HEADER SIGNALING PROTEIN 26-FEB-24 9AST TITLE CRYO-EM STRUCTURE OF XCR1 SIGNALING COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: LYMPHOTACTIN; COMPND 9 CHAIN: L; COMPND 10 SYNONYM: ATAC,C MOTIF CHEMOKINE 1,CYTOKINE SCM-1,LYMPHOTAXIN,SCM-1- COMPND 11 ALPHA,SMALL-INDUCIBLE CYTOKINE C1,XC CHEMOKINE LIGAND 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: CHEMOKINE XC RECEPTOR 1,NON STRUCTURAL POLYPROTEIN; COMPND 15 CHAIN: R; COMPND 16 SYNONYM: G-PROTEIN COUPLED RECEPTOR 5,LYMPHOTACTIN RECEPTOR,XC COMPND 17 CHEMOKINE RECEPTOR 1; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 21 BETA-1; COMPND 22 CHAIN: B; COMPND 23 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 27 GAMMA-2; COMPND 28 CHAIN: G; COMPND 29 SYNONYM: G GAMMA-I; COMPND 30 ENGINEERED: YES; COMPND 31 MOL_ID: 6; COMPND 32 MOLECULE: SCFV16; COMPND 33 CHAIN: E; COMPND 34 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: GNAI1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: XCL1, LTN, SCYC1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: XCR1, CCXCR1, GPR5; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: GNB1; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 GENE: GNG2; SOURCE 34 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 38 ORGANISM_TAXID: 10090; SOURCE 39 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, XCL1, MEMBRANE PROTEIN, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR X.ZHANG,C.ZHANG REVDAT 1 11-DEC-24 9AST 0 JRNL AUTH X.ZHANG,R.R.SCHLIMGEN,S.SINGH,M.P.TOMANI,B.F.VOLKMAN,C.ZHANG JRNL TITL MOLECULAR BASIS FOR CHEMOKINE RECOGNITION AND ACTIVATION OF JRNL TITL 2 XCR1. JRNL REF PROC.NATL.ACAD.SCI.USA V. 121 32121 2024 JRNL REFN ESSN 1091-6490 JRNL PMID 39565315 JRNL DOI 10.1073/PNAS.2405732121 REMARK 2 REMARK 2 RESOLUTION. 3.07 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.070 REMARK 3 NUMBER OF PARTICLES : 255110 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 9AST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1000281872. 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 : XCL1-XCR1-GI COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TECNAI SPIRIT REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 5500.00 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, R, B, G, E 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 MET A 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 ILE A 55 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 LEU A 234 REMARK 465 ALA A 235 REMARK 465 GLU A 236 REMARK 465 ASP A 237 REMARK 465 GLU A 238 REMARK 465 GLU A 239 REMARK 465 VAL L 12 REMARK 465 SER L 13 REMARK 465 LEU L 14 REMARK 465 THR L 15 REMARK 465 THR L 16 REMARK 465 GLN L 17 REMARK 465 ARG L 18 REMARK 465 LEU L 19 REMARK 465 PRO L 20 REMARK 465 CYS L 21 REMARK 465 SER L 22 REMARK 465 ARG L 23 REMARK 465 ILE L 24 REMARK 465 LYS L 25 REMARK 465 THR L 26 REMARK 465 TYR L 27 REMARK 465 THR L 28 REMARK 465 ILE L 29 REMARK 465 THR L 30 REMARK 465 GLU L 31 REMARK 465 GLY L 32 REMARK 465 SER L 33 REMARK 465 LEU L 34 REMARK 465 ARG L 35 REMARK 465 ALA L 36 REMARK 465 VAL L 37 REMARK 465 ILE L 38 REMARK 465 PHE L 39 REMARK 465 ILE L 40 REMARK 465 THR L 41 REMARK 465 LYS L 42 REMARK 465 ARG L 43 REMARK 465 GLY L 44 REMARK 465 LEU L 45 REMARK 465 LYS L 46 REMARK 465 VAL L 47 REMARK 465 CYS L 48 REMARK 465 ALA L 49 REMARK 465 ASP L 50 REMARK 465 PRO L 51 REMARK 465 GLN L 52 REMARK 465 ALA L 53 REMARK 465 THR L 54 REMARK 465 TRP L 55 REMARK 465 VAL L 56 REMARK 465 ARG L 57 REMARK 465 ASP L 58 REMARK 465 CYS L 59 REMARK 465 VAL L 60 REMARK 465 ARG L 61 REMARK 465 SER L 62 REMARK 465 MET L 63 REMARK 465 ASP L 64 REMARK 465 ARG L 65 REMARK 465 LYS L 66 REMARK 465 SER L 67 REMARK 465 ASN L 68 REMARK 465 THR L 69 REMARK 465 ARG L 70 REMARK 465 ASN L 71 REMARK 465 ASN L 72 REMARK 465 MET L 73 REMARK 465 ILE L 74 REMARK 465 GLN L 75 REMARK 465 THR L 76 REMARK 465 LYS L 77 REMARK 465 PRO L 78 REMARK 