HEADER VIRAL PROTEIN 15-FEB-17 5X5B TITLE PREFUSION STRUCTURE OF SARS-COV SPIKE GLYCOPROTEIN, CONFORMATION 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SARS CORONAVIRUS BJ01; SOURCE 3 ORGANISM_TAXID: 228407; SOURCE 4 STRAIN: BJ01; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS SARS-COV, SPIKE GLYCOPROTEIN, PREFUSION, SINGLE PARTICLE, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.YUAN,D.CAO,Y.ZHANG,J.MA,J.QI,Q.WANG,G.LU,Y.WU,J.YAN,Y.SHI,X.ZHANG, AUTHOR 2 G.F.GAO REVDAT 2 24-MAY-17 5X5B 1 REMARK REVDAT 1 03-MAY-17 5X5B 0 JRNL AUTH Y.YUAN,D.CAO,Y.ZHANG,J.MA,J.QI,Q.WANG,G.LU,Y.WU,J.YAN,Y.SHI, JRNL AUTH 2 X.ZHANG,G.F.GAO JRNL TITL CRYO-EM STRUCTURES OF MERS-COV AND SARS-COV SPIKE JRNL TITL 2 GLYCOPROTEINS REVEAL THE DYNAMIC RECEPTOR BINDING DOMAINS JRNL REF NAT COMMUN V. 8 15092 2017 JRNL REFN ESSN 2041-1723 JRNL PMID 28393837 JRNL DOI 10.1038/NCOMMS15092 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 2AJF REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 60000 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 5X5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-17. REMARK 100 THE DEPOSITION ID IS D_1300002954. 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 : SARS-COV SPIKE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 8.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 14 REMARK 465 ASP A 15 REMARK 465 LEU A 16 REMARK 465 ASP A 17 REMARK 465 PRO A 240 REMARK 465 ALA A 241 REMARK 465 GLN A 242 REMARK 465 ASP A 243 REMARK 465 PHE A 316 REMARK 465 PRO A 317 REMARK 465 ASN A 318 REMARK 465 ILE A 319 REMARK 465 THR A 320 REMARK 465 ASN A 321 REMARK 465 LEU A 503 REMARK 465 LEU A 504 REMARK 465 ASN A 505 REMARK 465 ALA A 506 REMARK 465 PRO A 507 REMARK 465 ALA A 508 REMARK 465 THR A 509 REMARK 465 VAL A 510 REMARK 465 CYS A 511 REMARK 465 GLY A 512 REMARK 465 PRO A 513 REMARK 465 LYS A 514 REMARK 465 LEU A 515 REMARK 465 SER A 516 REMARK 465 THR A 517 REMARK 465 VAL A 663 REMARK 465 SER A 664 REMARK 465 LEU A 665 REMARK 465 LEU A 666 REMARK 465 ARG A 667 REMARK 465 SER A 668 REMARK 465 THR A 669 REMARK 465 SER A 670 REMARK 465 GLN A 671 REMARK 465 LEU A 810 REMARK 465 ALA A 811 REMARK 465 ASP A 812 REMARK 465 ALA A 813 REMARK 465 GLY A 814 REMARK 465 PHE A 815 REMARK 465 MET A 816 REMARK 465 LYS A 817 REMARK 465 GLN A 818 REMARK 465 TYR A 819 REMARK 465 GLY A 820 REMARK 465 GLU A 821 REMARK 465 CYS A 822 REMARK 465 LEU A 823 REMARK 465 GLY A 824 REMARK 465 ASP A 825 REMARK 465 ILE A 826 REMARK 465 ASN A 827 REMARK 465 ALA A 828 REMARK 465 ARG A 829 REMARK 465 SER A 1105 REMARK 465 GLY A 1106 REMARK 465 ASN A 1107 REMARK 465 CYS A 1108 REMARK 465 ASP A 1109 REMARK 465 VAL A 1110 REMARK 465 VAL A 1111 REMARK 465 ILE A 1112 REMARK 465 GLY A 1113 REMARK 465 ILE A 1114 REMARK 465 ILE A 1115 REMARK 465 ASN A 1116 REMARK 465 ASN A 1117 REMARK 465 THR A 1118 REMARK 465 VAL A 1119 REMARK 465 TYR A 1120 REMARK 465 ASP A 1121 REMARK 465 PRO A 1122 REMARK 465 LEU A 1123 REMARK 465 GLN A 1124 REMARK 465 PRO A 1125 REMARK 465 GLU A 1126 REMARK 465 LEU A 1127 REMARK 465 ASP A 1128 REMARK 465 SER A 1129 REMARK 465 PHE A 1130 REMARK 465 LYS A 1131 REMARK 465 GLU A 1132 REMARK 465 GLU A 1133 REMARK 465 LEU A 1134 REMARK 465 ASP A 1135 REMARK 465 LYS A 1136 REMARK 465 TYR A 1137 REMARK 465 PHE A 1138 REMARK 465 LYS A 1139 REMARK 465 ASN A 1140 REMARK 465 HIS A 1141 REMARK 465 THR A 1142 REMARK 465 SER A 1143 REMARK 465 PRO A 1144 REMARK 465 ASP A 1145 REMARK 465 VAL A 1146 REMARK 465 ASP A 1147 REMARK 465 LEU A 1148 REMARK 465 GLY A 1149 REMARK 465 ASP A 1150 REMARK 465 ILE A 1151 REMARK 465 SER A 1152 REMARK 465 GLY A 1153 REMARK 465 ILE A 1154 REMARK 465 ASN A 1155 REMARK 465 ALA A 1156 REMARK 465 SER A 1157 REMARK 465 VAL A 1158 REMARK 465 VAL A 1159 REMARK 465 ASN A 1160 REMARK 465 ILE A 1161 REMARK 465 GLN A 1162 REMARK 465 LYS A 1163 REMARK 465 GLU A 1164 REMARK 465 ILE A 1165 REMARK 465 ASP A 1166 REMARK 465 ARG A 1167 REMARK 465 LEU A 1168 REMARK 465 ASN A 1169 REMARK 465 GLU A 1170 REMARK 465 VAL A 1171 REMARK 465 ALA A 1172 REMARK 465 LYS A 1173 REMARK 465 ASN A 1174 REMARK 465 LEU A 1175 REMARK 465 ASN A 1176 REMARK 465 GLU A 1177 REMARK 465 SER A 1178 REMARK 465 LEU A 1179 REMARK 465 ILE A 1180 REMARK 465 ASP A 1181 REMARK 465 LEU A 1182 REMARK 465 GLN A 1183 REMARK 465 GLU A 1184 REMARK 465 LEU A 1185 REMARK 465 GLY A 1186 REMARK 465 LYS A 1187 REMARK 465 TYR A 1188 REMARK 465 GLU A 1189 REMARK 465 GLN A 1190 REMARK 465 TYR A 1191 REMARK 465 ILE A 1192 REMARK 465 LYS A 1193 REMARK 465 ILE A 1194 REMARK 465 LYS A 1195 REMARK 465 ARG A 1196 REMARK 465 MET A 1197 REMARK 465 LYS A 1198 REMARK 465 GLN A 1199 REMARK 465 ILE A 1200 REMARK 465 GLU A 1201 REMARK 465 ASP A 1202 REMARK 465 LYS A 1203 REMARK 465 ILE A 1204 REMARK 465 GLU A 1205 REMARK 465 GLU A 1206 REMARK 465 ILE A 1207 REMARK 465 GLU A 1208 REMARK 465 SER A 1209 REMARK 465 LYS A 1210 REMARK 465 GLN A 1211 REMARK 465 LYS A 1212 REMARK 465 LYS A 1213 REMARK 465 ILE A 1214 REMARK 465 GLU A 1215 REMARK 465 ASN A 1216 REMARK 465 GLU A 1217 REMARK 465 ILE A 1218 REMARK 465 ALA A 1219 REMARK 465 ARG A 1220 REMARK 465 ILE A 1221 REMARK 465 LYS A 1222 REMARK 465 LYS A 1223 REMARK 465 ILE A 1224 REMARK 465 LYS A 1225 REMARK 465 LEU A 1226 REMARK 465 VAL A 1227 REMARK 465 PRO A 1228 REMARK 465 ARG A 1229 REMARK 465 GLY A 1230 REMARK 465 SER A 1231 REMARK 465 LEU A 1232 REMARK 465 GLU A 1233 REMARK 465 TRP A 1234 REMARK 465 SER A 1235 REMARK 465 HIS A 1236 REMARK 465 PRO A 1237 REMARK 465 GLN A 1238 REMARK 465 PHE A 1239 REMARK 465 GLU A 1240 REMARK 465 LYS A 1241 REMARK 465 SER B 14 REMARK 465 ASP B 15 REMARK 465 LEU B 16 REMARK 465 ASP B 17 REMARK 465 PRO B 240 REMARK 465 ALA B 241 REMARK 465 GLN B 242 REMARK 465 ASP B 243 REMARK 465 VAL B 663 REMARK 465 SER B 664 REMARK 465 LEU B 665 REMARK 465 LEU B 666 REMARK 465 ARG B 667 REMARK 465 SER B 668 REMARK 465 THR B 669 REMARK 465 SER B 670 REMARK 465 GLN B 671 REMARK 465 LEU B 810 REMARK 465 ALA B 811 REMARK 465 ASP B 812 REMARK 465 ALA B 813 REMARK 465 GLY B 814 REMARK 465 PHE B 815 REMARK 465 MET B 816 REMARK 465 