HEADER VIRAL PROTEIN 24-MAY-23 8P5M TITLE SARS-COV-2 SPIKE RBD IN COMPLEX WITH MAB-23 (FAB) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MAB-23 (HEAVY CHAIN VARIABLE DOMAIN); COMPND 7 CHAIN: G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAB-23 (LIGHT CHAIN VARIABLE DOMAIN); COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, SPIKE, COMPLEX, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.DAS,B.M.HALLBERG JRNL AUTH H.DAS,B.M.HALLBERG JRNL TITL SARS-COV-2 SPIKE RBD IN COMPLEX WITH MAB-23 (FAB DOMAINS) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, EPU, WARP, COOT, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7KSG REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 135612 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 8P5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292127783. 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 : SPIKE RBD (TWO MOLECULES) IN REMARK 245 COMPLEX WITH TWO FU2 NANOBODIES; REMARK 245 SARS-COV-2 SPIKE (RBD); REMARK 245 MONOCLONAL ANTIBODY MAB-23 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.10 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 : 4774 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 48.60 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, G, L 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 LYS I 528 REMARK 465 ALA G 118 REMARK 465 SER G 119 REMARK 465 THR G 120 REMARK 465 LYS G 121 REMARK 465 GLY G 122 REMARK 465 PRO G 123 REMARK 465 SER G 124 REMARK 465 VAL G 125 REMARK 465 PHE G 126 REMARK 465 PRO G 127 REMARK 465 LEU G 128 REMARK 465 ALA G 129 REMARK 465 PRO G 130 REMARK 465 SER G 131 REMARK 465 SER G 132 REMARK 465 LYS G 133 REMARK 465 SER G 134 REMARK 465 THR G 135 REMARK 465 SER G 136 REMARK 465 GLY G 137 REMARK 465 GLY G 138 REMARK 465 THR G 139 REMARK 465 ALA G 140 REMARK 465 ALA G 141 REMARK 465 LEU G 142 REMARK 465 GLY G 143 REMARK 465 LEU G 144 REMARK 465 VAL G 145 REMARK 465 LYS G 146 REMARK 465 ASP G 147 REMARK 465 TYR G 148 REMARK 465 PHE G 149 REMARK 465 PRO G 150 REMARK 465 GLU G 151 REMARK 465 VAL G 152 REMARK 465 THR G 153 REMARK 465 SER G 154 REMARK 465 TRP G 155 REMARK 465 ASN G 156 REMARK 465 SER G 157 REMARK 465 GLY G 158 REMARK 465 ALA G 159 REMARK 465 LEU G 160 REMARK 465 THR G 161 REMARK 465 SER G 162 REMARK 465 GLY G 163 REMARK 465 VAL G 164 REMARK 465 HIS G 165 REMARK 465 THR G 166 REMARK 465 PHE G 167 REMARK 465 PRO G 168 REMARK 465 ALA G 169 REMARK 465 VAL G 170 REMARK 465 LEU G 171 REMARK 465 GLN G 172 REMARK 465 SER G 173 REMARK 465 SER G 174 REMARK 465 GLY G 175 REMARK 465 LEU G 176 REMARK 465 TYR G 177 REMARK 465 SER G 178 REMARK 465 LEU G 179 REMARK 465 SER G 180 REMARK 465 SER G 181 REMARK 465 VAL G 182 REMARK 465 VAL G 183 REMARK 465 THR G 184 REMARK 465 VAL G 185 REMARK 465 PRO G 186 REMARK 465 SER G 187 REMARK 465 SER G 188 REMARK 465 SER G 189 REMARK 465 LEU G 190 REMARK 465 GLY G 191 REMARK 465 THR G 192 REMARK 465 GLN G 193 REMARK 465 THR G 194 