465 THR L 79 REMARK 465 GLY L 80 REMARK 465 THR L 81 REMARK 465 GLN L 82 REMARK 465 GLN L 83 REMARK 465 SER L 84 REMARK 465 THR L 85 REMARK 465 ASN L 86 REMARK 465 THR L 87 REMARK 465 ALA L 88 REMARK 465 VAL L 89 REMARK 465 THR L 90 REMARK 465 LEU L 91 REMARK 465 THR L 92 REMARK 465 GLY L 93 REMARK 465 GLY L 94 REMARK 465 SER L 95 REMARK 465 GLY L 96 REMARK 465 SER L 97 REMARK 465 GLY L 98 REMARK 465 SER L 99 REMARK 465 GLY L 100 REMARK 465 SER L 101 REMARK 465 GLY L 102 REMARK 465 SER L 103 REMARK 465 GLY L 104 REMARK 465 SER L 105 REMARK 465 GLY L 106 REMARK 465 SER L 107 REMARK 465 GLY L 108 REMARK 465 SER L 109 REMARK 465 GLY L 110 REMARK 465 SER L 111 REMARK 465 GLY L 112 REMARK 465 SER L 113 REMARK 465 GLY L 114 REMARK 465 SER L 115 REMARK 465 LEU L 116 REMARK 465 GLU L 117 REMARK 465 VAL L 118 REMARK 465 LEU L 119 REMARK 465 PHE L 120 REMARK 465 GLN L 121 REMARK 465 GLY L 122 REMARK 465 PRO L 123 REMARK 465 ASP L 124 REMARK 465 TYR L 125 REMARK 465 LYS L 126 REMARK 465 ASP L 127 REMARK 465 ASP L 128 REMARK 465 ASP L 129 REMARK 465 ASP L 130 REMARK 465 LYS L 131 REMARK 465 GLY L 132 REMARK 465 SER L 133 REMARK 465 GLU R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 465 GLY R 5 REMARK 465 ASN R 6 REMARK 465 PRO R 7 REMARK 465 GLU R 8 REMARK 465 SER R 9 REMARK 465 THR R 10 REMARK 465 THR R 11 REMARK 465 PHE R 12 REMARK 465 PHE R 13 REMARK 465 TYR R 14 REMARK 465 TYR R 15 REMARK 465 ASP R 16 REMARK 465 LEU R 17 REMARK 465 GLN R 18 REMARK 465 SER R 19 REMARK 465 GLN R 20 REMARK 465 GLN R 304 REMARK 465 PHE R 305 REMARK 465 TRP R 306 REMARK 465 PHE R 307 REMARK 465 CYS R 308 REMARK 465 ARG R 309 REMARK 465 LEU R 310 REMARK 465 GLN R 311 REMARK 465 ALA R 312 REMARK 465 PRO R 313 REMARK 465 SER R 314 REMARK 465 PRO R 315 REMARK 465 ALA R 316 REMARK 465 SER R 317 REMARK 465 ILE R 318 REMARK 465 PRO R 319 REMARK 465 HIS R 320 REMARK 465 SER R 321 REMARK 465 PRO R 322 REMARK 465 GLY R 323 REMARK 465 ALA R 324 REMARK 465 PHE R 325 REMARK 465 ALA R 326 REMARK 465 TYR R 327 REMARK 465 GLU R 328 REMARK 465 GLY R 329 REMARK 465 ALA R 330 REMARK 465 SER R 331 REMARK 465 PHE R 332 REMARK 465 TYR R 333 REMARK 465 GLY R 334 REMARK 465 SER R 335 REMARK 465 VAL R 336 REMARK 465 PHE R 337 REMARK 465 THR R 338 REMARK 465 LEU R 339 REMARK 465 GLU R 340 REMARK 465 ASP R 341 REMARK 465 PHE R 342 REMARK 465 VAL R 343 REMARK 465 GLY R 344 REMARK 465 ASP R 345 REMARK 465 TRP R 346 REMARK 465 GLU R 347 REMARK 465 GLN R 348 REMARK 465 THR R 349 REMARK 465 ALA R 350 REMARK 465 ALA R 351 REMARK 465 TYR R 352 REMARK 465 ASN R 353 REMARK 465 LEU R 354 REMARK 465 ASP R 355 REMARK 465 GLN R 356 REMARK 465 VAL R 357 REMARK 465 LEU R 358 REMARK 465 GLU R 359 REMARK 465 GLN R 360 REMARK 465 GLY R 361 REMARK 465 GLY R 362 REMARK 465 VAL R 363 REMARK 465 SER R 364 REMARK 465 SER R 365 REMARK 465 LEU R 366 REMARK 465 LEU R 367 REMARK 465 GLN R 368 REMARK 465 ASN R 369 REMARK 465 LEU R 370 REMARK 465 ALA R 371 REMARK 465 VAL R 372 REMARK 465 SER R 373 REMARK 465 VAL R 374 REMARK 465 THR R 375 REMARK 465 PRO R 376 REMARK 465 ILE R 377 REMARK 465 GLN R 378 REMARK 465 ARG R 379 REMARK 465 ILE R 380 REMARK 465 VAL R 381 REMARK 465 ARG R 382 REMARK 465 SER R 383 REMARK 465 GLY R 384 REMARK 465 GLU R 385 REMARK 465 ASN R 386 REMARK 465 ALA R 387 REMARK 465 LEU R 388 REMARK 465 LYS R 389 REMARK 465 ILE R 390 REMARK 465 ASP R 391 REMARK 465 ILE R 392 REMARK 465 HIS R 393 REMARK 465 VAL R 394 REMARK 465 ILE R 395 REMARK 465 ILE R 396 REMARK 465 PRO R 397 REMARK 465 TYR R 398 REMARK 465 GLU R 399 REMARK 465 GLY R 400 REMARK 465 LEU R 401 REMARK 465 SER R 402 REMARK 465 ALA R 403 REMARK 465 ASP R 404 REMARK 465 GLN R 405 REMARK 465 MET R 406 REMARK 465 ALA R 407 REMARK 465 GLN R 408 REMARK 465 ILE R 409 REMARK 465 GLU R 410 REMARK 465 GLU R 411 REMARK 465 VAL R 412 REMARK 465 PHE R 413 REMARK 465 LYS R 414 REMARK 465 VAL R 415 REMARK 465 VAL R 416 REMARK 465 TYR R 417 REMARK 465 