HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 19-JUL-24 9CQ7 TITLE G115 TCR EXTRACELLULAR DOMAIN BOUND TO FAB 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: G115 TCR DELTA CHAIN; COMPND 3 CHAIN: D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: G115 TCR GAMMA CHAIN; COMPND 7 CHAIN: G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ANTI TCR VARIABLE DELTA 2 FAB HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ANTI TCR VARIABLE DELTA 2 FAB LIGHT CHAIN; COMPND 15 CHAIN: I; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_COMMON: MOUSE; SOURCE 25 ORGANISM_TAXID: 10090; SOURCE 26 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS TCR, CD3, GAMMA DELTA, FAB, OKT3, IMMUNE RECEPTOR, T CELL, MEMBRANE KEYWDS 2 PROTEIN, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR M.HOQUE,K.SAOTOME,M.C.FRANKLIN REVDAT 1 15-JAN-25 9CQ7 0 JRNL AUTH M.HOQUE,J.B.GRIGG,T.RAMLALL,J.JONES,L.L.MCGOLDRICK,J.C.LIN, JRNL AUTH 2 W.C.OLSON,E.SMITH,M.C.FRANKLIN,T.ZHANG,K.SAOTOME JRNL TITL STRUCTURAL CHARACTERIZATION OF TWO GAMMA DELTA TCR/CD3 JRNL TITL 2 COMPLEXES. JRNL REF NAT COMMUN V. 16 318 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39747888 JRNL DOI 10.1038/S41467-024-55467-5 REMARK 2 REMARK 2 RESOLUTION. 3.21 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) : 3.210 REMARK 3 NUMBER OF PARTICLES : 156210 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 9CQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000286083. 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 : G115 GAMMA DELTA TCR/CD3 REMARK 245 COMPLEX BOUND BY OKT3 FAB 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 : 8.00 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) : 1000.00 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) : 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) : 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G, H, I, 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 VAL D 207 REMARK 465 LYS D 208 REMARK 465 THR D 209 REMARK 465 ASP D 210 REMARK 465 SER D 211 REMARK 465 THR D 212 REMARK 465 ASP D 213 REMARK 465 HIS D 214 REMARK 465 VAL D 215 REMARK 465 LYS D 216 REMARK 465 PRO D 217 REMARK 465 LYS D 218 REMARK 465 GLU D 219 REMARK 465 THR D 220 REMARK 465 GLU D 221 REMARK 465 ASN D 222 REMARK 465 THR D 223 REMARK 465 LYS D 224 REMARK 465 GLN D 225 REMARK 465 PRO D 226 REMARK 465 SER D 227 REMARK 465 LYS D 228 REMARK 465 SER D 229 REMARK 465 CYS D 230 REMARK 465 HIS D 231 REMARK 465 LYS D 232 REMARK 465 PRO D 233 REMARK 465 LYS D 234 REMARK 465 ALA D 235 REMARK 465 ILE