LYS B 817 REMARK 465 GLN B 818 REMARK 465 TYR B 819 REMARK 465 GLY B 820 REMARK 465 GLU B 821 REMARK 465 CYS B 822 REMARK 465 LEU B 823 REMARK 465 GLY B 824 REMARK 465 ASP B 825 REMARK 465 ILE B 826 REMARK 465 ASN B 827 REMARK 465 ALA B 828 REMARK 465 ARG B 829 REMARK 465 ASP B 830 REMARK 465 SER B 1105 REMARK 465 GLY B 1106 REMARK 465 ASN B 1107 REMARK 465 CYS B 1108 REMARK 465 ASP B 1109 REMARK 465 VAL B 1110 REMARK 465 VAL B 1111 REMARK 465 ILE B 1112 REMARK 465 GLY B 1113 REMARK 465 ILE B 1114 REMARK 465 ILE B 1115 REMARK 465 ASN B 1116 REMARK 465 ASN B 1117 REMARK 465 THR B 1118 REMARK 465 VAL B 1119 REMARK 465 TYR B 1120 REMARK 465 ASP B 1121 REMARK 465 PRO B 1122 REMARK 465 LEU B 1123 REMARK 465 GLN B 1124 REMARK 465 PRO B 1125 REMARK 465 GLU B 1126 REMARK 465 LEU B 1127 REMARK 465 ASP B 1128 REMARK 465 SER B 1129 REMARK 465 PHE B 1130 REMARK 465 LYS B 1131 REMARK 465 GLU B 1132 REMARK 465 GLU B 1133 REMARK 465 LEU B 1134 REMARK 465 ASP B 1135 REMARK 465 LYS B 1136 REMARK 465 TYR B 1137 REMARK 465 PHE B 1138 REMARK 465 LYS B 1139 REMARK 465 ASN B 1140 REMARK 465 HIS B 1141 REMARK 465 THR B 1142 REMARK 465 SER B 1143 REMARK 465 PRO B 1144 REMARK 465 ASP B 1145 REMARK 465 VAL B 1146 REMARK 465 ASP B 1147 REMARK 465 LEU B 1148 REMARK 465 GLY B 1149 REMARK 465 ASP B 1150 REMARK 465 ILE B 1151 REMARK 465 SER B 1152 REMARK 465 GLY B 1153 REMARK 465 ILE B 1154 REMARK 465 ASN B 1155 REMARK 465 ALA B 1156 REMARK 465 SER B 1157 REMARK 465 VAL B 1158 REMARK 465 VAL B 1159 REMARK 465 ASN B 1160 REMARK 465 ILE B 1161 REMARK 465 GLN B 1162 REMARK 465 LYS B 1163 REMARK 465 GLU B 1164 REMARK 465 ILE B 1165 REMARK 465 ASP B 1166 REMARK 465 ARG B 1167 REMARK 465 LEU B 1168 REMARK 465 ASN B 1169 REMARK 465 GLU B 1170 REMARK 465 VAL B 1171 REMARK 465 ALA B 1172 REMARK 465 LYS B 1173 REMARK 465 ASN B 1174 REMARK 465 LEU B 1175 REMARK 465 ASN B 1176 REMARK 465 GLU B 1177 REMARK 465 SER B 1178 REMARK 465 LEU B 1179 REMARK 465 ILE B 1180 REMARK 465 ASP B 1181 REMARK 465 LEU B 1182 REMARK 465 GLN B 1183 REMARK 465 GLU B 1184 REMARK 465 LEU B 1185 REMARK 465 GLY B 1186 REMARK 465 LYS B 1187 REMARK 465 TYR B 1188 REMARK 465 GLU B 1189 REMARK 465 GLN B 1190 REMARK 465 TYR B 1191 REMARK 465 ILE B 1192 REMARK 465 LYS B 1193 REMARK 465 ILE B 1194 REMARK 465 LYS B 1195 REMARK 465 ARG B 1196 REMARK 465 MET B 1197 REMARK 465 LYS B 1198 REMARK 465 GLN B 1199 REMARK 465 ILE B 1200 REMARK 465 GLU B 1201 REMARK 465 ASP B 1202 REMARK 465 LYS B 1203 REMARK 465 ILE B 1204 REMARK 465 GLU B 1205 REMARK 465 GLU B 1206 REMARK 465 ILE B 1207 REMARK 465 GLU B 1208 REMARK 465 SER B 1209 REMARK 465 LYS B 1210 REMARK 465 GLN B 1211 REMARK 465 LYS B 1212 REMARK 465 LYS B 1213 REMARK 465 ILE B 1214 REMARK 465 GLU B 1215 REMARK 465 ASN B 1216 REMARK 465 GLU B 1217 REMARK 465 ILE B 1218 REMARK 465 ALA B 1219 REMARK 465 ARG B 1220 REMARK 465 ILE B 1221 REMARK 465 LYS B 1222 REMARK 465 LYS B 1223 REMARK 465 ILE B 1224 REMARK 465 LYS B 1225 REMARK 465 LEU B 1226 REMARK 465 VAL B 1227 REMARK 465 PRO B 1228 REMARK 465 ARG B 1229 REMARK 465 GLY B 1230 REMARK 465 SER B 1231 REMARK 465 LEU B 1232 REMARK 465 GLU B 1233 REMARK 465 TRP B 1234 REMARK 465 SER B 1235 REMARK 465 HIS B 1236 REMARK 465 PRO B 1237 REMARK 465 GLN B 1238 REMARK 465 PHE B 1239 REMARK 465 GLU B 1240 REMARK 465 LYS B 1241 REMARK 465 SER C 14 REMARK 465 ASP C 15 REMARK 465 LEU C 16 REMARK 465 ASP C 17 REMARK 465 PRO C 240 REMARK 465 ALA C 241 REMARK 465 GLN C 242 REMARK 465 ASP C 243 REMARK 465 VAL C 663 REMARK 465 SER C 664 REMARK 465 LEU C 665 REMARK 465 LEU C 666 REMARK 465 ARG C 667 REMARK 465 SER C 668 REMARK 465 THR C 669 REMARK 465 SER C 670 REMARK 465 GLN C 671 REMARK 465 LEU C 810 REMARK 465 ALA C 811 REMARK 465 ASP C 812 REMARK 465 ALA C 813 REMARK 465 GLY C 814 REMARK 465 PHE C 815 REMARK 465 MET C 816 REMARK 465 LYS C 817 REMARK 465 GLN C 818 REMARK 465 TYR C 819 REMARK 465 GLY C 820 REMARK 465 GLU C 821 REMARK 465 CYS C 822 REMARK 465 LEU C 823 REMARK 465 GLY C 824 REMARK 465 ASP C 825 REMARK 465 ILE C 826 REMARK 465 ASN C 827 REMARK 465 ALA C 828 REMARK 465 ARG C 829 REMARK 465 ASP C 830 REMARK 465 SER C 1105 REMARK 465 GLY C 1106 REMARK 465 ASN C 1107 REMARK 465 CYS C 1108 REMARK 465 ASP C 1109 REMARK 465 VAL C 1110 REMARK 465 VAL C 1111 REMARK 465 ILE C 1112 REMARK 465 GLY C 1113 REMARK 465 ILE C 1114 REMARK 465 ILE C 1115 REMARK 465 ASN C 1116 REMARK 465 ASN C 1117 REMARK 465 THR C 1118 REMARK 465 VAL C 1119 REMARK 465 TYR C 1120 REMARK 465 ASP C 1121 REMARK 465 PRO C 1122 REMARK 465 LEU C 1123 REMARK 465 GLN C 1124 REMARK 465 PRO C 1125 REMARK 465 GLU C 1126 REMARK 465 LEU C 1127 REMARK 465 ASP C 1128 REMARK 465 SER C 1129 REMARK 465 PHE C 1130 REMARK 465 LYS C 1131 REMARK 465 GLU C 1132 REMARK 465 GLU C 1133 REMARK 465 LEU C 1134 REMARK 465 ASP C 1135 REMARK 465 LYS C 1136 REMARK 465 TYR C 1137 REMARK 465 PHE C 1138 REMARK 465 LYS C 1139 REMARK 465 ASN C 1140 REMARK 465 HIS C 1141 REMARK 465 THR C 1142 REMARK 465 SER C 1143 REMARK 465 PRO C 1144 REMARK 465 ASP C 1145 REMARK 465 VAL C 1146 REMARK 465 ASP C 1147 REMARK 465 LEU C 1148 REMARK 465 GLY C 1149 REMARK 465 ASP C 1150 REMARK 465 ILE C 1151 REMARK 465 SER C 1152 REMARK 465 GLY C 1153 REMARK 465 ILE C 1154 REMARK 465 ASN C 1155 REMARK 465 ALA C 1156 REMARK 465 SER C 1157 REMARK 465 VAL C 1158 REMARK 465 VAL C 1159 REMARK 465 ASN C 1160 REMARK 465 ILE C 1161 REMARK 465 GLN C 1162 REMARK 465 LYS C 1163 REMARK 465 GLU C 1164 REMARK 465 ILE C 1165 REMARK 465 ASP C 1166 REMARK 465 ARG C 1167 REMARK 465 LEU C 1168 REMARK 465 ASN C 1169 REMARK 465 GLU C 1170 REMARK 465 VAL C 1171 REMARK 465 ALA C 1172 REMARK 465 LYS C 1173 REMARK 465 ASN C 1174 REMARK 465 LEU C 1175 REMARK 465 ASN C 1176 REMARK 465 GLU C 1177 REMARK 465 SER C 1178 REMARK 465 LEU C 1179 REMARK 465 ILE C 1180 REMARK 465 ASP C 1181 REMARK 465 LEU C 1182 REMARK 465 GLN C 1183 REMARK 465 GLU C 1184 REMARK 465 LEU C 1185 REMARK 465 GLY C 1186 REMARK 465 LYS C 1187 REMARK 465 TYR C 1188 REMARK 465 GLU C 1189 REMARK 465 GLN C 1190 REMARK 465 TYR C 1191 REMARK 465 ILE C 1192 REMARK 465 LYS C 1193 REMARK 465 ILE C 1194 