HEADER IMMUNE SYSTEM 02-JUN-25 9OWE TITLE CRYOEM STRUCTURE OF STABILIZED DENGUE 3 VIRUS ENVELOPE GLYCOPROTEIN IN TITLE 2 COMPLEX WITH FAB OF F25.S02 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GENOME POLYPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F25.S02 HEAVY CHAIN; COMPND 7 CHAIN: C, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: F25.S02 LIGHT CHAIN; COMPND 11 CHAIN: D, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS TYPE 3; SOURCE 3 ORGANISM_TAXID: 11069; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK 293E; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293E KEYWDS ORTHOFLAVIVIRUS, DENGUE, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR N.K.HURLBURT,M.PANCERA REVDAT 1 04-MAR-26 9OWE 0 JRNL AUTH N.K.HURLBURT,M.PANCERA JRNL TITL STRUCTURAL BASIS FOR ANTIBODY CROSS-NEUTRALIZATION OF DENGUE JRNL TITL 2 AND ZIKA VIRUSES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.16 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.160 REMARK 3 NUMBER OF PARTICLES : 111111 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 9OWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000296332. 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 F25.S02 FAB BOUND TO REMARK 245 DENV3 SE SC30 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 : TFS GLACIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 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) : 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, L, E, F 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 GLY A 393 REMARK 465 SER A 394 REMARK 465 SER A 395 REMARK 465 GLY A 396 REMARK 465 GLY A 397 REMARK 465 SER A 398 REMARK 465 HIS A 399 REMARK 465 HIS A 400 REMARK 465 HIS A 401 REMARK 465 HIS A 402 REMARK 465 HIS A 403 REMARK 465 HIS A 404 REMARK 465 HIS A 405 REMARK 465 HIS A 406 REMARK 465 GLY B 393 REMARK 465 SER B 394 REMARK 465 SER B 395 REMARK 465 GLY B 396 REMARK 465 GLY B 397 REMARK 465 SER B 398 REMARK 465 HIS B 399 REMARK 465 HIS B 400 REMARK 465 HIS B 401 REMARK 465 HIS B 402 REMARK 465 HIS B 403 REMARK 465 HIS B 404 REMARK 465 HIS B 405 REMARK 465 HIS B 406 REMARK 465 SER C 112 REMARK 465 SER C 113 REMARK 465 ARG C 114 REMARK 465 SER C 115 REMARK 465 THR C 116 REMARK 465 LYS C 117 REMARK 465 GLY C 118 REMARK 465 PRO C 119 REMARK 465 SER C 120 REMARK 465 VAL C 121 REMARK 465 PHE C 122 REMARK 465 PRO C 123 REMARK 465 LEU C 124 REMARK 465 ALA C 125 REMARK 465 PRO C 126 REMARK 465 SER C 127 REMARK 465 SER C 128 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 THR C 135 REMARK 465 ALA C 136 REMARK 465 ALA C 137 REMARK 465 LEU C 138 REMARK 465 GLY C 139 REMARK 465 CYS C 140 REMARK 465 LEU C 141 REMARK 465 VAL C 142 REMARK 465 LYS C 143 REMARK 465 ASP C 144 REMARK 465 TYR C 145 REMARK 465 PHE C 146 REMARK 465 PRO C 147 REMARK 465 GLU C 148 REMARK 465 PRO C 149 REMARK 465 VAL C 150 REMARK 465 THR C 151 REMARK 465 VAL C 152 REMARK 465 SER C 153 REMARK 465 TRP C 154 REMARK 465 ASN C 155 REMARK 465 SER C 156 REMARK 465 GLY C 157 REMARK 465 ALA C 158 REMARK 465 LEU C 159 REMARK 465 THR C 160 REMARK 465 SER C 161 REMARK 465 GLY C 162 REMARK 465 VAL C 163 REMARK 465 HIS C 164 REMARK 465 THR C 165 REMARK 465 PHE C 166 REMARK 465 PRO C 167 REMARK 465 ALA C 168 REMARK 465 VAL C 169 REMARK 465 LEU C 170 REMARK 465 GLN C 171 REMARK 465 SER C 172 REMARK 465 SER C 173 REMARK 465 GLY C 174 REMARK 465 LEU C 175 REMARK 465 TYR C 176 REMARK 465 SER C 177 REMARK 465 LEU C 178 REMARK 465 SER C 179 REMARK 465 SER C 180 REMARK 465 VAL C 181 REMARK 465 VAL C 182 