HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 30-NOV-21 7T0W TITLE COMPLEX OF GABA-A SYNAPTIC RECEPTOR WITH AUTOIMMUNE ANTIBODY FAB115 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-2; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 8 CHAIN: B, D; COMPND 9 SYNONYM: GABA(A) RECEPTOR SUBUNIT ALPHA-1; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT GAMMA-2; COMPND 13 CHAIN: E; COMPND 14 SYNONYM: GABA(A) RECEPTOR SUBUNIT GAMMA-2; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: FAB115 LIGHT CHAIN, IGG1; COMPND 18 CHAIN: L2, L; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: FAB115 HEAVY CHAIN, IGG1; COMPND 22 CHAIN: H, H2; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GABRB2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GABRA1; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GABRG2; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 MOL_ID: 5; SOURCE 33 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 34 ORGANISM_COMMON: HUMAN; SOURCE 35 ORGANISM_TAXID: 9606; SOURCE 36 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 37 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS AUTOIMMUNITY, ENCEPHALITIS, GABA, INHIBITORY, MEMBRANE PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR C.M.NOVIELLO,R.E.HIBBS,J.KREYE,J.TENG,H.PRUSS JRNL AUTH C.M.NOVIELLO,J.KREYE,J.TENG,H.PRUSS,R.E.HIBBS JRNL TITL STRUCTURAL MECHANISMS OF GABA A RECEPTOR AUTOIMMUNE JRNL TITL 2 ENCEPHALITIS. JRNL REF CELL V. 185 2469 2022 JRNL REFN ISSN 1097-4172 JRNL PMID 35803245 JRNL DOI 10.1016/J.CELL.2022.06.025 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, RELION 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 788748 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 7T0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000261404. 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 BETWEEN AUTOANTIBODY REMARK 245 FAB115 AND THE A2B2G2 GABA-A REMARK 245 RECEPTOR 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 : 7.40 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 K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 40.00 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, L2, H, H2, L, REMARK 350 AND CHAINS: F, G, I, J, K, M, N 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 GLN A 1 REMARK 465 SER A 2 REMARK 465 VAL A 3 REMARK 465 ASN A 4 REMARK 465 ASP A 5 REMARK 465 PRO A 6 REMARK 465 GLN B 1 REMARK 465 PRO B 2 REMARK 465 SER B 3 REMARK 465 LEU B 4 REMARK 465 GLN B 5 REMARK 465 ASP B 6 REMARK 465 GLU B 7 REMARK 465 LEU B 8 REMARK 465 LYS B 9 REMARK 465 GLN C 1 REMARK 465 SER C 2 REMARK 465 VAL C 3 REMARK 465 ASN C 4 REMARK 465 ASP C 5 REMARK 465 PRO C 6 REMARK 465 GLN D 1 REMARK 465 PRO D 2 REMARK 465 SER D 3 REMARK 465 LEU D 4 REMARK 465 GLN D 5 REMARK 465 ASP D 6 REMARK 465 GLU D 7 REMARK 465 LEU D 8 REMARK 465 LYS D 9 REMARK 465 TRP E -36 REMARK 465 SER E -35 REMARK 465 HIS E -34 REMARK 465 PRO E -33 REMARK 465 GLN E -32 REMARK 465 PHE E -31 REMARK 465 GLU E -30 REMARK 465 LYS E -29 REMARK 465 GLY E -28 REMARK 465 GLY E -27 REMARK 465 GLY E -26 REMARK 465 SER E -25 REMARK 465 GLY E -24 REMARK 465 GLY E -23 REMARK 465 GLY E -22 REMARK 465 SER E -21 REMARK 465 GLY E -20 REMARK 465 GLY E -19 REMARK 465 SER E -18 REMARK 465 SER E -17 REMARK 465 ALA E -16 REMARK 465 TRP E -15 REMARK 465 SER E -14 REMARK 465 HIS E -13 REMARK 465 PRO E -12 REMARK 465 GLN E -11 REMARK 465 PHE E -10 REMARK 465 GLU E -9 REMARK 465 LYS E -8 REMARK 465 LEU E -7 REMARK 465 GLU E -6 REMARK 465 VAL E -5 REMARK 465 LEU E -4 REMARK 465 PHE E -3 REMARK 465 GLN E -2 REMARK 465 GLY E -1 REMARK 465 PRO E 0 REMARK 465 GLN E 1 REMARK 465 LYS E 2 REMARK 465 SER E 3 REMARK 465 ASP E 4 REMARK 465 ASP E 5 REMARK 465 ASP E 6 REMARK 465 TYR E 7 REMARK 465 GLU E 8 REMARK 465 ASP E 9 REMARK 465 TYR E 10 REMARK 465 ALA E 11 REMARK 465 SER E 12 REMARK 465 ASN E 13 REMARK 465 LYS E 14 REMARK 465 THR E 15 REMARK 465 TRP E 16 REMARK 465 VAL E 17 REMARK 465 LEU E 18 REMARK 465 THR E 19 REMARK 465 PRO E 20 REMARK 465 LYS E 21 REMARK 465 VAL E 22 REMARK 465 PRO E 23 REMARK 465 GLU E 24 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLN L 113 REMARK 465 PRO L 114 REMARK 465 LYS L 115 REMARK 465 ALA L 116 REMARK 465 ALA L 117 REMARK 465 PRO L 118 REMARK 465 SER L 119 REMARK 465 VAL L 120 REMARK 465 THR L 121 REMARK 465 LEU L 122 REMARK 465 PHE L 123 REMARK 465 PRO L 124 REMARK 465 PRO L 125 REMARK 465 SER L 126 REMARK 465 SER L 127 REMARK 465 GLU L 128 REMARK 465 GLU L 129 REMARK 465 LEU L 130 REMARK 465 GLN L 131 REMARK 465 ALA L 132 REMARK 465 ASN L 133 REMARK 465 LYS L 134 REMARK 465 ALA L 135 REMARK 465 THR L 136 REMARK 465 LEU L 137 REMARK 465 VAL L 138 REMARK 465 CYS L 139 REMARK 465 LEU L 140 REMARK 465 ILE L 141 REMARK 465 SER L 142 REMARK 465 ASP L 143 REMARK 465 PHE L 144 REMARK 465 TYR L 145 REMARK 465 PRO L 146 REMARK 465 GLY L 147 REMARK 465 ALA L 148 REMARK 465 VAL L 149 REMARK 465 THR L 150 REMARK 465 VAL L 151 REMARK 465 ALA L 152 REMARK 465 TRP L 153 REMARK 465 LYS L 154 REMARK 465 ALA L 155 REMARK 465 ASP L 156 REMARK 465 SER L 157 REMARK 465 SER L 158 REMARK 465 PRO L 159 REMARK 465 VAL L 160 REMARK 465 LYS L 161 REMARK 465 ALA L 162 REMARK 465 GLY L 163 REMARK 465 VAL L 164 REMARK 465 GLU L 165 REMARK 465 THR L 166 REMARK 465 THR L 167 REMARK 465 THR L 168 REMARK 465 PRO L 169 REMARK 465 SER L 170 REMARK 465 LYS L 171 REMARK 465 GLN L 172 REMARK 465 SER