REMARK 465 LYS C 1195 REMARK 465 ARG C 1196 REMARK 465 MET C 1197 REMARK 465 LYS C 1198 REMARK 465 GLN C 1199 REMARK 465 ILE C 1200 REMARK 465 GLU C 1201 REMARK 465 ASP C 1202 REMARK 465 LYS C 1203 REMARK 465 ILE C 1204 REMARK 465 GLU C 1205 REMARK 465 GLU C 1206 REMARK 465 ILE C 1207 REMARK 465 GLU C 1208 REMARK 465 SER C 1209 REMARK 465 LYS C 1210 REMARK 465 GLN C 1211 REMARK 465 LYS C 1212 REMARK 465 LYS C 1213 REMARK 465 ILE C 1214 REMARK 465 GLU C 1215 REMARK 465 ASN C 1216 REMARK 465 GLU C 1217 REMARK 465 ILE C 1218 REMARK 465 ALA C 1219 REMARK 465 ARG C 1220 REMARK 465 ILE C 1221 REMARK 465 LYS C 1222 REMARK 465 LYS C 1223 REMARK 465 ILE C 1224 REMARK 465 LYS C 1225 REMARK 465 LEU C 1226 REMARK 465 VAL C 1227 REMARK 465 PRO C 1228 REMARK 465 ARG C 1229 REMARK 465 GLY C 1230 REMARK 465 SER C 1231 REMARK 465 LEU C 1232 REMARK 465 GLU C 1233 REMARK 465 TRP C 1234 REMARK 465 SER C 1235 REMARK 465 HIS C 1236 REMARK 465 PRO C 1237 REMARK 465 GLN C 1238 REMARK 465 PHE C 1239 REMARK 465 GLU C 1240 REMARK 465 LYS C 1241 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 LEU A 920 CA - CB - CG ANGL. DEV. = 16.6 DEGREES REMARK 500 LEU A 927 CA - CB - CG ANGL. DEV. = 15.2 DEGREES REMARK 500 LEU B 515 CA - CB - CG ANGL. DEV. = 16.8 DEGREES REMARK 500 LEU B 597 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU B 920 CA - CB - CG ANGL. DEV. = 16.8 DEGREES REMARK 500 LEU B 927 CA - CB - CG ANGL. DEV. = 16.6 DEGREES REMARK 500 LEU C 515 CA - CB - CG ANGL. DEV. = 16.8 DEGREES REMARK 500 LEU C 597 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU C 920 CA - CB - CG ANGL. DEV. = 16.7 DEGREES REMARK 500 LEU C 927 CA - CB - CG ANGL. DEV. = 16.6 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 SER A 35 38.75 -99.14 REMARK 500 GLU A 45 43.90 -87.89 REMARK 500 LEU A 52 76.28 -100.46 REMARK 500 ASN A 78 80.76 -152.21 REMARK 500 ASN A 119 33.76 -95.55 REMARK 500 ASN A 135 84.94 -159.17 REMARK 500 ARG A 207 -1.65 -142.85 REMARK 500 LEU A 224 -72.32 -94.77 REMARK 500 THR A 302 110.26 -163.58 REMARK 500 ARG A 306 73.91 61.88 REMARK 500 VAL A 313 -60.12 -109.66 REMARK 500 CYS A 323 72.77 53.03 REMARK 500 ASP A 351 100.45 62.91 REMARK 500 SER A 353 -8.20 71.20 REMARK 500 PRO A 470 48.57 -92.49 REMARK 500 CYS A 524 70.32 55.27 REMARK 500 PHE A 529 -159.31 -89.66 REMARK 500 THR A 533 30.46 -95.02 REMARK 500 PHE A 545 73.61 57.84 REMARK 500 ASP A 600 34.66 -96.54 REMARK 500 ILE A 637 -63.44 -121.04 REMARK 500 TYR A 646 -69.22 -94.59 REMARK 500 GLU A 647 148.57 -177.38 REMARK 500 ALA A 654 15.45 59.29 REMARK 500 ASP A 727 108.09 -51.47 REMARK 500 THR A 743 -10.95 72.29 REMARK 500 LEU A 788 77.59 61.90 REMARK 500 LYS A 807 48.46 -93.40 REMARK 500 GLN A 835 70.87 58.59 REMARK 500 ILE A 955 -61.64 -91.35 REMARK 500 ARG A 965 29.58 -144.71 REMARK 500 LEU A 966 41.42 -141.32 REMARK 500 ASP A 967 -10.97 65.70 REMARK 500 LYS A 968 17.05 55.27 REMARK 500 VAL A1050 78.14 53.76 REMARK 500 GLU A1066 70.16 63.84 REMARK 500 THR A1098 -168.70 -102.54 REMARK 500 SER B 36 -21.06 71.44 REMARK 500 MET B 37 85.99 -154.42 REMARK 500 LYS B 110 49.34 -88.09 REMARK 500 ASN B 119 31.07 -94.97 REMARK 500 SER B 120 -6.37 67.62 REMARK 500 ASN B 135 81.27 -154.75 REMARK 500 ILE B 152 -50.93 -120.30 REMARK 500 ARG B 207 43.81 -143.76 REMARK 500 ARG B 306 75.45 64.39 REMARK 500 CYS B 323 73.56 52.04 REMARK 500 ALA B 339 34.44 -96.97 REMARK 500 ILE B 428 -63.52 -99.43 REMARK 500 PRO B 470 47.83 -94.54 REMARK 500 REMARK 500 THIS ENTRY HAS 112 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 SER A 35 SER A 36 -148.15 REMARK 500 GLN A 301 THR A 302 143.67 REMARK 500 THR A 302 SER A 303 -148.05 REMARK 500 TYR A 598 GLN A 599 145.02 REMARK 500 GLY A 726 ASP A 727 -144.44 REMARK 500 PHE A 741 CYS A 742 148.17 REMARK 500 PHE B 305 ARG B 306 142.30 REMARK 500 PHE B 316 PRO B 317 -146.15 REMARK 500 TYR B 598 GLN B 599 143.16 REMARK 500 THR B 616 PRO B 617 139.32 REMARK 500 SER B 701 ILE B 702 149.98 REMARK 500 GLN B 947 LEU B 948 147.92 REMARK 500 ASP B 967 LYS B 968 146.16 REMARK 500 PHE C 305 ARG C 306 142.23 REMARK 500 PHE C 316 PRO C 317 -146.18 REMARK 500 TYR C 598 GLN C 599 143.15 REMARK 500 THR C 616 PRO C 617 139.21 REMARK 500 GLN C 947 LEU C 948 147.92 REMARK 500 ASP C 967 LYS C 968 146.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5X58 RELATED DB: PDB REMARK 900 5X58 CONTAINS THE SAME PROTEIN IN DIFFERENT CONFORMATION REMARK 900 RELATED ID: EMD-6705 RELATED DB: EMDB REMARK 900 PREFUSION STRUCTURE OF SARS-COV SPIKE GLYCOPROTEIN, CONFORMATION 2 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE REFERENCE SEQUENCE DATABASE OF THIS PROTEIN IS RESIDUES 14-1193 REMARK 999 IN GENBANK AAP30030.1. RESIDUES 1194-1241 ARE EXPRESSION TAGS. DBREF 5X5B A 14 1241 PDB 5X5B 5X5B 14 1241 DBREF 5X5B B 14 1241 PDB 5X5B 5X5B 14 1241 DBREF 5X5B C 14 1241 PDB 5X5B 5X5B 14 1241 SEQRES 1 A 1228 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN SEQRES 2 A 1228 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY SEQRES 3 A 1228 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU SEQRES 4 A 1228 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN SEQRES 5 A 1228 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE ASP ASN SEQRES 6 A 1228 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA SEQRES 7 A 1228 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY SEQRES 8 A 1228 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE SEQRES 9 A 1228 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE SEQRES 10 A 1228 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO SEQRES 11 A 1228 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA SEQRES 12 A 1228 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER SEQRES 13 A 1228 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU SEQRES 14 A 1228 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR SEQRES 15 A 1228 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP SEQRES 16 A 1228 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS SEQRES 17 A 1228 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE SEQRES 18 A 1228 LEU THR