HEADER VIRAL PROTEIN 05-MAY-23 8OYT TITLE STABILISED BA.1 SARS-COV-2 SPIKE WITH H6 NANOBODIES IN '3 UP' RBD TITLE 2 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, G, F; COMPND 10 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: 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.CORNISH,J.HUO,L.JONES,P.SHARMA,J.W.THRUSH,S.ABDELKARIM, JRNL AUTH 2 A.KIPAR,S.RAMADURAI,M.WECKENER,H.MIKOLAJEK,S.LIU,I.BUCKLE, JRNL AUTH 3 E.BENTLEY,A.KIRBY,X.HAN,S.M.LAIDLAW,M.HILL,L.EYSSEN, JRNL AUTH 4 C.NORMAN,A.LE BAS,J.CLARKE,W.JAMES,J.P.STEWART,M.CARROLL, JRNL AUTH 5 J.H.NAISMITH,R.J.OWENS JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF NANOBODIES JRNL TITL 2 THAT NEUTRALIZE OMICRON VARIANTS OF SARS-COV-2. JRNL REF OPEN BIOLOGY V. 14 30252 2024 JRNL REFN ESSN 2046-2441 JRNL PMID 38835241 JRNL DOI 10.1098/RSOB.230252 REMARK 2 REMARK 2 RESOLUTION. 3.80 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) : 3.800 REMARK 3 NUMBER OF PARTICLES : 104001 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 8OYT 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_1292129585. 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 THREE H6 NANOBODIES; H6 REMARK 245 NANOBODY; STABILISED HEXAPRO REMARK 245 OMICRON BA.1 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, G, F, D, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R 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 HIS A 68A REMARK 465 VAL A 68B REMARK 465 VAL A 140A REMARK 465 TYR A 140B REMARK 465 ASN A 205A 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 HIS B 68A REMARK 465 VAL B 68B REMARK 465 VAL B 140A REMARK 465 TYR B 140B REMARK 465 ASN B 205A 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 VAL B 442 REMARK 465 SER B 443 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 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 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 HIS C 68A REMARK 465 VAL C 68B REMARK 465 VAL C 140A REMARK 465 TYR C 140B REMARK 465 ASN C 205A 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 465 LYS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 HIS E 132 REMARK 465 HIS E 133 REMARK 465 HIS E 134 REMARK 465 LYS G 128 REMARK 465 HIS G 129 REMARK 465 HIS G 130 REMARK 465 HIS G 131 REMARK 465 HIS G 132 REMARK 465 HIS G 133 REMARK 465 HIS G 134 REMARK 465 LYS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 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 B 838 CG CD1 CD2 REMARK 470 ASP B 845 CG OD1 OD2 REMARK 470 LEU B 846 CG CD1 CD2 REMARK 470 ILE B 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 OG SER A 346 O LEU A 449 2.08 REMARK 500 OG1 THR A 29 OD1 ASP A 212 2.09 REMARK 500 OE1 GLN A 52 OG1 THR A 271 2.10 REMARK 500 O HIS B 66 NH2 ARG B 76 2.11 REMARK 500 OG1 THR B 1113 OD1 ASP B 1115 2.13 REMARK 500 OG1 THR B 29 OD1 ASP B 212 2.13 REMARK 500 NH2 ARG B 400 O TYR B 492 2.13 REMARK 500 N PHE C 326 OD1 ASN C 529 2.17 REMARK 500 O THR C 1003 OG1 THR C 1006 2.17 REMARK 500 NH1 ARG A 34 O PRO A 214 2.17 REMARK 500 OG1 THR C 909 OD1 ASN C 911 2.18 REMARK 500 OE1 GLN B 52 OG1 THR B 271 2.19 REMARK 500 OG1 THR B 107 OG1 THR B 112 2.19 REMARK 500 ND2 ASN B 798 O5 NAG L 1 2.19 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 CYS A 740 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 MET A1026 CA - CB - CG ANGL. DEV. = 14.6 DEGREES REMARK 500 MET A1047 CA - CB - CG ANGL. DEV. = 12.4 DEGREES REMARK 500 GLY B 499 C - N - CA ANGL. DEV. = -13.8 DEGREES REMARK 500 CYS B 535 CA - CB - SG ANGL. DEV. = 11.1 DEGREES REMARK 500 LEU B 862 CA - CB - CG ANGL. DEV. = 16.4 DEGREES REMARK 500 LEU B1001 CA - CB - CG ANGL. DEV. = 17.9 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 THR A 20 52.69 -91.90 REMARK 500 PHE A 32 -153.18 60.78 REMARK 500 ASP A 78 51.49 -92.42 REMARK 500 ASN A 85 -107.83 56.44 REMARK 500 ALA A 121 -106.87 54.72 REMARK 500 SER A 146 -94.54 57.19 REMARK 500 TRP A 147 170.78 -59.57 REMARK 500 MET A 148 -70.22 -59.08 REMARK 500 GLU A 149 143.05 -175.65 REMARK 500 ASN A 160 153.70 65.64 REMARK 500 ASN A 180 -4.84 72.32 REMARK 500 ASP A 193 47.80 39.89 REMARK 500 ARG A 243 -174.88 -170.30 REMARK 500 SER A 244 95.00 -66.29 REMARK 500 ILE A 323 -7.09 -53.91 REMARK 500 VAL A 324 -20.11 64.30 REMARK 500 ARG A 325 106.10 62.34 REMARK 500 PRO A 327 6.31 -60.92 REMARK 500 ASN A 328 69.35 62.24 REMARK 500 ASN A 331 66.91 70.75 REMARK 500 GLU A 337 58.57 33.96 REMARK 500 VAL A 338 85.99 69.11 REMARK 500 PHE A 344 167.82 178.82 REMARK 500 ARG A 352 45.79 -85.10 REMARK 500 ASN A 357 52.23 39.54 REMARK 500 PHE A 461 52.50 73.96 REMARK 500 CYS A 477 2.90 -62.77 REMARK 500 VAL A 480 -166.27 62.65 REMARK 500 HIS A 502 -11.89 82.56 REMARK 500 LYS A 526 -131.35 45.92 REMARK 500 SER A 527 -1.78 83.55 REMARK 500 THR A 528 146.65 61.86 REMARK 500 LEU A 530 149.86 172.95 REMARK 500 VAL A 531 126.92 177.47 REMARK 500 ASP A 565 -169.46 -126.95 REMARK 500 LEU A 579 33.82 -89.05 REMARK 500 SER A 602 163.30 60.03 REMARK 500 THR A 627 71.69 59.39 REMARK 500 TYR A 633 -125.60 57.20 REMARK 500 VAL A 726 -54.99 -123.02 REMARK 500 ASP A 742 64.90 60.33 REMARK 500 THR A 824 9.00 -69.43 REMARK 500 PHE A 830 -9.87 70.69 REMARK 500 TYR A 834 -7.52 69.30 REMARK 500 PHE A 852 4.22 -65.18 REMARK 500 PRO A 939 76.41 -66.10 REMARK 500 GLU A1108 81.72 -150.46 REMARK 500 ASP A1124 28.97 -140.71 REMARK 500 ASN A1132 -169.49 -163.43 REMARK 500 PHE B 32 -150.21 61.60 REMARK 500 REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-17295 RELATED DB: EMDB REMARK 900 STABILISED BA.1 SARS-COV-2 SPIKE WITH H6 NANOBODIES IN '3 UP' RBD REMARK 900 CONFORMATION DBREF 8OYT A 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYT A 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYT B 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYT B 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYT C 1 1205 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 8OYT C 1208 1234 UNP P10104 WAC_BPT4 458 484 DBREF 8OYT E 2 134 PDB 8OYT 8OYT 2 134 DBREF 8OYT G 2 134 PDB 8OYT 8OYT 2 134 DBREF 8OYT F 2 134 PDB 8OYT 8OYT 2 134 SEQADV 8OYT VAL A 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYT ILE A 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYT ASP A 140 UNP P0DTC2 GLY 142 VARIANT SEQADV 8OYT A UNP P0DTC2 TYR 144 DELETION SEQADV 8OYT ILE A 206 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYT GLU A 209 UNP P0DTC2 INSERTION SEQADV 8OYT PRO A 210 UNP P0DTC2 INSERTION SEQADV 8OYT GLU A 211 UNP P0DTC2 INSERTION SEQADV 8OYT ASP A 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYT LEU A 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYT PRO A 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYT PHE A 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYT ASN A 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYT LYS A 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYT SER A 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYT ASN A 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYT LYS A 