELIX 46 AF1 CYS C 757 ALA C 780 1 24 HELIX 47 AF2 SER C 813 THR C 824 1 12 HELIX 48 AF3 LEU C 846 PHE C 852 1 7 HELIX 49 AF4 THR C 863 GLY C 882 1 20 HELIX 50 AF5 TRP C 883 GLY C 888 5 6 HELIX 51 AF6 PRO C 894 GLY C 905 1 12 HELIX 52 AF7 THR C 909 SER C 937 1 29 HELIX 53 AF8 LEU C 942 GLN C 962 1 21 HELIX 54 AF9 LEU C 963 SER C 965 5 3 HELIX 55 AG1 VAL C 973 ARG C 980 1 8 HELIX 56 AG2 ASP C 982 VAL C 1030 1 49 HELIX 57 AG3 HIS E 57 THR E 61 5 5 HELIX 58 AG4 LYS E 90 THR E 94 5 5 HELIX 59 AG5 LYS D 90 THR D 94 5 5 SHEET 1 AA1 2 TYR A 28 ASN A 30 0 SHEET 2 AA1 2 ASN A 61 THR A 63 -1 O VAL A 62 N THR A 29 SHEET 1 AA2 3 LEU A 48 PHE A 55 0 SHEET 2 AA2 3 GLN A 268 TYR A 276 -1 O LEU A 274 N HIS A 49 SHEET 3 AA2 3 ILE A 282 ASP A 287 -1 O VAL A 286 N LEU A 273 SHEET 1 AA3 3 HIS A 66 VAL A 67 0 SHEET 2 AA3 3 ALA A 260 TYR A 263 -1 O ALA A 260 N VAL A 67 SHEET 3 AA3 3 ALA A 91 SER A 92 -1 N ALA A 91 O TYR A 263 SHEET 1 AA4 3 GLN A 113 SER A 114 0 SHEET 2 AA4 3 ILE A 126 PHE A 133 -1 O CYS A 129 N SER A 114 SHEET 3 AA4 3 TYR A 155 TYR A 165 -1 O TYR A 165 N ILE A 126 SHEET 1 AA5 3 GLU A 186 ILE A 192 0 SHEET 2 AA5 3 TYR A 195 LYS A 201 -1 O LYS A 197 N LYS A 190 SHEET 3 AA5 3 PRO A 222 LEU A 226 -1 O LEU A 223 N ILE A 198 SHEET 1 AA6 5 GLY A 308 ARG A 316 0 SHEET 2 AA6 5 PHE A 589 THR A 596 -1 O GLY A 590 N PHE A 315 SHEET 3 AA6 5 ALA A 606 GLN A 610 -1 O ALA A 606 N ILE A 595 SHEET 4 AA6 5 GLY A 645 ILE A 648 -1 O CYS A 646 N TYR A 609 SHEET 5 AA6 5 PHE A 640 GLN A 641 -1 N PHE A 640 O LEU A 647 SHEET 1 AA7 4 LYS A 353 ILE A 355 0 SHEET 2 AA7 4 THR A 390 ALA A 394 -1 O ALA A 394 N LYS A 353 SHEET 3 AA7 4 TYR A 505 GLU A 513 -1 O GLU A 513 N THR A 390 SHEET 4 AA7 4 PHE A 397 ILE A 399 -1 N ILE A 399 O TYR A 505 SHEET 1 AA8 4 LYS A 353 ILE A 355 0 SHEET 2 AA8 4 THR A 390 ALA A 394 -1 O ALA A 394 N LYS A 353 SHEET 3 AA8 4 TYR A 505 GLU A 513 -1 O GLU A 513 N THR A 390 SHEET 4 AA8 4 CYS A 429 ASN A 434 -1 N TRP A 433 O ARG A 506 SHEET 1 AA9 4 CYS A 535 VAL A 536 0 SHEET 2 AA9 4 GLY A 547 GLU A 551 -1 O GLY A 547 N VAL A 536 SHEET 3 AA9 4 LEU A 582 THR A 585 -1 O THR A 585 N VAL A 548 SHEET 4 AA9 4 ALA A 572 VAL A 573 -1 N VAL A 573 O LEU A 582 SHEET 1 AB1 4 GLU A 651 TYR A 652 0 SHEET 2 AB1 4 SER A 688 THR A 693 1 O ALA A 691 N GLU A 651 SHEET 3 AB1 4 ILE A 667 GLN A 672 -1 N GLN A 672 O SER A 688 