ALA PHE SER PRO ALA GLN ASP THR TRP GLY THR SEQRES 19 A 1228 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR SEQRES 20 A 1228 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR SEQRES 21 A 1228 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU SEQRES 22 A 1228 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE SEQRES 23 A 1228 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP SEQRES 24 A 1228 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 A 1228 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR SEQRES 26 A 1228 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP SEQRES 27 A 1228 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE SEQRES 28 A 1228 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU SEQRES 29 A 1228 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS SEQRES 30 A 1228 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 A 1228 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 A 1228 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP SEQRES 33 A 1228 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR SEQRES 34 A 1228 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE SEQRES 35 A 1228 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR SEQRES 36 A 1228 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR SEQRES 37 A 1228 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR SEQRES 38 A 1228 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO SEQRES 39 A 1228 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE SEQRES 40 A 1228 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR SEQRES 41 A 1228 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN SEQRES 42 A 1228 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR SEQRES 43 A 1228 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP SEQRES 44 A 1228 ILE SER PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR SEQRES 45 A 1228 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR SEQRES 46 A 1228 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS SEQRES 47 A 1228 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR SEQRES 48 A 1228 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE SEQRES 49 A 1228 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE SEQRES 50 A 1228 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL SEQRES 51 A 1228 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA SEQRES 52 A 1228 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR SEQRES 53 A 1228 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE SEQRES 54 A 1228 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS SEQRES 55 A 1228 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER SEQRES 56 A 1228 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE SEQRES 57 A 1228 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA SEQRES 58 A 1228 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL SEQRES 59 A 1228 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY SEQRES 60 A 1228 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS SEQRES 61 A 1228 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN SEQRES 62 A 1228 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR SEQRES 63 A 1228 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE SEQRES 64 A 1228 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO SEQRES 65 A 1228 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA SEQRES 66 A 1228 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY SEQRES 67 A 1228 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET SEQRES 68 A 1228 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL SEQRES 69 A 1228 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN SEQRES 70 A 1228 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR SEQRES 71 A 1228 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN SEQRES 72 A 1228 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SEQRES 73 A 1228 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE SEQRES 74 A 1228 LEU SER ARG LEU ASP LYS VAL GLU ALA GLU VAL GLN ILE SEQRES 75 A 1228 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR SEQRES 76 A 1228 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG SEQRES 77 A 1228 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS SEQRES 78 A 1228 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS SEQRES 79 A 1228 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS SEQRES 80 A 1228 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN SEQRES 81 A 1228 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU SEQRES 82 A 1228 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE SEQRES 83 A 1228 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE SEQRES 84 A 1228 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER SEQRES 85 A 1228 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR SEQRES 86 A 1228 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS SEQRES 87 A 1228 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO SEQRES 88 A 1228 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER SEQRES 89 A 1228 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU SEQRES 90 A 1228 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN SEQRES 91 A 1228 GLU LEU GLY LYS TYR GLU GLN TYR ILE LYS ILE LYS ARG SEQRES 92 A 1228 MET LYS GLN ILE GLU ASP LYS ILE GLU GLU ILE GLU SER SEQRES 93 A 1228 LYS GLN LYS LYS ILE GLU ASN GLU ILE ALA ARG ILE LYS SEQRES 94 A 1228 LYS ILE LYS LEU VAL PRO ARG GLY SER LEU GLU TRP SER SEQRES 95 A 1228 HIS PRO GLN PHE GLU LYS SEQRES 1 B 1228 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN SEQRES 2 B 1228 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY SEQRES 3 B 1228 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU SEQRES 4 B 1228 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN SEQRES 5 B 1228 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE ASP ASN SEQRES 6 B 1228 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA SEQRES 7 B 1228 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY SEQRES 8 B 1228 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE SEQRES 9 B 1228 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE SEQRES 10 B 1228 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO SEQRES 11 B 1228 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA SEQRES 12 B 1228 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER SEQRES 13 B 1228 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU SEQRES 14 B 1228 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR SEQRES 15 B 1228 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP SEQRES 16 B 1228 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS SEQRES 17 B 1228 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE SEQRES 18 B 1228 LEU THR ALA PHE SER PRO ALA GLN ASP THR TRP GLY THR SEQRES 19 B 1228 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR SEQRES 20 B 1228 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR SEQRES 21 B 1228 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU SEQRES 22 B 1228 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE SEQRES 23 B 1228 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP SEQRES 24 B 1228 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 B 1228 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR SEQRES 26 B 1228 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP SEQRES 27 B 1228 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE SEQRES 28 B 1228 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU SEQRES 29 B 1228 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS SEQRES 30 B 1228 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 B 1228 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 B 1228 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP SEQRES 33 B 1228 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR SEQRES 34 B 1228 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE SEQRES 35 B 1228 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR SEQRES 36 B 1228 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR SEQRES 37 B 1228 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR SEQRES 38 B 1228 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO SEQRES 39 B 1228 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE SEQRES 40 B 1228 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR SEQRES 41 B 1228 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN SEQRES 42 B 1228 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR SEQRES 43 B 1228 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP SEQRES 44 B 1228 ILE SER PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR SEQRES 45 B 1228 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR SEQRES 46 B 1228 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS SEQRES 47 B 1228 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR SEQRES 48 B 1228 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE SEQRES 49 B 1228 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE SEQRES 50 B 1228 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL SEQRES 51 B 1228 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA SEQRES 52 B 1228 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR SEQRES 53 B 1228 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE SEQRES 54 B 1228 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS SEQRES 55 B 1228 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER SEQRES 56 B 1228 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE SEQRES 57 B 1228 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA SEQRES 58 B 1228 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL SEQRES 59 B 1228 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY SEQRES 60 B 1228 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS SEQRES 61 B 1228 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN SEQRES 62 B 1228 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR SEQRES 63 B 1228 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE SEQRES 64 B 1228 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO SEQRES 65 B 1228 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA SEQRES 66 B 1228 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY SEQRES 67 B 1228 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET SEQRES 68 B 1228 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL SEQRES 69 B 1228 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN SEQRES 70 B 1228 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR SEQRES 71 B 1228 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN SEQRES 72 B 1228 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SEQRES 73 B 1228 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE SEQRES 74 B 1228 LEU SER ARG LEU ASP LYS VAL GLU ALA GLU VAL GLN ILE SEQRES 75 B 1228 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR SEQRES 76 B 1228 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG SEQRES 77 B 1228 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS SEQRES 78 B 1228 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS SEQRES 79 B 1228 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS SEQRES 80 B 1228 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN SEQRES 81 B 1228 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU SEQRES 82 B 1228 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE SEQRES 83 B 1228 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE SEQRES 84 B 1228 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER SEQRES 85 B 1228 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR SEQRES 86 B 1228 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS SEQRES 87 B 1228 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO SEQRES 88 B 1228 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER SEQRES 89 B 1228 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU SEQRES 90 B 1228 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN SEQRES 91 B 1228 GLU LEU GLY LYS TYR GLU GLN TYR ILE LYS ILE LYS ARG SEQRES 92 B 1228 MET LYS GLN ILE GLU ASP LYS ILE GLU GLU ILE GLU SER SEQRES 93 B 1228 LYS GLN LYS LYS