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYT ALA A 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYT LYS A 490 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8OYT SER A 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYT ARG A 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYT TYR A 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYT HIS A 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYT LYS A 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYT GLY A 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYT TYR A 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYT LYS A 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYT HIS A 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYT GLY A 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYT SER A 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYT SER A 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYT LYS A 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYT TYR A 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYT PRO A 814 UNP P0DTC2 PHE 817 CONFLICT SEQADV 8OYT LYS A 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYT PRO A 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYT PRO A 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYT PRO A 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYT HIS A 951 UNP P0DTC2 GLN 954 ENGINEERED MUTATION SEQADV 8OYT LYS A 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYT PHE A 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYT PRO A 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYT PRO A 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYT GLY A 1206 UNP P0DTC2 LINKER SEQADV 8OYT SER A 1207 UNP P0DTC2 LINKER SEQADV 8OYT LEU A 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYT GLY A 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYT ARG A 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYT SER A 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU A 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLU A 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYT VAL A 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU A 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYT PHE A 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLN A 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY A 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYT PRO A 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY A 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS A 1254 UNP P10104 EXPRESSION TAG SEQADV 8OYT VAL B 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYT ILE B 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYT ASP B 140 UNP P0DTC2 GLY 142 VARIANT SEQADV 8OYT B UNP P0DTC2 TYR 144 DELETION SEQADV 8OYT ILE B 206 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYT GLU B 209 UNP P0DTC2 INSERTION SEQADV 8OYT PRO B 210 UNP P0DTC2 INSERTION SEQADV 8OYT GLU B 211 UNP P0DTC2 INSERTION SEQADV 8OYT ASP B 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYT LEU B 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYT PRO B 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYT PHE B 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYT ASN B 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYT LYS B 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYT SER B 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYT ASN B 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYT LYS B 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYT ALA B 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYT LYS B 490 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8OYT SER B 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYT ARG B 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYT TYR B 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYT HIS B 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYT LYS B 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYT GLY B 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYT TYR B 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYT LYS B 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYT HIS B 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYT GLY B 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYT SER B 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYT SER B 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYT LYS B 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYT TYR B 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYT PRO B 814 UNP P0DTC2 PHE 817 CONFLICT SEQADV 8OYT LYS B 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYT PRO B 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYT PRO B 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYT PRO B 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYT HIS B 951 UNP P0DTC2 GLN 954 ENGINEERED MUTATION SEQADV 8OYT LYS B 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYT PHE B 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYT PRO B 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYT PRO B 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYT GLY B 1206 UNP P0DTC2 LINKER SEQADV 8OYT SER B 1207 UNP P0DTC2 LINKER SEQADV 8OYT LEU B 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYT GLY B 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYT ARG B 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYT SER B 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU B 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLU B 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYT VAL B 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU B 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYT PHE B 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLN B 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY B 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYT PRO B 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY B 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS B 1254 UNP P10104 EXPRESSION TAG SEQADV 8OYT VAL C 67 UNP P0DTC2 ALA 67 VARIANT SEQADV 8OYT ILE C 93 UNP P0DTC2 THR 95 VARIANT SEQADV 8OYT ASP C 140 UNP P0DTC2 GLY 142 VARIANT SEQADV 8OYT C UNP P0DTC2 TYR 144 DELETION SEQADV 8OYT ILE C 206 UNP P0DTC2 LEU 212 VARIANT SEQADV 8OYT GLU C 209 UNP P0DTC2 INSERTION SEQADV 8OYT PRO C 210 UNP P0DTC2 INSERTION SEQADV 8OYT GLU C 211 UNP P0DTC2 INSERTION SEQADV 8OYT ASP C 336 UNP P0DTC2 GLY 339 VARIANT SEQADV 8OYT LEU C 368 UNP P0DTC2 SER 371 VARIANT SEQADV 8OYT PRO C 370 UNP P0DTC2 SER 373 VARIANT SEQADV 8OYT PHE C 372 UNP P0DTC2 SER 375 VARIANT SEQADV 8OYT ASN C 414 UNP P0DTC2 LYS 417 VARIANT SEQADV 8OYT LYS C 437 UNP P0DTC2 ASN 440 VARIANT SEQADV 8OYT SER C 443 UNP P0DTC2 GLY 446 VARIANT SEQADV 8OYT ASN C 474 UNP P0DTC2 SER 477 VARIANT SEQADV 8OYT LYS C 475 UNP P0DTC2 THR 478 VARIANT SEQADV 8OYT ALA C 481 UNP P0DTC2 GLU 484 VARIANT SEQADV 8OYT LYS C 490 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8OYT SER C 