SHEET 4 AB1 4 ILE A 661 GLY A 664 -1 N ILE A 661 O ALA A 669 SHEET 1 AB2 2 ALA A 698 SER A 701 0 SHEET 2 AB2 2 GLN B 784 LYS B 787 1 O ILE B 785 N ALA A 698 SHEET 1 AB3 3 ILE A 709 PRO A 725 0 SHEET 2 AB3 3 GLY A1056 THR A1074 -1 O ALA A1067 N ASN A 714 SHEET 3 AB3 3 TYR A1044 ALA A1053 -1 N GLN A1051 O VAL A1058 SHEET 1 AB4 4 ILE A 709 PRO A 725 0 SHEET 2 AB4 4 GLY A1056 THR A1074 -1 O ALA A1067 N ASN A 714 SHEET 3 AB4 4 VAL A1091 SER A1094 -1 O SER A1094 N THR A1073 SHEET 4 AB4 4 TRP A1099 THR A1102 -1 O THR A1102 N VAL A1091 SHEET 1 AB5 2 THR A 731 VAL A 733 0 SHEET 2 AB5 2 LEU A 855 VAL A 857 -1 O THR A 856 N SER A 732 SHEET 1 AB6 2 GLN A 784 TYR A 786 0 SHEET 2 AB6 2 ALA C 698 ASN C 700 1 O ASN C 700 N ILE A 785 SHEET 1 AB7 4 THR A1117 VAL A1119 0 SHEET 2 AB7 4 ALA A1084 PRO A1087 -1 N PHE A1086 O PHE A1118 SHEET 3 AB7 4 ILE A1078 CYS A1079 -1 N ILE A1078 O HIS A1085 SHEET 4 AB7 4 VAL A1130 ASN A1131 1 O VAL A1130 N CYS A1079 SHEET 1 AB8 2 TYR B 28 ASN B 30 0 SHEET 2 AB8 2 ASN B 61 THR B 63 -1 O VAL B 62 N THR B 29 SHEET 1 AB9 2 VAL B 36 TYR B 37 0 SHEET 2 AB9 2 ALA B 219 LEU B 220 1 O LEU B 220 N VAL B 36 SHEET 1 AC1 3 LEU B 48 PHE B 55 0 SHEET 2 AC1 3 GLN B 268 TYR B 276 -1 O LEU B 274 N HIS B 49 SHEET 3 AC1 3 ILE B 282 ASP B 287 -1 O VAL B 286 N LEU B 273 SHEET 1 AC2 3 HIS B 66 VAL B 67 0 SHEET 2 AC2 3 ALA B 260 TYR B 263 -1 O ALA B 260 N VAL B 67 SHEET 3 AC2 3 ALA B 91 SER B 92 -1 N ALA B 91 O TYR B 263 SHEET 1 AC3 3 LEU B 82 PRO B 83 0 SHEET 2 AC3 3 ARG B 234 PHE B 235 -1 O PHE B 235 N LEU B 82 SHEET 3 AC3 3 PHE B 104 GLY B 105 -1 N GLY B 105 O ARG B 234 SHEET 1 AC4 4 GLY B 87 VAL B 88 0 SHEET 2 AC4 4 GLU B 186 ILE B 192 -1 O PHE B 189 N VAL B 88 SHEET 3 AC4 4 TYR B 195 LYS B 201 -1 O LYS B 197 N LYS B 190 SHEET 4 AC4 4 PRO B 222 LEU B 226 -1 O LEU B 223 N ILE B 198 SHEET 1 AC5 3 SER B 114 LEU B 116 0 SHEET 2 AC5 3 ILE B 126 PHE B 133 -1 O LYS B 127 N LEU B 116 SHEET 3 AC5 3 TYR B 155 TYR B 165 -1 O TYR B 165 N ILE B 126 SHEET 1 AC6 5 GLY B 308 ARG B 316 0 SHEET 2 AC6 5 PHE B 589 THR B 596 -1 O VAL B 594 N TYR B 310 SHEET 3 AC6 5 ALA B 606 GLN B 610 -1 O ALA B 606 N ILE B 595 SHEET 4 AC6 5 GLY B 645 ILE B 648 -1 O CYS B 646 N TYR B 609 SHEET 5 AC6 5 PHE B 640 THR B 642 -1 N THR B 642 O GLY B 645 SHEET 1 AC7 5 SER B 322 ILE B 323 0 SHEET 2 AC7 5 CYS B 535 PHE B 540 1 O ASN B 537 