D 236 REMARK 465 VAL D 237 REMARK 465 HIS D 238 REMARK 465 THR D 239 REMARK 465 GLU D 240 REMARK 465 LYS D 241 REMARK 465 VAL D 242 REMARK 465 ASN D 243 REMARK 465 MET D 244 REMARK 465 MET D 245 REMARK 465 SER D 246 REMARK 465 LEU D 247 REMARK 465 THR D 248 REMARK 465 VAL D 249 REMARK 465 LEU D 250 REMARK 465 GLY D 251 REMARK 465 LEU D 252 REMARK 465 ARG D 253 REMARK 465 MET D 254 REMARK 465 LEU D 255 REMARK 465 PHE D 256 REMARK 465 ALA D 257 REMARK 465 LYS D 258 REMARK 465 THR D 259 REMARK 465 VAL D 260 REMARK 465 ALA D 261 REMARK 465 VAL D 262 REMARK 465 ASN D 263 REMARK 465 PHE D 264 REMARK 465 LEU D 265 REMARK 465 LEU D 266 REMARK 465 THR D 267 REMARK 465 ALA D 268 REMARK 465 LYS D 269 REMARK 465 LEU D 270 REMARK 465 PHE D 271 REMARK 465 PHE D 272 REMARK 465 LEU D 273 REMARK 465 SER D 274 REMARK 465 ARG D 275 REMARK 465 GLY D 276 REMARK 465 ARG D 277 REMARK 465 ALA D 278 REMARK 465 LYS D 279 REMARK 465 ARG D 280 REMARK 465 GLY D 281 REMARK 465 SER D 282 REMARK 465 GLY D 283 REMARK 465 THR G 232 REMARK 465 ASP G 233 REMARK 465 VAL G 234 REMARK 465 ILE G 235 REMARK 465 THR G 236 REMARK 465 MET G 237 REMARK 465 ASP G 238 REMARK 465 PRO G 239 REMARK 465 LYS G 240 REMARK 465 ASP G 241 REMARK 465 ASN G 242 REMARK 465 CYS G 243 REMARK 465 SER G 244 REMARK 465 LYS G 245 REMARK 465 ASP G 246 REMARK 465 ALA G 247 REMARK 465 ASN G 248 REMARK 465 ASP G 249 REMARK 465 THR G 250 REMARK 465 LEU G 251 REMARK 465 LEU G 252 REMARK 465 LEU G 253 REMARK 465 GLN G 254 REMARK 465 LEU G 255 REMARK 465 THR G 256 REMARK 465 ASN G 257 REMARK 465 THR G 258 REMARK 465 SER G 259 REMARK 465 ALA G 260 REMARK 465 TYR G 261 REMARK 465 TYR G 262 REMARK 465 MET G 263 REMARK 465 TYR G 264 REMARK 465 LEU G 265 REMARK 465 LEU G 266 REMARK 465 LEU G 267 REMARK 465 LEU G 268 REMARK 465 LEU G 269 REMARK 465 LYS G 270 REMARK 465 SER G 271 REMARK 465 VAL G 272 REMARK 465 VAL G 273 REMARK 465 TYR G 274 REMARK 465 PHE G 275 REMARK 465 ALA G 276 REMARK 465 ILE G 277 REMARK 465 ILE G 278 REMARK 465 THR G 279 REMARK 465 CYS G 280 REMARK 465 CYS G 281 REMARK 465 LEU G 282 REMARK 465 LEU G 283 REMARK 465 ARG G 284 REMARK 465 ARG G 285 REMARK 465 THR G 286 REMARK 465 ALA G 287 REMARK 465 PHE G 288 REMARK 465 CYS G 289 REMARK 465 CYS G 290 REMARK 465 ASN G 291 REMARK 465 GLY G 292 REMARK 465 GLU G 293 REMARK 465 LYS G 294 REMARK 465 SER G 295 REMARK 465 SER H 120 REMARK 465 SER H 121 REMARK 465 ALA H 122 REMARK 465 LYS H 123 REMARK 465 THR H 124 REMARK 465 THR H 125 REMARK 465 PRO H 126 REMARK 465 PRO H 127 REMARK 465 SER H 128 REMARK 465 VAL H 129 REMARK 465 TYR