L 173 REMARK 465 ASN L 174 REMARK 465 ASN L 175 REMARK 465 LYS L 176 REMARK 465 TYR L 177 REMARK 465 ALA L 178 REMARK 465 ALA L 179 REMARK 465 SER L 180 REMARK 465 SER L 181 REMARK 465 TYR L 182 REMARK 465 LEU L 183 REMARK 465 SER L 184 REMARK 465 LEU L 185 REMARK 465 THR L 186 REMARK 465 PRO L 187 REMARK 465 GLU L 188 REMARK 465 GLN L 189 REMARK 465 TRP L 190 REMARK 465 LYS L 191 REMARK 465 SER L 192 REMARK 465 HIS L 193 REMARK 465 ARG L 194 REMARK 465 SER L 195 REMARK 465 TYR L 196 REMARK 465 SER L 197 REMARK 465 CYS L 198 REMARK 465 GLN L 199 REMARK 465 VAL L 200 REMARK 465 THR L 201 REMARK 465 HIS L 202 REMARK 465 GLU L 203 REMARK 465 GLY L 204 REMARK 465 SER L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 GLU L 208 REMARK 465 LYS L 209 REMARK 465 THR L 210 REMARK 465 VAL L 211 REMARK 465 ALA L 212 REMARK 465 PRO L 213 REMARK 465 THR L 214 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 SER L 217 REMARK 465 GLN H 1 REMARK 465 VAL H 123 REMARK 465 SER H 124 REMARK 465 SER H 125 REMARK 465 ALA H 126 REMARK 465 SER H 127 REMARK 465 THR H 128 REMARK 465 LYS H 129 REMARK 465 GLY H 130 REMARK 465 PRO H 131 REMARK 465 SER H 132 REMARK 465 VAL H 133 REMARK 465 PHE H 134 REMARK 465 PRO H 135 REMARK 465 LEU H 136 REMARK 465 ALA H 137 REMARK 465 PRO H 138 REMARK 465 SER H 139 REMARK 465 SER H 140 REMARK 465 LYS H 141 REMARK 465 SER H 142 REMARK 465 THR H 143 REMARK 465 SER H 144 REMARK 465 GLY H 145 REMARK 465 GLY H 146 REMARK 465 THR H 147 REMARK 465 ALA H 148 REMARK 465 ALA H 149 REMARK 465 LEU H 150 REMARK 465 GLY H 151 REMARK 465 CYS H 152 REMARK 465 LEU H 153 REMARK 465 VAL H 154 REMARK 465 LYS H 155 REMARK 465 ASP H 156 REMARK 465 TYR H 157 REMARK 465 PHE H 158 REMARK 465 PRO H 159 REMARK 465 GLU H 160 REMARK 465 PRO H 161 REMARK 465 VAL H 162 REMARK 465 THR H 163 REMARK 465 VAL H 164 REMARK 465 SER H 165 REMARK 465 TRP H 166 REMARK 465 ASN H 167 REMARK 465 SER H 168 REMARK 465 GLY H 169 REMARK 465 ALA H 170 REMARK 465 LEU H 171 REMARK 465 THR H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 VAL H 175 REMARK 465 HIS H 176 REMARK 465 THR H 177 REMARK 465 PHE H 178 REMARK 465 PRO H 179 REMARK 465 ALA H 180 REMARK 465 VAL H 181 REMARK 465 LEU H 182 REMARK 465 GLN H 183 REMARK 465 SER H 184 REMARK 465 SER H 185 REMARK 465 GLY H 186 REMARK 465 LEU H 187 REMARK 465 TYR H 188 REMARK 465 SER H 189 REMARK 465 LEU H 190 REMARK 465 SER H 191 REMARK 465 SER H 192 REMARK 465 VAL H 193 REMARK 465 VAL H 194 REMARK 465 THR H 195 REMARK 465 VAL H 196 REMARK 465 PRO H 197 REMARK 465 SER H 198 REMARK 465 SER H 199 REMARK 465 SER H 200 REMARK 465 LEU H 201 REMARK 465 GLY H 202 REMARK 465 THR H 203 REMARK 465 GLN H 204 REMARK 465 THR H 205 REMARK 465 TYR H 206 REMARK 465 ILE H 207 REMARK 465 CYS H 208 REMARK 465 ASN H 209 REMARK 465 VAL H 210 REMARK 465 ASN H 211 REMARK 465 HIS H 212 REMARK 465 LYS H 213 REMARK 465 PRO H 214 REMARK 465 SER H 215 REMARK 465 ASN H 216 REMARK 465 THR H 217 REMARK 465 LYS H 218 REMARK 465 VAL H 219 REMARK 465 ASP H 220 REMARK 465 LYS H 221 REMARK 465 ARG H 222 REMARK 465 VAL H 223 REMARK 465 GLU H 224 REMARK 465 PRO H 225 REMARK 465 LYS H 226 REMARK 465 SER H 227 REMARK 465 CYS H 228 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 ASP H 233 REMARK 465 TYR H 234 REMARK 465 LYS H 235 REMARK 465 ASP H 236 REMARK 465 ASP H 237 REMARK 465 ASP H 238 REMARK 465 ASP H 239 REMARK 465 LYS H 240 REMARK 465 HIS H 241 REMARK 465 HIS H 242 REMARK 465 HIS H 243 REMARK 465 HIS H 244 REMARK 465 HIS H 245 REMARK 465 HIS H 246 REMARK 465 GLN H 1 REMARK 465 VAL H 123 REMARK 465 SER H 124 REMARK 465 SER H 125 REMARK 465 ALA H 126 REMARK 465 SER H 127 REMARK 465 THR H 128 REMARK 465 LYS H 129 REMARK 465 GLY H 130 REMARK 465 PRO H 131 REMARK 465 SER H 132 REMARK 465 VAL H 133 REMARK 465 PHE H 134 REMARK 465 PRO H 135 REMARK 465 LEU H 136 REMARK 465 ALA H 137 REMARK 465 PRO H 138 REMARK 465 SER H 139 REMARK 465 SER H 140 REMARK 465 LYS H 141 REMARK 465 SER H 142 REMARK 465 THR H 143 REMARK 465 SER H 144 REMARK 465 GLY H 145 REMARK 465 GLY H 146 REMARK 465 THR H 147 REMARK 465 ALA H 148 REMARK 465 ALA H 149 REMARK 465 LEU H 150 REMARK 465 GLY H 151 REMARK 465 CYS H 152 REMARK 465 LEU H 153 REMARK 465 VAL H 154 REMARK 465 LYS H 155 REMARK 465 ASP H 156 REMARK 465 TYR H 157 REMARK 465 PHE H 158 REMARK 465 PRO H 159 REMARK 465 GLU H 160 REMARK 465 PRO H 161 REMARK 465 VAL H 162 REMARK 465 THR H 163 REMARK 465 VAL H 164 REMARK 465 SER H 165 REMARK 465 TRP H 166 REMARK 465 ASN H 167 REMARK 465 SER H 168 REMARK 465 GLY H 169 REMARK 465 ALA H 170 REMARK 465 LEU H 171 REMARK 465 THR H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 VAL H 175 REMARK 465 HIS H 176 REMARK 465 THR H 177 REMARK 465 PHE H 178 REMARK 465 PRO H 179 REMARK 465 ALA H 180 REMARK 465 VAL H 181 REMARK 465 LEU H 182 REMARK 465 GLN H 183 REMARK 465 SER H 184 REMARK 465 SER H 185 REMARK 465 GLY H 186 REMARK 465 LEU H 187 REMARK 465 TYR H 188 REMARK 465 SER H 189 REMARK 465 LEU H 190 REMARK 465 SER H 191 REMARK 465 SER H 192 REMARK 465 VAL H 193 REMARK 465 VAL H 194 REMARK 465 THR H 195 REMARK 465 VAL H 196 REMARK 465 PRO H 197 REMARK 465 SER H 198 REMARK 465 SER H 199 REMARK 465 SER H 200 REMARK 465 LEU H 201 REMARK 465 GLY H 202 REMARK 465 THR H 203 REMARK 465 GLN H 204 REMARK 465 THR H 205 REMARK 465 TYR H 206 REMARK 465 ILE H 207 REMARK 465 CYS H 208 REMARK 465 ASN H 209 REMARK 465 VAL H 210 REMARK 465 ASN H 211 REMARK 465 