493 UNP P0DTC2 GLY 496 VARIANT SEQADV 8OYT ARG C 495 UNP P0DTC2 GLN 498 VARIANT SEQADV 8OYT TYR C 498 UNP P0DTC2 ASN 501 VARIANT SEQADV 8OYT HIS C 502 UNP P0DTC2 TYR 505 VARIANT SEQADV 8OYT LYS C 544 UNP P0DTC2 THR 547 VARIANT SEQADV 8OYT GLY C 611 UNP P0DTC2 ASP 614 VARIANT SEQADV 8OYT TYR C 652 UNP P0DTC2 HIS 655 VARIANT SEQADV 8OYT LYS C 676 UNP P0DTC2 ASN 679 VARIANT SEQADV 8OYT HIS C 678 UNP P0DTC2 PRO 681 VARIANT SEQADV 8OYT GLY C 679 UNP P0DTC2 ARG 682 ENGINEERED MUTATION SEQADV 8OYT SER C 680 UNP P0DTC2 ARG 683 ENGINEERED MUTATION SEQADV 8OYT SER C 682 UNP P0DTC2 ARG 685 ENGINEERED MUTATION SEQADV 8OYT LYS C 761 UNP P0DTC2 ASN 764 VARIANT SEQADV 8OYT TYR C 793 UNP P0DTC2 ASP 796 VARIANT SEQADV 8OYT PRO C 814 UNP P0DTC2 PHE 817 CONFLICT SEQADV 8OYT LYS C 853 UNP P0DTC2 ASN 856 VARIANT SEQADV 8OYT PRO C 889 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 8OYT PRO C 896 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 8OYT PRO C 939 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 8OYT HIS C 951 UNP P0DTC2 GLN 954 ENGINEERED MUTATION SEQADV 8OYT LYS C 966 UNP P0DTC2 ASN 969 VARIANT SEQADV 8OYT PHE C 978 UNP P0DTC2 LEU 981 VARIANT SEQADV 8OYT PRO C 983 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 8OYT PRO C 984 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 8OYT GLY C 1206 UNP P0DTC2 LINKER SEQADV 8OYT SER C 1207 UNP P0DTC2 LINKER SEQADV 8OYT LEU C 1229 UNP P10104 PHE 479 ENGINEERED MUTATION SEQADV 8OYT GLY C 1235 UNP P10104 EXPRESSION TAG SEQADV 8OYT ARG C 1236 UNP P10104 EXPRESSION TAG SEQADV 8OYT SER C 1237 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU C 1238 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLU C 1239 UNP P10104 EXPRESSION TAG SEQADV 8OYT VAL C 1240 UNP P10104 EXPRESSION TAG SEQADV 8OYT LEU C 1241 UNP P10104 EXPRESSION TAG SEQADV 8OYT PHE C 1242 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLN C 1243 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY C 1244 UNP P10104 EXPRESSION TAG SEQADV 8OYT PRO C 1245 UNP P10104 EXPRESSION TAG SEQADV 8OYT GLY C 1246 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1247 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1248 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1249 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1250 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1251 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1252 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1253 UNP P10104 EXPRESSION TAG SEQADV 8OYT HIS C 1254 UNP P10104 EXPRESSION TAG SEQRES 1 A 1259 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 A 1259 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 A 1259 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 A 1259 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 A 1259 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 A 1259 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 7 A 1259 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 8 A 1259 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 9 A 1259 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 10 A 1259 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 11 A 1259 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 12 A 1259 TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU PHE SEQRES 13 A 1259 ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU TYR SEQRES 14 A 1259 VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS GLN SEQRES 15 A 1259 GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS ASN SEQRES 16 A 1259 ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR PRO SEQRES 17 A 1259 ILE ASN ILE VAL ARG GLU PRO GLU ASP LEU PRO GLN GLY SEQRES 18 A 1259 PHE SER ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY SEQRES 19 A 1259 ILE ASN ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS SEQRES 20 A 1259 ARG SER TYR LEU THR PRO GLY ASP SER SER SER GLY TRP SEQRES 21 A 1259 THR ALA GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN SEQRES 22 A 1259 PRO ARG THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR SEQRES 23 A 1259 ILE THR ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER SEQRES 24 A 1259 GLU THR LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS SEQRES 25 A 1259 GLY ILE TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR SEQRES 26 A 1259 GLU SER ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS SEQRES 27 A 1259 PRO PHE ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER SEQRES 28 A 1259 VAL TYR ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL SEQRES 29 A 1259 ALA ASP TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE SEQRES 30 A 1259 THR PHE LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN SEQRES 31 A 1259 ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL SEQRES 32 A 1259 ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN SEQRES 33 A 1259 THR GLY ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP SEQRES 34 A 1259 ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS SEQRES 35 A 1259 LEU ASP SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR SEQRES 36 A 1259 ARG LEU PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG SEQRES 37 A 1259 ASP ILE SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO SEQRES 38 A 1259 CYS ASN GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU SEQRES 39 A 1259 LYS SER TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS SEQRES 40 A 1259 GLN PRO TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU SEQRES 41 A 1259 HIS ALA PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR SEQRES 42 A 1259 ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN SEQRES 43 A 1259 GLY LEU LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS SEQRES 44 A 1259 LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA SEQRES 45 A 1259 ASP THR THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU SEQRES 46 A 1259 ILE LEU ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER SEQRES 47 A 1259 VAL ILE THR PRO GLY THR ASN THR SER ASN GLN VAL ALA SEQRES 48 A 1259 VAL LEU TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL SEQRES 49 A 1259 ALA ILE HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL SEQRES 50 A 1259 TYR SER THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY SEQRES 51 A 1259 CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU SEQRES 52 A 1259 CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR SEQRES 53 A 1259 GLN THR GLN THR LYS SER HIS GLY SER ALA SER SER VAL SEQRES 54 A 1259 ALA SER GLN SER ILE ILE ALA TYR THR MET SER LEU GLY SEQRES 55 A 1259 ALA GLU ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA SEQRES 56 A 1259 ILE PRO THR ASN PHE THR ILE SER VAL THR THR GLU ILE SEQRES 57 A 1259 LEU PRO VAL SER MET THR LYS THR SER VAL ASP CYS THR SEQRES 58 A 1259 MET TYR ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU SEQRES 59 A 1259 LEU LEU GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG SEQRES 60 A 1259 