PRO R 418 REMARK 465 VAL R 419 REMARK 465 ASP R 420 REMARK 465 ASP R 421 REMARK 465 HIS R 422 REMARK 465 HIS R 423 REMARK 465 PHE R 424 REMARK 465 LYS R 425 REMARK 465 VAL R 426 REMARK 465 ILE R 427 REMARK 465 LEU R 428 REMARK 465 PRO R 429 REMARK 465 TYR R 430 REMARK 465 GLY R 431 REMARK 465 THR R 432 REMARK 465 LEU R 433 REMARK 465 VAL R 434 REMARK 465 ILE R 435 REMARK 465 ASP R 436 REMARK 465 GLY R 437 REMARK 465 VAL R 438 REMARK 465 THR R 439 REMARK 465 PRO R 440 REMARK 465 ASN R 441 REMARK 465 MET R 442 REMARK 465 LEU R 443 REMARK 465 ASN R 444 REMARK 465 TYR R 445 REMARK 465 PHE R 446 REMARK 465 GLY R 447 REMARK 465 ARG R 448 REMARK 465 PRO R 449 REMARK 465 TYR R 450 REMARK 465 GLU R 451 REMARK 465 GLY R 452 REMARK 465 ILE R 453 REMARK 465 ALA R 454 REMARK 465 VAL R 455 REMARK 465 PHE R 456 REMARK 465 ASP R 457 REMARK 465 GLY R 458 REMARK 465 LYS R 459 REMARK 465 LYS R 460 REMARK 465 ILE R 461 REMARK 465 THR R 462 REMARK 465 VAL R 463 REMARK 465 THR R 464 REMARK 465 GLY R 465 REMARK 465 THR R 466 REMARK 465 LEU R 467 REMARK 465 TRP R 468 REMARK 465 ASN R 469 REMARK 465 GLY R 470 REMARK 465 ASN R 471 REMARK 465 LYS R 472 REMARK 465 ILE R 473 REMARK 465 ILE R 474 REMARK 465 ASP R 475 REMARK 465 GLU R 476 REMARK 465 ARG R 477 REMARK 465 LEU R 478 REMARK 465 ILE R 479 REMARK 465 THR R 480 REMARK 465 PRO R 481 REMARK 465 ASP R 482 REMARK 465 GLY R 483 REMARK 465 SER R 484 REMARK 465 MET R 485 REMARK 465 LEU R 486 REMARK 465 PHE R 487 REMARK 465 ARG R 488 REMARK 465 VAL R 489 REMARK 465 THR R 490 REMARK 465 ILE R 491 REMARK 465 ASN R 492 REMARK 465 SER R 493 REMARK 465 GLY R 494 REMARK 465 GLY R 495 REMARK 465 SER R 496 REMARK 465 GLY R 497 REMARK 465 HIS R 498 REMARK 465 HIS R 499 REMARK 465 HIS R 500 REMARK 465 HIS R 501 REMARK 465 HIS R 502 REMARK 465 HIS R 503 REMARK 465 HIS R 504 REMARK 465 HIS R 505 REMARK 465 TRP R 506 REMARK 465 SER R 507 REMARK 465 HIS R 508 REMARK 465 PRO R 509 REMARK 465 GLN R 510 REMARK 465 PHE R 511 REMARK 465 GLU R 512 REMARK 465 LYS R 513 REMARK 465 GLY R 514 REMARK 465 GLY R 515 REMARK 465 GLY R 516 REMARK 465 SER R 517 REMARK 465 GLY R 518 REMARK 465 GLY R 519 REMARK 465 GLY R 520 REMARK 465 SER R 521 REMARK 465 GLY R 522 REMARK 465 GLY R 523 REMARK 465 SER R 524 REMARK 465 ALA R 525 REMARK 465 TRP R 526 REMARK 465 SER R 527 REMARK 465 HIS R 528 REMARK 465 PRO R 529 REMARK 465 GLN R 530 REMARK 465 PHE R 531 REMARK 465 GLU R 532 REMARK 465 LYS R 533 REMARK 465 MET B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 LEU B -1 REMARK 465 LEU B 0 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 SER G 8 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 GLY E 121A REMARK 465 GLY E 121B REMARK 465 GLY E 121C REMARK 465 GLY E 121D REMARK 465 SER E 121E REMARK 465 GLY E 121F REMARK 465 GLY E 121G REMARK 465 GLY E 121H REMARK 465 GLY E 121I REMARK 465 SER E 121J REMARK 465 GLY E 121K REMARK 465 GLY E 121L REMARK 465 GLY E 121M REMARK 465 GLY E 121N REMARK 465 SER E 121O REMARK 465 LEU E 236 REMARK 465 GLU E 237 REMARK 465 GLU E 238 REMARK 465 ASN E 239 REMARK 465 LEU E 240 REMARK 465 TYR E 241 REMARK 465 PHE E 242 REMARK 465 GLN E 243 REMARK 465 GLY E 244 REMARK 465 ALA E 245 REMARK 465 SER E 246 REMARK 465 HIS E 247 REMARK 465 HIS E 248 REMARK 465 HIS E 249 REMARK 465 HIS E 250 REMARK 465 HIS E 251 REMARK 465 HIS E 252 REMARK 465 HIS E 253 REMARK 465 HIS E 254 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LEU R 46 CG CD1 CD2 REMARK 470 GLU R 63 CG CD OE1 OE2 REMARK 470 ARG R 139 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 144 CG CD NE CZ NH1 NH2 REMARK 470 MET R 151 CG SD CE REMARK 470 PHE R 213 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG R 214 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 216 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 218 CG CD CE NZ REMARK 470 ARG R 219 CG CD NE CZ NH1 NH2 REMARK 470 HIS R 221 CG ND1 CD2 CE1 NE2 REMARK 470 ARG R 303 