HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 30-NOV-21 7T0Z TITLE COMPLEX OF GABA-A SYNAPTIC RECEPTOR WITH AUTOIMMUNE ANTIBODY FAB175 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: FAB175 IGG1 HEAVY CHAIN; COMPND 18 CHAIN: H; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: FAB175 IGG1 LIGHT CHAIN; COMPND 22 CHAIN: L; 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 : 126510 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 7T0Z 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_1000261458. 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 FAB175 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: HEPTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, H, L, F, G, I, REMARK 350 AND CHAINS: J, K, M 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 SER H 126 REMARK 465 THR H 127 REMARK 465 LYS H 128 REMARK 465 GLY H 129 REMARK 465 PRO H 130 REMARK 465 SER H 131 REMARK 465 VAL H 132 REMARK 465 PHE H 133 REMARK 465 PRO H 134 REMARK 465 LEU H 135 REMARK 465 ALA H 136 REMARK 465 PRO H 137 REMARK 465 SER H 138 REMARK 465 SER H 139 REMARK 465 LYS H 140 REMARK 465 SER H 141 REMARK 465 THR H 142 REMARK 465 SER H 143 REMARK 465 GLY H 144 REMARK 465 GLY H 145 REMARK 465 THR H 146 REMARK 465 ALA H 147 REMARK 465 ALA H 148 REMARK 465 LEU H 149 REMARK 465 GLY H 150 REMARK 465 CYS H 151 REMARK 465 LEU H 152 REMARK 465 VAL H 153 REMARK 465 LYS H 154 REMARK 465 ASP H 155 REMARK 465 TYR H 156 REMARK 465 PHE H 157 REMARK 465 PRO H 158 REMARK 465 GLU H 159 REMARK 465 PRO H 160 REMARK 465 VAL H 161 REMARK 465 THR H 162 REMARK 465 VAL H 163 REMARK 465 SER H 164 REMARK 465 TRP H 165 REMARK 465 ASN H 166 REMARK 465 SER H 167 REMARK 465 GLY H 168 REMARK 465 ALA H 169 REMARK 465 LEU H 170 REMARK 465 THR H 171 REMARK 465 SER H 172 REMARK 465 GLY H 173 REMARK 465 VAL H 174 REMARK 465 HIS H 175 REMARK 465 THR H 176 REMARK 465 PHE H 177 REMARK 465 PRO H 178 REMARK 465 ALA H 179 REMARK 465 VAL H 180 REMARK 465 LEU H 181 REMARK 465 GLN H 182 REMARK 465 SER H 183 REMARK 465 SER H 184 REMARK 465 GLY H 185 REMARK 465 LEU H 186 REMARK 465 TYR H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 SER H 190 REMARK 465 SER H 191 REMARK 465 VAL H 192 REMARK 465 VAL H 193 REMARK 465 THR H 194 REMARK 465 VAL H 195 REMARK 465 PRO H 196 REMARK 465 SER H 197 REMARK 465 SER H 198 REMARK 465 SER H 199 REMARK 465 LEU H 200 REMARK 465 GLY H 201 REMARK 465 THR H 202 REMARK 465 GLN H 203 REMARK 465 THR H 204 REMARK 465 TYR H 205 REMARK 465 ILE H 206 REMARK 465 CYS H 207 REMARK 465 ASN H 208 REMARK 465 VAL H 209 REMARK 465 ASN H 210 REMARK 465 HIS H 211 REMARK 465 LYS H 212 REMARK 465 PRO H 213 REMARK 465 SER H 214 REMARK 465 ASN H 215 REMARK 465 THR H 216 REMARK 465 LYS H 217 REMARK 465 VAL H 218 REMARK 465 ASP H 219 REMARK 465 LYS H 220 REMARK 465 ARG H 221 REMARK 465 VAL H 222 REMARK 465 GLU H 223 REMARK 465 PRO H 224 REMARK 465 LYS H 225 REMARK 465 SER H 226 REMARK 465 CYS H 227 REMARK 465 ASP H 228 REMARK 465 LYS H 229 REMARK 465 THR H 230 REMARK 465 HIS H 231 REMARK 465 ASP H 232 REMARK 465 TYR H 233 REMARK 465 LYS H 234 REMARK 465 ASP H 235 REMARK 465 ASP H 236 REMARK 465 ASP H 237 REMARK 465 ASP H 238 REMARK 465 LYS H 239 REMARK 465 HIS 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 THR L 110 REMARK 465 VAL