H 130 REMARK 465 PRO H 131 REMARK 465 LEU H 132 REMARK 465 ALA H 133 REMARK 465 PRO H 134 REMARK 465 GLY H 135 REMARK 465 SER H 136 REMARK 465 ALA H 137 REMARK 465 ALA H 138 REMARK 465 GLN H 139 REMARK 465 THR H 140 REMARK 465 ASN H 141 REMARK 465 SER H 142 REMARK 465 MET H 143 REMARK 465 VAL H 144 REMARK 465 THR H 145 REMARK 465 LEU H 146 REMARK 465 GLY H 147 REMARK 465 CYS H 148 REMARK 465 LEU H 149 REMARK 465 VAL H 150 REMARK 465 LYS H 151 REMARK 465 GLY H 152 REMARK 465 TYR H 153 REMARK 465 PHE H 154 REMARK 465 PRO H 155 REMARK 465 GLU H 156 REMARK 465 PRO H 157 REMARK 465 VAL H 158 REMARK 465 THR H 159 REMARK 465 VAL H 160 REMARK 465 THR H 161 REMARK 465 TRP H 162 REMARK 465 ASN H 163 REMARK 465 SER H 164 REMARK 465 GLY H 165 REMARK 465 SER H 166 REMARK 465 LEU H 167 REMARK 465 SER H 168 REMARK 465 SER H 169 REMARK 465 GLY H 170 REMARK 465 VAL H 171 REMARK 465 HIS H 172 REMARK 465 THR H 173 REMARK 465 PHE H 174 REMARK 465 PRO H 175 REMARK 465 ALA H 176 REMARK 465 VAL H 177 REMARK 465 LEU H 178 REMARK 465 GLN H 179 REMARK 465 SER H 180 REMARK 465 ASP H 181 REMARK 465 LEU H 182 REMARK 465 TYR H 183 REMARK 465 THR H 184 REMARK 465 LEU H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 VAL H 189 REMARK 465 THR H 190 REMARK 465 VAL H 191 REMARK 465 PRO H 192 REMARK 465 SER H 193 REMARK 465 SER H 194 REMARK 465 THR H 195 REMARK 465 TRP H 196 REMARK 465 PRO H 197 REMARK 465 SER H 198 REMARK 465 GLU H 199 REMARK 465 THR H 200 REMARK 465 VAL H 201 REMARK 465 THR H 202 REMARK 465 CYS H 203 REMARK 465 ASN H 204 REMARK 465 VAL H 205 REMARK 465 ALA H 206 REMARK 465 HIS H 207 REMARK 465 PRO H 208 REMARK 465 ALA H 209 REMARK 465 SER H 210 REMARK 465 SER H 211 REMARK 465 THR H 212 REMARK 465 LYS H 213 REMARK 465 VAL H 214 REMARK 465 ASP H 215 REMARK 465 LYS H 216 REMARK 465 LYS H 217 REMARK 465 ILE H 218 REMARK 465 VAL H 219 REMARK 465 PRO H 220 REMARK 465 ARG H 221 REMARK 465 ASP H 222 REMARK 465 CYS H 223 REMARK 465 GLY H 224 REMARK 465 LYS I 105 REMARK 465 ARG I 106 REMARK 465 ALA I 107 REMARK 465 ASP I 108 REMARK 465 ALA I 109 REMARK 465 ALA I 110 REMARK 465 PRO I 111 REMARK 465 THR I 112 REMARK 465 VAL I 113 REMARK 465 SER I 114 REMARK 465 ILE I 115 REMARK 465 PHE I 116 REMARK 465 PRO I 117 REMARK 465 PRO I 118 REMARK 465 SER I 119 REMARK 465 SER I 120 REMARK 465 GLU I 121 REMARK 465 GLN I 122 REMARK 465 LEU I 123 REMARK 465 THR I 124 REMARK 465 SER I 125 REMARK 465 GLY I 126 REMARK 465 GLY I 127 REMARK 465 ALA I 128 REMARK 465 SER I 129 REMARK 465 VAL I 130 REMARK 465 VAL I 131 REMARK 465 CYS I 132 REMARK 465 PHE I 