ALA LEU THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR SEQRES 61 A 1259 GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR SEQRES 62 A 1259 PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN SEQRES 63 A 1259 ILE LEU PRO ASP PRO SER LYS PRO SER LYS ARG SER PRO SEQRES 64 A 1259 ILE GLU ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP SEQRES 65 A 1259 ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP SEQRES 66 A 1259 ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS SEQRES 67 A 1259 GLY LEU THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET SEQRES 68 A 1259 ILE ALA GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE SEQRES 69 A 1259 THR SER GLY TRP THR PHE GLY ALA GLY PRO ALA LEU GLN SEQRES 70 A 1259 ILE PRO PHE PRO MET GLN MET ALA TYR ARG PHE ASN GLY SEQRES 71 A 1259 ILE GLY VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS SEQRES 72 A 1259 LEU ILE ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE SEQRES 73 A 1259 GLN ASP SER LEU SER SER THR PRO SER ALA LEU GLY LYS SEQRES 74 A 1259 LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN SEQRES 75 A 1259 THR LEU VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SEQRES 76 A 1259 SER SER VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO SEQRES 77 A 1259 PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY SEQRES 78 A 1259 ARG LEU GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU SEQRES 79 A 1259 ILE ARG ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA SEQRES 80 A 1259 ALA THR LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS SEQRES 81 A 1259 ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER SEQRES 82 A 1259 PHE PRO GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS SEQRES 83 A 1259 VAL THR TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR SEQRES 84 A 1259 ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO SEQRES 85 A 1259 ARG GLU GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE SEQRES 86 A 1259 VAL THR GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR SEQRES 87 A 1259 THR ASP ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL SEQRES 88 A 1259 ILE GLY ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN SEQRES 89 A 1259 PRO GLU LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR SEQRES 90 A 1259 PHE LYS ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP SEQRES 91 A 1259 ILE SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS SEQRES 92 A 1259 GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN SEQRES 93 A 1259 GLU SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU SEQRES 94 A 1259 GLN GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 95 A 1259 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 96 A 1259 SER THR PHE LEU GLY ARG SER LEU GLU VAL LEU PHE GLN SEQRES 97 A 1259 GLY PRO GLY HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 B 1259 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 B 1259 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 B 1259 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 B 1259 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 B 1259 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 B 1259 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 7 B 1259 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 8 B 1259 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 9 B 1259 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 10 B 1259 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 11 B 1259 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 12 B 1259 TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU PHE SEQRES 13 B 1259 ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU TYR SEQRES 14 B 1259 VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS GLN SEQRES 15 B 1259 GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS ASN SEQRES 16 B 1259 ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR PRO SEQRES 17 B 1259 ILE ASN ILE VAL ARG GLU PRO GLU ASP LEU PRO GLN GLY SEQRES 18 B 1259 PHE SER ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY SEQRES 19 B 1259 ILE ASN ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS SEQRES 20 B 1259 ARG SER TYR LEU THR PRO GLY ASP SER SER SER GLY TRP SEQRES 21 B 1259 THR ALA GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN SEQRES 22 B 1259 PRO ARG THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR SEQRES 23 B 1259 ILE THR ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER SEQRES 24 B 1259 GLU THR LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS SEQRES 25 B 1259 GLY ILE TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR SEQRES 26 B 1259 GLU SER ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS SEQRES 27 B 1259 PRO PHE ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER SEQRES 28 B 1259 VAL TYR ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL SEQRES 29 B 1259 ALA ASP TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE SEQRES 30 B 1259 THR PHE LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN SEQRES 31 B 1259 ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL SEQRES 32 B 1259 ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN SEQRES 33 B 1259 THR GLY ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP SEQRES 34 B 1259 ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS SEQRES 35 B 1259 LEU ASP SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR SEQRES 36 B 1259 ARG LEU PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG SEQRES 37 B 1259 ASP ILE SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO SEQRES 38 B 1259 CYS ASN GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU SEQRES 39 B 1259 LYS SER TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS SEQRES 40 B 1259 GLN PRO TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU SEQRES 41 B 1259 HIS ALA PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR SEQRES 42 B 1259 ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN SEQRES 43 B 1259 GLY LEU LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS SEQRES 44 B 1259 LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA SEQRES 45 B 1259 ASP THR THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU SEQRES 46 B 1259 ILE LEU ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER SEQRES 47 B 1259 VAL ILE THR PRO GLY THR ASN THR SER ASN GLN VAL ALA SEQRES 48 B 1259 VAL LEU TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL SEQRES 49 B 1259 ALA ILE HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL SEQRES 50 B 1259 TYR SER THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY SEQRES 51 B 1259 CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU SEQRES 52 B 1259 CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR SEQRES 53 B 1259 GLN THR GLN THR LYS SER HIS GLY SER ALA SER SER VAL SEQRES 54 B 1259 ALA SER GLN SER ILE ILE ALA TYR THR MET SER LEU GLY SEQRES 55 B 1259 ALA GLU ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA SEQRES 56 B 1259 ILE PRO THR ASN PHE THR ILE SER VAL THR THR GLU ILE SEQRES 57 B 1259 LEU PRO VAL SER MET THR LYS THR SER VAL ASP CYS THR SEQRES 58 B 1259 MET TYR ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU SEQRES 59 B 1259 LEU LEU GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG SEQRES 60 B 1259 ALA LEU THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR SEQRES 61 B 1259 GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR SEQRES 62 B 1259 PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN SEQRES 63 B 1259 ILE LEU PRO ASP PRO SER LYS PRO SER LYS ARG SER PRO SEQRES 64 B 1259 ILE GLU ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP SEQRES 65 B 1259 ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP SEQRES 66 B 1259 ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS SEQRES 67 B 1259 GLY LEU THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET SEQRES 68 B 1259 ILE ALA GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE SEQRES 69 B 1259 THR SER GLY TRP THR PHE GLY ALA GLY PRO ALA LEU GLN SEQRES 70 B 1259 ILE PRO PHE PRO MET GLN MET ALA TYR ARG PHE ASN GLY SEQRES 71 B 1259 ILE GLY VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS SEQRES 72 B 1259 LEU ILE ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE SEQRES 73 B 1259 GLN ASP SER LEU SER SER THR PRO SER ALA LEU GLY LYS SEQRES 74 B 1259 LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN SEQRES 75 B 1259 THR LEU VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SEQRES 76 B 1259 SER SER VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO SEQRES 77 B 1259 PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY SEQRES 78 B 1259 ARG LEU GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU SEQRES 79 B 1259 ILE ARG ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA SEQRES 80 B 1259 ALA THR LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS SEQRES 81 B 1259 ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER SEQRES 82 B 1259 PHE PRO GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS SEQRES 83 B 1259 VAL THR TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR SEQRES 84 B 1259 ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO SEQRES 85 B 1259 ARG GLU GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE SEQRES 86 B 1259 VAL THR GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR SEQRES 87 B 1259 THR ASP ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL SEQRES 88 B 1259 ILE GLY ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN SEQRES 89 B 1259 PRO GLU LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR SEQRES 90 B 1259 PHE LYS ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP SEQRES 91 B 1259 ILE SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS SEQRES 92 B 1259 GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN SEQRES 93 B 1259 GLU SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU SEQRES 94 B 1259 GLN GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 95 B 1259 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 96 B 1259 SER THR PHE LEU GLY ARG SER LEU GLU VAL LEU PHE GLN SEQRES 97 B 1259 GLY PRO GLY HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 C 1259 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 C 1259 GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO SEQRES 3 C 1259 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 4 C 1259 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 5 C 1259 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 6 C 1259 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 7 C 1259 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 8 C 1259 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 9 C 1259 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 10 C 1259 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 11 C 1259 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 12 C 1259 TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU PHE SEQRES 13 C 1259 ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU TYR SEQRES 14 C 1259 VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS GLN SEQRES 15 C 1259 GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS ASN SEQRES 16 C 1259 ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR PRO SEQRES 17 C 1259 ILE ASN ILE VAL ARG GLU PRO GLU ASP LEU PRO GLN GLY SEQRES 18 C 1259 PHE SER ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY SEQRES 19 C 1259 ILE ASN ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS SEQRES 20 C 1259 ARG SER TYR LEU THR PRO GLY ASP SER SER SER GLY TRP SEQRES 21 C 1259 THR ALA GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN SEQRES 22 C 1259 PRO ARG THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR SEQRES 23 C 1259 ILE THR ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER SEQRES 24 C 1259 GLU THR LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS SEQRES 25 C 1259 GLY ILE TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR SEQRES 26 C 1259 GLU SER ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS SEQRES 27 C 1259 PRO PHE ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER SEQRES 28 C 1259 VAL TYR ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL SEQRES 29 C 1259 ALA ASP TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE SEQRES 30 C 1259 THR PHE LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN SEQRES 31 C 1259 ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL SEQRES 32 C 1259 ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN SEQRES 33 C 1259 THR GLY ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP SEQRES 34 C 1259 ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS SEQRES 35 C 1259 LEU ASP SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR SEQRES 36 C 1259 ARG LEU PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG SEQRES 37 C 1259 ASP ILE SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO SEQRES 38 C 1259 CYS ASN GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU SEQRES 39 C 1259 LYS SER TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS SEQRES 40 C 1259 GLN PRO TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU SEQRES 41 C 1259 HIS ALA PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR SEQRES 42 C 1259 ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN SEQRES 43 C 1259 GLY LEU LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS SEQRES 44 C 1259 LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA SEQRES 45 C 1259 ASP THR THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU SEQRES 46 C 1259 ILE LEU ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER SEQRES 47 C 1259 VAL ILE THR PRO GLY THR ASN THR SER ASN GLN VAL ALA SEQRES 48 C 1259 VAL LEU TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL SEQRES 49 C 1259 ALA ILE HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL SEQRES 50 C 1259 TYR SER THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY SEQRES 51 C 1259 CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU SEQRES 52 C 1259 CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR SEQRES 53 C 1259 GLN THR GLN THR LYS SER HIS GLY SER ALA SER SER VAL SEQRES 54 C 1259 ALA SER GLN SER ILE ILE ALA TYR THR MET SER LEU GLY SEQRES 55 C 1259 ALA GLU ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA SEQRES 56 C 1259 ILE PRO THR ASN PHE THR ILE SER VAL THR THR GLU ILE SEQRES 57 C 1259 LEU PRO VAL SER MET THR LYS THR SER VAL ASP CYS THR SEQRES 58 C 1259 MET TYR ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU SEQRES 59 C 1259 LEU LEU GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG SEQRES 60 C 1259 ALA LEU THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR SEQRES 61 C 1259 GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR SEQRES 62 C 1259 PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN SEQRES 63 C 1259 ILE LEU PRO ASP PRO SER LYS PRO SER LYS ARG SER PRO SEQRES 64 C 1259 ILE GLU ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP SEQRES 65 C 1259 ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP SEQRES 66 C 1259 ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS SEQRES 67 C 1259 GLY LEU THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET SEQRES 68 C 1259 ILE ALA GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE SEQRES 69 C 1259 THR SER GLY TRP THR PHE GLY ALA GLY PRO ALA LEU GLN SEQRES 70 C 1259 ILE PRO PHE PRO MET GLN MET ALA TYR ARG PHE ASN GLY SEQRES 71 C 1259 ILE GLY VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS SEQRES 72 C 1259 LEU ILE ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE SEQRES 73 C 1259 GLN ASP SER LEU SER SER THR PRO SER ALA LEU GLY LYS SEQRES 74 C 1259 LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN SEQRES 75 C 1259 THR LEU VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SEQRES 76 C 1259 SER SER VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO SEQRES 77 C 1259 PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY SEQRES 78 C 1259 ARG LEU GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU SEQRES 79 C 1259 ILE ARG ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA SEQRES 80 C 1259 ALA THR LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS SEQRES 81 C 1259 ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER SEQRES 82 C 1259 PHE PRO GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS SEQRES 83 C 1259 VAL THR TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR SEQRES 84 C 1259 ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO SEQRES 85 C 1259 ARG GLU GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE SEQRES 86 C 1259 VAL THR GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR SEQRES 87 C 1259 THR ASP ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL SEQRES 88 C 1259 ILE GLY ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN SEQRES 89 C 1259 PRO GLU LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR SEQRES 90 C 1259 PHE LYS ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP SEQRES 91 C 1259 ILE SER GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS SEQRES 92 C 1259 GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN SEQRES 93 C 1259 GLU SER LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU SEQRES 94 C 1259 GLN GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 95 C 1259 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 96 C 1259 SER THR PHE LEU GLY ARG SER LEU GLU VAL LEU PHE GLN SEQRES 97 C 1259 GLY PRO GLY HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 E 133 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 133 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3 E 133 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4 E 133 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 E 133 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6 E 133 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7 E 133 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8 E 133 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9 E 133 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10 E 133 GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS SEQRES 11 E 133 HIS HIS HIS SEQRES 1 G 133 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 133 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3 G 133 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4 G 133 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 G 133 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6 G 133 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7 G 133 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8 G 133 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9 G 133 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10 G 133 GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS SEQRES 11 G 133 HIS HIS HIS SEQRES 1 F 133 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 133 PRO GLY GLY SER LEU THR LEU SER CYS VAL ALA SER GLU SEQRES 3 F 133 SER SER LEU ALA PRO TYR ARG VAL ALA TRP PHE ARG GLN SEQRES 4 F 133 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 F 133 ARG ASP ALA HIS PRO THR SER THR TYR TYR THR ALA SER SEQRES 6 F 133 VAL LYS GLY ARG PHE THR MET SER ARG ASP ASN ALA LYS SEQRES 7 F 133 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO SER SEQRES 8 F 133 ASP THR ALA VAL TYR TYR CYS ALA THR ASP LEU GLY GLY SEQRES 9 F 133 TYR CYS SER ASP SER ASN TYR PRO ARG ALA TRP TRP GLY SEQRES 10 F 133 GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS SEQRES 11 F 133 HIS HIS HIS HET NAG A1301 14 HET NAG A1302 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 D 1 14 HET NAG D 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 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 7 NAG 33(C8 H15 N O6) HELIX 1 AA1 SER A 69 GLY A 73 5 5 HELIX 2 AA2 GLU A 149 ARG A 153 5 5 HELIX 3 AA3 ASP A 291 LYS A 301 1 11 HELIX 4 AA4 TYR A 362 LEU A 368 1 7 HELIX 5 AA5 SER A 380 ASN A 385 1 6 HELIX 6 AA6 GLU A 403 ALA A 408 1 6 HELIX 7 AA7 SER A 435 SER A 440 1 6 HELIX 8 AA8 ARG A 495 GLY A 499 5 5 HELIX 9 AA9 ASN A 539 LEU A 543 5 5 HELIX 10 AB1 ASP A 734 CYS A 740 1 7 HELIX 11 AB2 SER A 743 GLN A 752 1 10 HELIX 12 AB3 CYS A 757 ALA A 780 1 24 HELIX 13 AB4 SER A 813 THR A 824 1 12 HELIX 14 AB5 LEU A 846 PHE A 852 1 7 HELIX 15 AB6 THR A 863 SER A 881 1 19 HELIX 16 AB7 PRO A 894 GLY A 905 1 12 HELIX 17 AB8 THR A 909 SER A 937 1 29 HELIX 18 AB9 LEU A 942 GLN A 962 1 21 HELIX 19 AC1 LEU A 963 SER A 965 5 3 HELIX 20 AC2 VAL A 973 LEU A 981 1 9 HELIX 21 AC3 ASP A 982 VAL A 1030 1 49 HELIX 22 AC4 ASP B 291 LYS B 301 1 11 HELIX 23 AC5 PHE B 335 ASN B 340 1 6 HELIX 24 AC6 TYR B 362 LEU B 368 1 7 HELIX 25 AC7 SER B 380 LEU B 384 5 5 HELIX 26 AC8 VAL B 404 ALA B 408 5 5 HELIX 27 AC9 GLY B 413 ASN B 419 1 7 HELIX 28 AD1 PRO B 618 HIS B 622 5 5 HELIX 29 AD2 ASP B 734 CYS B 740 1 7 HELIX 30 AD3 SER B 743 GLN B 752 1 10 HELIX 31 AD4 CYS B 757 ALA B 780 1 24 HELIX 32 AD5 SER B 813 THR B 824 