N ILE B 323 SHEET 3 AC7 5 LEU B 543 GLU B 551 -1 O GLY B 545 N PHE B 538 SHEET 4 AC7 5 ILE B 581 THR B 585 -1 O THR B 585 N VAL B 548 SHEET 5 AC7 5 ALA B 572 ARG B 574 -1 N VAL B 573 O LEU B 582 SHEET 1 AC8 2 ARG B 352 ILE B 355 0 SHEET 2 AC8 2 VAL B 392 ASP B 395 -1 O ALA B 394 N LYS B 353 SHEET 1 AC9 2 CYS B 358 VAL B 359 0 SHEET 2 AC9 2 VAL B 521 CYS B 522 1 O CYS B 522 N CYS B 358 SHEET 1 AD1 3 LYS B 375 CYS B 376 0 SHEET 2 AD1 3 CYS B 429 ASN B 434 -1 O VAL B 430 N LYS B 375 SHEET 3 AD1 3 TYR B 505 VAL B 509 -1 O ARG B 506 N TRP B 433 SHEET 1 AD2 4 GLU B 651 TYR B 652 0 SHEET 2 AD2 4 SER B 688 THR B 693 1 O ALA B 691 N GLU B 651 SHEET 3 AD2 4 ILE B 667 GLN B 672 -1 N GLN B 672 O SER B 688 SHEET 4 AD2 4 ILE B 661 ILE B 663 -1 N ILE B 663 O ILE B 667 SHEET 1 AD3 2 ALA B 698 ASN B 700 0 SHEET 2 AD3 2 GLN C 784 TYR C 786 1 O ILE C 785 N ASN B 700 SHEET 1 AD4 3 SER B 708 PRO B 725 0 SHEET 2 AD4 3 GLY B1056 ALA B1075 -1 O VAL B1065 N THR B 716 SHEET 3 AD4 3 TYR B1044 ALA B1053 -1 N GLN B1051 O VAL B1058 SHEET 1 AD5 4 SER B 708 PRO B 725 0 SHEET 2 AD5 4 GLY B1056 ALA B1075 -1 O VAL B1065 N THR B 716 SHEET 3 AD5 4 VAL B1091 SER B1094 -1 O SER B1094 N THR B1073 SHEET 4 AD5 4 PHE B1100 THR B1102 -1 O PHE B1100 N VAL B1093 SHEET 1 AD6 2 THR B 731 VAL B 733 0 SHEET 2 AD6 2 LEU B 855 VAL B 857 -1 O THR B 856 N SER B 732 SHEET 1 AD7 4 THR B1117 ASN B1122 0 SHEET 2 AD7 4 LYS B1083 PRO B1087 -1 N PHE B1086 O PHE B1118 SHEET 3 AD7 4 ILE B1078 CYS B1079 -1 N ILE B1078 O HIS B1085 SHEET 4 AD7 4 VAL B1130 ASN B1131 1 O VAL B1130 N CYS B1079 SHEET 1 AD8 2 TYR C 28 ASN C 30 0 SHEET 2 AD8 2 ASN C 61 THR C 63 -1 O VAL C 62 N THR C 29 SHEET 1 AD9 3 LEU C 48 PHE C 55 0 SHEET 2 AD9 3 GLN C 268 TYR C 276 -1 O LEU C 274 N HIS C 49 SHEET 3 AD9 3 ILE C 282 ASP C 287 -1 O VAL C 286 N LEU C 273 SHEET 1 AE1 3 HIS C 66 VAL C 67 0 SHEET 2 AE1 3 ALA C 260 TYR C 263 -1 O ALA C 260 N VAL C 67 SHEET 3 AE1 3 ALA C 91 SER C 92 -1 N ALA C 91 O TYR C 263 SHEET 1 AE2 3 GLN C 113 SER C 114 0 SHEET 2 AE2 3 ILE C 126 PHE C 133 -1 O CYS C 129 N SER C 114 SHEET 3 AE2 3 TYR C 155 TYR C 165 -1 O TYR C 165 N ILE C 126 SHEET 1 AE3 2 PHE C 138 LEU C 139 0 SHEET 2 AE3 2 LEU C 239 ALA C 240 1 O LEU C 239 N LEU C 139 SHEET 1 AE4 3 GLU C 186 ILE C 192 0 SHEET 2 AE4 3 TYR C 195 LYS C 201 -1 O LYS C 197 N LYS C 190 SHEET 3 AE4 3 GLU C 221 