REMARK 465 THR C 183 REMARK 465 VAL C 184 REMARK 465 PRO C 185 REMARK 465 SER C 186 REMARK 465 SER C 187 REMARK 465 SER C 188 REMARK 465 LEU C 189 REMARK 465 GLY C 190 REMARK 465 THR C 191 REMARK 465 GLN C 192 REMARK 465 THR C 193 REMARK 465 TYR C 194 REMARK 465 ILE C 195 REMARK 465 CYS C 196 REMARK 465 ASN C 197 REMARK 465 VAL C 198 REMARK 465 ASN C 199 REMARK 465 HIS C 200 REMARK 465 LYS C 201 REMARK 465 PRO C 202 REMARK 465 SER C 203 REMARK 465 ASN C 204 REMARK 465 THR C 205 REMARK 465 LYS C 206 REMARK 465 VAL C 207 REMARK 465 ASP C 208 REMARK 465 LYS C 209 REMARK 465 ARG C 210 REMARK 465 VAL C 211 REMARK 465 GLU C 212 REMARK 465 PRO C 213 REMARK 465 LYS C 214 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 ASP C 217 REMARK 465 LYS C 218 REMARK 465 THR C 219 REMARK 465 HIS C 220 REMARK 465 HIS C 221 REMARK 465 HIS C 222 REMARK 465 HIS C 223 REMARK 465 HIS C 224 REMARK 465 HIS C 225 REMARK 465 GLN D 1 REMARK 465 SER D 2 REMARK 465 GLN D 108 REMARK 465 PRO D 109 REMARK 465 LYS D 110 REMARK 465 ALA D 111 REMARK 465 ASN D 112 REMARK 465 PRO D 113 REMARK 465 THR D 114 REMARK 465 VAL D 115 REMARK 465 THR D 116 REMARK 465 LEU D 117 REMARK 465 PHE D 118 REMARK 465 PRO D 119 REMARK 465 PRO D 120 REMARK 465 SER D 121 REMARK 465 SER D 122 REMARK 465 GLU D 123 REMARK 465 GLU D 124 REMARK 465 LEU D 125 REMARK 465 GLN D 126 REMARK 465 ALA D 127 REMARK 465 ASN D 128 REMARK 465 LYS D 129 REMARK 465 ALA D 130 REMARK 465 THR D 131 REMARK 465 LEU D 132 REMARK 465 VAL D 133 REMARK 465 CYS D 134 REMARK 465 LEU D 135 REMARK 465 ILE D 136 REMARK 465 SER D 137 REMARK 465 ASP D 138 REMARK 465 PHE D 139 REMARK 465 TYR D 140 REMARK 465 PRO D 141 REMARK 465 GLY D 142 REMARK 465 ALA D 143 REMARK 465 VAL D 144 REMARK 465 THR D 145 REMARK 465 VAL D 146 REMARK 465 ALA D 147 REMARK 465 TRP D 148 REMARK 465 LYS D 149 REMARK 465 ALA D 150 REMARK 465 ASP D 151 REMARK 465 SER D 152 REMARK 465 SER D 153 REMARK 465 PRO D 154 REMARK 465 VAL D 155 REMARK 465 LYS D 156 REMARK 465 ALA D 157 REMARK 465 GLY D 158 REMARK 465 VAL D 159 REMARK 465 GLU D 160 REMARK 465 THR D 161 REMARK 465 THR D 162 REMARK 465 THR D 163 REMARK 465 PRO D 164 REMARK 465 SER D 165 REMARK 465 LYS D 166 REMARK 465 GLN D 167 REMARK 465 SER D 168 REMARK 465 ASN D 169 REMARK 465 ASN D 170 REMARK 465 LYS D 171 REMARK 465 TYR D 172 REMARK 465 ALA D 173 REMARK 465 ALA D 174 REMARK 465 SER D 175 REMARK 465 SER D 176 REMARK 465 TYR D 177 REMARK 465 LEU D 178 REMARK 465 SER D 179 REMARK 465 LEU D 180 REMARK 465 THR D 181 REMARK 465 PRO D 182 REMARK 465 GLU D 183 REMARK 465 GLN D 184 REMARK 465 TRP D 185 REMARK 465 LYS D 186 REMARK 465 SER D 187 REMARK 465 HIS D 188 REMARK 465 ARG D 189 REMARK 465 SER D 190 REMARK 465 TYR D 191 REMARK 465 SER D 192 REMARK 465 CYS D 193 REMARK 465 GLN D 194 REMARK 465 VAL D 195 REMARK 465 THR D 196 REMARK 465 HIS D 197 REMARK 465 GLU D 198 REMARK 465 GLY D 199 REMARK 465 SER D 200 REMARK 465 THR D 201 REMARK 465 VAL D 202 REMARK 465 GLU D 203 REMARK 465 LYS D 204 REMARK 465 THR D 205 REMARK 465 VAL D 206 REMARK 465 ALA D 207 REMARK 465 PRO D 208 REMARK 465 THR D 209 REMARK 465 GLU D 210 REMARK 465 CYS D 211 REMARK 465 SER D 212 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ARG H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLN L 108 REMARK 465 PRO L 109 REMARK 465 LYS L 110 REMARK 465 ALA L 111 REMARK 465 ASN L 112 REMARK 465 PRO L 113 REMARK 465 THR L 114 REMARK 465 VAL L 115 REMARK 465 THR L 116 REMARK 465 LEU L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 SER L 122 REMARK 465 GLU L 123 