REMARK 465 TYR G 195 REMARK 465 ILE G 196 REMARK 465 CYS G 197 REMARK 465 ASN G 198 REMARK 465 VAL G 199 REMARK 465 ASN G 200 REMARK 465 HIS G 201 REMARK 465 LYS G 202 REMARK 465 PRO G 203 REMARK 465 SER G 204 REMARK 465 ASN G 205 REMARK 465 THR G 206 REMARK 465 LYS G 207 REMARK 465 VAL G 208 REMARK 465 ASP G 209 REMARK 465 LYS G 210 REMARK 465 VAL G 211 REMARK 465 GLU G 212 REMARK 465 PRO G 213 REMARK 465 LYS G 214 REMARK 465 SER G 215 REMARK 465 CYS G 216 REMARK 465 ASP G 217 REMARK 465 LYS G 218 REMARK 465 THR G 219 REMARK 465 HIS G 220 REMARK 465 THR G 221 REMARK 465 CYS G 222 REMARK 465 PRO G 223 REMARK 465 PRO G 224 REMARK 465 CYS G 225 REMARK 465 PRO G 226 REMARK 465 ALA G 227 REMARK 465 PRO G 228 REMARK 465 GLU G 229 REMARK 465 LEU G 230 REMARK 465 LEU G 231 REMARK 465 GLY G 232 REMARK 465 GLY G 233 REMARK 465 PRO G 234 REMARK 465 SER G 235 REMARK 465 VAL G 236 REMARK 465 PHE G 237 REMARK 465 LEU G 238 REMARK 465 PHE G 239 REMARK 465 PRO G 240 REMARK 465 PRO G 241 REMARK 465 LYS G 242 REMARK 465 PRO G 243 REMARK 465 LYS G 244 REMARK 465 ASP G 245 REMARK 465 THR G 246 REMARK 465 LEU G 247 REMARK 465 MET G 248 REMARK 465 ILE G 249 REMARK 465 SER G 250 REMARK 465 ARG G 251 REMARK 465 THR G 252 REMARK 465 PRO G 253 REMARK 465 GLU G 254 REMARK 465 VAL G 255 REMARK 465 THR G 256 REMARK 465 CYS G 257 REMARK 465 VAL G 258 REMARK 465 VAL G 259 REMARK 465 VAL G 260 REMARK 465 ASP G 261 REMARK 465 VAL G 262 REMARK 465 SER G 263 REMARK 465 HIS G 264 REMARK 465 GLU G 265 REMARK 465 ASP G 266 REMARK 465 PRO G 267 REMARK 465 GLU G 268 REMARK 465 VAL G 269 REMARK 465 LYS G 270 REMARK 465 PHE G 271 REMARK 465 ASN G 272 REMARK 465 TRP G 273 REMARK 465 TYR G 274 REMARK 465 VAL G 275 REMARK 465 ASP G 276 REMARK 465 GLY G 277 REMARK 465 VAL G 278 REMARK 465 GLU G 279 REMARK 465 VAL G 280 REMARK 465 HIS G 281 REMARK 465 ASN G 282 REMARK 465 ALA G 283 REMARK 465 LYS G 284 REMARK 465 THR G 285 REMARK 465 LYS G 286 REMARK 465 PRO G 287 REMARK 465 ARG G 288 REMARK 465 GLU G 289 REMARK 465 GLU G 290 REMARK 465 GLN G 291 REMARK 465 TYR G 292 REMARK 465 ASN G 293 REMARK 465 SER G 294 REMARK 465 THR G 295 REMARK 465 TYR G 296 REMARK 465 ARG G 297 REMARK 465 VAL G 298 REMARK 465 VAL G 299 REMARK 465 SER G 300 REMARK 465 VAL G 301 REMARK 465 LEU G 302 REMARK 465 THR G 303 REMARK 465 VAL G 304 REMARK 465 LEU G 305 REMARK 465 HIS G 306 REMARK 465 GLN G 307 REMARK 465 ASP G 308 REMARK 465 TRP G 309 REMARK 465 LEU G 310 REMARK 465 ASN G 311 REMARK 465 GLY G 312 REMARK 465 LYS G 313 REMARK 465 GLU G 314 REMARK 465 TYR G 315 REMARK 465 LYS G 316 REMARK 465 CYS G 317 REMARK 465 LYS G 318 REMARK 465 VAL G 319 REMARK 465 SER G 320 REMARK 465 ASN G 321 REMARK 465 LYS G 322 REMARK 465 ALA G 323 REMARK 465 LEU G 324 REMARK 465 PRO G 325 REMARK 465 ALA G 326 REMARK 465 PRO G 327 REMARK 465 ILE G 328 REMARK 465 GLU G 329 REMARK 465 LYS G 330 REMARK 465 THR G 331 REMARK 465 ILE G 332 REMARK 465 SER G 333 REMARK 465 LYS G 334 REMARK 465 ALA G 335 REMARK 