LEU C 226 -1 O LEU C 226 N PHE C 196 SHEET 1 AE5 3 GLU C 306 TYR C 310 0 SHEET 2 AE5 3 PHE C 589 GLY C 598 -1 O VAL C 594 N TYR C 310 SHEET 3 AE5 3 ASN C 314 ARG C 316 -1 N PHE C 315 O GLY C 590 SHEET 1 AE6 5 GLU C 306 TYR C 310 0 SHEET 2 AE6 5 PHE C 589 GLY C 598 -1 O VAL C 594 N TYR C 310 SHEET 3 AE6 5 ALA C 606 GLN C 610 -1 O LEU C 608 N SER C 593 SHEET 4 AE6 5 GLY C 645 ILE C 648 -1 O CYS C 646 N TYR C 609 SHEET 5 AE6 5 PHE C 640 GLN C 641 -1 N PHE C 640 O LEU C 647 SHEET 1 AE7 4 LYS C 353 ILE C 355 0 SHEET 2 AE7 4 THR C 390 ALA C 394 -1 O ALA C 394 N LYS C 353 SHEET 3 AE7 4 TYR C 505 GLU C 513 -1 O GLU C 513 N THR C 390 SHEET 4 AE7 4 PHE C 397 ILE C 399 -1 N ILE C 399 O TYR C 505 SHEET 1 AE8 4 LYS C 353 ILE C 355 0 SHEET 2 AE8 4 THR C 390 ALA C 394 -1 O ALA C 394 N LYS C 353 SHEET 3 AE8 4 TYR C 505 GLU C 513 -1 O GLU C 513 N THR C 390 SHEET 4 AE8 4 CYS C 429 ASN C 434 -1 N TRP C 433 O ARG C 506 SHEET 1 AE9 4 CYS C 535 ASN C 537 0 SHEET 2 AE9 4 THR C 546 GLU C 551 -1 O GLY C 547 N VAL C 536 SHEET 3 AE9 4 LEU C 582 THR C 585 -1 O THR C 585 N VAL C 548 SHEET 4 AE9 4 ALA C 572 VAL C 573 -1 N VAL C 573 O LEU C 582 SHEET 1 AF1 4 GLU C 651 TYR C 652 0 SHEET 2 AF1 4 SER C 688 THR C 693 1 O ALA C 691 N GLU C 651 SHEET 3 AF1 4 ILE C 667 GLN C 672 -1 N GLN C 672 O SER C 688 SHEET 4 AF1 4 ILE C 661 GLY C 664 -1 N GLY C 664 O ILE C 667 SHEET 1 AF2 3 SER C 708 PRO C 725 0 SHEET 2 AF2 3 GLY C1056 THR C1074 -1 O HIS C1061 N THR C 720 SHEET 3 AF2 3 TYR C1044 ALA C1053 -1 N MET C1047 O VAL C1062 SHEET 1 AF3 4 SER C 708 PRO C 725 0 SHEET 2 AF3 4 GLY C1056 THR C1074 -1 O HIS C1061 N THR C 720 SHEET 3 AF3 4 VAL C1091 SER C1094 -1 O SER C1094 N THR C1073 SHEET 4 AF3 4 TRP C1099 THR C1102 -1 O PHE C1100 N VAL C1093 SHEET 1 AF4 2 THR C 731 VAL C 733 0 SHEET 2 AF4 2 LEU C 855 VAL C 857 -1 O THR C 856 N SER C 732 SHEET 1 AF5 4 THR C1117 VAL C1119 0 SHEET 2 AF5 4 ALA C1084 PRO C1087 -1 N PHE C1086 O PHE C1118 SHEET 3 AF5 4 ILE C1078 CYS C1079 -1 N ILE C1078 O HIS C1085 SHEET 4 AF5 4 VAL C1130 ASN C1131 1 O VAL C1130 N CYS C1079 SHEET 1 AF6 4 GLN E 4 SER E 8 0 SHEET 2 AF6 4 LEU E 19 SER E 26 -1 O SER E 22 N SER E 8 SHEET 3 AF6 4 THR E 81 MET E 86 -1 O MET E 86 N LEU E 19 SHEET 4 AF6 4 PHE E 71 ASP E 76 -1 N SER E 74 O TYR E 83 SHEET 1 AF7 6 LEU E 12 VAL E 13 0 SHEET 2 AF7 6 THR E 121 VAL E 125 1 O THR E 124 N