L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 PHE L 117 REMARK 465 ILE L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 ASP L 123 REMARK 465 GLU L 124 REMARK 465 GLN L 125 REMARK 465 LEU L 126 REMARK 465 LYS L 127 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 THR L 130 REMARK 465 ALA L 131 REMARK 465 SER L 132 REMARK 465 VAL L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 LEU L 137 REMARK 465 ASN L 138 REMARK 465 ASN L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 ARG L 143 REMARK 465 GLU L 144 REMARK 465 ALA L 145 REMARK 465 LYS L 146 REMARK 465 VAL L 147 REMARK 465 GLN L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 ASP L 152 REMARK 465 ASN L 153 REMARK 465 ALA L 154 REMARK 465 LEU L 155 REMARK 465 GLN L 156 REMARK 465 SER L 157 REMARK 465 GLY L 158 REMARK 465 ASN L 159 REMARK 465 SER L 160 REMARK 465 GLN L 161 REMARK 465 GLU L 162 REMARK 465 SER L 163 REMARK 465 VAL L 164 REMARK 465 THR L 165 REMARK 465 GLU L 166 REMARK 465 GLN L 167 REMARK 465 ASP L 168 REMARK 465 SER L 169 REMARK 465 LYS L 170 REMARK 465 ASP L 171 REMARK 465 SER L 172 REMARK 465 THR L 173 REMARK 465 TYR L 174 REMARK 465 SER L 175 REMARK 465 LEU L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 THR L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 LEU L 182 REMARK 465 SER L 183 REMARK 465 LYS L 184 REMARK 465 ALA L 185 REMARK 465 ASP L 186 REMARK 465 TYR L 187 REMARK 465 GLU L 188 REMARK 465 LYS L 189 REMARK 465 HIS L 190 REMARK 465 LYS L 191 REMARK 465 VAL L 192 REMARK 465 TYR L 193 REMARK 465 ALA L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLN L 200 REMARK 465 GLY L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 VAL L 206 REMARK 465 THR L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 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 ASP B 145 H MET B 148 1.53 REMARK 500 O SER B 92 HH12 ARG C 86 1.56 REMARK 500 HH TYR B 60 O PRO B 154 1.58 REMARK 500 OD1 ASP A 101 HH22 ARG B 132 1.58 REMARK 500 OE1 GLU D 59 HZ2 LYS D 105 1.58 REMARK 500 O ASN E 258 HE ARG E 265 1.59 REMARK 500 O HIS D 56 OH TYR E 199 1.97 REMARK 500 OD1 ASN D 248 OG SER D 251 2.04 REMARK 500 OH TYR A 284 OD1 ASN A 332 2.06 REMARK 500 OH TYR B 60 O PRO B 154 2.13 REMARK 500 O3 NAG F 1 O5 NAG F 2 2.15 REMARK 500 O VAL B 238 OG SER B 241 2.15 REMARK 500 O3 NAG G 1 O5 NAG G 2 2.16 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 ASP A 48 -169.23 -114.68 REMARK 500 MET A 49 122.98 -38.46 REMARK 500 LEU A 145 50.67 -91.83 REMARK 500 ASP A 171 -106.02 50.65 REMARK 500 TYR A 244 2.05 -66.96 REMARK 500 ASP B 98 56.32 -93.69 REMARK 500 ASN B 111 44.19 -141.69 REMARK 500 LEU B 143 54.93 -91.75 REMARK 500 LYS B 312 -5.01 71.56 REMARK 500 ASP C 171 -114.95 59.54 REMARK 500 PHE C 200 -167.29 -114.74 REMARK 500 GLN C 309 76.82 -166.69 REMARK 500 LEU D 143 34.02 -95.87 REMARK 500 PRO D 147 35.84 -95.46 REMARK 500 ALA D 161 -2.34 82.70 REMARK 500 LYS D 312 -6.42 74.99 REMARK 500 SER D 313 -40.04 -131.36 REMARK 500 VAL E 48 -59.48 -123.05 REMARK 500 ASP E 110 55.60 -92.70 REMARK 500 ASN E 128 37.94 -93.06 REMARK 500 ASP E 148 76.41 -100.64 REMARK 500 LEU E 155 49.84 -92.72 REMARK 500 ASN E 157 0.09 81.11 REMARK 500 MET E 160 51.71 -93.11 REMARK 500 PRO E 175 -176.21 -69.63 REMARK 500 SER E 187 -61.24 -90.88 REMARK 500 THR E 193 -5.86 77.98 REMARK 500 ARG E 197 31.43 -91.46 REMARK 500 TRP E 256 54.58 -95.31 REMARK 500 ILE E 257 -68.50 -123.15 REMARK 500 ASN E 258 166.45 176.88 REMARK 500 VAL H 48 -61.82 -103.38 REMARK 500 TRP H 105 -137.16 38.22 REMARK 500 SER L 30 -131.34 54.69 REMARK 500 ALA L 51 -10.01 75.24 REMARK 500 SER L 77 66.15 60.42 REMARK 500 ALA L 84 -167.36 -162.