HIS H 212 REMARK 465 LYS H 213 REMARK 465 PRO H 214 REMARK 465 SER H 215 REMARK 465 ASN H 216 REMARK 465 THR H 217 REMARK 465 LYS H 218 REMARK 465 VAL H 219 REMARK 465 ASP H 220 REMARK 465 LYS H 221 REMARK 465 ARG H 222 REMARK 465 VAL H 223 REMARK 465 GLU H 224 REMARK 465 PRO H 225 REMARK 465 LYS H 226 REMARK 465 SER H 227 REMARK 465 CYS H 228 REMARK 465 ASP H 229 REMARK 465 LYS H 230 REMARK 465 THR H 231 REMARK 465 HIS H 232 REMARK 465 ASP H 233 REMARK 465 TYR H 234 REMARK 465 LYS H 235 REMARK 465 ASP H 236 REMARK 465 ASP H 237 REMARK 465 ASP H 238 REMARK 465 ASP H 239 REMARK 465 LYS H 240 REMARK 465 HIS H 241 REMARK 465 HIS H 242 REMARK 465 HIS H 243 REMARK 465 HIS H 244 REMARK 465 HIS H 245 REMARK 465 HIS H 246 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLN L 113 REMARK 465 PRO L 114 REMARK 465 LYS L 115 REMARK 465 ALA L 116 REMARK 465 ALA L 117 REMARK 465 PRO L 118 REMARK 465 SER L 119 REMARK 465 VAL L 120 REMARK 465 THR L 121 REMARK 465 LEU L 122 REMARK 465 PHE L 123 REMARK 465 PRO L 124 REMARK 465 PRO L 125 REMARK 465 SER L 126 REMARK 465 SER L 127 REMARK 465 GLU L 128 REMARK 465 GLU L 129 REMARK 465 LEU L 130 REMARK 465 GLN L 131 REMARK 465 ALA L 132 REMARK 465 ASN L 133 REMARK 465 LYS L 134 REMARK 465 ALA L 135 REMARK 465 THR L 136 REMARK 465 LEU L 137 REMARK 465 VAL L 138 REMARK 465 CYS L 139 REMARK 465 LEU L 140 REMARK 465 ILE L 141 REMARK 465 SER L 142 REMARK 465 ASP L 143 REMARK 465 PHE L 144 REMARK 465 TYR L 145 REMARK 465 PRO L 146 REMARK 465 GLY L 147 REMARK 465 ALA L 148 REMARK 465 VAL L 149 REMARK 465 THR L 150 REMARK 465 VAL L 151 REMARK 465 ALA L 152 REMARK 465 TRP L 153 REMARK 465 LYS L 154 REMARK 465 ALA L 155 REMARK 465 ASP L 156 REMARK 465 SER L 157 REMARK 465 SER L 158 REMARK 465 PRO L 159 REMARK 465 VAL L 160 REMARK 465 LYS L 161 REMARK 465 ALA L 162 REMARK 465 GLY L 163 REMARK 465 VAL L 164 REMARK 465 GLU L 165 REMARK 465 THR L 166 REMARK 465 THR L 167 REMARK 465 THR L 168 REMARK 465 PRO L 169 REMARK 465 SER L 170 REMARK 465 LYS L 171 REMARK 465 GLN L 172 REMARK 465 SER L 173 REMARK 465 ASN L 174 REMARK 465 ASN L 175 REMARK 465 LYS L 176 REMARK 465 TYR L 177 REMARK 465 ALA L 178 REMARK 465 ALA L 179 REMARK 465 SER L 180 REMARK 465 SER L 181 REMARK 465 TYR L 182 REMARK 465 LEU L 183 REMARK 465 SER L 184 REMARK 465 LEU L 185 REMARK 465 THR L 186 REMARK 465 PRO L 187 REMARK 465 GLU L 188 REMARK 465 GLN L 189 REMARK 465 TRP L 190 REMARK 465 LYS L 191 REMARK 465 SER L 192 REMARK 465 HIS L 193 REMARK 465 ARG L 194 REMARK 465 SER L 195 REMARK 465 TYR L 196 REMARK 465 SER L 197 REMARK 465 CYS L 198 REMARK 465 GLN L 199 REMARK 465 VAL L 200 REMARK 465 THR L 201 REMARK 465 HIS L 202 REMARK 465 GLU L 203 REMARK 465 GLY L 204 REMARK 465 SER L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 GLU L 208 REMARK 465 LYS L 209 REMARK 465 THR L 210 REMARK 465 VAL L 211 REMARK 465 ALA L 212 REMARK 465 PRO L 213 REMARK 465 THR L 214 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 SER L 217 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 HD22 ASN A 149 C1 NAG M 1 0.59 REMARK 500 HD22 ASN A 80 C1 NAG F 1 0.60 REMARK 500 OH TYRH2 60 H METH2 70 1.49 REMARK 500 O THR C 233 HG SER C 236 1.53 REMARK 500 O ALA E 295 HH TYR E 350 1.54 REMARK 500 OE1 GLU A 155 HH21 ARG A 207 1.56 REMARK 500 OD1 ASP C 121 HG1 THR C 123 1.57 REMARK 500 O ALA D 273 HG SER D 276 1.58 REMARK 500 O PHE A 221 HG1 THR A 225 1.58 REMARK 500 HH TYR C 23 OD2 ASP C 69 1.59 REMARK 500 OH TYRL2 37 H PHEH2 112 1.60 REMARK 500 OE1 GLU D 59 HH11 ARG D 136 1.60 REMARK 500 O GLYL2 24 OG1 THRL2 70 2.04 REMARK 500 OD1 ASP C 43 OG1 THR C 176 2.06 REMARK 500 NH2 ARGL2 62 OD1 ASPL2 83 2.15 REMARK 500 O ALA E 295 OH TYR E 350 2.17 REMARK 500 OE1 GLN H 6 O GLN H 117 2.19 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 LEU A 72 51.17 -90.16 REMARK 500 ASP A 171 -9.47 74.39 REMARK 500 ASP A 172 -32.12 -131.16 REMARK 500 THR A 225 -36.98 -131.09 REMARK 500 ASP B 98 58.57 -93.77 REMARK 500 LYS B 106 111.35 -161.22 REMARK 500 ALA B 161 -8.88 77.86 REMARK 500 ARG B 173 -153.49 -134.01 REMARK 500 LYS B 279 81.78 -69.85 REMARK 500 LYS B 312 -10.54 77.46 REMARK 500 SER C 46 147.32 -170.39 REMARK 500 LEU C 72 55.36 -96.12 REMARK 500 ASP C 171 -11.66 74.98 REMARK 500 PRO C 276 21.59 -76.60 REMARK 500 GLN C 309 80.07 -162.39 REMARK 500 ASP D 44 135.46 -174.52 REMARK 500 TRP D 70 -167.48 -115.07 REMARK 500 ASP D 98 56.27 -96.00 REMARK 500 MET D 148 32.89 -97.52 REMARK 500 ARG D 173 -152.07 -107.70 REMARK 500 PRO D 278 170.99 -55.62 REMARK 500 LYS D 279 54.43 -94.77 REMARK 500 LYS D 312 -2.06 74.23 REMARK 500 SER D 313 -30.81 -130.06 REMARK 500 VAL E 48 -62.00 -93.01 REMARK 500 LEU E 87 51.37 -95.98 REMARK 500 ASP E 110 53.28 -91.49 REMARK 500 LYS E 118 115.36 -162.13 REMARK 500 PRO E 127 134.01 -37.51 REMARK 500 MET E 160 55.03 -90.66 REMARK 500 TYR E 199 -63.02 -96.45 REMARK 500 SER E 291 52.35 -92.69 REMARK 500 SERL2 25 -179.96 -68.32 REMARK 500 THRL2 52 -15.91 73.85 REMARK 500 ASNL2 53 -52.93 -127.73 REMARK 500 PRO H 53 -7.48 -58.73 REMARK 500 THR H 106 75.99 -102.20 REMARK 500 TRP H 115 171.49 59.15 REMARK 500 GLN H 117 -157.50 -141.08 REMARK 500 THRH2 106 62.89 -100.66 REMARK 500 TRPH2 115 171.93 59.39 REMARK 500 GLNH2 117 -156.29 -150.89 REMARK 500 SER L 25 -179.90 -69.25 REMARK 500 THR L 52 -13.87 75.30 REMARK 500 ASN L 53 -39.66 -131.