VAL E 13 SHEET 3 AF7 6 ALA E 95 THR E 101 -1 N TYR E 97 O THR E 121 SHEET 4 AF7 6 VAL E 35 GLN E 40 -1 N PHE E 38 O TYR E 98 SHEET 5 AF7 6 GLU E 47 ILE E 52 -1 O SER E 50 N TRP E 37 SHEET 6 AF7 6 TYR E 62 TYR E 63 -1 O TYR E 62 N CYS E 51 SHEET 1 AF8 4 LEU E 12 VAL E 13 0 SHEET 2 AF8 4 THR E 121 VAL E 125 1 O THR E 124 N VAL E 13 SHEET 3 AF8 4 ALA E 95 THR E 101 -1 N TYR E 97 O THR E 121 SHEET 4 AF8 4 TRP E 116 TRP E 117 -1 O TRP E 116 N THR E 101 SHEET 1 AF9 4 GLN D 4 SER D 8 0 SHEET 2 AF9 4 LEU D 19 SER D 26 -1 O VAL D 24 N VAL D 6 SHEET 3 AF9 4 THR D 81 MET D 86 -1 O LEU D 84 N LEU D 21 SHEET 4 AF9 4 PHE D 71 ASP D 76 -1 N THR D 72 O GLN D 85 SHEET 1 AG1 3 LEU D 12 VAL D 13 0 SHEET 2 AG1 3 THR D 121 VAL D 125 1 O THR D 124 N VAL D 13 SHEET 3 AG1 3 ALA D 95 TYR D 97 -1 N TYR D 97 O THR D 121 SHEET 1 AG2 5 TYR D 62 TYR D 63 0 SHEET 2 AG2 5 GLU D 47 ILE D 52 -1 N CYS D 51 O TYR D 62 SHEET 3 AG2 5 VAL D 35 ARG D 39 -1 N VAL D 35 O ILE D 52 SHEET 4 AG2 5 CYS D 99 THR D 101 -1 O ALA D 100 N ALA D 36 SHEET 5 AG2 5 TRP D 116 TRP D 117 -1 O TRP D 116 N THR D 101 SSBOND 1 CYS A 129 CYS A 161 1555 1555 2.03 SSBOND 2 CYS A 288 CYS A 298 1555 1555 2.03 SSBOND 3 CYS A 333 CYS A 358 1555 1555 2.03 SSBOND 4 CYS A 376 CYS A 429 1555 1555 2.03 SSBOND 5 CYS A 388 CYS A 522 1555 1555 2.03 SSBOND 6 CYS A 477 CYS A 485 1555 1555 2.03 SSBOND 7 CYS A 535 CYS A 587 1555 1555 2.03 SSBOND 8 CYS A 614 CYS A 646 1555 1555 2.03 SSBOND 9 CYS A 659 CYS A 668 1555 1555 2.03 SSBOND 10 CYS A 735 CYS A 757 1555 1555 2.03 SSBOND 11 CYS A 740 CYS A 746 1555 1555 2.03 SSBOND 12 CYS A 837 CYS A 848 1555 1555 2.03 SSBOND 13 CYS A 1029 CYS A 1040 1555 1555 2.03 SSBOND 14 CYS A 1079 CYS A 1123 1555 1555 2.03 SSBOND 15 CYS B 129 CYS B 161 1555 1555 2.03 SSBOND 16 CYS B 288 CYS B 298 1555 1555 2.03 SSBOND 17 CYS B 333 CYS B 358 1555 1555 2.03 SSBOND 18 CYS B 376 CYS B 429 1555 1555 2.03 SSBOND 19 CYS B 388 CYS B 522 1555 1555 2.03 SSBOND 20 CYS B 477 CYS B 485 1555 1555 2.03 SSBOND 21 CYS B 535 CYS B 587 1555 1555 2.03 SSBOND 22 CYS B 614 CYS B 646 1555 1555 2.03 SSBOND 23 CYS B 659 CYS B 668 1555 1555 2.04 SSBOND 24 CYS B 735 CYS B 757 1555 1555 2.03 SSBOND 25 CYS B 740 CYS B 746 1555 1555 2.03 SSBOND 26 CYS B 837 CYS B 848 1555 1555 2.03 SSBOND 27 CYS B 1029 CYS B 1040 1555 1555 2.03 SSBOND 28 CYS B 1079 CYS B 1123 1555 1555 