1 12 HELIX 33 AD6 LEU B 846 LYS B 853 1 8 HELIX 34 AD7 THR B 863 GLY B 882 1 20 HELIX 35 AD8 TRP B 883 ALA B 887 5 5 HELIX 36 AD9 PRO B 894 GLY B 905 1 12 HELIX 37 AE1 THR B 909 SER B 937 1 29 HELIX 38 AE2 LEU B 942 GLN B 962 1 21 HELIX 39 AE3 LEU B 963 SER B 965 5 3 HELIX 40 AE4 VAL B 973 ARG B 980 1 8 HELIX 41 AE5 ASP B 982 VAL B 1030 1 49 HELIX 42 AE6 SER C 69 GLY C 73 5 5 HELIX 43 AE7 ASP C 291 LYS C 301 1 11 HELIX 44 AE8 PHE C 335 ASN C 340 1 6 HELIX 45 AE9 TYR C 362 LEU C 368 1 7 HELIX 46 AF1 GLU C 403 ALA C 408 1 6 HELIX 47 AF2 SER C 435 SER C 440 1 6 HELIX 48 AF3 ASN C 539 LEU C 543 5 5 HELIX 49 AF4 ALA C 620 ASP C 624 5 5 HELIX 50 AF5 ASP C 734 CYS C 740 1 7 HELIX 51 AF6 SER C 743 GLN C 752 1 10 HELIX 52 AF7 CYS C 757 ALA C 780 1 24 HELIX 53 AF8 SER C 813 THR C 824 1 12 HELIX 54 AF9 LEU C 846 PHE C 852 1 7 HELIX 55 AG1 THR C 863 GLY C 882 1 20 HELIX 56 AG2 TRP C 883 ALA C 887 5 5 HELIX 57 AG3 PRO C 894 GLY C 905 1 12 HELIX 58 AG4 THR C 909 SER C 937 1 29 HELIX 59 AG5 LEU C 942 GLN C 962 1 21 HELIX 60 AG6 LEU C 963 SER C 965 5 3 HELIX 61 AG7 VAL C 973 ARG C 980 1 8 HELIX 62 AG8 ASP C 982 VAL C 1030 1 49 HELIX 63 AG9 ALA E 65 LYS E 68 5 4 HELIX 64 AH1 LYS E 90 THR E 94 5 5 HELIX 65 AH2 ALA G 65 LYS G 68 5 4 HELIX 66 AH3 LYS G 90 THR G 94 5 5 HELIX 67 AH4 ALA F 65 LYS F 68 5 4 HELIX 68 AH5 LYS F 90 THR F 94 5 5 SHEET 1 AA1 2 THR A 29 ASN A 30 0 SHEET 2 AA1 2 ASN A 61 VAL A 62 -1 O VAL A 62 N THR A 29 SHEET 1 AA2 4 VAL A 36 TYR A 37 0 SHEET 2 AA2 4 ALA A 219 LEU A 226 1 O LEU A 220 N VAL A 36 SHEET 3 AA2 4 TYR A 195 LYS A 201 -1 N ILE A 198 O LEU A 223 SHEET 4 AA2 4 GLU A 186 ILE A 192 -1 N LYS A 190 O LYS A 197 SHEET 1 AA3 3 LEU A 48 PHE A 55 0 SHEET 2 AA3 3 GLN A 268 TYR A 276 -1 O LEU A 274 N HIS A 49 SHEET 3 AA3 3 ILE A 282 ASP A 287 -1 O VAL A 286 N LEU A 273 SHEET 1 AA4 3 HIS A 66 VAL A 67 0 SHEET 2 AA4 3 ALA A 260 TYR A 263 -1 O ALA A 260 N VAL A 67 SHEET 3 AA4 3 ALA A 91 SER A 92 -1 N ALA A 91 O TYR A 263 SHEET 1 AA5 2 LEU A 82 PRO A 83 0 SHEET 2 AA5 2 ARG A 234 PHE A 235 -1 O PHE A 235 N LEU A 82 SHEET 1 AA6 2 ILE A 99 ARG A 100 0 SHEET 2 AA6 2 LEU A 238 LEU A 239 -1 O LEU A 238 N ARG A 100 SHEET 1 AA7 4 PHE A 104 GLY A 105 0 SHEET 2 AA7 4 GLN A 113 LEU A 116 -1 O LEU A 115 N PHE A 104 SHEET 3 AA7 4 ILE A 126 PHE A 133 -1 N LYS A 127 O LEU A 116 SHEET 4 AA7 4 TYR A 155 TYR A 165 -1 O TYR A 165 N ILE A 126 SHEET 1 AA8 5 GLY A 308 ARG A 316 0 SHEET 2 AA8 5 PHE A 589 THR A 596 -1 O VAL A 594 N TYR A 310 SHEET 3 AA8 5 ALA A 606 GLN A 610 -1 O LEU A 608 N SER A 593 SHEET 4 AA8 5 GLY A 645 ILE A 648 -1 O CYS A 646 N TYR A 609 SHEET 5 AA8 5 VAL A 639 GLN A 641 -1 N PHE A 640 O LEU A 647 SHEET 1 AA9 2 ARG A 354 ILE A 355 0 SHEET 2 AA9 2 VAL A 392 TYR A 393 -1 O VAL A 392 N ILE A 355 SHEET 1 AB1 3 VAL A 398 ILE A 399 0 SHEET 2 AB1 3 TYR A 505 VAL A 509 -1 O TYR A 505 N ILE A 399 SHEET 3 AB1 3 VAL A 430 TRP A 433 -1 N ILE A 431 O VAL A 508 SHEET 1 AB2 5 CYS A 535 ASN A 537 0 SHEET 2 AB2 5 THR A 546 GLU A 551 -1 O GLY A 547 N VAL A 536 SHEET 3 AB2 5 ILE A 581 THR A 585 -1 O THR A 585 N VAL A 548 SHEET 4 AB2 5 THR A 570 ARG A 574 -1 N VAL A 573 O LEU A 582 SHEET 5 AB2 5 GLY A 563 ARG A 564 -1 N GLY A 563 O ASP A 571 SHEET 1 AB3 4 GLU A 651 TYR A 652 0 SHEET 2 AB3 4 SER A 688 THR A 693 1 O ALA A 691 N GLU A 651 SHEET 3 AB3 4 ILE A 667 GLN A 672 -1 N SER A 670 O ILE A 690 SHEET 4 AB3 4 ILE A 661 GLY A 664 -1 N ILE A 663 O ILE A 667 SHEET 1 AB4 2 ALA A 698 GLU A 699 0 SHEET 2 AB4 2 GLN B 784 ILE B 785 1 O ILE B 785 N ALA A 698 SHEET 1 AB5 3 SER A 708 PRO A 725 0 SHEET 2 AB5 3 GLY A1056 THR A1074 -1 O HIS A1061 N THR A 720 SHEET 3 AB5 3 TYR A1044 ALA A1053 -1 N GLN A1051 O VAL A1058 SHEET 1 AB6 5 SER A 708 PRO A 725 0 SHEET 2 AB6 5 GLY A1056 THR A1074 -1 O HIS A1061 N THR A 720 SHEET 3 AB6 5 VAL A1091 SER A1094 -1 O SER A1094 N THR A1073 SHEET 4 AB6 5 PHE A1100 THR A1102 -1 O THR A1102 N VAL A1091 SHEET 5 AB6 5 GLN A1110 ILE A1111 -1 O GLN A1110 N VAL A1101 SHEET 1 AB7 2 LYS A 730 SER A 732 0 SHEET 2 AB7 2 THR A 856 LEU A 858 -1 O LEU A 858 N LYS A 730 SHEET 1 AB8 2 GLN A 784 ILE A 785 0 SHEET 2 AB8 2 ALA C 698 GLU C 699 1 O ALA C 698 N ILE A 785 SHEET 1 AB9 4 THR A1117 VAL A1119 0 SHEET 2 AB9 4 ALA A1084 PRO A1087 -1 N PHE A1086 O PHE A1118 SHEET 3 AB9 4 ILE A1078 CYS A1079 -1 N ILE A1078 O HIS A1085 SHEET 4 AB9 4 VAL A1130 ASN A1131 1 O VAL A1130 N CYS A1079 SHEET 1 AC1 2 THR B 29 ASN B 30 0 SHEET 2 AC1 2 ASN B 61 VAL B 62 -1 O VAL B 62 N THR B 29 SHEET 1 AC2 3 LEU B 48 PHE B 55 0 SHEET 2 AC2 3 GLN B 268 TYR B 276 -1 O LEU B 274 N HIS B 49 SHEET 3 AC2 3 ILE B 282 ASP B 287 -1 O VAL B 286 N LEU B 273 SHEET 1 AC3 3 HIS B 66 VAL B 67 0 SHEET 2 AC3 3 ALA B 260 TYR B 263 -1 O ALA B 260 N VAL B 67 SHEET 3 AC3 3 ALA B 91 SER B 92 -1 N ALA B 91 O TYR B 263 SHEET 1 AC4 2 LEU B 82 PRO B 83 0 SHEET 2 AC4 2 ARG B 234 PHE B 235 -1 O PHE B 235 N LEU B 82 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 3 GLU B 186 ILE B 192 0 SHEET 2 AC6 3 TYR B 195 LYS B 201 -1 O TYR B 195 N ILE B 192 SHEET 3 AC6 3 GLU B 221 LEU B 226 -1 O LEU B 223 N ILE B 198 SHEET 1 AC7 5 GLY B 308 ARG B 316 0 SHEET 2 AC7 5 PHE B 589 THR B 596 -1 O THR B 596 N GLY B 308 SHEET 3 AC7 5 ALA B 606 GLN B 610 -1 O ALA B 606 N ILE B 595 SHEET 4 AC7 5 GLY B 645 ILE B 648 -1 O CYS B 646 N TYR B 609 SHEET 5 AC7 5 PHE B 640 THR B 642 -1 N THR B 642 O GLY B 645 SHEET 1 AC8 4 LYS B 353 ARG B 354 0 SHEET 2 AC8 4 TYR B 393 PHE B 397 -1 O ALA B 394 N LYS B 353 SHEET 3 AC8 4 VAL B 507 VAL B 509 -1 O VAL B 507 N PHE B 397 SHEET 4 AC8 4 VAL B 430 ALA B 432 -1 N ILE B 431 O VAL B 508 SHEET 1 AC9 4 CYS B 535 PHE B 540 0 SHEET 2 AC9 4 LEU B 543 GLU B 551 -1 O GLY B 545 N PHE B 538 SHEET 3 AC9 4 LEU B 582 THR B 585 -1 O ASP B 583 N THR B 550 SHEET 4 AC9 4 ALA B 572 VAL B 573 -1 N VAL B 573 O LEU B 582 SHEET 1 AD1 4 GLU B 651 TYR B 652 0 SHEET 2 AD1 4 SER B 688 THR B 693 1 O ALA B 691 N GLU B 651 SHEET 3 AD1 4 ILE B 667 GLN B 672 -1 N SER B 670 O ILE B 690 SHEET 4 AD1 4 PRO B 662 GLY B 664 -1 N ILE B 663 O ILE B 667 SHEET 1 AD2 2 ALA B 698 GLU B 699 0 SHEET 2 AD2 2 GLN C 784 ILE C 785 1 O ILE C 785 N ALA B 698 SHEET 1 AD3 3 ILE B 709 PRO B 725 0 SHEET 2 AD3 3 GLY B1056 ALA B1075 -1 O ALA B1067 N ASN B 714 SHEET 3 AD3 3 TYR B1044 ALA B1053 -1 N GLN B1051 O VAL B1058 SHEET 1 AD4 4 ILE B 709 PRO B 725 0 SHEET 2 AD4 4 GLY B1056 ALA B1075 -1 O ALA B1067 N ASN B 714 SHEET 3 AD4 4 VAL B1091 SER B1094 -1 O SER B1094 N THR B1073 SHEET 4 AD4 4 TRP B1099 THR B1102 -1 O PHE B1100 N VAL B1093 SHEET 1 AD5 2 LYS B 730 SER B 732 0 SHEET 2 AD5 2 THR B 856 LEU B 858 -1 O LEU B 858 N LYS B 730 SHEET 1 AD6 4 THR B1117 VAL B1119 0 SHEET 2 AD6 4 ALA B1084 PRO B1087 -1 N PHE B1086 O PHE B1118 SHEET 3 AD6 4 ILE B1078 CYS B1079 -1 N ILE B1078 O HIS B1085 SHEET 4 AD6 4 VAL B1130 ASN B1131 1 O VAL B1130 N CYS B1079 SHEET 1 AD7 2 THR C 29 ASN C 30 0 SHEET 2 AD7 2 ASN C 61 VAL C 62 -1 O VAL C 62 N THR C 29 SHEET 1 AD8 3 LEU C 48 PHE C 55 0 SHEET 2 AD8 3 GLN C 268 TYR C 276 -1 O LEU C 274 N HIS C 49 SHEET 3 AD8 3 ILE C 282 