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG C 402 REMARK 610 MAN E 401 REMARK 610 NAG F 1 REMARK 610 NAG G 1 REMARK 610 NAG I 1 REMARK 610 NAG J 1 REMARK 610 NAG K 1 REMARK 610 NAG M 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25585 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25583 RELATED DB: EMDB DBREF 7T0Z A 1 307 UNP P47870 GBRB2_HUMAN 25 331 DBREF 7T0Z A 317 340 UNP P47870 GBRB2_HUMAN 488 511 DBREF 7T0Z B 1 312 UNP P14867 GBRA1_HUMAN 28 339 DBREF 7T0Z B 320 347 UNP P14867 GBRA1_HUMAN 418 445 DBREF 7T0Z C 1 307 UNP P47870 GBRB2_HUMAN 25 331 DBREF 7T0Z C 317 340 UNP P47870 GBRB2_HUMAN 488 511 DBREF 7T0Z D 1 312 UNP P14867 GBRA1_HUMAN 28 339 DBREF 7T0Z D 320 347 UNP P14867 GBRA1_HUMAN 418 445 DBREF 7T0Z E 1 322 UNP P18507 GBRG2_HUMAN 40 361 DBREF 7T0Z E 330 357 UNP P18507 GBRG2_HUMAN 440 467 DBREF 7T0Z H 1 245 PDB 7T0Z 7T0Z 1 245 DBREF 7T0Z L 1 215 PDB 7T0Z 7T0Z 1 215 SEQADV 7T0Z SER A 308 UNP P47870 LINKER SEQADV 7T0Z GLN A 309 UNP P47870 LINKER SEQADV 7T0Z PRO A 310 UNP P47870 LINKER SEQADV 7T0Z ALA A 311 UNP P47870 LINKER SEQADV 7T0Z ARG A 312 UNP P47870 LINKER SEQADV 7T0Z ALA A 313 UNP P47870 LINKER SEQADV 7T0Z ALA A 314 UNP P47870 LINKER SEQADV 7T0Z ALA A 315 UNP P47870 LINKER SEQADV 7T0Z ILE A 316 UNP P47870 LINKER SEQADV 7T0Z SER B 313 UNP P14867 LINKER SEQADV 7T0Z GLN B 314 UNP P14867 LINKER SEQADV 7T0Z PRO B 315 UNP P14867 LINKER SEQADV 7T0Z ALA B 316 UNP P14867 LINKER SEQADV 7T0Z ARG B 317 UNP P14867 LINKER SEQADV 7T0Z ALA B 318 UNP P14867 LINKER SEQADV 7T0Z ALA B 319 UNP P14867 LINKER SEQADV 7T0Z SER C 308 UNP P47870 LINKER SEQADV 7T0Z GLN C 309 UNP P47870 LINKER SEQADV 7T0Z PRO C 310 UNP P47870 LINKER SEQADV 7T0Z ALA C 311 UNP P47870 LINKER SEQADV 7T0Z ARG C 312 UNP P47870 LINKER SEQADV 7T0Z ALA C 313 UNP P47870 LINKER SEQADV 7T0Z ALA C 314 UNP P47870 LINKER SEQADV 7T0Z ALA C 315 UNP P47870 LINKER SEQADV 7T0Z ILE C 316 UNP P47870 LINKER SEQADV 7T0Z SER D 313 UNP P14867 LINKER SEQADV 7T0Z GLN D 314 UNP P14867 LINKER SEQADV 7T0Z PRO D 315 UNP P14867 LINKER SEQADV 7T0Z ALA D 316 UNP P14867 LINKER SEQADV 7T0Z ARG D 317 UNP P14867 LINKER SEQADV 7T0Z ALA D 318 UNP P14867 LINKER SEQADV 7T0Z ALA D 319 UNP P14867 LINKER SEQADV 7T0Z TRP E -36 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -35 UNP P18507 EXPRESSION TAG SEQADV 7T0Z HIS E -34 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PRO E -33 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLN E -32 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PHE E -31 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLU E -30 UNP P18507 EXPRESSION TAG SEQADV 7T0Z LYS E -29 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -28 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -27 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -26 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -25 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -24 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -23 