465 LYS G 336 REMARK 465 GLY G 337 REMARK 465 GLN G 338 REMARK 465 PRO G 339 REMARK 465 ARG G 340 REMARK 465 GLU G 341 REMARK 465 PRO G 342 REMARK 465 GLN G 343 REMARK 465 VAL G 344 REMARK 465 TYR G 345 REMARK 465 THR G 346 REMARK 465 LEU G 347 REMARK 465 PRO G 348 REMARK 465 PRO G 349 REMARK 465 SER G 350 REMARK 465 ARG G 351 REMARK 465 ASP G 352 REMARK 465 GLU G 353 REMARK 465 THR G 354 REMARK 465 LYS G 355 REMARK 465 ASN G 356 REMARK 465 GLN G 357 REMARK 465 VAL G 358 REMARK 465 SER G 359 REMARK 465 LEU G 360 REMARK 465 THR G 361 REMARK 465 CYS G 362 REMARK 465 LEU G 363 REMARK 465 VAL G 364 REMARK 465 LYS G 365 REMARK 465 GLY G 366 REMARK 465 PHE G 367 REMARK 465 TYR G 368 REMARK 465 PRO G 369 REMARK 465 SER G 370 REMARK 465 ASP G 371 REMARK 465 ILE G 372 REMARK 465 ALA G 373 REMARK 465 VAL G 374 REMARK 465 GLU G 375 REMARK 465 TRP G 376 REMARK 465 GLU G 377 REMARK 465 SER G 378 REMARK 465 ASN G 379 REMARK 465 GLY G 380 REMARK 465 GLN G 381 REMARK 465 PRO G 382 REMARK 465 GLU G 383 REMARK 465 ASN G 384 REMARK 465 ASN G 385 REMARK 465 TYR G 386 REMARK 465 LYS G 387 REMARK 465 THR G 388 REMARK 465 THR G 389 REMARK 465 PRO G 390 REMARK 465 PRO G 391 REMARK 465 VAL G 392 REMARK 465 LEU G 393 REMARK 465 ASP G 394 REMARK 465 SER G 395 REMARK 465 ASP G 396 REMARK 465 GLY G 397 REMARK 465 SER G 398 REMARK 465 PHE G 399 REMARK 465 PHE G 400 REMARK 465 LEU G 401 REMARK 465 TYR G 402 REMARK 465 SER G 403 REMARK 465 LYS G 404 REMARK 465 LEU G 405 REMARK 465 THR G 406 REMARK 465 VAL G 407 REMARK 465 ASP G 408 REMARK 465 LYS G 409 REMARK 465 SER G 410 REMARK 465 ARG G 411 REMARK 465 TRP G 412 REMARK 465 GLN G 413 REMARK 465 GLN G 414 REMARK 465 GLY G 415 REMARK 465 ASN G 416 REMARK 465 VAL G 417 REMARK 465 PHE G 418 REMARK 465 SER G 419 REMARK 465 CYS G 420 REMARK 465 SER G 421 REMARK 465 VAL G 422 REMARK 465 MET G 423 REMARK 465 HIS G 424 REMARK 465 GLU G 425 REMARK 465 ALA G 426 REMARK 465 LEU G 427 REMARK 465 HIS G 428 REMARK 465 ASN G 429 REMARK 465 HIS G 430 REMARK 465 TYR G 431 REMARK 465 THR G 432 REMARK 465 GLN G 433 REMARK 465 LYS G 434 REMARK 465 SER G 435 REMARK 465 LEU G 436 REMARK 465 SER G 437 REMARK 465 LEU G 438 REMARK 465 SER G 439 REMARK 465 PRO G 440 REMARK 465 GLY G 441 REMARK 465 LYS G 442 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ALA I 352 57.67 -97.19 REMARK 500 ASP I 442 55.18 -102.05 REMARK 500 ASP G 66 -2.41 80.00 REMARK 500 ASP L 30 -130.23 57.34 REMARK 500 ALA L 51 -46.50 72.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-17451 RELATED DB: EMDB REMARK 900 SARS-COV-2 SPIKE RBD IN COMPLEX WITH MAB-23 (FAB) DBREF 8P5M I 333 528 UNP P0DTC2 SPIKE_SARS2 333 528 DBREF 8P5M G 1 442 PDB 8P5M 8P5M 1 442 DBREF 8P5M L 1 214 PDB 8P5M 8P5M 1 214 SEQRES 1 I 196 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 I 196 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 I 196 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 I 196 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 