REMARK 465 GLU L 124 REMARK 465 LEU L 125 REMARK 465 GLN L 126 REMARK 465 ALA L 127 REMARK 465 ASN L 128 REMARK 465 LYS L 129 REMARK 465 ALA L 130 REMARK 465 THR L 131 REMARK 465 LEU L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 ILE L 136 REMARK 465 SER L 137 REMARK 465 ASP L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 GLY L 142 REMARK 465 ALA L 143 REMARK 465 VAL L 144 REMARK 465 THR L 145 REMARK 465 VAL L 146 REMARK 465 ALA L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 ALA L 150 REMARK 465 ASP L 151 REMARK 465 SER L 152 REMARK 465 SER L 153 REMARK 465 PRO L 154 REMARK 465 VAL L 155 REMARK 465 LYS L 156 REMARK 465 ALA L 157 REMARK 465 GLY L 158 REMARK 465 VAL L 159 REMARK 465 GLU L 160 REMARK 465 THR L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 PRO L 164 REMARK 465 SER L 165 REMARK 465 LYS L 166 REMARK 465 GLN L 167 REMARK 465 SER L 168 REMARK 465 ASN L 169 REMARK 465 ASN L 170 REMARK 465 LYS L 171 REMARK 465 TYR L 172 REMARK 465 ALA L 173 REMARK 465 ALA L 174 REMARK 465 SER L 175 REMARK 465 SER L 176 REMARK 465 TYR L 177 REMARK 465 LEU L 178 REMARK 465 SER L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 PRO L 182 REMARK 465 GLU L 183 REMARK 465 GLN L 184 REMARK 465 TRP L 185 REMARK 465 LYS L 186 REMARK 465 SER L 187 REMARK 465 HIS L 188 REMARK 465 ARG L 189 REMARK 465 SER L 190 REMARK 465 TYR L 191 REMARK 465 SER L 192 REMARK 465 CYS L 193 REMARK 465 GLN L 194 REMARK 465 VAL L 195 REMARK 465 THR L 196 REMARK 465 HIS L 197 REMARK 465 GLU L 198 REMARK 465 GLY L 199 REMARK 465 SER L 200 REMARK 465 THR L 201 REMARK 465 VAL L 202 REMARK 465 GLU L 203 REMARK 465 LYS L 204 REMARK 465 THR L 205 REMARK 465 VAL L 206 REMARK 465 ALA L 207 REMARK 465 PRO L 208 REMARK 465 THR L 209 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 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 O PCA C 1 N VAL C 2 1.56 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 B 257 CA - CB - SG ANGL. DEV. = 21.2 DEGREES REMARK 500 PCA C 1 O - C - N ANGL. DEV. = -48.0 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 ASN A 8 51.97 -92.55 REMARK 500 ALA A 18 -173.75 60.68 REMARK 500 HIS A 149 33.05 -94.50 REMARK 500 LEU A 173 75.33 45.51 REMARK 500 PRO A 174 131.28 -39.12 REMARK 500 SER A 184 75.27 -154.02 REMARK 500 MET A 199 -166.99 -125.75 REMARK 500 ASN A 201 31.32 -142.80 REMARK 500 ALA A 222 -162.17 50.97 REMARK 500 THR A 224 -24.88 -142.32 REMARK 500 THR A 226 107.16 -47.90 REMARK 500 ALA B 18 -169.22 60.25 REMARK 500 GLN B 46 -164.47 -79.22 REMARK 500 ASP B 71 139.70 -171.36 REMARK 500 LEU B 173 75.04 48.39 REMARK 500 GLU B 175 -7.31 75.81 REMARK 500 ALA B 222 -137.93 49.42 REMARK 500 THR B 224 0.05 -67.01 REMARK 500 SER B 271 -128.29 50.76 REMARK 500 SER C 7 -161.48 61.16 REMARK 500 PRO C 14 155.31 -46.71 REMARK 500 SER C 16 -159.87 59.76 REMARK 500 SER C 30 -108.55 48.50 REMARK 500 VAL D 27C -54.54 -127.31 REMARK 500 THR D 52 -8.83 73.89 REMARK 500 ALA D 84 -175.37 -172.05 REMARK 500 SER H 16 -176.86 72.17 REMARK 500 SER H 30 -109.21 48.06 REMARK 500 GLN H 39 114.91 -161.14 REMARK 500 ASP L 27B -158.03 -147.08 REMARK 500 THR L 52 -8.36 72.80 REMARK 500 ALA L 84 -169.68 -169.73 REMARK 500 TYR L 95 30.75 -140.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PCA C 1 51.67 REMARK 500 PCA H 1 -13.