2.03 SSBOND 29 CYS C 129 CYS C 161 1555 1555 2.03 SSBOND 30 CYS C 288 CYS C 298 1555 1555 2.03 SSBOND 31 CYS C 333 CYS C 358 1555 1555 2.03 SSBOND 32 CYS C 376 CYS C 429 1555 1555 2.03 SSBOND 33 CYS C 388 CYS C 522 1555 1555 2.03 SSBOND 34 CYS C 477 CYS C 485 1555 1555 2.03 SSBOND 35 CYS C 535 CYS C 587 1555 1555 2.03 SSBOND 36 CYS C 614 CYS C 646 1555 1555 2.03 SSBOND 37 CYS C 659 CYS C 668 1555 1555 2.03 SSBOND 38 CYS C 735 CYS C 757 1555 1555 2.03 SSBOND 39 CYS C 740 CYS C 746 1555 1555 2.03 SSBOND 40 CYS C 837 CYS C 848 1555 1555 2.03 SSBOND 41 CYS C 1029 CYS C 1040 1555 1555 2.03 SSBOND 42 CYS C 1079 CYS C 1123 1555 1555 2.03 SSBOND 43 CYS E 23 CYS E 99 1555 1555 2.03 SSBOND 44 CYS E 51 CYS E 107 1555 1555 2.03 SSBOND 45 CYS D 23 CYS D 99 1555 1555 2.03 SSBOND 46 CYS D 51 CYS D 107 1555 1555 2.03 LINK ND2 ASN A 279 C1 NAG A1301 1555 1555 1.44 LINK ND2 ASN A 706 C1 NAG A1302 1555 1555 1.44 LINK ND2 ASN A 714 C1 NAG H 1 1555 1555 1.46 LINK ND2 ASN A 798 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A1095 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A1131 C1 NAG F 1 1555 1555 1.45 LINK ND2 ASN B 120 C1 NAG B1304 1555 1555 1.45 LINK ND2 ASN B 279 C1 NAG B1303 1555 1555 1.45 LINK ND2 ASN B 706 C1 NAG B1302 1555 1555 1.44 LINK ND2 ASN B 714 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN B 798 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN B1071 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN B1095 C1 NAG M 1 1555 1555 1.46 LINK ND2 ASN B1131 C1 NAG B1301 1555 1555 1.45 LINK ND2 ASN C 61 C1 NAG C1302 1555 1555 1.44 LINK ND2 ASN C 279 C1 NAG C1305 1555 1555 1.44 LINK ND2 ASN C 600 C1 NAG C1301 1555 1555 1.44 LINK ND2 ASN C 613 C1 NAG C1303 1555 1555 1.44 LINK ND2 ASN C 654 C1 NAG C1304 1555 1555 1.44 LINK ND2 ASN C 706 C1 NAG C1306 1555 1555 1.44 LINK ND2 ASN C 714 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 798 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C1071 C1 NAG C1308 1555 1555 1.44 LINK ND2 ASN C1095 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C1131 C1 NAG C1307 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.46 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.46 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.46 CISPEP 1 ASN B 798 PHE B 799 0 4.85 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