I 196 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 I 196 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 7 I 196 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 8 I 196 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 I 196 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 I 196 ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 I 196 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 I 196 GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 13 I 196 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 14 I 196 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 I 196 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 I 196 LYS SEQRES 1 G 442 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 442 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 G 442 PHE THR PHE SER ASN TYR GLY PHE HIS TRP VAL ARG GLN SEQRES 4 G 442 ALA PRO GLY LYS GLY LEU GLU TRP VAL THR ILE ILE SER SEQRES 5 G 442 TYR ASP GLY ILE THR LYS HIS TYR ALA ASP SER VAL LYS SEQRES 6 G 442 ASP ARG PHE THR VAL SER ARG ASP ASN SER LYS THR MET SEQRES 7 G 442 VAL TYR LEU GLN MET ASN ASN LEU LYS LEU ASP ASP THR SEQRES 8 G 442 ALA VAL TYR TYR CYS ALA ARG ASP LEU GLY THR TYR ASP SEQRES 9 G 442 ASP SER TRP GLY GLN GLY VAL LEU VAL THR VAL SER SER SEQRES 10 G 442 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 G 442 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 G 442 LEU VAL LYS ASP TYR PHE PRO GLU VAL THR SER TRP ASN SEQRES 13 G 442 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 G 442 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 G 442 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 G 442 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 G 442 ASP LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 18 G 442 CYS PRO PRO CYS PRO ALA PRO GLU LEU LEU GLY GLY PRO SEQRES 19 G 442 SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR LEU SEQRES 20 G 442 MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL VAL SEQRES 21 G 442 ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE ASN TRP SEQRES 22 G 442 TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS THR LYS SEQRES 23 G 442 PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG VAL VAL SEQRES 24 G 442 SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU ASN GLY SEQRES 25 G 442 LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU PRO SEQRES 26 G 442 ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY GLN SEQRES 27 G 442 PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO SER ARG SEQRES 28 G 442 ASP GLU THR LYS ASN GLN VAL SER LEU THR CYS LEU VAL SEQRES 29 G 442 LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SEQRES 30 G 442 SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO SEQRES 31 G 442 PRO VAL LEU ASP SER ASP GLY SER PHE PHE LEU TYR SER SEQRES 32 G 442 LYS LEU THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN SEQRES 33 G 442 VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN SEQRES 34 G 442 HIS TYR THR GLN LYS SER LEU SER LEU SER PRO GLY LYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER ALA LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 L 214 GLN ASN ILE ASP GLY PHE LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 ARG LEU GLN SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA ALA TYR TYR CYS GLN GLN VAL SEQRES 8 L 214 TYR SER ALA PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 214 GLU PHE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HELIX 1 AA1 PRO I 337 ASN I 343 1 7 HELIX 2 AA2 ASP I 364 ALA I 372 1 9 HELIX 3 AA3 ASP I 405 ARG I 408 5 4 HELIX 4 AA4 GLY I 416 ASN I 422 1 7 HELIX 5 AA5 LYS G 87 THR G 91 5 5 SHEET 1 AA1 5 ASN I 354 ILE I 358 0 SHEET 2 AA1 5 ASN I 394 ARG I 403 -1 O VAL I 395 N ILE I 358 SHEET 3 AA1 5 PRO I 507 GLU I 516 -1 O VAL I 510 N PHE I 400 SHEET 4 AA1 5 GLY I 431 ASN I 437 -1 N ILE I 434 O VAL I 511 SHEET 5 AA1 5 THR I 376 TYR I 380 -1 N TYR I 380 O GLY I 431 SHEET 1 AA2 2 TYR I 453 ARG I 454 0 SHEET 2 AA2 2 LEU I 492 GLN I 493 -1 O GLN I 493 N TYR I 453 SHEET 1 AA3 2 TYR I 473 GLN I 474 0 SHEET 2 AA3 2 CYS I 488 TYR I 489 -1 O TYR I 489 N TYR I 473 SHEET 1 AA4 4 GLN G 3 SER G 7 0 SHEET 2 AA4 4 LEU G 18 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AA4 4 MET G 78 MET G 83 -1 O VAL G 79 N CYS G 22 SHEET 4 AA4 4 PHE G 68 ASP G 73 -1 N THR G 69 O GLN G 82 SHEET 1 AA5 6 LEU G 11 VAL G 12 0 SHEET 2 AA5 6 VAL G 111 VAL G 115 1 O THR G 114 N VAL G 12 SHEET 3 AA5 6 ALA G 92 ARG G 98 -1 N TYR G 94 O VAL G 111 SHEET 4 AA5 6 PHE G 34 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AA5 6 LEU G 45 ILE G 51 -1 O VAL G 48 N TRP G 36 SHEET 6 AA5 6 LYS G 58 TYR G 60 -1 O HIS G 59 N ILE G 50 SHEET 1 AA6 4 LEU G 11 VAL G 12 0 SHEET 2 AA6 4 VAL G 111 VAL G 115 1 O THR G 114 N VAL G 12 SHEET 3 AA6 4 ALA G 92 ARG G 98 -1 N TYR G 94 O VAL G 111 SHEET 4 AA6 4 SER G 106 TRP G 107 -1 O SER G 106 N ARG G 98 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 2 SER L 12 ALA L 13 0 SHEET 2 AA8 2 GLU L 105 PHE L 106 1 O GLU L 105 N ALA L 13 SHEET 1 AA9 5 ARG L 53 LEU L 54 0 SHEET 2 AA9 5 LYS L 45 TYR L 49 -1 N TYR L 49 O ARG L 53 SHEET 3 AA9 5 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 4 AA9 5 ALA L 85 GLN L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 AA9 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 5 ARG L 53 LEU L 54 0 SHEET 2 AB1 5 LYS L 45 TYR L 49 -1 N TYR L 49 O ARG L 53 SHEET 3 AB1 5 LEU L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 4 AB1 5 ALA L 85 GLN L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 AB1 5 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 86 SSBOND 1 CYS I 336 CYS I 361 1555 1555 2.03 SSBOND 2 CYS I 379 CYS I 432 1555 1555 2.03 SSBOND 3 CYS I 391 CYS I 525 1555 1555 2.02 SSBOND 4 CYS I 480 CYS I 488 1555 1555 2.02 SSBOND 5 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.03 CISPEP 1 SER L 7 PRO L 8 0 4.88 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