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25583 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25585 RELATED DB: EMDB DBREF 7T0W A 1 307 UNP P47870 GBRB2_HUMAN 25 331 DBREF 7T0W A 317 340 UNP P47870 GBRB2_HUMAN 488 511 DBREF 7T0W B 1 312 UNP P14867 GBRA1_HUMAN 28 339 DBREF 7T0W B 320 347 UNP P14867 GBRA1_HUMAN 418 445 DBREF 7T0W C 1 307 UNP P47870 GBRB2_HUMAN 25 331 DBREF 7T0W C 317 340 UNP P47870 GBRB2_HUMAN 488 511 DBREF 7T0W D 1 312 UNP P14867 GBRA1_HUMAN 28 339 DBREF 7T0W D 320 347 UNP P14867 GBRA1_HUMAN 418 445 DBREF 7T0W E 1 322 UNP P18507 GBRG2_HUMAN 40 361 DBREF 7T0W E 330 357 UNP P18507 GBRG2_HUMAN 440 467 DBREF 7T0WL2 1 217 PDB 7T0W 7T0W 1 217 DBREF 7T0W H 1 246 PDB 7T0W 7T0W 1 246 DBREF 7T0WH2 1 246 PDB 7T0W 7T0W 1 246 DBREF 7T0W L 1 217 PDB 7T0W 7T0W 1 217 SEQADV 7T0W SER A 308 UNP P47870 LINKER SEQADV 7T0W GLN A 309 UNP P47870 LINKER SEQADV 7T0W PRO A 310 UNP P47870 LINKER SEQADV 7T0W ALA A 311 UNP P47870 LINKER SEQADV 7T0W ARG A 312 UNP P47870 LINKER SEQADV 7T0W ALA A 313 UNP P47870 LINKER SEQADV 7T0W ALA A 314 UNP P47870 LINKER SEQADV 7T0W ALA A 315 UNP P47870 LINKER SEQADV 7T0W ILE A 316 UNP P47870 LINKER SEQADV 7T0W SER B 313 UNP P14867 LINKER SEQADV 7T0W GLN B 314 UNP P14867 LINKER SEQADV 7T0W PRO B 315 UNP P14867 LINKER SEQADV 7T0W ALA B 316 UNP P14867 LINKER SEQADV 7T0W ARG B 317 UNP P14867 LINKER SEQADV 7T0W ALA B 318 UNP P14867 LINKER SEQADV 7T0W ALA B 319 UNP P14867 LINKER SEQADV 7T0W SER C 308 UNP P47870 LINKER SEQADV 7T0W GLN C 309 UNP P47870 LINKER SEQADV 7T0W PRO C 310 UNP P47870 LINKER SEQADV 7T0W ALA C 311 UNP P47870 LINKER SEQADV 7T0W ARG C 312 UNP P47870 LINKER SEQADV 7T0W ALA C 313 UNP P47870 LINKER SEQADV 7T0W ALA C 314 UNP P47870 LINKER SEQADV 7T0W ALA C 315 UNP P47870 LINKER SEQADV 7T0W ILE C 316 UNP P47870 LINKER SEQADV 7T0W SER D 313 UNP P14867 LINKER SEQADV 7T0W GLN D 314 UNP P14867 LINKER SEQADV 7T0W PRO D 315 UNP P14867 LINKER SEQADV 7T0W ALA D 316 UNP P14867 LINKER SEQADV 7T0W ARG D 317 UNP P14867 LINKER SEQADV 7T0W ALA D 318 UNP P14867 LINKER SEQADV 7T0W ALA D 319 UNP P14867 LINKER SEQADV 7T0W TRP E -36 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -35 UNP P18507 EXPRESSION TAG SEQADV 7T0W HIS E -34 UNP P18507 EXPRESSION TAG SEQADV 7T0W PRO E -33 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLN E -32 UNP P18507 EXPRESSION TAG SEQADV 7T0W PHE E -31 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLU E -30 UNP P18507 EXPRESSION TAG SEQADV 7T0W LYS E -29 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -28 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -27 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -26 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -25 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -24 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -23 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -22 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -21 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -20 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -19 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -18 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -17 UNP P18507 EXPRESSION TAG SEQADV 7T0W ALA E -16 UNP P18507 EXPRESSION TAG SEQADV 7T0W TRP E -15 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E -14 UNP P18507 EXPRESSION TAG SEQADV 7T0W HIS E -13 UNP P18507 EXPRESSION TAG SEQADV 7T0W PRO E -12 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLN E -11 UNP P18507 EXPRESSION TAG SEQADV 7T0W PHE E -10 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLU E -9 UNP P18507 EXPRESSION TAG SEQADV 7T0W LYS E -8 UNP P18507 EXPRESSION TAG SEQADV 7T0W LEU E -7 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLU E -6 UNP P18507 EXPRESSION TAG SEQADV 7T0W VAL E -5 UNP P18507 EXPRESSION TAG SEQADV 7T0W LEU E -4 UNP P18507 EXPRESSION TAG SEQADV 7T0W PHE E -3 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLN E -2 UNP P18507 EXPRESSION TAG SEQADV 7T0W GLY E -1 UNP P18507 EXPRESSION TAG SEQADV 7T0W PRO E 0 UNP P18507 EXPRESSION TAG SEQADV 7T0W SER E 323 UNP P18507 LINKER SEQADV 7T0W GLN E 324 UNP P18507 LINKER SEQADV 7T0W PRO E 325 UNP P18507 LINKER SEQADV 7T0W ALA E 326 UNP P18507 LINKER SEQADV 7T0W ARG E 327 UNP P18507 LINKER SEQADV 7T0W ALA E 328 UNP P18507 LINKER SEQADV 7T0W ALA E 329 UNP P18507 LINKER SEQRES 1 A 340 GLN SER VAL ASN ASP PRO SER ASN MET SER LEU VAL LYS SEQRES 2 A 340 GLU THR VAL ASP ARG LEU LEU LYS GLY TYR ASP ILE ARG SEQRES 3 A 340 LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL ALA VAL GLY SEQRES 4 A 340 MET ASN ILE ASP ILE ALA SER ILE ASP MET VAL SER GLU SEQRES 5 A 340 VAL ASN MET ASP TYR THR LEU THR MET TYR PHE GLN GLN SEQRES 6 A 340 ALA TRP ARG ASP LYS ARG LEU SER TYR ASN VAL ILE PRO SEQRES 7 A 340 LEU ASN LEU THR LEU ASP ASN ARG VAL ALA ASP GLN LEU SEQRES 8 A 340 TRP VAL PRO ASP THR TYR PHE LEU ASN ASP LYS LYS SER SEQRES 9 A 340 PHE VAL HIS GLY VAL THR VAL LYS ASN ARG MET ILE ARG SEQRES 10 A 340 LEU HIS PRO ASP GLY THR VAL LEU TYR GLY LEU ARG ILE SEQRES 11 A 340 THR THR THR ALA ALA CYS MET MET ASP LEU ARG ARG TYR SEQRES 12 A 340 PRO LEU ASP GLU GLN ASN CYS THR LEU GLU ILE GLU SER SEQRES 13 A 340 TYR GLY TYR THR THR ASP ASP ILE GLU PHE TYR TRP ARG SEQRES 14 A 340 GLY ASP ASP ASN ALA VAL THR GLY VAL THR LYS ILE GLU SEQRES 15 A 340 LEU PRO GLN PHE SER ILE VAL ASP TYR LYS LEU ILE THR SEQRES 16 A 340 LYS LYS VAL VAL PHE SER THR GLY SER TYR PRO ARG LEU SEQRES 17 A 340 SER LEU SER PHE LYS LEU LYS ARG ASN ILE