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 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 SER G 57 CD GLN G 58 0.11 REMARK 500 C SER G 57 NE2 GLN G 58 0.37 REMARK 500 O ASN G 59 N PHE G 61 0.93 REMARK 500 O GLN G 58 N PRO G 60 1.18 REMARK 500 O SER G 57 OE1 GLN G 58 1.20 REMARK 500 CA SER G 57 NE2 GLN G 58 1.21 REMARK 500 C SER G 57 CD GLN G 58 1.27 REMARK 500 O SER G 57 NE2 GLN G 58 1.30 REMARK 500 O GLN G 58 CD PRO G 60 1.40 REMARK 500 SG CYS R 22 SG CYS R 259 1.59 REMARK 500 O SER G 57 CG GLN G 58 1.59 REMARK 500 C ASN G 59 N PHE G 61 1.94 REMARK 500 O ASN G 59 CA PHE G 61 1.99 REMARK 500 C GLN G 58 CD PRO G 60 2.01 REMARK 500 O PRO G 55 N SER G 57 2.05 REMARK 500 C GLN G 58 N PRO G 60 2.15 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 39 65.62 -104.80 REMARK 500 LYS A 314 48.77 -91.74 REMARK 500 LEU R 62 55.41 -90.34 REMARK 500 VAL R 288 -59.84 -123.86 REMARK 500 GLU B 130 -168.65 -73.20 REMARK 500 GLU B 215 -60.53 -90.75 REMARK 500 LEU G 19 -76.58 -83.56 REMARK 500 MET G 21 -75.40 -98.46 REMARK 500 ASN G 24 76.01 -105.02 REMARK 500 ALA G 56 16.82 -48.67 REMARK 500 SER G 57 69.40 -102.81 REMARK 500 GLN G 58 -53.60 158.63 REMARK 500 ASN G 59 30.59 -10.35 REMARK 500 PRO G 60 -7.12 -6.68 REMARK 500 VAL E 48 -62.28 -121.14 REMARK 500 MET E 180 -11.64 72.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43825 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF XCR1 SIGNALING COMPLEX DBREF 9AST A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 9AST L 1 93 UNP P47992 XCL1_HUMAN 22 114 DBREF 9AST R 2 333 UNP P46094 XCR1_HUMAN 2 333 DBREF1 9AST R 335 492 UNP A0A482LYE4_9VIRU DBREF2 9AST R A0A482LYE4 71 228 DBREF 9AST B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9AST G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9AST E 2 254 PDB 9AST 9AST 2 254 SEQADV 9AST ASN A 47 UNP P63096 SER 47 ENGINEERED MUTATION SEQADV 9AST ALA A 203 UNP P63096 GLY 203 ENGINEERED MUTATION SEQADV 9AST ALA A 245 UNP P63096 GLU 245 ENGINEERED MUTATION SEQADV 9AST SER A 326 UNP P63096 ALA 326 ENGINEERED MUTATION SEQADV 9AST CYS L 21 UNP P47992 VAL 42 CONFLICT SEQADV 9AST CYS L 59 UNP P47992 VAL 80 CONFLICT SEQADV 9AST GLY L 94 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 95 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 96 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 97 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 98 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 99 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 100 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 101 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 102 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 103 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 104 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 105 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 106 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 107 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 108 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 109 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 110 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 111 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 112 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 113 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 114 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 115 UNP P47992 EXPRESSION TAG SEQADV 9AST LEU L 116 UNP P47992 EXPRESSION TAG SEQADV 9AST GLU L 117 UNP P47992 EXPRESSION TAG SEQADV 9AST VAL L 118 UNP P47992 EXPRESSION TAG SEQADV 9AST LEU L 119 UNP P47992 EXPRESSION TAG SEQADV 9AST PHE L 120 UNP P47992 EXPRESSION TAG SEQADV 9AST GLN L 121 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 122 UNP P47992 EXPRESSION TAG SEQADV 9AST PRO L 123 UNP P47992 EXPRESSION TAG SEQADV 9AST ASP L 124 UNP P47992 EXPRESSION TAG SEQADV 9AST TYR L 125 UNP P47992 EXPRESSION TAG SEQADV 