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70931 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF STABILIZED DENGUE 3 VIRUS ENVELOPE GLYCOPROTEIN REMARK 900 IN COMPLEX WITH FAB OF F25.S01 DBREF 9OWE A 1 397 UNP Q07019 Q07019_9FLAV 167 563 DBREF 9OWE B 1 397 UNP Q07019 Q07019_9FLAV 167 563 DBREF 9OWE C 1 225 PDB 9OWE 9OWE 1 225 DBREF 9OWE D 1 212 PDB 9OWE 9OWE 1 212 DBREF 9OWE H 1 225 PDB 9OWE 9OWE 1 225 DBREF 9OWE L 1 212 PDB 9OWE 9OWE 1 212 SEQADV 9OWE LYS A 29 UNP Q07019 GLY 195 CONFLICT SEQADV 9OWE VAL A 33 UNP Q07019 THR 199 CONFLICT SEQADV 9OWE MET A 35 UNP Q07019 ALA 201 CONFLICT SEQADV 9OWE ASP A 106 UNP Q07019 GLY 272 CONFLICT SEQADV 9OWE CYS A 257 UNP Q07019 ALA 423 CONFLICT SEQADV 9OWE TRP A 277 UNP Q07019 PHE 443 CONFLICT SEQADV 9OWE PRO A 278 UNP Q07019 ALA 444 CONFLICT SEQADV 9OWE GLY A 396 UNP Q07019 ILE 562 CONFLICT SEQADV 9OWE SER A 398 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 399 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 400 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 401 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 402 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 403 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 404 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 405 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS A 406 UNP Q07019 EXPRESSION TAG SEQADV 9OWE LYS B 29 UNP Q07019 GLY 195 CONFLICT SEQADV 9OWE VAL B 33 UNP Q07019 THR 199 CONFLICT SEQADV 9OWE MET B 35 UNP Q07019 ALA 201 CONFLICT SEQADV 9OWE ASP B 106 UNP Q07019 GLY 272 CONFLICT SEQADV 9OWE CYS B 257 UNP Q07019 ALA 423 CONFLICT SEQADV 9OWE TRP B 277 UNP Q07019 PHE 443 CONFLICT SEQADV 9OWE PRO B 278 UNP Q07019 ALA 444 CONFLICT SEQADV 9OWE GLY B 396 UNP Q07019 ILE 562 CONFLICT SEQADV 9OWE SER B 398 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 399 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 400 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 401 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 402 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 403 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 404 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 405 UNP Q07019 EXPRESSION TAG SEQADV 9OWE HIS B 406 UNP Q07019 EXPRESSION TAG SEQRES 1 A 406 MET ARG CYS VAL GLY VAL GLY ASN ARG ASP PHE VAL GLU SEQRES 2 A 406 GLY LEU SER GLY ALA THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 A 406 HIS GLY LYS CYS VAL THR VAL MET MET LYS ASN LYS PRO SEQRES 4 A 406 THR LEU ASP ILE GLU LEU GLN LYS THR GLU ALA THR GLN SEQRES 5 A 406 LEU ALA THR LEU ARG LYS LEU CYS ILE GLU GLY LYS ILE SEQRES 6 A 406 THR ASN ILE THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 406 GLU ALA ILE LEU PRO GLU GLU GLN ASP GLN ASN TYR VAL SEQRES 8 A 406 CYS LYS HIS THR TYR VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 406 CYS ASP LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 A 406 LYS PHE GLN CYS LEU GLU SER ILE GLU GLY LYS VAL VAL SEQRES 11 A 406 GLN HIS GLU ASN LEU LYS TYR THR VAL ILE ILE THR VAL SEQRES 12 A 406 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU THR GLN SEQRES 13 A 406 GLY VAL THR ALA GLU ILE THR PRO GLN ALA SER THR VAL SEQRES 14 A 406 GLU ALA ILE LEU PRO GLU TYR GLY THR LEU GLY LEU GLU SEQRES 15 A 406 CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU MET ILE SEQRES 16 A 406 LEU LEU THR MET LYS ASN LYS ALA TRP MET VAL HIS ARG SEQRES 17 A 406 GLN TRP PHE PHE ASP LEU PRO LEU PRO TRP THR SER GLY SEQRES 18 A 406 ALA THR THR GLU THR PRO THR TRP ASN ARG LYS GLU LEU SEQRES 19 A 406 LEU VAL THR PHE LYS ASN ALA HIS ALA LYS LYS GLN GLU SEQRES 20 A 406 VAL VAL VAL LEU GLY SER GLN GLU GLY CYS MET HIS THR SEQRES 21 A 406 ALA LEU THR GLY ALA THR GLU ILE GLN ASN SER GLY GLY SEQRES 22 A 406 THR SER ILE