GLY TYR PHE SEQRES 18 A 340 ILE LEU GLN THR TYR MET PRO SER ILE LEU ILE THR ILE SEQRES 19 A 340 LEU SER TRP VAL SER PHE TRP ILE ASN TYR ASP ALA SER SEQRES 20 A 340 ALA ALA ARG VAL ALA LEU GLY ILE THR THR VAL LEU THR SEQRES 21 A 340 MET THR THR ILE ASN THR HIS LEU ARG GLU THR LEU PRO SEQRES 22 A 340 LYS ILE PRO TYR VAL LYS ALA ILE ASP MET TYR LEU MET SEQRES 23 A 340 GLY CYS PHE VAL PHE VAL PHE MET ALA LEU LEU GLU TYR SEQRES 24 A 340 ALA LEU VAL ASN TYR ILE PHE PHE SER GLN PRO ALA ARG SEQRES 25 A 340 ALA ALA ALA ILE ASP ARG TRP SER ARG ILE PHE PHE PRO SEQRES 26 A 340 VAL VAL PHE SER PHE PHE ASN ILE VAL TYR TRP LEU TYR SEQRES 27 A 340 TYR VAL SEQRES 1 B 347 GLN PRO SER LEU GLN ASP GLU LEU LYS ASP ASN THR THR SEQRES 2 B 347 VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP GLY TYR SEQRES 3 B 347 ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG VAL THR SEQRES 4 B 347 GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE GLY PRO SEQRES 5 B 347 VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP VAL PHE SEQRES 6 B 347 PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS PHE LYS SEQRES 7 B 347 GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU MET ALA SEQRES 8 B 347 SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS ASN GLY SEQRES 9 B 347 LYS LYS SER VAL ALA HIS ASN MET THR MET PRO ASN LYS SEQRES 10 B 347 LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU TYR THR SEQRES 11 B 347 MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET HIS LEU SEQRES 12 B 347 GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO LEU LYS SEQRES 13 B 347 PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL VAL TYR SEQRES 14 B 347 GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL VAL ALA SEQRES 15 B 347 GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU LEU GLY SEQRES 16 B 347 GLN THR VAL ASP SER GLY ILE VAL GLN SER SER THR GLY SEQRES 17 B 347 GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU LYS ARG SEQRES 18 B 347 LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU PRO CYS SEQRES 19 B 347 ILE MET THR VAL ILE LEU SER GLN VAL SER PHE TRP LEU SEQRES 20 B 347 ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE GLY VAL SEQRES 21 B 347 THR THR VAL LEU THR MET THR THR LEU SER ILE SER ALA SEQRES 22 B 347 ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR ALA MET SEQRES 23 B 347 ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL PHE SER SEQRES 24 B 347 ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE THR LYS SEQRES 25 B 347 SER GLN PRO ALA ARG ALA ALA LYS ILE ASP ARG LEU SER SEQRES 26 B 347 ARG ILE ALA PHE PRO LEU LEU PHE GLY ILE PHE ASN LEU SEQRES 27 B 347 VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 C 340 GLN SER VAL ASN ASP PRO SER ASN MET SER LEU VAL LYS SEQRES 2 C 340 GLU THR VAL ASP ARG LEU LEU LYS GLY TYR ASP ILE ARG SEQRES 3 C 340 LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL ALA VAL GLY SEQRES 4 C 340 MET ASN ILE ASP ILE ALA SER ILE ASP MET VAL SER GLU SEQRES 5 C 340 VAL ASN MET ASP TYR THR LEU THR MET TYR PHE GLN GLN SEQRES 6 C 340 ALA TRP ARG ASP LYS ARG LEU SER TYR ASN VAL ILE PRO SEQRES 7 C 340 LEU ASN LEU THR LEU ASP ASN ARG VAL ALA ASP GLN LEU SEQRES 8 C 340 TRP VAL PRO ASP THR TYR PHE LEU ASN ASP LYS LYS SER SEQRES 9 C 340 PHE VAL HIS GLY VAL THR VAL LYS ASN ARG MET ILE ARG SEQRES 10 C 340 LEU HIS PRO ASP GLY THR VAL LEU TYR GLY LEU ARG ILE SEQRES 11 C 340 THR THR THR ALA ALA CYS MET MET ASP LEU ARG ARG TYR SEQRES 12 C 340 PRO LEU ASP GLU GLN ASN CYS THR LEU GLU ILE GLU SER SEQRES 13 C 340 TYR GLY TYR THR THR ASP ASP ILE GLU PHE TYR TRP ARG SEQRES 14 C 340 GLY ASP ASP ASN ALA VAL THR GLY VAL THR LYS ILE GLU SEQRES 15 C 340 LEU PRO GLN PHE SER ILE VAL ASP TYR LYS LEU ILE THR SEQRES 16 C 340 LYS LYS VAL VAL PHE SER THR GLY SER TYR PRO ARG LEU SEQRES 17 C 340 SER LEU SER PHE LYS LEU LYS ARG ASN ILE GLY TYR PHE SEQRES 18 C 340 ILE LEU GLN THR TYR MET PRO SER ILE LEU ILE THR ILE SEQRES 19 C 340 LEU SER TRP VAL SER PHE TRP ILE ASN TYR ASP ALA SER SEQRES 20 C 340 ALA ALA ARG VAL ALA LEU GLY ILE THR THR VAL LEU THR SEQRES 21 C 340 MET THR THR ILE ASN THR HIS LEU ARG GLU THR LEU PRO SEQRES 22 C 340 LYS ILE PRO TYR VAL LYS ALA ILE ASP MET TYR LEU MET SEQRES 23 C 340 GLY CYS PHE VAL PHE VAL PHE MET ALA LEU LEU GLU TYR SEQRES 24 C 340 ALA LEU VAL ASN TYR ILE PHE PHE SER GLN PRO ALA ARG SEQRES 25 C 340 ALA ALA ALA ILE ASP ARG TRP SER ARG ILE PHE PHE PRO SEQRES 26 C 340 VAL VAL PHE SER PHE PHE ASN ILE VAL TYR TRP LEU TYR SEQRES 27 C 340 TYR VAL SEQRES 1 D 347 GLN PRO SER LEU GLN ASP GLU LEU LYS ASP ASN THR THR SEQRES 2 D 347 VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP GLY TYR SEQRES 3 D 347 ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG VAL THR SEQRES 4 D 347 GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE GLY PRO SEQRES 5 D 347 VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP VAL PHE SEQRES 6 D 347 PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS PHE LYS SEQRES 7 D 347 GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU MET ALA SEQRES 8 D 347 SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS ASN GLY SEQRES 9 D 347 LYS LYS SER VAL ALA HIS ASN MET THR MET PRO ASN LYS SEQRES 10 D 347 LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU TYR THR SEQRES 11 D 347 MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET HIS LEU SEQRES 12 D 347 GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO LEU LYS SEQRES 13 D 347 PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL VAL TYR SEQRES 14 D 347 GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL VAL ALA SEQRES 15 D 347 GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU LEU GLY SEQRES 16 D 347 GLN THR VAL ASP SER GLY ILE VAL GLN SER SER THR GLY SEQRES 17 D 347 GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU LYS ARG SEQRES 18 D 347 LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU PRO CYS SEQRES 19 D 347 ILE MET THR VAL ILE LEU SER GLN VAL SER PHE TRP LEU SEQRES 20 D 347 ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE GLY VAL SEQRES 21 D 347 THR THR VAL LEU THR MET THR THR LEU SER ILE SER ALA SEQRES 22 D 347 ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR ALA MET SEQRES 23 D 347 ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL PHE SER SEQRES 24 D 347 ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE THR LYS SEQRES 25 D 347 SER GLN PRO ALA ARG ALA ALA LYS ILE ASP ARG LEU SER SEQRES 26 D 347 ARG ILE ALA PHE PRO LEU LEU PHE GLY ILE PHE ASN LEU SEQRES 27 D 347 VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 E 394 TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SER GLY SEQRES 2 E 394 GLY GLY SER GLY GLY SER SER ALA TRP SER HIS PRO GLN SEQRES 3 E 394 PHE GLU LYS LEU GLU VAL LEU PHE GLN GLY PRO GLN LYS SEQRES 4 E 394 SER ASP ASP ASP TYR GLU ASP TYR ALA SER ASN LYS THR SEQRES 5 E 394 TRP VAL LEU THR PRO LYS VAL PRO GLU GLY ASP VAL THR SEQRES 6 E 394 VAL ILE LEU ASN ASN LEU LEU GLU GLY TYR ASP ASN LYS SEQRES 7 E 394 LEU ARG PRO ASP ILE GLY VAL LYS PRO THR LEU ILE HIS SEQRES 8 E 394 THR ASP MET TYR VAL ASN SER ILE GLY PRO VAL ASN ALA SEQRES 9 E 394 ILE ASN MET GLU TYR THR ILE ASP ILE PHE PHE ALA GLN SEQRES 10 E 394 THR TRP TYR ASP ARG ARG LEU LYS PHE ASN SER THR ILE SEQRES 11 E 394 LYS VAL LEU ARG LEU ASN SER ASN MET VAL GLY LYS ILE SEQRES 12 E 394 TRP ILE PRO ASP THR PHE PHE ARG ASN SER LYS LYS ALA SEQRES 13 E 394 ASP ALA HIS TRP ILE THR THR PRO ASN ARG MET LEU ARG SEQRES 14 E 394 ILE TRP ASN ASP GLY ARG VAL LEU TYR THR LEU ARG LEU SEQRES 15 E 394 THR ILE ASP ALA GLU CYS GLN LEU GLN LEU HIS ASN PHE SEQRES 16 E 394 PRO MET ASP GLU HIS SER CYS PRO LEU GLU PHE SER SER SEQRES 17 E 394 TYR GLY TYR PRO ARG GLU GLU ILE VAL TYR GLN TRP LYS SEQRES 18 E 394 ARG SER SER VAL GLU VAL GLY ASP THR ARG SER TRP ARG SEQRES 19 E 394 LEU TYR GLN PHE SER PHE VAL GLY LEU ARG ASN THR THR SEQRES 20 E 394 GLU VAL VAL LYS THR THR SER GLY ASP TYR VAL VAL MET SEQRES 21 E 394 SER VAL TYR PHE ASP LEU SER ARG ARG MET GLY TYR PHE SEQRES 22 E 394 THR ILE GLN THR TYR ILE PRO CYS THR LEU ILE VAL VAL SEQRES 23 E 394 LEU SER TRP VAL SER PHE TRP ILE ASN LYS ASP ALA VAL SEQRES 24 E 394 PRO ALA ARG THR SER LEU GLY ILE THR THR VAL LEU THR SEQRES 25 E 394 MET THR THR LEU SER THR ILE ALA ARG LYS SER LEU PRO SEQRES 26 E 394 LYS VAL SER TYR VAL THR ALA MET ASP LEU PHE VAL SER SEQRES 27 E 394 VAL CYS PHE ILE PHE VAL PHE SER ALA LEU VAL GLU TYR SEQRES 28 E 394 GLY THR LEU HIS TYR PHE VAL SER SER GLN PRO ALA ARG SEQRES 29 E 394 ALA ALA LYS MET ASP SER TYR ALA ARG ILE PHE PHE PRO SEQRES 30 E 394 THR ALA PHE CYS LEU PHE ASN LEU VAL TYR TRP VAL SER SEQRES 31 E 394 TYR LEU TYR LEU SEQRES 1L2 217 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2L2 217 PRO GLY GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3L2 217 SER ASN ILE GLY SER ASN THR VAL SER TRP TYR GLN GLN SEQRES 4L2 217 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER THR SEQRES 5L2 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6L2 217 SER LYS SER GLY THR SER ALA SER LEU ALA ILE GLY GLY SEQRES 7L2 217 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8L2 217 TRP ASP ASP SER LEU LYS ARG LEU VAL VAL PHE GLY GLY SEQRES 9L2 217 GLY THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10L2 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11L2 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12L2 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13L2 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14L2 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15L2 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16L2 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17L2 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 246 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 246 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 246 TYR THR PHE ILE SER TYR ASP ILE ASN TRP VAL ARG GLN SEQRES 4 H 246 ALA THR GLY GLN GLY LEU GLU TRP MET GLY GLY MET ASP SEQRES 5 H 246 PRO LYS SER GLY ASN THR GLY TYR ALA GLN LYS PHE GLN SEQRES 6 H 246 GLY ARG VAL THR MET THR THR ASN THR ALA ILE SER THR SEQRES 7 H 246 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 246 ALA VAL TYR TYR CYS VAL ARG GLY GLU GLN SER TYR ASP SEQRES 9 H 246 ARG THR GLY TYR SER ASP TRP PHE ASP PRO TRP GLY GLN SEQRES 10 H 246 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 246 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 246 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 246 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 246 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 246 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 246 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 246 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 246 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS ASP TYR SEQRES 19 H 246 