ILE GLU ASN GLU ILE ALA ARG ILE LYS SEQRES 94 B 1228 LYS ILE LYS LEU VAL PRO ARG GLY SER LEU GLU TRP SER SEQRES 95 B 1228 HIS PRO GLN PHE GLU LYS SEQRES 1 C 1228 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN SEQRES 2 C 1228 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY SEQRES 3 C 1228 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU SEQRES 4 C 1228 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN SEQRES 5 C 1228 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE ASP ASN SEQRES 6 C 1228 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA SEQRES 7 C 1228 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY SEQRES 8 C 1228 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE SEQRES 9 C 1228 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE SEQRES 10 C 1228 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO SEQRES 11 C 1228 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA SEQRES 12 C 1228 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER SEQRES 13 C 1228 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU SEQRES 14 C 1228 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR SEQRES 15 C 1228 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP SEQRES 16 C 1228 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS SEQRES 17 C 1228 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE SEQRES 18 C 1228 LEU THR ALA PHE SER PRO ALA GLN ASP THR TRP GLY THR SEQRES 19 C 1228 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR SEQRES 20 C 1228 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR SEQRES 21 C 1228 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU SEQRES 22 C 1228 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE SEQRES 23 C 1228 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP SEQRES 24 C 1228 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 C 1228 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR SEQRES 26 C 1228 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP SEQRES 27 C 1228 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE SEQRES 28 C 1228 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU SEQRES 29 C 1228 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS SEQRES 30 C 1228 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 C 1228 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 C 1228 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP SEQRES 33 C 1228 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR SEQRES 34 C 1228 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE SEQRES 35 C 1228 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR SEQRES 36 C 1228 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR SEQRES 37 C 1228 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR SEQRES 38 C 1228 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO SEQRES 39 C 1228 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE SEQRES 40 C 1228 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR SEQRES 41 C 1228 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN SEQRES 42 C 1228 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR SEQRES 43 C 1228 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP SEQRES 44 C 1228 ILE SER PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR SEQRES 45 C 1228 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR SEQRES 46 C 1228 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS SEQRES 47 C 1228 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR SEQRES 48 C 1228 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE SEQRES 49 C 1228 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE SEQRES 50 C 1228 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL SEQRES 51 C 1228 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA SEQRES 52 C 1228 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR SEQRES 53 C 1228 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE SEQRES 54 C 1228 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS SEQRES 55 C 1228 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER SEQRES 56 C 1228 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE SEQRES 57 C 1228 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA SEQRES 58 C 1228 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL SEQRES 59 C 1228 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY SEQRES 60 C 1228 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS SEQRES 61 C 1228 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN SEQRES 62 C 1228 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR SEQRES 63 C 1228 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE SEQRES 64 C 1228 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO SEQRES 65 C 1228 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA SEQRES 66 C 1228 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY SEQRES 67 C 1228 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET SEQRES 68 C 1228 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL SEQRES 69 C 1228 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN SEQRES 70 C 1228 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR SEQRES 71 C 1228 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN SEQRES 72 C 1228 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SEQRES 73 C 1228 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE SEQRES 74 C 1228 LEU SER ARG LEU ASP LYS VAL GLU ALA GLU VAL GLN ILE SEQRES 75 C 1228 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR SEQRES 76 C 1228 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG SEQRES 77 C 1228 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS SEQRES 78 C 1228 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS SEQRES 79 C 1228 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS SEQRES 80 C 1228 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN SEQRES 81 C 1228 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU SEQRES 82 C 1228 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE SEQRES 83 C 1228 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE SEQRES 84 C 1228 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER SEQRES 85 C 1228 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR SEQRES 86 C 1228 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS SEQRES 87 C 1228 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO SEQRES 88 C 1228 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER SEQRES 89 C 1228 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU SEQRES 90 C 1228 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN SEQRES 91 C 1228 GLU LEU GLY LYS TYR GLU GLN TYR ILE LYS ILE LYS ARG SEQRES 92 C 1228 MET LYS GLN ILE GLU ASP LYS ILE GLU GLU ILE GLU SER SEQRES 93 C 1228 LYS GLN LYS LYS ILE GLU ASN GLU ILE ALA ARG ILE LYS SEQRES 94 C 1228 LYS ILE LYS LEU VAL PRO ARG GLY SER LEU GLU TRP SER SEQRES 95 C 1228 HIS PRO GLN PHE GLU LYS HELIX 1 AA1 ASN A 281 LYS A 291 1 11 HELIX 2 AA2 CYS A 323 GLU A 327 5 5 HELIX 3 AA3 LYS A 390 ILE A 397 1 8 HELIX 4 AA4 GLY A 488 GLN A 492 5 5 HELIX 5 AA5 ASN A 602 ALA A 612 1 11 HELIX 6 AA6 ASP A 719 CYS A 725 1 7 HELIX 7 AA7 SER A 728 GLN A 737 1 10 HELIX 8 AA8 GLN A 744 LEU A 749 1 6 HELIX 9 AA9 LEU A 749 PHE A 764 1 16 HELIX 10 AB1 SER A 798 PHE A 805 1 8 HELIX 11 AB2 THR A 848 ALA A 866 1 19 HELIX 12 AB3 TRP A 868 GLY A 873 1 6 HELIX 13 AB4 PRO A 879 GLY A 892 1 14 HELIX 14 AB5 GLN A 895 ASN A 901 1 7 HELIX 15 AB6 ASN A 901 THR A 923 1 23 HELIX 16 AB7 SER A 924 VAL A 945 1 22 HELIX 17 AB8 VAL A 958 ARG A 965 1 8 HELIX 18 AB9 GLU A 970 ILE A 975 1 6 HELIX 19 AC1 ILE A 975 CYS A 1014 1 40 HELIX 20 AC2 ASN B 281 LYS B 291 1 11 HELIX 21 AC3 PHE B 325 ASN B 330 1 6 HELIX 22 AC4 ASP B 351 SER B 358 1 8 HELIX 23 AC5 SER B 370 ASN B 375 1 6 HELIX 24 AC6 ASP B 392 VAL B 394 5 3 HELIX 25 AC7 GLY B 488 TYR B 491 5 4 HELIX 26 AC8 ASN B 602 THR B 608 1 7 HELIX 27 AC9 ASP B 719 GLY B 726 1 8 HELIX 28 AD1 SER B 728 GLN B 737 1 10 HELIX 29 AD2 THR B 743 ASP B 757 1 15 HELIX 30 AD3 ASP B 757 ALA B 765 1 9 HELIX 31 AD4 SER B 798 PHE B 805 1 8 HELIX 32 AD5 THR B 848 ALA B 866 1 19 HELIX 33 AD6 TRP B 868 GLY B 873 1 6 HELIX 34 AD7 PRO B 879 GLY B 892 1 14 HELIX 35 AD8 THR B 894 ASN B 901 1 8 HELIX 36 AD9 ASN B 901 SER B 919 1 19 HELIX 37 AE1 LEU B 927 GLN B 947 1 21 HELIX 38 AE2 VAL B 958 ASP B 967 1 10 HELIX 39 AE3 GLU B 970 CYS B 1014 1 45 HELIX 40 AE4 ASN C 281 LYS C 291 1 11 HELIX 41 AE5 PHE C 325 ASN C 330 1 6 HELIX 42 AE6 ASP C 351 SER C 358 1 8 HELIX 43 AE7 SER C 370 ASN C 375 1 6 HELIX 44 AE8 ASP C 392 VAL C 394 5 3 HELIX 45 AE9 GLY C 488 TYR C 491 5 4 HELIX 46 AF1 ASN C 602 THR C 608 1 7 HELIX 47 AF2 ASP C 719 GLY C 726 1 8 HELIX 48 AF3 SER C 728 GLN C 737 1 10 HELIX 49 AF4 THR C 743 ASP C 757 1 15 HELIX 50 AF5 ASP C 757 ALA C 765 1 9 HELIX 51 AF6 SER C 798 PHE C 805 1 8 HELIX 52 AF7 THR C 848 ALA C 866 1 19 HELIX 53 AF8 TRP C 868 GLY C 873 1 6 HELIX 54 AF9 PRO C 879 GLY C 892 1 14 HELIX 55 AG1 THR C 894 ASN C 901 1 8 HELIX 56 AG2 ASN C 901 SER C 919 1 19 HELIX 57 AG3 LEU C 927 GLN C 947 1 21 HELIX 58 AG4 VAL C 958 ASP C 967 1 10 HELIX 59 AG5 GLU C 970 CYS C 1014 1 45 SHEET 1 AA1 8 THR A 31 HIS A 33 0 SHEET 2 AA1 8 VAL A 66 PHE A 69 -1 O VAL A 66 N HIS A 33 SHEET 3 AA1 8 TYR A 252 TYR A 256 -1 O VAL A 254 N THR A 67 SHEET 4 AA1 8 ILE A 87 ALA A 91 -1 N TYR A 88 O GLY A 255 SHEET 5 AA1 8 ARG A 183 LYS A 190 -1 O PHE A 185 N PHE A 89 SHEET 6 AA1 8 PHE A 193 TYR A 200 -1 O TYR A 195 N LYS A 188 SHEET 7 AA1 8 THR A 215 LYS A 221 -1 O ILE A 219 N VAL A 196 SHEET 8 AA1 8 VAL A 40 TYR A 41 1 N VAL A 40 O LEU A 216 SHEET 1 AA2 3 THR A 51 PHE A 59 0 SHEET 2 AA2 3 LYS A 258 TYR A 266 -1 O LEU A 264 N TYR A 53 SHEET 3 AA2 3 ILE A 272 ASP A 277 -1 O ASP A 274 N LYS A 265 SHEET 1 AA3 6 ILE A 81 PRO A 82 0 SHEET 2 AA3 6 ASN A 230 LEU A 235 -1 O PHE A 231 N ILE A 81 SHEET 3 AA3 6 VAL A 98 GLY A 104 -1 N GLY A 100 O ILE A 234 SHEET 4 AA3 6 GLN A 112 ASN A 118 -1 O ILE A 116 N TRP A 101 SHEET 5 AA3 6 ASN A 122 PHE A 130 -1 O VAL A 124 N ILE A 117 SHEET 6 AA3 6 ALA A 156 ALA A 167 -1 O SER A 165 N VAL A 123 SHEET 1 AA4 2 VAL A 140 SER A 141 0 SHEET 2 AA4 2 PHE A 238 SER A 239 1 O SER A 239 N VAL A 140 SHEET 1 AA5 4 GLY A 298 ILE A 299 0 SHEET 2 AA5 4 VAL A 583 THR A 585 -1 O THR A 585 N GLY A 298 SHEET 3 AA5 4 VAL A 596 GLN A 599 -1 O VAL A 596 N ILE A 584 SHEET 4 AA5 4 CYS A 635 LEU A 636 -1 O CYS A 635 N GLN A 599 SHEET 1 AA6 5 GLU A 341 ILE A 345 0 SHEET 2 AA6 5 VAL A 382 VAL A 389 -1 O ALA A 384 N LYS A 343 SHEET 3 AA6 5 TYR A 494 SER A 500 -1 O VAL A 496 N PHE A 387 SHEET 4 AA6 5 CYS A 419 ASN A 424 -1 N CYS A 419 O LEU A 499 SHEET 5 AA6 5 THR A 363 CYS A 366 -1 N LYS A 365 O VAL A 420 SHEET 1 AA7 6 VAL A 525 ASN A 526 0 SHEET 2 AA7 6 THR A 535 PRO A 540 -1 O GLY A 536 N VAL A 525 SHEET 3 AA7 6 ILE A 570 PRO A 575 -1 O SER A 574 N VAL A 537 SHEET 4 AA7 6 THR A 559 ARG A 563 -1 N ASP A 560 O ILE A 573 SHEET 5 AA7 6 PHE A 551 ARG A 553 -1 N GLY A 552 O SER A 561 SHEET 6 AA7 6 ILE B 46 ARG B 48 1 O PHE B 47 N ARG A 553 SHEET 1 AA8 4 GLU A 640 HIS A 641 0 SHEET 2 AA8 4 VAL A 675 THR A 678 1 O ALA A 676 N GLU A 640 SHEET 3 AA8 4 ILE A 656 SER A 659 -1 N CYS A 657 O TYR A 677 SHEET 4 AA8 4 ILE A 650 GLY A 653 -1 N ILE A 650 O ALA A 658 SHEET 1 AA9 2 ASP A 684 SER A 685 0 SHEET 2 AA9 2 MET B 770 TYR B 771 1 O MET B 770 N SER A 685 SHEET 1 AB1 4 THR A 693 PHE A 700 0 SHEET 2 AB1 4 PRO A1051 THR A1059 -1 O PHE A1057 N ILE A 694 SHEET 3 AB1 4 VAL A1078 ASN A1080 -1 O PHE A1079 N THR A1058 SHEET 4 AB1 4 SER A1083 TRP A1084 -1 O SER A1083 N ASN A1080 SHEET 1 AB2 3 THR A 706 PRO A 710 0 SHEET 2 AB2 3 GLY A1041 THR A1048 -1 O PHE A1044 N GLU A 707 SHEET 3 AB2 3 HIS A1030 ALA A1038 -1 N GLN A1036 O VAL A1043 SHEET 1 AB3 2 LYS A 715 THR A 716 0 SHEET 2 AB3 2 VAL A 842 LEU A 843 -1 O LEU A 843 N LYS A 715 SHEET 1 AB4 2 MET A 770 TYR A 771 0 SHEET 2 AB4 2 ASP C 684 SER C 685 1 O SER C 685 N MET A 770 SHEET 1 AB5 2 PHE A1071 PRO A1072 0 SHEET 2 AB5 2 THR A1102 PHE A1103 -1 O PHE A1103 N PHE A1071 SHEET 1 AB6 8 THR B 31 THR B 34 0 SHEET 2 AB6 8 ASN B 65 PHE B 69 -1 O GLY B 68 N THR B 31 SHEET 3 AB6 8 TYR B 252 TYR B 256 -1 O TYR B 252 N PHE B 69 SHEET 4 AB6 8 