133 REMARK 465 LEU I 134 REMARK 465 ASN I 135 REMARK 465 ASN I 136 REMARK 465 PHE I 137 REMARK 465 TYR I 138 REMARK 465 PRO I 139 REMARK 465 LYS I 140 REMARK 465 ASP I 141 REMARK 465 ILE I 142 REMARK 465 ASN I 143 REMARK 465 VAL I 144 REMARK 465 LYS I 145 REMARK 465 TRP I 146 REMARK 465 LYS I 147 REMARK 465 ILE I 148 REMARK 465 ASP I 149 REMARK 465 GLY I 150 REMARK 465 SER I 151 REMARK 465 GLU I 152 REMARK 465 ARG I 153 REMARK 465 GLN I 154 REMARK 465 ASN I 155 REMARK 465 GLY I 156 REMARK 465 VAL I 157 REMARK 465 LEU I 158 REMARK 465 ASN I 159 REMARK 465 SER I 160 REMARK 465 TRP I 161 REMARK 465 THR I 162 REMARK 465 ASP I 163 REMARK 465 GLN I 164 REMARK 465 ASP I 165 REMARK 465 SER I 166 REMARK 465 LYS I 167 REMARK 465 ASP I 168 REMARK 465 SER I 169 REMARK 465 THR I 170 REMARK 465 TYR I 171 REMARK 465 SER I 172 REMARK 465 MET I 173 REMARK 465 SER I 174 REMARK 465 SER I 175 REMARK 465 THR I 176 REMARK 465 LEU I 177 REMARK 465 THR I 178 REMARK 465 LEU I 179 REMARK 465 THR I 180 REMARK 465 LYS I 181 REMARK 465 ASP I 182 REMARK 465 GLU I 183 REMARK 465 TYR I 184 REMARK 465 GLU I 185 REMARK 465 ARG I 186 REMARK 465 HIS I 187 REMARK 465 ASN I 188 REMARK 465 SER I 189 REMARK 465 TYR I 190 REMARK 465 THR I 191 REMARK 465 CYS I 192 REMARK 465 GLU I 193 REMARK 465 ALA I 194 REMARK 465 THR I 195 REMARK 465 HIS I 196 REMARK 465 LYS I 197 REMARK 465 THR I 198 REMARK 465 SER I 199 REMARK 465 THR I 200 REMARK 465 SER I 201 REMARK 465 PRO I 202 REMARK 465 ILE I 203 REMARK 465 VAL I 204 REMARK 465 LYS I 205 REMARK 465 SER I 206 REMARK 465 PHE I 207 REMARK 465 ASN I 208 REMARK 465 ARG I 209 REMARK 465 GLY I 210 REMARK 465 GLU I 211 REMARK 465 CYS I 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 OE1 GLN G 6 OG1 THR G 117 2.16 REMARK 500 O LYS D 143 ND2 ASN D 176 2.17 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 D 97 -5.38 67.66 REMARK 500 ARG D 114 98.20 -69.66 REMARK 500 ASP D 196 -125.72 56.84 REMARK 500 LYS D 198 -155.06 63.95 REMARK 500 ASP D 204 -7.85 71.19 REMARK 500 SER G 31 -120.72 62.73 REMARK 500 LEU G 49 -60.82 -102.54 REMARK 500 ILE G 64 74.02 53.52 REMARK 500 ASP G 123 -169.67 -76.71 REMARK 500 LYS G 124 93.70 -68.06 REMARK 500 ASP G 129 60.67 38.10 REMARK 500 THR G 187 -168.20 -118.85 REMARK 500 ASP G 189 -30.09 -130.28 REMARK 500 ASN G 216 32.61 -97.16 REMARK 500 THR H 87 -169.02 -127.07 REMARK 500 ALA H 92 -168.99 -160.82 REMARK 500 SER I 27 -169.39 -128.88 REMARK 500 THR I 50 71.55 46.92 REMARK 500 SER I 51 11.82 82.61 REMARK 500 SER I 92 -5.96 77.56 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 