LYS ASP ASP ASP ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1H2 246 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2H2 246 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3H2 246 TYR THR PHE ILE SER TYR ASP ILE ASN TRP VAL ARG GLN SEQRES 4H2 246 ALA THR GLY GLN GLY LEU GLU TRP MET GLY GLY MET ASP SEQRES 5H2 246 PRO LYS SER GLY ASN THR GLY TYR ALA GLN LYS PHE GLN SEQRES 6H2 246 GLY ARG VAL THR MET THR THR ASN THR ALA ILE SER THR SEQRES 7H2 246 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8H2 246 ALA VAL TYR TYR CYS VAL ARG GLY GLU GLN SER TYR ASP SEQRES 9H2 246 ARG THR GLY TYR SER ASP TRP PHE ASP PRO TRP GLY GLN SEQRES 10H2 246 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11H2 246 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12H2 246 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13H2 246 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14H2 246 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15H2 246 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16H2 246 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17H2 246 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18H2 246 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS ASP TYR SEQRES 19H2 246 LYS ASP ASP ASP ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 217 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2 L 217 PRO GLY GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 L 217 SER ASN ILE GLY SER ASN THR VAL SER TRP TYR GLN GLN SEQRES 4 L 217 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER THR SEQRES 5 L 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 L 217 SER LYS SER GLY THR SER ALA SER LEU ALA ILE GLY GLY SEQRES 7 L 217 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8 L 217 TRP ASP ASP SER LEU LYS ARG LEU VAL VAL PHE GLY GLY SEQRES 9 L 217 GLY THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER 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 NAG F 1 26 HET NAG F 2 27 HET NAG G 1 26 HET NAG G 2 27 HET NAG I 1 26 HET NAG I 2 26 HET BMA I 3 21 HET NAG J 1 26 HET NAG J 2 27 HET NAG K 1 26 HET NAG K 2 27 HET NAG M 1 26 HET NAG M 2 26 HET BMA M 3 21 HET NAG N 1 26 HET NAG N 2 26 HET BMA N 3 19 HET MAN N 4 19 HET MAN N 5 18 HET MAN N 6 20 HET MAN N 7 19 HET MAN N 8 20 HET MAN N 9 19 HET MAN N 10 21 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 10 NAG 14(C8 H15 N O6) FORMUL 12 BMA 3(C6 H12 O6) FORMUL 16 MAN 7(C6 H12 O6) HELIX 1 AA1 SER A 7 LYS A 21 1 15 HELIX 2 AA2 LYS A 70 SER A 73 5 4 HELIX 3 AA3 ASP A 84 GLN A 90 5 7 HELIX 4 AA4 ILE A 218 ILE A 242 1 25 HELIX 5 AA5 ALA A 246 LEU A 272 1 27 HELIX 6 AA6 LYS A 279 PHE A 306 1 28 HELIX 7 AA7 GLN A 309 TYR A 339 1 31 HELIX 8 AA8 ASN B 11 LEU B 22 1 12 HELIX 9 AA9 GLU B 73 LYS B 76 5 4 HELIX 10 AB1 ASN B 87 SER B 92 1 6 HELIX 11 AB2 GLU B 174 ARG B 177 5 4 HELIX 12 AB3 ILE B 223 SER B 244 1 22 HELIX 13 AB4 PHE B 245 LEU B 247 5 3 HELIX 14 AB5 SER B 251 ASN B 275 1 25 HELIX 15 AB6 THR B 284 THR B 311 1 28 HELIX 16 AB7 GLN B 314 ASN B 346 1 33 HELIX 17 AB8 ASN C 8 LYS C 21 1 14 HELIX 18 AB9 LYS C 70 SER C 73 5 4 HELIX 19 AC1 ASP C 84 GLN C 90 5 7 HELIX 20 AC2 ILE C 218 VAL C 238 1 21 HELIX 21 AC3 SER C 239 TRP C 241 5 3 HELIX 22 AC4 ALA C 246 LEU C 272 1 27 HELIX 23 AC5 LYS C 279 PHE C 307 1 29 HELIX 24 AC6 GLN C 309 TYR C 339 1 31 HELIX 25 AC7 THR D 12 LEU D 23 1 12 HELIX 26 AC8 GLU D 73 LYS D 76 5 4 HELIX 27 AC9 ASN D 87 SER D 92 1 6 HELIX 28 AD1 HIS D 142 PHE D 146 5 5 HELIX 29 AD2 GLU D 174 ARG D 177 5 4 HELIX 30 AD3 GLU D 183 SER D 186 5 4 HELIX 31 AD4 ILE D 223 THR D 230 1 8 HELIX 32 AD5 THR D 230 SER D 244 1 15 HELIX 33 AD6 PHE D 245 LEU D 247 5 3 HELIX 34 AD7 SER D 251 LEU D 277 1 27 HELIX 35 AD8 THR D 284 THR D 311 1 28 HELIX 36 AD9 GLN D 314 ARG D 347 1 34 HELIX 37 AE1 ASP E 26 GLU E 36 1 11 HELIX 38 AE2 ARG E 85 LYS E 88 5 4 HELIX 39 AE3 ASN E 99 LYS E 105 5 7 HELIX 40 AE4 MET E 233 THR E 240 1 8 HELIX 41 AE5 THR E 240 TRP E 252 1 13 HELIX 42 AE6 TRP E 252 ILE E 257 1 6 HELIX 43 AE7 ALA E 261 SER E 286 1 26 HELIX 44 AE8 THR E 294 SER E 322 1 29 HELIX 45 AE9 GLN E 324 TYR E 356 1 33 HELIX 46 AF1 GLNL2 80 GLUL2 84 5 5 HELIX 47 AF2 ALA H 61 GLN H 65 5 5 HELIX 48 AF3 ARG H 87 THR H 91 5 5 HELIX 49 AF4 ALAH2 61 GLNH2 65 5 5 HELIX 50 AF5 ARGH2 87 THRH2 91 5 5 HELIX 51 AF6 GLN L 80 GLU L 84 5 5 SHEET 1 AA1 8 VAL A 36 SER A 51 0 SHEET 2 AA1 8 ASP A 56 ARG A 68 -1 O GLN A 64 N ASN A 41 SHEET 3 AA1 8 LEU A 81 LEU A 83 0 SHEET 4 AA1 8 ASP A 101 VAL A 106 0 SHEET 5 AA1 8 ARG A 114 LEU A 118 -1 O ILE A 116 N LEU A 83 SHEET 6 AA1 8 THR A 123 ALA A 135 -1 O LEU A 125 N ARG A 117 SHEET 7 AA1 8 ILE A 164 TRP A 168 1 O GLU A 165 N VAL A 36 SHEET 8 AA1 8 VAL A 175 THR A 176 1 O THR A 176 N ILE A 42 SHEET 1 AA2 4 THR A 96 PHE A 98 0 SHEET 2 AA2 4 GLU A 147 SER A 156 -1 O GLU A 155 N TYR A 97 SHEET 3 AA2 4 GLY A 203 LYS A 215 -1 O LEU A 214 N GLN A 148 SHEET 4 AA2 4 ILE A 188 PHE A 200 -1 N PHE A 200 O GLY A 203 SHEET 1 AA3 9 THR B 39 SER B 49 0 SHEET 2 AA3 9 VAL B 53 SER B 54 0 SHEET 3 AA3 9 GLU B 59 LYS B 71 -1 O GLU B 59 N SER B 54 SHEET 4 AA3 9 VAL B 83 LEU B 86 0 SHEET 5 AA3 9 GLY B 104 ALA B 109 0 SHEET 6 AA3 9 LYS B 117 THR B 122 -1 O LEU B 119 N LEU B 86 SHEET 7 AA3 9 THR B 126 GLU B 138 -1 O LEU B 128 N ARG B 120 SHEET 8 AA3 9 VAL B 167 TRP B 171 1 O VAL B 168 N VAL B 41 SHEET 9 AA3 9 VAL B 179 VAL B 181 1 O VAL B 180 N VAL B 47 SHEET 1 AA4 5 THR B 99 PHE B 101 0 SHEET 2 AA4 5 ALA