TRP PRO GLY HIS LEU LYS CYS ARG LEU LYS SEQRES 23 A 406 MET ASP LYS LEU GLU LEU LYS GLY MET SER TYR ALA MET SEQRES 24 A 406 CYS LEU ASN THR PHE VAL LEU LYS LYS GLU VAL SER GLU SEQRES 25 A 406 THR GLN HIS GLY THR ILE LEU ILE LYS VAL GLU TYR LYS SEQRES 26 A 406 GLY GLU ASP ALA PRO CYS LYS ILE PRO PHE SER THR GLU SEQRES 27 A 406 ASP GLY GLN GLY LYS ALA HIS ASN GLY ARG LEU ILE THR SEQRES 28 A 406 ALA ASN PRO VAL VAL THR LYS LYS GLU GLU PRO VAL ASN SEQRES 29 A 406 ILE GLU ALA GLU PRO PRO PHE GLY GLU SER ASN ILE VAL SEQRES 30 A 406 ILE GLY ILE GLY ASP LYS ALA LEU LYS ILE ASN TRP TYR SEQRES 31 A 406 LYS LYS GLY SER SER GLY GLY SER HIS HIS HIS HIS HIS SEQRES 32 A 406 HIS HIS HIS SEQRES 1 B 406 MET ARG CYS VAL GLY VAL GLY ASN ARG ASP PHE VAL GLU SEQRES 2 B 406 GLY LEU SER GLY ALA THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 B 406 HIS GLY LYS CYS VAL THR VAL MET MET LYS ASN LYS PRO SEQRES 4 B 406 THR LEU ASP ILE GLU LEU GLN LYS THR GLU ALA THR GLN SEQRES 5 B 406 LEU ALA THR LEU ARG LYS LEU CYS ILE GLU GLY LYS ILE SEQRES 6 B 406 THR ASN ILE THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 B 406 GLU ALA ILE LEU PRO GLU GLU GLN ASP GLN ASN TYR VAL SEQRES 8 B 406 CYS LYS HIS THR TYR VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 B 406 CYS ASP LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 B 406 LYS PHE GLN CYS LEU GLU SER ILE GLU GLY LYS VAL VAL SEQRES 11 B 406 GLN HIS GLU ASN LEU LYS TYR THR VAL ILE ILE THR VAL SEQRES 12 B 406 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU THR GLN SEQRES 13 B 406 GLY VAL THR ALA GLU ILE THR PRO GLN ALA SER THR VAL SEQRES 14 B 406 GLU ALA ILE LEU PRO GLU TYR GLY THR LEU GLY LEU GLU SEQRES 15 B 406 CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU MET ILE SEQRES 16 B 406 LEU LEU THR MET LYS ASN LYS ALA TRP MET VAL HIS ARG SEQRES 17 B 406 GLN TRP PHE PHE ASP LEU PRO LEU PRO TRP THR SER GLY SEQRES 18 B 406 ALA THR THR GLU THR PRO THR TRP ASN ARG LYS GLU LEU SEQRES 19 B 406 LEU VAL THR PHE LYS ASN ALA HIS ALA LYS LYS GLN GLU SEQRES 20 B 406 VAL VAL VAL LEU GLY SER GLN GLU GLY CYS MET HIS THR SEQRES 21 B 406 ALA LEU THR GLY ALA THR GLU ILE GLN ASN SER GLY GLY SEQRES 22 B 406 THR SER ILE TRP PRO GLY HIS LEU LYS CYS ARG LEU LYS SEQRES 23 B 406 MET ASP LYS LEU GLU LEU LYS GLY MET SER TYR ALA MET SEQRES 24 B 406 CYS LEU ASN THR PHE VAL LEU LYS LYS GLU VAL SER GLU SEQRES 25 B 406 THR GLN HIS GLY THR ILE LEU ILE LYS VAL GLU TYR LYS SEQRES 26 B 406 GLY GLU ASP ALA PRO CYS LYS ILE PRO PHE SER THR GLU SEQRES 27 B 406 ASP GLY GLN GLY LYS ALA HIS ASN GLY ARG LEU ILE THR SEQRES 28 B 406 ALA ASN PRO VAL VAL THR LYS LYS GLU GLU PRO VAL ASN SEQRES 29 B 406 ILE GLU ALA GLU PRO PRO PHE GLY GLU SER ASN ILE VAL SEQRES 30 B 406 ILE GLY ILE GLY ASP LYS ALA LEU LYS ILE ASN TRP TYR SEQRES 31 B 406 LYS LYS GLY SER SER GLY GLY SER HIS HIS HIS HIS HIS SEQRES 32 B 406 HIS HIS HIS SEQRES 1 C 238 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 238 PRO GLY SER SER ALA LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 238 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 C 238 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE MET SEQRES 5 C 238 PRO ILE PHE GLY THR VAL ASN TYR ALA GLN LYS PHE GLN SEQRES 6 C 238 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 C 238 ALA TYR MET GLU LEU SER ARG LEU ARG SER GLU ASP THR SEQRES 8 C 238 ALA VAL TYR PHE CYS ALA ARG GLY TRP GLY GLY ASN TYR SEQRES 9 C 238 ARG SER ALA ASP LEU TRP ILE TYR PHE ASP LEU TRP GLY SEQRES 10 C 238 GLN GLY THR LEU VAL THR VAL SER SER ARG SER THR LYS