F 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45810 RELATED DB: EMDB REMARK 900 G115 GAMMA DELTA TCR/CD3 COMPLEX BOUND BY OKT3 FAB DBREF 9CQ7 D 1 283 PDB 9CQ7 9CQ7 1 283 DBREF 9CQ7 G 1 295 PDB 9CQ7 9CQ7 1 295 DBREF 9CQ7 H 1 224 PDB 9CQ7 9CQ7 1 224 DBREF 9CQ7 I 1 212 PDB 9CQ7 9CQ7 1 212 SEQRES 1 D 283 ALA ILE GLU LEU VAL PRO GLU HIS GLN THR VAL PRO VAL SEQRES 2 D 283 SER ILE GLY VAL PRO ALA THR LEU ARG CYS SER MET LYS SEQRES 3 D 283 GLY GLU ALA ILE GLY ASN TYR TYR ILE ASN TRP TYR ARG SEQRES 4 D 283 LYS THR GLN GLY ASN THR MET THR PHE ILE TYR ARG GLU SEQRES 5 D 283 LYS ASP ILE TYR GLY PRO GLY PHE LYS ASP ASN PHE GLN SEQRES 6 D 283 GLY ASP ILE ASP ILE ALA LYS ASN LEU ALA VAL LEU LYS SEQRES 7 D 283 ILE LEU ALA PRO SER GLU ARG ASP GLU GLY SER TYR TYR SEQRES 8 D 283 CYS ALA CYS ASP THR LEU GLY MET GLY GLY GLU TYR THR SEQRES 9 D 283 ASP LYS LEU ILE PHE GLY LYS GLY THR ARG VAL THR VAL SEQRES 10 D 283 GLU PRO ARG SER GLN PRO HIS THR LYS PRO SER VAL PHE SEQRES 11 D 283 VAL MET LYS ASN GLY THR ASN VAL ALA CYS LEU VAL LYS SEQRES 12 D 283 GLU PHE TYR PRO LYS ASP ILE ARG ILE ASN LEU VAL SER SEQRES 13 D 283 SER LYS LYS ILE THR GLU PHE ASP PRO ALA ILE VAL ILE SEQRES 14 D 283 SER PRO SER GLY LYS TYR ASN ALA VAL LYS LEU GLY LYS SEQRES 15 D 283 TYR GLU ASP SER ASN SER VAL THR CYS SER VAL GLN HIS SEQRES 16 D 283 ASP ASN LYS THR VAL HIS SER THR ASP PHE GLU VAL LYS SEQRES 17 D 283 THR ASP SER THR ASP HIS VAL LYS PRO LYS GLU THR GLU SEQRES 18 D 283 ASN THR LYS GLN PRO SER LYS SER CYS HIS LYS PRO LYS SEQRES 19 D 283 ALA ILE VAL HIS THR GLU LYS VAL ASN MET MET SER LEU SEQRES 20 D 283 THR VAL LEU GLY LEU ARG MET LEU PHE ALA LYS THR VAL SEQRES 21 D 283 ALA VAL ASN PHE LEU LEU THR ALA LYS LEU PHE PHE LEU SEQRES 22 D 283 SER ARG GLY ARG ALA LYS ARG GLY SER GLY SEQRES 1 G 295 ALA GLY HIS LEU GLU GLN PRO GLN ILE SER SER THR LYS SEQRES 2 G 295 THR LEU SER LYS THR ALA ARG LEU GLU CYS VAL VAL SER SEQRES 3 G 295 GLY ILE THR ILE SER ALA THR SER VAL TYR TRP TYR ARG SEQRES 4 G 295 GLU ARG PRO GLY GLU VAL ILE GLN PHE LEU VAL SER ILE SEQRES 5 G 295 SER TYR ASP GLY THR VAL ARG LYS GLU SER GLY ILE PRO SEQRES 6 G 295 SER GLY LYS PHE GLU VAL ASP ARG ILE PRO GLU THR SER SEQRES 7 G 295 THR SER THR LEU THR ILE HIS ASN VAL GLU LYS GLN ASP SEQRES 8 G 295 ILE ALA THR TYR TYR CYS ALA LEU TRP GLU ALA GLN GLN SEQRES 9 G 295 GLU LEU GLY LYS LYS ILE LYS VAL PHE GLY PRO GLY THR SEQRES 10 G 295 LYS LEU ILE ILE THR ASP LYS GLN LEU ASP ALA ASP VAL SEQRES 11 G 295 SER PRO LYS PRO THR ILE PHE LEU PRO SER ILE ALA GLU SEQRES 12 G 295 THR LYS LEU GLN LYS ALA GLY THR TYR