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -22 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -21 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -20 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -19 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -18 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -17 UNP P18507 EXPRESSION TAG SEQADV 7T0Z ALA E -16 UNP P18507 EXPRESSION TAG SEQADV 7T0Z TRP E -15 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E -14 UNP P18507 EXPRESSION TAG SEQADV 7T0Z HIS E -13 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PRO E -12 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLN E -11 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PHE E -10 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLU E -9 UNP P18507 EXPRESSION TAG SEQADV 7T0Z LYS E -8 UNP P18507 EXPRESSION TAG SEQADV 7T0Z LEU E -7 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLU E -6 UNP P18507 EXPRESSION TAG SEQADV 7T0Z VAL E -5 UNP P18507 EXPRESSION TAG SEQADV 7T0Z LEU E -4 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PHE E -3 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLN E -2 UNP P18507 EXPRESSION TAG SEQADV 7T0Z GLY E -1 UNP P18507 EXPRESSION TAG SEQADV 7T0Z PRO E 0 UNP P18507 EXPRESSION TAG SEQADV 7T0Z SER E 323 UNP P18507 LINKER SEQADV 7T0Z GLN E 324 UNP P18507 LINKER SEQADV 7T0Z PRO E 325 UNP P18507 LINKER SEQADV 7T0Z ALA E 326 UNP P18507 LINKER SEQADV 7T0Z ARG E 327 UNP P18507 LINKER SEQADV 7T0Z ALA E 328 UNP P18507 LINKER SEQADV 7T0Z 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 1 H 245 GLU VAL GLN LEU LEU GLU SER GLY GLU GLY LEU VAL GLN SEQRES 2 H 245 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 245 PHE THR PHE LYS THR TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 245 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 H 245 GLY SER GLY ALA SER THR TYR TYR ALA ASP PHE VAL GLU SEQRES 6 H 245 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 245 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 245 ALA VAL TYR TYR CYS ALA LYS GLU PRO PRO ALA MET VAL SEQRES 9 H 245 TRP PHE GLY GLY GLY TYR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 245 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 245 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 245 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 245 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 245 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 245 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 245 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 245 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 H 245 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ASP TYR LYS SEQRES 19 H 245 ASP ASP ASP ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 215 SER ASN TRP PRO PRO TYR SER PHE GLY GLN GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET ABU B 401 7 HET ABU C 401 7 HET NAG C 402 27 HET NAG D 401 27 HET MAN E 401 21 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 26 HET BMA K 3 21 HET NAG M 1 26 HET NAG M 2 26 HET BMA M 3 18 HET MAN M 4 19 HET MAN M 5 19 HET MAN M 6 21 HET MAN M 7 19 HET MAN M 8 20 HET MAN M 9 21 HETNAM ABU GAMMA-AMINO-BUTANOIC ACID HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAN ALPHA-D-MANNOSE HETNAM BMA BETA-D-MANNOSE HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID FORMUL 8 ABU 2(C4 H9 N O2) FORMUL 10 NAG 14(C8 H15 N O6) FORMUL 12 MAN 7(C6 H12 O6) FORMUL 15 BMA 3(C6 H12 O6) HELIX 1 AA1 SER A 7 LYS A 21 1 15 HELIX 2 AA2 ASP A 84 GLN A 90 5 7 HELIX 3 AA3 GLY A 170 ASN A 173 5 4 HELIX 4 AA4 GLY A 177 ILE A 181 5 5 HELIX 5 AA5 ILE A 218 SER A 239 1 22 HELIX 6 AA6 PHE A 240 ILE A 242 5 3 HELIX 7 AA7 ALA A 246 LEU A 272 1 27 HELIX 8 AA8 LYS A 279 PHE A 307 1 29 HELIX 9 AA9 GLN A 309 TYR A 339 1 31 HELIX 10 AB1 ASN B 11 LEU B 22 1 12 HELIX 11 AB2 GLU B 73 LYS B 76 5 4 HELIX 12 AB3 ASN B 87 SER B 92 1 6 HELIX 13 AB4 GLU B 174 ARG B 177 5 4 HELIX 14 AB5 ILE B 223 TRP B 246 1 24 HELIX 15 AB6 SER B 251 LEU B 277 1 27 HELIX 16 AB7 THR B 284 THR B 311 1 28 HELIX 17 AB8 GLN B 314 LEU B 345 1 32 HELIX 18 AB9 ASN C 8 LYS C 21 1 14 HELIX 19 AC1 LYS C 70 SER C 73 5 4 HELIX 20 AC2 ASP C 84 GLN C 90 5 7 HELIX 21 AC3 GLY C 170 ASN C 173 5 4 HELIX 22 AC4 ILE C 218 SER C 239 1 22 HELIX 23 AC5 ALA C 246 LEU C 272 1 27 HELIX 24 AC6 LYS C 279 PHE C 307 1 29 HELIX 25 AC7 GLN C 309 TYR C 339 1 31 HELIX 26 AC8 THR D 12 LEU D 23 1 12 HELIX 27 AC9 GLU D 73 LYS D 76 5 4 HELIX 28 AD1 ASN D 87 SER D 92 1 6 HELIX 29 AD2 GLU D 174 ARG D 177 5 4 HELIX 30 AD3 ILE D 223 THR D 230 1 8 HELIX 31 AD4 THR D 230 SER D 244 1 15 HELIX 32 AD5 PHE D 245 LEU D 247 5 3 HELIX 33 AD6 SER D 251 LEU D 277 1 27 HELIX 34 AD7 THR D 284 THR D 311 1 28 HELIX 35 AD8 GLN D 314 ARG D 347 1 34 HELIX 36 AD9 GLY E 25 LEU E 35 1 11 HELIX 37 AE1 ARG E 85 LYS E 88 5 4 HELIX 38 AE2 MET E 233 TRP E 256 1 24 HELIX 39 AE3 ALA E 261 ALA E 283 1 23 HELIX 40 AE4 THR E 294 VAL E 321 1 28 HELIX 41 AE5 GLN E 324 LEU E 357 1 34 HELIX 42 AE6 THR H 28 TYR H 32 5 5 HELIX 43 AE7 ARG H 87 THR H 91 5 5 HELIX 44 AE8 GLU L 79 PHE L 83 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 THR A 58 N ASP A 48 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 LEU A 118 N LEU A 81 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 38 SHEET 8 AA1 8 VAL A 175 THR A 176 1 O THR A 176 N ILE A 44 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 SER A 204 ARG A 216 -1 O LEU A 214 N GLN A 148 SHEET 4 AA2 4 PHE A 186 VAL A 199 -1 N ILE A 194 O SER A 209 SHEET 1 AA3 8 THR B 39 SER B 54 0 SHEET 2 AA3 8 GLU B 59 LYS B 71 -1 O SER B 69 N LYS B 42 SHEET 3 AA3 8 VAL B 83 LEU B 86 0 SHEET 4 AA3 8 VAL B 108 ALA B 109 0 SHEET 5 AA3 8 LYS B 117 THR B 122 -1 O ILE B 121 N LEU B 84 SHEET 6 AA3 8 THR B 126 GLU B 138 -1 O THR B 126 N THR B 122 SHEET 7 AA3 8 VAL B 167 TRP B 171 1 O VAL B 168 N THR B 39 SHEET 8 AA3 8 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 PRO B 154 0 SHEET 3 AA4 5 PHE B 157 SER B 159 -1 O GLY B 158 N PHE B 100 SHEET 4 AA4 5 TYR B 191 GLN B 204 0 SHEET 5 AA4 5 GLU B 209 ARG B 221 -1 O HIS B 218 N GLY B 195 SHEET 1 AA5 8 VAL C 36 ILE C 47 0 SHEET 2 AA5 8 ASP C 56 ARG C 68 -1 O THR C 60 N ALA C 45 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 LEU C 118 N LEU C 81 SHEET 6 AA5 8 THR C 123 ALA C 135 -1 O GLY C 127 N MET C 115 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 44 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 LEU C 214 N GLN C 148 SHEET 4 AA6 4 ILE C 188 PHE C 200 -1 N VAL C 198 O TYR C 205 SHEET 1 AA7 9 THR D 39 SER D 