9AST LYS L 126 UNP P47992 EXPRESSION TAG SEQADV 9AST ASP L 127 UNP P47992 EXPRESSION TAG SEQADV 9AST ASP L 128 UNP P47992 EXPRESSION TAG SEQADV 9AST ASP L 129 UNP P47992 EXPRESSION TAG SEQADV 9AST ASP L 130 UNP P47992 EXPRESSION TAG SEQADV 9AST LYS L 131 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY L 132 UNP P47992 EXPRESSION TAG SEQADV 9AST SER L 133 UNP P47992 EXPRESSION TAG SEQADV 9AST GLY R 334 UNP P46094 LINKER SEQADV 9AST GLU R 347 UNP A0A482LYE ARG 83 CONFLICT SEQADV 9AST ALA R 351 UNP A0A482LYE GLY 87 CONFLICT SEQADV 9AST LEU R 367 UNP A0A482LYE PHE 103 CONFLICT SEQADV 9AST ALA R 371 UNP A0A482LYE GLY 107 CONFLICT SEQADV 9AST ARG R 382 UNP A0A482LYE LEU 118 CONFLICT SEQADV 9AST ALA R 387 UNP A0A482LYE GLY 123 CONFLICT SEQADV 9AST ALA R 403 UNP A0A482LYE GLY 139 CONFLICT SEQADV 9AST ALA R 407 UNP A0A482LYE GLY 143 CONFLICT SEQADV 9AST GLU R 411 UNP A0A482LYE LYS 147 CONFLICT SEQADV 9AST VAL R 412 UNP A0A482LYE ILE 148 CONFLICT SEQADV 9AST PRO R 429 UNP A0A482LYE HIS 165 CONFLICT SEQADV 9AST LEU R 443 UNP A0A482LYE ILE 179 CONFLICT SEQADV 9AST ASN R 444 UNP A0A482LYE ASP 180 CONFLICT SEQADV 9AST THR R 480 UNP A0A482LYE ASN 216 CONFLICT SEQADV 9AST MET R 485 UNP A0A482LYE LEU 221 CONFLICT SEQADV 9AST SER R 493 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 494 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 495 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 496 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 497 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 498 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 499 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 500 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 501 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 502 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 503 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 504 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 505 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST TRP R 506 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 507 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 508 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST PRO R 509 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLN R 510 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST PHE R 511 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLU R 512 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST LYS R 513 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 514 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 515 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 516 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 517 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 518 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 519 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 520 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 521 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 522 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLY R 523 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 524 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST ALA R 525 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST TRP R 526 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST SER R 527 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST HIS R 528 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST PRO R 529 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLN R 530 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST PHE R 531 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST GLU R 532 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST LYS R 533 UNP A0A482LYE EXPRESSION TAG SEQADV 9AST MET B -10 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -9 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -8 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -7 