LEU CYS LEU LEU SEQRES 13 G 295 GLU LYS PHE PHE PRO ASP VAL ILE LYS ILE HIS TRP GLN SEQRES 14 G 295 GLU LYS LYS SER ASN THR ILE LEU GLY SER GLN GLU GLY SEQRES 15 G 295 ASN THR MET LYS THR ASN ASP THR TYR MET LYS PHE SER SEQRES 16 G 295 TRP LEU THR VAL PRO GLU LYS SER LEU ASP LYS GLU HIS SEQRES 17 G 295 ARG CYS ILE VAL ARG HIS GLU ASN ASN LYS ASN GLY VAL SEQRES 18 G 295 ASP GLN GLU ILE ILE PHE PRO PRO ILE LYS THR ASP VAL SEQRES 19 G 295 ILE THR MET ASP PRO LYS ASP ASN CYS SER LYS ASP ALA SEQRES 20 G 295 ASN ASP THR LEU LEU LEU GLN LEU THR ASN THR SER ALA SEQRES 21 G 295 TYR TYR MET TYR LEU LEU LEU LEU LEU LYS SER VAL VAL SEQRES 22 G 295 TYR PHE ALA ILE ILE THR CYS CYS LEU LEU ARG ARG THR SEQRES 23 G 295 ALA PHE CYS CYS ASN GLY GLU LYS SER SEQRES 1 H 224 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS SEQRES 2 H 224 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 224 TYR THR PHE THR ASN HIS TRP ILE SER TRP VAL LYS GLN SEQRES 4 H 224 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ASN ILE PHE SEQRES 5 H 224 PRO GLY SER SER SER PRO ASN TYR ASN GLU LYS PHE LYS SEQRES 6 H 224 SER LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 224 ALA TYR MET GLN LEU SER SER LEU THR SER ASP ALA SER SEQRES 8 H 224 ALA VAL TYR TYR CYS THR ARG TRP GLY ASN TYR GLY TYR SEQRES 9 H 224 TYR TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 H 224 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR SEQRES 11 H 224 PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET SEQRES 12 H 224 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 H 224 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 H 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 15 H 224 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER THR SEQRES 16 H 224 TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO SEQRES 17 H 224 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 18 H 224 ASP CYS GLY SEQRES 1 I 212 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 I 212 SER LEU GLY GLU GLU ILE THR LEU THR CYS SER ALA SER SEQRES 3 I 212 SER ARG VAL ASN TYR MET HIS TRP TYR GLN GLN LYS SER SEQRES 4 I 212 GLY THR SER PRO LYS LEU LEU ILE TYR SER THR SER ASN SEQRES 5 I 212 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 I 212 SER GLY THR PHE TYR SER LEU THR ILE ILE SER VAL GLU SEQRES 7 I 212 ALA GLU ASP ALA ALA ASP TYR TYR CYS HIS GLN TRP SER SEQRES 8 I 212 SER TYR PRO THR PHE GLY GLY GLY THR LYS LEU GLU ILE SEQRES 9 I 212 LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO SEQRES 10 I 212 PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL SEQRES 11 I 212 VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN SEQRES 12 I 212 VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY SEQRES 13 I 212 VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER SEQRES 14 I 212 THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP SEQRES 15 I 212 GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR SEQRES 16 I 212 HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN SEQRES 17 I 212 ARG GLY GLU CYS HET NAG F 1 14 HET NAG F 2 14 HET NAG D 301 14 HET NAG G 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 5 NAG 4(C8 H15 N O6) HELIX 1 AA1 GLU G 143 LYS G 148 1 6 HELIX 2 AA2 PRO G 200 ASP G 205 1 6 HELIX 3 AA3 ASN G 217 VAL G 221 5 5 HELIX 4 AA4 GLU I 78 ALA I 82 5 5 SHEET 1 AA1 4 GLU D 3 PRO D 6 0 SHEET 2 AA1 4 ALA D 19 LYS D 26 -1 O SER D 24 N VAL D 5 SHEET 3 AA1 4 LEU D 74 ILE D 79 -1 O LEU D 77 N LEU D 21 SHEET 4 AA1 4 PHE D 64 ASP D 69 -1 N GLN D 65 O LYS D 78 SHEET 1 AA2 2 VAL D 13 SER D 14 0 SHEET 2 AA2 2 VAL D 117 GLU D 118 1 O GLU D 118 N VAL D 13 SHEET 1 AA3 4 THR D 47 PHE D 48 0 SHEET 2 AA3 4 TYR D 34 LYS D 40 -1 N ARG D 39 O THR D 47 SHEET 3 AA3 4 GLY D 88 ASP D 95 -1 O ASP D 95 N TYR D 34 SHEET 4 AA3 4 LEU D 107 PHE D 109 -1 O ILE D 108 N CYS D 94 SHEET 1 AA4 4 THR D 47 PHE D 48 0 SHEET 2 AA4 4 TYR D 34 LYS D 40 -1 N ARG D 39 O THR D 47 SHEET 3 AA4 4 GLY D 88 ASP D 95 -1 O ASP D 95 N TYR D 34 SHEET 4 AA4 4 THR D 113 VAL D 115 -1 O THR D 113 N TYR D 90 SHEET 1 AA5 2 TYR D 50 ARG D 51 0 SHEET 2 AA5 2 ILE D 55 TYR D 56 -1 O ILE D 55 N ARG D 51 SHEET 1 AA6 4 LYS D 133 ASN D 134 0 SHEET 2 AA6 4 ASN D 137 PHE D 145 -1 O ASN D 137 N ASN D 134 SHEET 3 AA6 4 TYR D 175 LYS D 182 -1 O GLY D 181 N VAL D 138 SHEET 4 AA6 4 ALA D 166 ILE D 169 -1 N VAL D 168 O ASN D 176 SHEET 1 AA7 3 ARG D 151 LEU D 154 0 SHEET 2 AA7 3 CYS D 191 GLN D 194 -1 O GLN D 194 N ARG D 151 SHEET 3 AA7 3 VAL D 200 HIS D 201 -1 O VAL D 200 N VAL D 193 SHEET 1 AA8 4 LEU G 4 GLU G 5 0 SHEET 2 AA8 4 ALA G 19 VAL G 25 -1 O VAL G 24 N GLU G 5 SHEET 3 AA8 4 THR G 79 ILE G 84 -1 O LEU G 82 N LEU G 21 SHEET 4 AA8 4 VAL G 71 ILE G 74 -1 N ILE G 74 O THR G 79 SHEET 1 AA9 2 SER G 11 THR G 14 0 SHEET 2 AA9 2 LEU G 119 THR G 122 1 O ILE G 120 N SER G 11 SHEET 1 AB1 5 VAL G 58 ARG G 59 0 SHEET 2 AB1 5 GLN G 47 ILE G 52 -1 N SER G 51 O ARG G 59 SHEET 3 AB1 5 VAL G 35 GLU G 40 -1 N TRP G 37 O LEU G 49 SHEET 4 AB1 5 THR G 94 ALA G 102 -1 O ALA G 98 N TYR G 36 SHEET 5 AB1 5 LYS G 109 PHE G 113 -1 O ILE G 110 N GLU G 101 SHEET 1 AB2 4 THR G 135 PHE G 137 0 SHEET 2 AB2 4 LEU G 153 