SEQRES 11 C 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 C 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 C 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 C 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 C 238 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 C 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 C 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 C 238 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 19 C 238 HIS HIS HIS HIS SEQRES 1 D 217 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 D 217 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 D 217 SER ASP VAL GLY GLY TYR LYS TYR VAL SER TRP TYR GLN SEQRES 4 D 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 D 217 VAL THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 D 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 D 217 SER TYR ALA GLY SER TYR THR HIS VAL VAL PHE GLY GLY SEQRES 9 D 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ASN SEQRES 10 D 217 PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 D 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 D 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 D 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 D 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 D 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 D 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 D 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 238 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 238 PRO GLY SER SER ALA LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 238 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 238 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE MET SEQRES 5 H 238 PRO ILE PHE GLY THR VAL ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 238 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 238 ALA TYR MET GLU LEU SER ARG LEU ARG SER GLU ASP THR SEQRES 8 H 238 ALA VAL TYR PHE CYS ALA ARG GLY TRP GLY GLY ASN TYR SEQRES 9 H 238 ARG SER ALA ASP LEU TRP ILE TYR PHE ASP LEU TRP GLY SEQRES 10 H 238 GLN GLY THR LEU VAL THR VAL SER SER ARG SER THR LYS SEQRES 11 H 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 238 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 238 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 19 H 238 HIS HIS HIS HIS SEQRES 1 L 217 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 L 217 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 L 217 SER ASP VAL GLY GLY TYR LYS TYR VAL SER TRP TYR GLN SEQRES 4 L 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 L 217 VAL THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 L 217 SER TYR ALA GLY SER TYR THR HIS VAL VAL PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ASN SEQRES 10 L 217 PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER HET PCA C 1 13 HET PCA H 1 13 HET NAG E 1 27 HET NAG E 2 27 HET BMA E 3 22 HET NAG F 1 27 HET NAG F 2 27 HET BMA F 3 22 HET NAG A 501 28 HET NAG B 501 28 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 3 PCA 2(C5 H7 N O3) FORMUL 7 NAG 6(C8 H15 N O6) FORMUL 7 BMA 2(C6 H12 O6) HELIX 1 AA1 CYS A 74 GLY A 78 5 5 HELIX 2 AA2 LEU A 82 ASP A 87 5 6 HELIX 3 AA3 GLY A 100 GLY A 104 5 5 HELIX 4 AA4 GLN A 131 GLU A 133 5 3 HELIX 5 AA5 ASP A 147 VAL A 151 5 5 HELIX 6 AA6 THR A 163 ALA A 166 5 4 HELIX 7 AA7 ASP A 190 ASN A 192 5 3 HELIX 8 AA8 ARG A 208 LEU A 214 1 7 HELIX 9 AA9 ARG A 231 LEU A 234 5 4 HELIX 10 AB1 GLN A 254 LEU A 262 1 9 HELIX 11 AB2 ILE A 380 ALA A 384 5 5 HELIX 12 AB3 CYS B 74 GLY B 78 5 5 