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -6 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -5 UNP P62873 EXPRESSION TAG SEQADV 9AST HIS B -4 UNP P62873 EXPRESSION TAG SEQADV 9AST GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9AST SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9AST LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9AST LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9AST GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9AST GLN G 17 UNP P59768 GLU 17 CONFLICT SEQADV 9AST GLN G 58 UNP P59768 GLU 58 CONFLICT SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS ASN THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS ALA SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 L 133 VAL GLY SER GLU VAL SER ASP LYS ARG THR CYS VAL SER SEQRES 2 L 133 LEU THR THR GLN ARG LEU PRO CYS SER ARG ILE LYS THR SEQRES 3 L 133 TYR THR ILE THR GLU GLY SER LEU ARG ALA VAL ILE PHE SEQRES 4 L 133 ILE THR LYS ARG GLY LEU LYS VAL CYS ALA ASP PRO GLN SEQRES 5 L 133 ALA THR TRP VAL ARG ASP CYS VAL ARG SER MET ASP ARG SEQRES 6 L 133 LYS SER ASN THR ARG ASN ASN MET ILE GLN THR LYS PRO SEQRES 7 L 133 THR GLY THR GLN GLN SER THR ASN THR ALA VAL THR LEU SEQRES 8 L 133 THR GLY GLY SER GLY SER GLY SER GLY SER GLY SER GLY SEQRES 9 L 133 SER GLY SER GLY SER GLY SER GLY SER GLY SER LEU GLU SEQRES 10 L 133 VAL LEU PHE GLN GLY PRO ASP TYR LYS ASP ASP ASP ASP SEQRES 11 L 133 LYS GLY SER SEQRES 1 R 532 GLU SER SER GLY ASN PRO GLU SER THR THR PHE PHE TYR SEQRES 2 R 532 TYR ASP LEU GLN SER GLN PRO CYS GLU ASN GLN ALA TRP SEQRES 3 R 532 VAL PHE ALA THR LEU ALA THR THR VAL LEU TYR CYS LEU SEQRES 4 R 532 VAL PHE LEU LEU SER LEU VAL GLY ASN SER LEU VAL LEU SEQRES 5 R 532 TRP VAL LEU VAL LYS TYR GLU SER LEU GLU SER LEU THR SEQRES 6 R 532 ASN ILE PHE ILE LEU ASN LEU CYS LEU SER ASP LEU VAL SEQRES 7 R 532 PHE ALA CYS LEU LEU PRO VAL TRP ILE SER PRO TYR HIS SEQRES 8 R 532 TRP GLY TRP VAL LEU GLY ASP PHE LEU CYS LYS LEU LEU SEQRES 9 R 532 ASN MET ILE PHE SER ILE SER LEU TYR SER SER ILE PHE SEQRES 10 R 532 PHE LEU THR ILE MET THR ILE HIS ARG TYR LEU SER VAL SEQRES 11 R 532 VAL SER PRO LEU SER THR LEU ARG VAL PRO THR LEU ARG SEQRES 12 R 532 CYS ARG VAL LEU VAL THR MET ALA VAL TRP VAL ALA SER SEQRES 13 R 532 ILE LEU SER SER ILE LEU ASP THR ILE PHE HIS LYS VAL SEQRES 14 R 532 LEU SER SER GLY CYS ASP TYR SER GLU LEU THR TRP TYR SEQRES 15 R 532 LEU THR SER VAL TYR GLN HIS ASN LEU PHE PHE LEU LEU SEQRES 16 R 532 SER LEU GLY ILE ILE LEU PHE CYS TYR VAL GLU ILE LEU SEQRES 17 R 532 ARG THR LEU PHE ARG SER ARG SER LYS ARG ARG HIS ARG SEQRES 18 R 532 THR VAL LYS LEU ILE PHE ALA ILE VAL VAL ALA TYR PHE SEQRES 19 R 532 LEU SER TRP GLY PRO TYR ASN PHE THR LEU PHE LEU GLN SEQRES 20 R 532 THR LEU PHE ARG THR GLN ILE ILE ARG SER CYS GLU ALA SEQRES 21 R 532 LYS GLN GLN LEU GLU TYR ALA LEU LEU ILE CYS ARG ASN SEQRES 22 R 532 LEU ALA PHE SER HIS CYS CYS PHE ASN PRO VAL LEU TYR SEQRES 23 R 532 VAL PHE VAL GLY VAL LYS PHE ARG THR HIS LEU LYS HIS SEQRES 24 R 532 VAL LEU ARG GLN PHE TRP PHE CYS ARG LEU GLN ALA PRO SEQRES 25 R 532 SER PRO ALA SER ILE PRO HIS SER PRO GLY ALA PHE ALA SEQRES 26 R 532 TYR GLU GLY ALA SER PHE TYR GLY SER VAL PHE THR LEU SEQRES 27 R 532 GLU ASP PHE VAL GLY ASP TRP GLU GLN THR ALA ALA TYR SEQRES 28 R 532 ASN LEU ASP GLN VAL LEU GLU GLN GLY GLY VAL SER SER SEQRES 29 R 532 LEU LEU GLN ASN LEU ALA VAL SER VAL THR PRO ILE GLN SEQRES 30 R 532 ARG ILE VAL ARG SER GLY GLU ASN ALA LEU LYS ILE ASP SEQRES 31 R 532 ILE HIS VAL ILE ILE PRO TYR GLU GLY LEU SER ALA ASP SEQRES 32 R 532 GLN MET ALA GLN ILE GLU GLU VAL PHE LYS VAL VAL TYR SEQRES 33 R 532 PRO VAL ASP ASP HIS HIS PHE LYS VAL ILE LEU PRO TYR SEQRES 34 R 532 GLY THR LEU VAL ILE ASP GLY VAL THR PRO ASN MET LEU SEQRES 35 R 532 ASN TYR PHE GLY ARG PRO TYR GLU GLY ILE ALA VAL PHE SEQRES 36 R 532 ASP GLY LYS LYS ILE THR VAL THR GLY THR LEU TRP ASN SEQRES 37 R 532 GLY ASN LYS ILE ILE ASP GLU ARG