B 150 SER B 159 -1 O GLY B 158 N PHE B 100 SHEET 3 AA4 5 TYR B 191 LEU B 193 0 SHEET 4 AA4 5 VAL B 198 GLN B 204 0 SHEET 5 AA4 5 GLU B 209 ARG B 221 -1 O TYR B 210 N VAL B 203 SHEET 1 AA5 8 VAL C 36 SER C 51 0 SHEET 2 AA5 8 ASP C 56 ARG C 68 -1 O ALA C 66 N GLY C 39 SHEET 3 AA5 8 LEU C 81 LEU C 83 0 SHEET 4 AA5 8 ASP C 101 VAL C 106 0 SHEET 5 AA5 8 ARG C 114 LEU C 118 -1 O ILE C 116 N LEU C 83 SHEET 6 AA5 8 THR C 123 ALA C 135 -1 O LEU C 125 N ARG C 117 SHEET 7 AA5 8 ILE C 164 TRP C 168 1 O GLU C 165 N VAL C 38 SHEET 8 AA5 8 VAL C 175 THR C 176 1 O THR C 176 N ILE C 42 SHEET 1 AA6 4 THR C 96 PHE C 98 0 SHEET 2 AA6 4 GLU C 147 SER C 156 -1 O GLU C 155 N TYR C 97 SHEET 3 AA6 4 GLY C 203 LYS C 215 -1 O PHE C 212 N CYS C 150 SHEET 4 AA6 4 ILE C 188 PHE C 200 -1 N PHE C 200 O GLY C 203 SHEET 1 AA7 8 LYS D 42 SER D 49 0 SHEET 2 AA7 8 VAL D 53 SER D 54 0 SHEET 3 AA7 8 GLU D 59 LYS D 71 -1 O GLU D 59 N SER D 54 SHEET 4 AA7 8 VAL D 83 LEU D 86 0 SHEET 5 AA7 8 VAL D 108 ALA D 109 0 SHEET 6 AA7 8 LYS D 117 THR D 122 -1 O ILE D 121 N LEU D 84 SHEET 7 AA7 8 THR D 126 GLU D 138 -1 O THR D 130 N LEU D 118 SHEET 8 AA7 8 VAL D 179 VAL D 181 1 O VAL D 180 N VAL D 47 SHEET 1 AA8 4 THR D 99 PHE D 101 0 SHEET 2 AA8 4 ALA D 150 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 3 AA8 4 GLY D 208 ARG D 221 -1 O MET D 213 N PHE D 157 SHEET 4 AA8 4 TYR D 191 SER D 205 -1 N SER D 205 O GLY D 208 SHEET 1 AA9 9 THR E 51 VAL E 59 0 SHEET 2 AA9 9 SER E 61 ASN E 66 0 SHEET 3 AA9 9 GLU E 71 TYR E 83 -1 O ASP E 75 N SER E 61 SHEET 4 AA9 9 VAL E 95 LEU E 98 0 SHEET 5 AA9 9 SER E 116 ALA E 121 0 SHEET 6 AA9 9 MET E 130 TRP E 134 -1 O ILE E 133 N LEU E 96 SHEET 7 AA9 9 ARG E 138 GLU E 150 -1 O LEU E 140 N ARG E 132 SHEET 8 AA9 9 ILE E 179 GLN E 182 1 O VAL E 180 N ILE E 53 SHEET 9 AA9 9 VAL E 188 VAL E 190 1 O GLU E 189 N VAL E 59 SHEET 1 AB1 4 THR E 111 PHE E 112 0 SHEET 2 AB1 4 GLU E 162 SER E 171 -1 O SER E 170 N PHE E 112 SHEET 3 AB1 4 ASP E 219 ARG E 231 -1 O MET E 223 N PHE E 169 SHEET 4 AB1 4 PHE E 201 LYS E 214 -1 N GLY E 205 O ASP E 228 SHEET 1 AB2 5 SERL2 9 ALAL2 10 0 SHEET 2 AB2 5 THRL2 106 LEUL2 108 1 O ARGL2 107 N ALAL2 10 SHEET 3 AB2 5 ALAL2 85 ALAL2 90 -1 N ALAL2 85 O LEUL2 108 SHEET 4 AB2 5 SERL2 35 GLNL2 39 -1 N TYRL2 37 O TYRL2 88 SHEET 5 AB2 5 LYSL2 46 ILEL2 49 -1 O LYSL2 46 N GLNL2 38 SHEET 1 AB3 3 VALL2 18 SERL2 23 0 SHEET 2 AB3 3 SERL2 71 ILEL2 76 -1 O LEUL2 74 N ILEL2 20 SHEET 3 AB3 3 PHEL2 63 SERL2 68 -1 N SERL2 68 O SERL2 71 SHEET 1 AB4 2 GLU H 10 VAL H 11 0 SHEET 2 AB4 2 LEU H 120 VAL H 121 1 O VAL H 121 N GLU H 10 SHEET 1 AB5 2 VAL H 18 VAL H 20 0 SHEET 2 AB5 2 MET H 81 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 1 AB6 3 LEU H 45 GLY H 49 0 SHEET 2 AB6 3 ASP H 33 GLN H 39 -1 N TRP H 36 O GLY H 49 SHEET 3 AB6 3 VAL H 93 GLY H 99 -1 O TYR H 95 N VAL H 37 SHEET 1 AB7 2 GLN H 101 TYR H 103 0 SHEET 2 AB7 2 TYR H 108 ASP H 110 -1 O SER H 109 N SER H 102 SHEET 1 AB8 4 GLNH2 3 GLNH2 6 0 SHEET 2 AB8 4 VALH2 20 SERH2 25 -1 O LYSH2 23 N VALH2 5 SHEET 3 AB8 4 THRH2 78 METH2 81 -1 O ALAH2 79 N CYSH2 22 SHEET 4 AB8 4 THRH2 71 ASNH2 73 -1 N THRH2 71 O TYRH2 80 SHEET 1 AB9 2 GLUH2 10 VALH2 11 0 SHEET 2 AB9 2 LEUH2 120 VALH2 121 1 O VALH2 121 N GLUH2 10 SHEET 1 AC1 4 LEUH2 45 METH2 51 0 SHEET 2 AC1 4 ASPH2 33 GLNH2 39 -1 N ARGH2 38 O GLUH2 46 SHEET 3 AC1 4 VALH2 93 ASPH2 104 -1 O VALH2 97 N ASNH2 35 SHEET 4 AC1 4 GLYH2 107 PHEH2 112 -1 O TRPH2 111 N GLUH2 100 SHEET 1 AC2 6 SER L 9 GLY L 12 0 SHEET 2 AC2 6 SER L 35 GLN L 39 0 SHEET 3 AC2 6 LYS L 46 ILE L 49 -1 O LEU L 48 N TRP L 36 SHEET 4 AC2 6 ASP L 86 ASP L 93 -1 O TYR L 88 N TYR L 37 SHEET 5 AC2 6 LEU L 99 PHE L 102 -1 O LEU L 99 N ASP L 93 SHEET 6 AC2 6 THR L 106 VAL L 110 -1 O THR L 106 N TYR L 87 SHEET 1 AC3 3 VAL L 18 SER L 23 0 SHEET 2 AC3 3 SER L 71 ILE L 76 -1 O LEU L 74 N ILE L 20 SHEET 3 AC3 3 PHE L 63 SER L 68 -1 N SER L 64 O ALA L 75 SSBOND 1 CYS A 136 CYS A 150 1555 1555 2.04 SSBOND 2 CYS B 139 CYS B 153 1555 1555 2.03 SSBOND 3 CYS C 136 CYS C 150 1555 1555 2.03 SSBOND 4 CYS D 139 CYS D 153 1555 1555 2.04 SSBOND 5 CYS E 151 CYS E 165 1555 1555 2.04 SSBOND 6 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 7 CYSH2 22 CYSH2 96 1555 1555 2.03 SSBOND 8 CYS L 22 CYS L 89 1555 1555 2.03 LINK ND2 ASN A 80 C1 NAG F 1 1555 1555 1.46 LINK ND2 ASN A 149 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN B 111 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN C 80 C1 NAG G 1 1555 1555 1.46 LINK ND2 ASN C 149 C1 NAG I 1 1555 1555 1.42 LINK ND2 ASN D 111 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN E 208 C1 NAG K 1 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.43 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.43 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44 LINK O6 BMA N 3 C1 MAN N 7 1555 1555 1.44 LINK O2 MAN N 4 C1 MAN N 5 1555 1555 1.43 LINK O2 MAN N 5 C1 MAN N 6 1555 1555 1.44 LINK O6 MAN N 7 C1 MAN N 8 1555 1555 1.44 LINK O3 MAN N 7 C1 MAN N 10 1555 1555 1.45 LINK O2 MAN N 8 C1 MAN N 9 1555 1555 1.43 CISPEP 1 VAL A 109 THR A 110 0 -1.71 CISPEP 2 TYR A 143 PRO A 144 0 0.18 CISPEP 3 MET B 112 THR B 113 0 -2.33 CISPEP 4 PHE B 146 PRO B 147 0 0.75 CISPEP 5 VAL C 109 THR C 110 0 -0.87 CISPEP 6 TYR C 143 PRO C 144 0 0.18 CISPEP 7 MET D 112 THR D 113 0 -2.49 CISPEP 8 PHE D 146 PRO D 147 0 -1.40 CISPEP 9 ILE E 124 THR E 125 0 -3.27 CISPEP 10 PHE E 158 PRO E 159 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