HELIX 13 AB4 LEU B 82 ASP B 87 5 6 HELIX 14 AB5 GLY B 100 GLY B 104 5 5 HELIX 15 AB6 GLN B 131 GLU B 133 5 3 HELIX 16 AB7 THR B 163 SER B 167 5 5 HELIX 17 AB8 ASP B 190 ASN B 192 5 3 HELIX 18 AB9 ARG B 208 ASP B 213 1 6 HELIX 19 AC1 ARG B 231 LEU B 234 5 4 HELIX 20 AC2 GLN B 254 THR B 263 1 10 HELIX 21 AC3 ILE B 380 ALA B 384 5 5 HELIX 22 AC4 GLN C 61 GLN C 64 5 4 HELIX 23 AC5 ARG C 83 THR C 87 5 5 HELIX 24 AC6 ALA C 100C ILE C 100G 5 5 HELIX 25 AC7 GLN D 79 GLU D 83 5 5 HELIX 26 AC8 GLN H 61 GLN H 64 5 4 HELIX 27 AC9 ARG H 83 THR H 87 5 5 HELIX 28 AD1 ASP H 100D TYR H 100H 5 5 SHEET 1 AA1 5 ARG A 9 VAL A 12 0 SHEET 2 AA1 5 CYS A 30 MET A 35 1 O THR A 32 N VAL A 12 SHEET 3 AA1 5 LYS A 38 ALA A 50 -1 O LEU A 41 N VAL A 33 SHEET 4 AA1 5 LEU A 135 VAL A 143 -1 O THR A 142 N ASP A 42 SHEET 5 AA1 5 VAL A 158 ILE A 162 -1 O ILE A 162 N TYR A 137 SHEET 1 AA2 4 TRP A 20 LEU A 25 0 SHEET 2 AA2 4 LEU A 281 LYS A 286 -1 O LEU A 281 N LEU A 25 SHEET 3 AA2 4 GLY A 180 CYS A 183 -1 N GLU A 182 O ARG A 284 SHEET 4 AA2 4 THR A 168 GLU A 170 -1 N VAL A 169 O LEU A 181 SHEET 1 AA3 4 TYR A 90 ARG A 99 0 SHEET 2 AA3 4 GLY A 109 VAL A 129 -1 O GLY A 109 N ARG A 99 SHEET 3 AA3 4 MET A 194 THR A 198 -1 O LEU A 196 N LYS A 128 SHEET 4 AA3 4 ALA A 203 HIS A 207 -1 O TRP A 204 N LEU A 197 SHEET 1 AA4 4 TYR A 90 ARG A 99 0 SHEET 2 AA4 4 GLY A 109 VAL A 129 -1 O GLY A 109 N ARG A 99 SHEET 3 AA4 4 ALA A 54 SER A 72 -1 N ARG A 57 O GLY A 127 SHEET 4 AA4 4 TRP A 218 THR A 219 -1 O THR A 219 N LYS A 58 SHEET 1 AA5 2 VAL A 236 ASN A 240 0 SHEET 2 AA5 2 GLN A 246 VAL A 250 -1 O VAL A 249 N THR A 237 SHEET 1 AA6 2 GLN A 269 SER A 271 0 SHEET 2 AA6 2 THR A 274 ILE A 276 -1 O THR A 274 N SER A 271 SHEET 1 AA7 3 ALA A 298 MET A 299 0 SHEET 2 AA7 3 CYS A 331 LYS A 332 1 O LYS A 332 N ALA A 298 SHEET 3 AA7 3 VAL A 355 VAL A 356 -1 O VAL A 356 N CYS A 331 SHEET 1 AA8 3 PHE A 304 VAL A 305 0 SHEET 2 AA8 3 ILE A 318 TYR A 324 -1 N GLU A 323 O VAL A 305 SHEET 3 AA8 3 VAL A 363 ALA A 367 -1 O ALA A 367 N ILE A 318 SHEET 1 AA9 3 PHE A 335 ASP A 339 0 SHEET 2 AA9 3 SER A 374 ILE A 378 -1 O VAL A 377 N SER A 336 SHEET 3 AA9 3 ILE A 387 TRP A 389 -1 O TRP A 389 N SER A 374 SHEET 1 AB1 5 ARG B 9 VAL B 12 0 SHEET 2 AB1 5 CYS B 30 MET B 35 1 O THR B 32 N VAL B 12 SHEET 3 AB1 5 LYS B 38 ALA B 50 -1 O LEU B 41 N VAL B 33 SHEET 4 AB1 5 LEU B 135 VAL B 143 -1 O LYS B 136 N GLU B 49 SHEET 5 AB1 5 VAL B 158 ILE B 162 -1 O ILE B 162 N TYR B 137 SHEET 1 AB2 2 VAL B 23 LEU B 25 0 SHEET 2 AB2 2 LEU B 281 CYS B 283 -1 O LEU B 281 N LEU B 25 SHEET 1 AB3 4 TYR B 90 ARG B 99 0 SHEET 2 AB3 4 GLY B 109 VAL B 129 -1 O GLY B 111 N VAL B 97 SHEET 3 AB3 4 MET B 194 THR B 198 -1 O THR B 198 N GLU B 126 SHEET 4 AB3 4 ALA B 203 HIS B 207 -1 O VAL B 206 N ILE B 195 SHEET 1 AB4 4 TYR B 90 ARG B 99 0 SHEET 2 AB4 4 GLY B 109 VAL B 129 -1 O GLY B 111 N VAL B 97 SHEET 3 AB4 4 ALA B 54 SER B 72 -1 N ILE B 61 O GLU B 123 SHEET 4 AB4 4 TRP B 218 SER B 220 -1 O THR B 219 N LYS B 58 SHEET 1 AB5 3 GLU B 170 ALA B 171 0 SHEET 2 AB5 3 GLY B 177 GLY B 180 -1 O LEU B 179 N ALA B 171 SHEET 3 AB5 3 LYS B 286 LEU B 290 -1 O LYS B 286 N GLY B 180 SHEET 1 AB6 2 VAL B 236 THR B 237 0 SHEET 2 AB6 2 VAL B 249 VAL B 250 -1 O VAL B 249 N THR B 237 SHEET 1 AB7 3 PHE B 304 SER B 311 0 SHEET 2 AB7 3 ILE B 318 TYR B 324 -1 O GLU B 323 N VAL B 305 SHEET 3 AB7 3 VAL B 363 ALA B 367 -1 O ILE B 365 N ILE B 320 SHEET 1 AB8 2 CYS B 331 LYS B 332 0 SHEET 2 AB8 2 VAL B 355 VAL B 356 -1 O VAL B 356 N CYS B 331 SHEET 1 AB9 3 PHE B 335 GLU B 338 0 SHEET 2 AB9 3 GLU B 373 ILE B 378 -1 