LEU ILE THR PRO ASP SEQRES 38 R 532 GLY SER MET LEU PHE ARG VAL THR ILE ASN SER GLY GLY SEQRES 39 R 532 SER GLY HIS HIS HIS HIS HIS HIS HIS HIS TRP SER HIS SEQRES 40 R 532 PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER SEQRES 41 R 532 GLY GLY SER ALA TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 B 351 MET HIS HIS HIS HIS HIS HIS GLY SER LEU LEU GLN SER SEQRES 2 B 351 GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS SEQRES 3 B 351 ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA SEQRES 4 B 351 THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY SEQRES 5 B 351 ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS SEQRES 6 B 351 LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER SEQRES 7 B 351 ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE SEQRES 8 B 351 ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE SEQRES 9 B 351 PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA SEQRES 10 B 351 PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN SEQRES 11 B 351 ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN SEQRES 12 B 351 VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR SEQRES 13 B 351 LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL SEQRES 14 B 351 THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE SEQRES 15 B 351 GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR SEQRES 16 B 351 GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG SEQRES 17 B 351 LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU SEQRES 18 B 351 TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR SEQRES 19 B 351 GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO SEQRES 20 B 351 ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR SEQRES 21 B 351 CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET SEQRES 22 B 351 THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER SEQRES 23 B 351 VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY SEQRES 24 B 351 TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS SEQRES 25 B 351 ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG SEQRES 26 B 351 VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL SEQRES 27 B 351 ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLN GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLN ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 E 266 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 E 266 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 3 E 266 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 E 266 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 E 266 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 6 E 266 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 7 E 266 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 8 E 266 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 9 E 266 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 10 E 266 VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 E 266 GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA SEQRES 12 E 266 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 266 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 266 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 266 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 266 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 266 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 266 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 266 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 E 266 LEU GLU GLU ASN LEU TYR PHE GLN GLY ALA SER HIS HIS SEQRES 21 E 266 HIS HIS HIS HIS HIS HIS HELIX 1 AA1 SER A 6 GLU A 33 1 28 HELIX 2 AA2 GLY A 45 GLN A 52 1 8 HELIX 3 AA3 GLU A 207 ILE A 212 1 6 HELIX 4 AA4 HIS A 213 GLU A 216 5 4 HELIX 5 AA5 SER A 228 TYR A 230 5 3 HELIX 6 AA6 ASN A 241 ASN A 255 1 15 HELIX 7 AA7 LYS A 270 SER A 281 1 12 HELIX 8 AA8 PRO A 282 CYS A 286 5 5 HELIX 9 AA9 THR A 295 LEU A 