49 0 SHEET 2 AA7 9 VAL D 53 SER D 54 0 SHEET 3 AA7 9 GLU D 59 LYS D 71 -1 O GLU D 59 N SER D 54 SHEET 4 AA7 9 VAL D 83 LEU D 86 0 SHEET 5 AA7 9 VAL D 108 ALA D 109 0 SHEET 6 AA7 9 LYS D 117 THR D 122 -1 O ILE D 121 N LEU D 84 SHEET 7 AA7 9 THR D 126 GLU D 138 -1 O THR D 126 N THR D 122 SHEET 8 AA7 9 VAL D 167 TRP D 171 1 O GLU D 170 N THR D 43 SHEET 9 AA7 9 VAL D 179 VAL D 181 1 O VAL D 180 N ILE D 45 SHEET 1 AA8 5 THR D 99 PHE D 101 0 SHEET 2 AA8 5 ALA D 150 HIS D 151 0 SHEET 3 AA8 5 PRO D 154 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 4 AA8 5 TYR D 191 SER D 205 0 SHEET 5 AA8 5 GLY D 208 ARG D 221 -1 O HIS D 218 N GLY D 195 SHEET 1 AA9 7 THR E 51 ASN E 66 0 SHEET 2 AA9 7 GLU E 71 TYR E 83 -1 O THR E 81 N HIS E 54 SHEET 3 AA9 7 VAL E 95 LEU E 98 0 SHEET 4 AA9 7 SER E 116 ALA E 121 0 SHEET 5 AA9 7 ARG E 129 TRP E 134 -1 O ILE E 133 N LEU E 96 SHEET 6 AA9 7 ARG E 138 GLU E 150 -1 O ARG E 138 N TRP E 134 SHEET 7 AA9 7 ILE E 179 VAL E 190 1 O GLU E 189 N VAL E 59 SHEET 1 AB1 4 THR E 111 PHE E 113 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 LEU E 229 N HIS E 163 SHEET 4 AB1 4 PHE E 201 LYS E 214 -1 N ARG E 207 O TYR E 226 SHEET 1 AB2 4 GLN H 3 GLU H 6 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB2 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB2 4 THR H 69 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB3 6 ALA H 33 GLN H 39 0 SHEET 2 AB3 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 3 AB3 6 THR H 58 TYR H 60 -1 O TYR H 59 N ALA H 50 SHEET 4 AB3 6 ALA H 92 GLU H 99 -1 O TYR H 95 N VAL H 37 SHEET 5 AB3 6 TYR H 113 TRP H 114 -1 O TYR H 113 N LYS H 98 SHEET 6 AB3 6 THR H 118 VAL H 120 -1 O THR H 118 N TYR H 94 SHEET 1 AB4 4 LEU L 4 SER L 7 0 SHEET 2 AB4 4 ARG L 18 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB4 4 ASP L 70 SER L 76 -1 O LEU L 73 N LEU L 21 SHEET 4 AB4 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB5 7 THR L 10 LEU L 13 0 SHEET 2 AB5 7 LEU L 33 GLN L 38 0 SHEET 3 AB5 7 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 4 AB5 7 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 5 AB5 7 VAL L 85 ARG L 91 -1 O TYR L 87 N TYR L 36 SHEET 6 AB5 7 TYR L 97 PHE L 99 -1 O SER L 98 N GLN L 90 SHEET 7 AB5 7 THR L 103 ILE L 107 -1 O THR L 103 N TYR L 86 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 2.04 SSBOND 4 CYS D 139 CYS D 153 1555 1555 2.03 SSBOND 5 CYS E 151 CYS E 165 1555 1555 2.04 SSBOND 6 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.04 LINK ND2 ASN D 111 C1 NAG D 401 1555 1555 1.44 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 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.44 LINK O6 BMA M 3 C1 MAN M 7 1555 1555 1.44 LINK O2 MAN M 4 C1 MAN M 5 1555 1555 1.44 LINK O2 MAN M 5 C1 MAN M 6 1555 1555 1.44 LINK O6 MAN M 7 C1 MAN M 8 1555 1555 1.43 LINK O2 MAN M 8 C1 MAN M 9 1555 1555 1.44 CISPEP 1 VAL A 109 THR A 110 0 2.88 CISPEP 2 TYR A 143 PRO A 144 0 2.00 CISPEP 3 MET B 112 THR B 113 0 2.14 CISPEP 4 PHE B 146 PRO B 147 0 1.94 CISPEP 5 VAL C 109 THR C 110 0 1.17 CISPEP 6 TYR C 143 PRO C 144 0 3.17 CISPEP 7 MET D 112 THR D 113 0 0.91 CISPEP 8 PHE D 146 PRO D 147 0 1.96 CISPEP 9 ILE E 124 THR E 125 0 0.37 CISPEP 10 PHE E 158 PRO E 159 0 7.07 CISPEP 11 SER L 7 PRO L 8 0 -1.93 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