ASP C 287 -1 O VAL C 286 N LEU C 273 SHEET 1 AD9 3 HIS C 66 VAL C 67 0 SHEET 2 AD9 3 ALA C 260 TYR C 263 -1 O ALA C 260 N VAL C 67 SHEET 3 AD9 3 ALA C 91 SER C 92 -1 N ALA C 91 O TYR C 263 SHEET 1 AE1 3 GLN C 113 SER C 114 0 SHEET 2 AE1 3 ILE C 126 PHE C 133 -1 O CYS C 129 N SER C 114 SHEET 3 AE1 3 TYR C 155 TYR C 165 -1 O TYR C 165 N ILE C 126 SHEET 1 AE2 3 GLU C 186 ILE C 192 0 SHEET 2 AE2 3 TYR C 195 LYS C 201 -1 O LYS C 197 N LYS C 190 SHEET 3 AE2 3 GLU C 221 LEU C 226 -1 O LEU C 223 N ILE C 198 SHEET 1 AE3 5 GLY C 308 ARG C 316 0 SHEET 2 AE3 5 PHE C 589 THR C 596 -1 O GLY C 590 N PHE C 315 SHEET 3 AE3 5 ALA C 606 GLN C 610 -1 O ALA C 606 N ILE C 595 SHEET 4 AE3 5 GLY C 645 ILE C 648 -1 O ILE C 648 N VAL C 607 SHEET 5 AE3 5 PHE C 640 GLN C 641 -1 N PHE C 640 O LEU C 647 SHEET 1 AE4 4 LYS C 353 ILE C 355 0 SHEET 2 AE4 4 THR C 390 ALA C 394 -1 O ALA C 394 N LYS C 353 SHEET 3 AE4 4 TYR C 505 GLU C 513 -1 O GLU C 513 N THR C 390 SHEET 4 AE4 4 PHE C 397 ILE C 399 -1 N ILE C 399 O TYR C 505 SHEET 1 AE5 4 LYS C 353 ILE C 355 0 SHEET 2 AE5 4 THR C 390 ALA C 394 -1 O ALA C 394 N LYS C 353 SHEET 3 AE5 4 TYR C 505 GLU C 513 -1 O GLU C 513 N THR C 390 SHEET 4 AE5 4 CYS C 429 ASN C 434 -1 N TRP C 433 O ARG C 506 SHEET 1 AE6 4 CYS C 535 ASN C 537 0 SHEET 2 AE6 4 THR C 546 GLU C 551 -1 O GLY C 547 N VAL C 536 SHEET 3 AE6 4 LEU C 582 THR C 585 -1 O THR C 585 N VAL C 548 SHEET 4 AE6 4 ALA C 572 VAL C 573 -1 N VAL C 573 O LEU C 582 SHEET 1 AE7 4 GLU C 651 TYR C 652 0 SHEET 2 AE7 4 SER C 688 THR C 693 1 O ALA C 691 N GLU C 651 SHEET 3 AE7 4 ILE C 667 GLN C 672 -1 N SER C 670 O ILE C 690 SHEET 4 AE7 4 ILE C 661 GLY C 664 -1 N GLY C 664 O ILE C 667 SHEET 1 AE8 3 ILE C 709 PRO C 725 0 SHEET 2 AE8 3 GLY C1056 THR C1074 -1 O VAL C1065 N THR C 716 SHEET 3 AE8 3 TYR C1044 ALA C1053 -1 N MET C1047 O VAL C1062 SHEET 1 AE9 4 ILE C 709 PRO C 725 0 SHEET 2 AE9 4 GLY C1056 THR C1074 -1 O VAL C1065 N THR C 716 SHEET 3 AE9 4 VAL C1091 SER C1094 -1 O SER C1094 N THR C1073 SHEET 4 AE9 4 TRP C1099 THR C1102 -1 O PHE C1100 N VAL C1093 SHEET 1 AF1 2 LYS C 730 VAL C 733 0 SHEET 2 AF1 2 LEU C 855 LEU C 858 -1 O LEU C 858 N LYS C 730 SHEET 1 AF2 4 THR C1117 VAL C1119 0 SHEET 2 AF2 4 ALA C1084 PRO C1087 -1 N PHE C1086 O PHE C1118 SHEET 3 AF2 4 ILE C1078 CYS C1079 -1 N ILE C1078 O HIS C1085 SHEET 4 AF2 4 VAL C1130 ASN C1131 1 O VAL C1130 N CYS C1079 SHEET 1 AF3 4 GLN E 4 SER E 8 0 SHEET 2 AF3 4 LEU E 19 SER E 26 -1 O VAL E 24 N VAL E 6 SHEET 3 AF3 4 THR E 81 MET E 86 -1 O MET E 86 N LEU E 19 SHEET 4 AF3 4 PHE E 71 THR E 72 -1 N THR E 72 O GLN E 85 SHEET 1 AF4 4 GLN E 4 SER E 8 0 SHEET 2 AF4 4 LEU E 19 SER E 26 -1 O VAL E 24 N VAL E 6 SHEET 3 AF4 4 THR E 81 MET E 86 -1 O MET E 86 N LEU E 19 SHEET 4 AF4 4 ARG E 75 ASP E 76 -1 N ASP E 76 O THR E 81 SHEET 1 AF5 6 LEU E 12 VAL E 13 0 SHEET 2 AF5 6 THR E 121 VAL E 125 1 O THR E 124 N VAL E 13 SHEET 3 AF5 6 ALA E 95 THR E 101 -1 N TYR E 97 O THR E 121 SHEET 4 AF5 6 VAL E 35 GLN E 40 -1 N PHE E 38 O TYR E 98 SHEET 5 AF5 6 GLU E 47 ILE E 52 -1 O ILE E 52 N VAL E 35 SHEET 6 AF5 6 TYR E 62 TYR E 63 -1 O TYR E 62 N CYS E 51 SHEET 1 AF6 4 LEU E 12 VAL E 13 0 SHEET 2 AF6 4 THR E 121 VAL E 125 1 O THR E 124 N VAL E 13 SHEET 3 AF6 4 ALA E 95 THR E 101 -1 N TYR E 97 O THR E 121 SHEET 4 AF6 4 TRP E 116 TRP E 117 -1 O TRP E 116 N THR E 101 SHEET 1 AF7 4 GLN G 4 SER G 8 0 SHEET 2 AF7 4 GLY G 17 SER G 26 -1 O VAL G 24 N VAL G 6 SHEET 3 AF7 4 THR G 81 LEU G 89 -1 O MET G 86 N LEU G 19 SHEET 4 AF7 4 THR G 72 ASP G 76 -1 N SER G 74 O TYR G 83 SHEET 1 AF8 6 LEU G 12 VAL G 13 0 SHEET 2 AF8 6 THR G 121 VAL G 125 1 O THR G 124 N VAL G 13 SHEET 3 AF8 6 ALA G 95 THR G 101 -1 N TYR G 97 O THR G 121 SHEET 4 AF8 6 VAL G 35 GLN G 40 -1 N PHE G 38 O TYR G 98 SHEET 5 AF8 6 GLU G 47 ILE G 52 -1 O SER G 50 N TRP G 37 SHEET 6 AF8 6 TYR G 62 TYR G 63 -1 O TYR G 62 N CYS G 51 SHEET 1 AF9 4 LEU G 12 VAL G 13 0 SHEET 2 AF9 4 THR G 121 VAL G 125 1 O THR G 124 N VAL G 13 SHEET 3 AF9 4 ALA G 95 THR G 101 -1 N TYR G 97 O THR G 121 SHEET 4 AF9 4 TRP G 116 TRP G 117 -1 O TRP G 116 N THR G 101 SHEET 1 AG1 4 GLN F 4 SER F 8 0 SHEET 2 AG1 4 LEU F 19 SER F 26 -1 O VAL F 24 N VAL F 6 SHEET 3 AG1 4 THR F 81 MET F 86 -1 O LEU F 84 N LEU F 21 SHEET 4 AG1 4 PHE F 71 ASP F 76 -1 N THR F 72 O GLN F 85 SHEET 1 AG2 6 LEU F 12 VAL F 13 0 SHEET 2 AG2 6 THR F 121 VAL F 125 1 O THR F 124 N VAL F 13 SHEET 3 AG2 6 ALA F 95 THR F 101 -1 N TYR F 97 O THR F 121 SHEET 4 AG2 6 VAL F 35 GLN F 40 -1 N PHE F 38 O TYR F 98 SHEET 5 AG2 6 GLU F 47 ILE F 52 -1 O SER F 50 N TRP F 37 SHEET 6 AG2 6 TYR F 62 TYR F 63 -1 O TYR F 62 N CYS F 51 SHEET 1 AG3 4 LEU F 12 VAL F 13 0 SHEET 2 AG3 4 THR F 121 VAL F 125 1 O THR F 124 N VAL F 13 SHEET 3 AG3 4 ALA F 95 THR F 101 -1 N TYR F 97 O THR F 121 SHEET 4 AG3 4 TRP F 116 TRP F 117 -1 O TRP F 116 N THR F 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 2.02 SSBOND 4 CYS A 376 CYS A 429 1555 1555 2.02 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 2.02 SSBOND 12 CYS A 837 CYS A 848 1555 1555 2.04 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 2.03 SSBOND 24 CYS B 735 CYS B 757 1555 1555 2.03 SSBOND 25 CYS B 740 CYS B 746 1555 1555 2.02 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 2.04 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 2.02 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 2.02 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 G 23 CYS G 99 1555 1555 2.03 SSBOND 46 CYS G 51 CYS G 107 1555 1555 2.03 SSBOND 47 CYS F 23 CYS F 99 1555 1555 2.03 SSBOND 48 CYS F 51 CYS F 107 1555 1555 2.03 LINK ND2 ASN A 279 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 706 C1 NAG A1301 1555 1555 1.45 LINK ND2 ASN A 714 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 798 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A1071 C1 NAG A1302 1555 1555 1.44 LINK ND2 ASN A1095 C1 NAG I 1 1555 1555 1.45 LINK ND2 ASN A1131 C1 NAG H 1 1555 1555 1.44 LINK ND2 ASN B 279 C1 NAG B1304 1555 1555 1.44 LINK ND2 ASN B 706 C1 NAG B1303 1555 1555 1.44 LINK ND2 ASN B 714 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN B 798 C1 NAG L 1 1555 1555 1.42 LINK ND2 ASN B1071 C1 NAG B1301 1555 1555 1.44 LINK ND2 ASN B1095 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN B1131 C1 NAG B1302 1555 1555 1.44 LINK ND2 ASN C 279 C1 NAG C1301 1555 1555 1.45 LINK ND2 ASN C 706 C1 NAG C1302 1555 1555 1.43 LINK ND2 ASN C 714 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 798 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN C1071 C1 NAG C1303 1555 1555 1.44 LINK ND2 ASN C1095 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C1131 C1 NAG O 1 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.46 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.46 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 1.46 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.46 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.46 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 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