310 1 16 HELIX 10 AB1 LYS A 330 GLY A 352 1 23 HELIX 11 AB2 GLN R 25 TYR R 59 1 35 HELIX 12 AB3 SER R 64 LEU R 84 1 21 HELIX 13 AB4 PRO R 85 TRP R 87 5 3 HELIX 14 AB5 ILE R 88 GLY R 94 1 7 HELIX 15 AB6 GLY R 98 SER R 133 1 36 HELIX 16 AB7 SER R 133 ARG R 139 1 7 HELIX 17 AB8 THR R 142 PHE R 167 1 26 HELIX 18 AB9 GLU R 179 SER R 215 1 37 HELIX 19 AC1 ARG R 219 THR R 253 1 35 HELIX 20 AC2 SER R 258 SER R 278 1 21 HELIX 21 AC3 SER R 278 VAL R 288 1 11 HELIX 22 AC4 GLY R 291 ARG R 303 1 13 HELIX 23 AC5 GLN B 6 CYS B 25 1 20 HELIX 24 AC6 THR B 29 THR B 34 1 6 HELIX 25 AC7 ASN B 35 ILE B 37 5 3 HELIX 26 AC8 ALA G 10 MET G 21 1 12 HELIX 27 AC9 LYS G 29 HIS G 44 1 16 HELIX 28 AD1 ALA E 28 PHE E 32 5 5 SHEET 1 AA1 6 VAL A 185 THR A 190 0 SHEET 2 AA1 6 HIS A 195 ASP A 200 -1 O ASP A 200 N VAL A 185 SHEET 3 AA1 6 VAL A 34 LEU A 38 1 N VAL A 34 O LYS A 197 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA1 6 SER A 263 ASN A 269 1 O ILE A 265 N PHE A 223 SHEET 6 AA1 6 ILE A 319 PHE A 323 1 O HIS A 322 N LEU A 268 SHEET 1 AA2 2 ARG L 9 THR L 10 0 SHEET 2 AA2 2 CYS R 22 GLU R 23 -1 O CYS R 22 N THR L 10 SHEET 1 AA3 2 LYS R 169 VAL R 170 0 SHEET 2 AA3 2 CYS R 175 ASP R 176 -1 O ASP R 176 N LYS R 169 SHEET 1 AA4 4 ARG B 46 LEU B 51 0 SHEET 2 AA4 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA4 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA4 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA5 4 ILE B 58 TRP B 63 0 SHEET 2 AA5 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA5 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA5 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA6 4 VAL B 100 TYR B 105 0 SHEET 2 AA6 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA6 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA6 4 ARG B 134 ALA B 140 -1 O LEU B 139 N CYS B 121 SHEET 1 AA7 4 LEU B 146 PHE B 151 0 SHEET 2 AA7 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA7 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA7 4 GLN B 176 THR B 181 -1 O PHE B 180 N CYS B 166 SHEET 1 AA8 4 VAL B 187 LEU B 192 0 SHEET 2 AA8 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA8 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA8 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208 SHEET 1 AA9 4 ILE B 229 PHE B 234 0 SHEET 2 AA9 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA9 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA9 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AB1 4 ILE B 273 PHE B 278 0 SHEET 2 AB1 4 LEU B 284 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AB1 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AB1 4 ARG B 304 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AB2 4 GLN E 3 SER E 7 0 SHEET 2 AB2 4 SER E 17 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AB2 4 THR E 78 THR E 84 -1 O MET E 83 N ARG E 18 SHEET 4 AB2 4 PHE E 68 ASP E 73 -1 N SER E 71 O PHE E 80 SHEET 1 AB3 6 GLY E 10 VAL E 12 0 SHEET 2 AB3 6 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10 SHEET 3 AB3 6 ALA E 92 SER E 99 -1 N ALA E 92 O LEU E 117 SHEET 4 AB3 6 GLY E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AB3 6 LEU E 45 ILE E 51 -1 O ILE E 51 N MET E 34 SHEET 6 AB3 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB4 4 MET E 128 THR E 129 0 SHEET 2 AB4 4 VAL E 143 SER E 149 -1 O ARG E 148 N THR E 129 SHEET 3 AB4 4 ALA E 199 ILE E 204 -1 O LEU E 202 N ILE E 145 SHEET 4 AB4 4 PHE E 191 SER E 196 -1 N SER E 192 O THR E 203 SHEET 1 AB5 5 ASN E 182 LEU E 183 0 SHEET 2 AB5 5 PRO E 173 TYR E 178 -1 N TYR E 178 O ASN E 182 SHEET 3 AB5 5 LEU E 162 GLN E 167 -1 N LEU E 166 O GLN E 174 SHEET 4 AB5 5 VAL E 214 GLN E 219 -1 O MET E 218 N TYR E 163 SHEET 5 AB5 5 THR E 231 LYS E 232 -1 O THR E 231 N TYR E 215 SSBOND 1 CYS R 102 CYS R 175 1555 1555 2.03 SSBOND 2 CYS E 147 CYS E 217 1555 1555 2.03 CISPEP 1 TYR E 223 PRO E 224 0 1.10 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