PHE G 159 -1 O LEU G 155 N THR G 135 SHEET 3 AB2 4 TYR G 191 TRP G 196 -1 O SER G 195 N CYS G 154 SHEET 4 AB2 4 GLN G 180 GLU G 181 -1 N GLN G 180 O TRP G 196 SHEET 1 AB3 4 THR G 135 PHE G 137 0 SHEET 2 AB3 4 LEU G 153 PHE G 159 -1 O LEU G 155 N THR G 135 SHEET 3 AB3 4 TYR G 191 TRP G 196 -1 O SER G 195 N CYS G 154 SHEET 4 AB3 4 MET G 185 LYS G 186 -1 N MET G 185 O MET G 192 SHEET 1 AB4 2 GLY G 150 THR G 151 0 SHEET 2 AB4 2 THR G 198 VAL G 199 -1 O VAL G 199 N GLY G 150 SHEET 1 AB5 3 LYS G 165 GLU G 170 0 SHEET 2 AB5 3 HIS G 208 ARG G 213 -1 O ARG G 213 N LYS G 165 SHEET 3 AB5 3 GLN G 223 PHE G 227 -1 O PHE G 227 N HIS G 208 SHEET 1 AB6 4 GLN H 3 GLN H 5 0 SHEET 2 AB6 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB6 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AB6 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AB7 6 ALA H 9 LEU H 11 0 SHEET 2 AB7 6 THR H 115 THR H 118 1 O SER H 116 N GLU H 10 SHEET 3 AB7 6 ALA H 92 TRP H 99 -1 N ALA H 92 O VAL H 117 SHEET 4 AB7 6 ILE H 34 GLN H 39 -1 N GLN H 39 O VAL H 93 SHEET 5 AB7 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AB7 6 ASN H 59 TYR H 60 -1 O ASN H 59 N ASN H 50 SHEET 1 AB8 4 ALA H 9 LEU H 11 0 SHEET 2 AB8 4 THR H 115 THR H 118 1 O SER H 116 N GLU H 10 SHEET 3 AB8 4 ALA H 92 TRP H 99 -1 N ALA H 92 O VAL H 117 SHEET 4 AB8 4 MET H 108 TRP H 111 -1 O TYR H 110 N ARG H 98 SHEET 1 AB9 4 LEU I 4 THR I 5 0 SHEET 2 AB9 4 ILE I 19 ALA I 25 -1 O SER I 24 N THR I 5 SHEET 3 AB9 4 PHE I 69 ILE I 74 -1 O LEU I 72 N LEU I 21 SHEET 4 AB9 4 PHE I 61 SER I 66 -1 N SER I 62 O THR I 73 SHEET 1 AC1 6 ILE I 10 SER I 12 0 SHEET 2 AC1 6 THR I 100 GLU I 103 1 O LYS I 101 N MET I 11 SHEET 3 AC1 6 ALA I 83 TRP I 90 -1 N ALA I 83 O LEU I 102 SHEET 4 AC1 6 MET I 32 GLN I 37 -1 N HIS I 33 O HIS I 88 SHEET 5 AC1 6 LYS I 44 TYR I 48 -1 O LYS I 44 N GLN I 36 SHEET 6 AC1 6 ASN I 52 LEU I 53 -1 O ASN I 52 N TYR I 48 SHEET 1 AC2 4 ILE I 10 SER I 12 0 SHEET 2 AC2 4 THR I 100 GLU I 103 1 O LYS I 101 N MET I 11 SHEET 3 AC2 4 ALA I 83 TRP I 90 -1 N ALA I 83 O LEU I 102 SHEET 4 AC2 4 PRO I 94 PHE I 96 -1 O THR I 95 N GLN I 89 SSBOND 1 CYS D 23 CYS D 92 1555 1555 2.03 SSBOND 2 CYS D 140 CYS D 191 1555 1555 2.03 SSBOND 3 CYS G 23 CYS G 97 1555 1555 2.03 SSBOND 4 CYS G 154 CYS G 210 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 6 CYS I 23 CYS I 87 1555 1555 2.04 LINK ND2 ASN D 197 C1 NAG D 301 1555 1555 1.44 LINK ND2 ASN G 188 C1 NAG G 301 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 CISPEP 1 SER I 7 PRO I 8 0 -0.09 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