O VAL B 377 N SER B 336 SHEET 3 AB9 3 ILE B 387 TYR B 390 -1 O ILE B 387 N ILE B 376 SHEET 1 AC1 4 GLN C 3 VAL C 5 0 SHEET 2 AC1 4 SER C 17 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AC1 4 THR C 77 SER C 82A-1 O ALA C 78 N CYS C 22 SHEET 4 AC1 4 VAL C 67 ASP C 72 -1 N THR C 68 O GLU C 81 SHEET 1 AC2 5 VAL C 57 TYR C 59 0 SHEET 2 AC2 5 LEU C 45 ILE C 51 -1 N SER C 50 O ASN C 58 SHEET 3 AC2 5 ILE C 34 GLN C 39 -1 N TRP C 36 O MET C 48 SHEET 4 AC2 5 ALA C 88 ARG C 94 -1 O ALA C 93 N SER C 35 SHEET 5 AC2 5 THR C 107 VAL C 109 -1 O THR C 107 N TYR C 90 SHEET 1 AC3 5 SER D 9 GLY D 13 0 SHEET 2 AC3 5 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC3 5 ASP D 85 SER D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AC3 5 SER D 34 GLN D 38 -1 N GLN D 38 O ASP D 85 SHEET 5 AC3 5 PRO D 44 ILE D 48 -1 O ILE D 48 N TRP D 35 SHEET 1 AC4 4 SER D 9 GLY D 13 0 SHEET 2 AC4 4 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC4 4 ASP D 85 SER D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AC4 4 VAL D 97 PHE D 98 -1 O VAL D 97 N SER D 90 SHEET 1 AC5 3 VAL D 19 THR D 24 0 SHEET 2 AC5 3 THR D 70 ILE D 75 -1 O ALA D 71 N CYS D 23 SHEET 3 AC5 3 SER D 63 SER D 67 -1 N SER D 67 O THR D 70 SHEET 1 AC6 4 GLN H 3 GLN H 6 0 SHEET 2 AC6 4 VAL H 20 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AC6 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AC6 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AC7 6 GLU H 10 VAL H 11 0 SHEET 2 AC7 6 THR H 107 THR H 110 1 O LEU H 108 N GLU H 10 SHEET 3 AC7 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AC7 6 ILE H 34 GLN H 39 -1 N SER H 35 O ALA H 93 SHEET 5 AC7 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AC7 6 VAL H 57 TYR H 59 -1 O ASN H 58 N SER H 50 SHEET 1 AC8 5 SER L 9 GLY L 13 0 SHEET 2 AC8 5 THR L 102 VAL L 106 1 O THR L 105 N GLY L 13 SHEET 3 AC8 5 ASP L 85 SER L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC8 5 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AC8 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AC9 4 SER L 9 GLY L 13 0 SHEET 2 AC9 4 THR L 102 VAL L 106 1 O THR L 105 N GLY L 13 SHEET 3 AC9 4 ASP L 85 SER L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC9 4 VAL L 97 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AD1 3 SER L 18 THR L 24 0 SHEET 2 AD1 3 THR L 70 SER L 76 -1 O ILE L 75 N VAL L 19 SHEET 3 AD1 3 PHE L 62 LYS L 66 -1 N SER L 63 O THR L 74 SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.03 SSBOND 2 CYS A 60 CYS A 121 1555 1555 2.03 SSBOND 3 CYS A 74 CYS A 105 1555 1555 2.04 SSBOND 4 CYS A 92 CYS A 116 1555 1555 2.03 SSBOND 5 CYS A 183 CYS A 283 1555 1555 2.03 SSBOND 6 CYS A 257 CYS B 257 1555 1555 2.03 SSBOND 7 CYS A 300 CYS A 331 1555 1555 2.03 SSBOND 8 CYS B 3 CYS B 30 1555 1555 2.03 SSBOND 9 CYS B 60 CYS B 121 1555 1555 2.03 SSBOND 10 CYS B 74 CYS B 105 1555 1555 2.04 SSBOND 11 CYS B 92 CYS B 116 1555 1555 2.03 SSBOND 12 CYS B 183 CYS B 283 1555 1555 2.03 SSBOND 13 CYS B 300 CYS B 331 1555 1555 2.03 SSBOND 14 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 17 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 67 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 153 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN B 67 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 153 C1 NAG F 1 1555 1555 1.44 LINK C PCA C 1 N VAL C 2 1555 1555 1.33 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 CISPEP 1 ALA A 329 PRO A 330 0 -0.79 CISPEP 2 ALA B 329 PRO B 330 0 1.19 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