ILE B 87 PHE B 89 -1 N TYR B 88 O GLY B 255 SHEET 5 AB6 8 PHE B 179 LYS B 188 -1 O PHE B 185 N PHE B 89 SHEET 6 AB6 8 TYR B 195 VAL B 205 -1 O GLY B 199 N GLU B 184 SHEET 7 AB6 8 THR B 215 LYS B 221 -1 O LYS B 217 N LYS B 198 SHEET 8 AB6 8 VAL B 40 TYR B 41 1 N VAL B 40 O LEU B 216 SHEET 1 AB7 3 LEU B 52 PHE B 59 0 SHEET 2 AB7 3 LYS B 258 TYR B 266 -1 O LYS B 258 N PHE B 59 SHEET 3 AB7 3 ILE B 272 ASP B 277 -1 O ASP B 274 N LYS B 265 SHEET 1 AB8 3 ILE B 81 PRO B 82 0 SHEET 2 AB8 3 ASN B 230 ILE B 234 -1 O PHE B 231 N ILE B 81 SHEET 3 AB8 3 GLY B 100 GLY B 104 -1 N GLY B 100 O ILE B 234 SHEET 1 AB9 3 GLN B 112 ILE B 116 0 SHEET 2 AB9 3 ASN B 122 PHE B 130 -1 O ARG B 126 N ILE B 115 SHEET 3 AB9 3 ALA B 156 ALA B 167 -1 O TYR B 163 N ILE B 125 SHEET 1 AC1 2 VAL B 140 SER B 141 0 SHEET 2 AC1 2 PHE B 238 SER B 239 1 O SER B 239 N VAL B 140 SHEET 1 AC2 3 GLY B 298 ILE B 299 0 SHEET 2 AC2 3 VAL B 583 THR B 585 -1 O THR B 585 N GLY B 298 SHEET 3 AC2 3 VAL B 596 LEU B 597 -1 O VAL B 596 N ILE B 584 SHEET 1 AC3 2 ASN B 321 LEU B 322 0 SHEET 2 AC3 2 CYS B 348 VAL B 349 1 O VAL B 349 N ASN B 321 SHEET 1 AC4 4 GLU B 341 LYS B 344 0 SHEET 2 AC4 4 TYR B 383 LYS B 390 -1 O SER B 386 N GLU B 341 SHEET 3 AC4 4 PRO B 493 SER B 500 -1 O VAL B 498 N ASP B 385 SHEET 4 AC4 4 VAL B 420 ASN B 424 -1 N LEU B 421 O VAL B 497 SHEET 1 AC5 4 ILE B 570 ASP B 572 0 SHEET 2 AC5 4 SER B 561 ARG B 563 -1 N VAL B 562 O LEU B 571 SHEET 3 AC5 4 PHE B 551 GLY B 552 -1 N GLY B 552 O SER B 561 SHEET 4 AC5 4 ILE C 46 PHE C 47 1 O PHE C 47 N PHE B 551 SHEET 1 AC6 3 ILE B 650 PRO B 651 0 SHEET 2 AC6 3 ILE B 656 SER B 659 -1 O ALA B 658 N ILE B 650 SHEET 3 AC6 3 VAL B 675 THR B 678 -1 O TYR B 677 N CYS B 657 SHEET 1 AC7 2 ASP B 684 SER B 685 0 SHEET 2 AC7 2 MET C 770 TYR C 771 1 O MET C 770 N SER B 685 SHEET 1 AC8 2 ALA B 695 PRO B 697 0 SHEET 2 AC8 2 GLU B1054 ASN B1056 -1 O ARG B1055 N ILE B 696 SHEET 1 AC9 3 ILE B 704 PRO B 710 0 SHEET 2 AC9 3 GLY B1041 THR B1048 -1 O VAL B1042 N MET B 709 SHEET 3 AC9 3 HIS B1030 ALA B1038 -1 N GLN B1036 O VAL B1043 SHEET 1 AD1 2 LYS B 715 VAL B 718 0 SHEET 2 AD1 2 LEU B 840 LEU B 843 -1 O LEU B 843 N LYS B 715 SHEET 1 AD2 4 THR B1058 THR B1059 0 SHEET 2 AD2 4 VAL B1078 ASN B1080 -1 O PHE B1079 N THR B1058 SHEET 3 AD2 4 SER B1083 GLN B1088 -1 O PHE B1085 N VAL B1078 SHEET 4 AD2 4 PHE B1091 ILE B1096 -1 O GLN B1095 N ILE B1086 SHEET 1 AD3 2 PHE B1071 PRO B1072 0 SHEET 2 AD3 2 THR B1102 PHE B1103 -1 O PHE B1103 N PHE B1071 SHEET 1 AD4 8 THR C 31 THR C 34 0 SHEET 2 AD4 8 ASN C 65 PHE C 69 -1 O GLY C 68 N THR C 31 SHEET 3 AD4 8 TYR C 252 TYR C 256 -1 O TYR C 252 N PHE C 69 SHEET 4 AD4 8 ILE C 87 PHE C 89 -1 N TYR C 88 O GLY C 255 SHEET 5 AD4 8 PHE C 179 LYS C 188 -1 O PHE C 185 N PHE C 89 SHEET 6 AD4 8 TYR C 195 VAL C 205 -1 O GLY C 199 N GLU C 184 SHEET 7 AD4 8 THR C 215 LYS C 221 -1 O LYS C 217 N LYS C 198 SHEET 8 AD4 8 VAL C 40 TYR C 41 1 N VAL C 40 O LEU C 216 SHEET 1 AD5 3 LEU C 52 PHE C 59 0 SHEET 2 AD5 3 LYS C 258 TYR C 266 -1 O LYS C 258 N PHE C 59 SHEET 3 AD5 3 ILE C 272 ASP C 277 -1 O ASP C 274 N LYS C 265 SHEET 1 AD6 3 ILE C 81 PRO C 82 0 SHEET 2 AD6 3 ASN C 230 ILE C 234 -1 O PHE C 231 N ILE C 81 SHEET 3 AD6 3 GLY C 100 GLY C 104 -1 N GLY C 100 O ILE C 234 SHEET 1 AD7 3 GLN C 112 ILE C 116 0 SHEET 2 AD7 3 ASN C 122 PHE C 130 -1 O ARG C 126 N ILE C 115 SHEET 3 AD7 3 ALA C 156 ALA C 167 -1 O TYR C 163 N ILE C 125 SHEET 1 AD8 2 VAL C 140 SER C 141 0 SHEET 2 AD8 2 PHE C 238 SER C 239 1 O SER C 239 N VAL C 140 SHEET 1 AD9 3 GLY C 298 ILE C 299 0 SHEET 2 AD9 3 VAL C 583 THR C 585 -1 O THR C 585 N GLY C 298 SHEET 3 AD9 3 VAL C 596 LEU C 597 -1 O VAL C 596 N ILE C 584 SHEET 1 AE1 2 ASN C 321 LEU C 322 0 SHEET 2 AE1 2 CYS C 348 VAL C 349 1 O VAL C 349 N ASN C 321 SHEET 1 AE2 4 GLU C 341 LYS C 344 0 SHEET 2 AE2 4 TYR C 383 LYS C 390 -1 O SER C 386 N GLU C 341 SHEET 3 AE2 4 PRO C 493 SER C 500 -1 O VAL C 498 N ASP C 385 SHEET 4 AE2 4 VAL C 420 ASN C 424 -1 N LEU C 421 O VAL C 497 SHEET 1 AE3 3 PHE C 551 GLY C 552 0 SHEET 2 AE3 3 SER C 561 ARG C 563 -1 O SER C 561 N GLY C 552 SHEET 3 AE3 3 ILE C 570 ASP C 572 -1 O LEU C 571 N VAL C 562 SHEET 1 AE4 3 ILE C 650 PRO C 651 0 SHEET 2 AE4 3 ILE C 656 SER C 659 -1 O ALA C 658 N ILE C 650 SHEET 3 AE4 3 VAL C 675 THR C 678 -1 O TYR C 677 N CYS C 657 SHEET 1 AE5 2 ALA C 695 PRO C 697 0 SHEET 2 AE5 2 GLU C1054 ASN C1056 -1 O ARG C1055 N ILE C 696 SHEET 1 AE6 3 ILE C 704 PRO C 710 0 SHEET 2 AE6 3 GLY C1041 THR C1048 -1 O VAL C1042 N MET C 709 SHEET 3 AE6 3 HIS C1030 ALA C1038 -1 N GLN C1036 O VAL C1043 SHEET 1 AE7 2 LYS C 715 VAL C 718 0 SHEET 2 AE7 2 LEU C 840 LEU C 843 -1 O LEU C 843 N LYS C 715 SHEET 1 AE8 4 THR C1058 THR C1059 0 SHEET 2 AE8 4 VAL C1078 ASN C1080 -1 O PHE C1079 N THR C1058 SHEET 3 AE8 4 SER C1083 GLN C1088 -1 O PHE C1085 N VAL C1078 SHEET 4 AE8 4 PHE C1091 ILE C1096 -1 O GLN C1095 N ILE C1086 SHEET 1 AE9 2 PHE C1071 PRO C1072 0 SHEET 2 AE9 2 THR C1102 PHE C1103 -1 O PHE C1103 N PHE C1071 SSBOND 1 CYS A 128 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 467 CYS A 474 1555 1555 2.04 SSBOND 3 CYS A 524 CYS A 576 1555 1555 2.04 SSBOND 4 CYS A 648 CYS A 657 1555 1555 2.04 SSBOND 5 CYS A 725 CYS A 731 1555 1555 2.02 SSBOND 6 CYS A 1014 CYS A 1025 1555 1555 2.01 SSBOND 7 CYS B 128 CYS B 159 1555 1555 2.03 SSBOND 8 CYS B 467 CYS B 474 1555 1555 2.02 SSBOND 9 CYS B 524 CYS B 576 1555 1555 2.03 SSBOND 10 CYS B 648 CYS B 657 1555 1555 2.03 SSBOND 11 CYS B 725 CYS B 731 1555 1555 2.02 SSBOND 12 CYS B 1014 CYS B 1025 1555 1555 2.03 SSBOND 13 CYS C 128 CYS C 159 1555 1555 2.03 SSBOND 14 CYS C 467 CYS C 474 1555 1555 2.02 SSBOND 15 CYS C 524 CYS C 576 1555 1555 2.03 SSBOND 16 CYS C 648 CYS C 657 1555 1555 2.03 SSBOND 17 CYS C 725 CYS C 731 1555 1555 2.02 SSBOND 18 CYS C 1014 CYS C 1025 1555 1555 2.03 CISPEP 1 PRO A 469 PRO A 470 0 0.86 CISPEP 2 THR A 624 GLY A 625 0 11.07 CISPEP 3 PRO B 469 PRO B 470 0 -3.46 CISPEP 4 THR B 624 GLY B 625 0 9.92 CISPEP 5 PRO C 469 PRO C 470 0 -3.42 CISPEP 6 THR C 624 GLY C 625 0 9.89 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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