HEADER MEMBRANE PROTEIN 18-JUN-24 9II2 TITLE CRYO-EM STRUCTURE OF THE 2:2 COMPLEX OF MGLU3 AND BETA-ARRESTIN1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: METABOTROPIC GLUTAMATE RECEPTOR 3; COMPND 3 CHAIN: R, B; COMPND 4 SYNONYM: MGLUR3; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-ARRESTIN-1; COMPND 8 CHAIN: A, C; COMPND 9 SYNONYM: ARRESTIN BETA-1,NON-VISUAL ARRESTIN-2; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: SCFV30; COMPND 13 CHAIN: S, D; COMPND 14 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: GRM3, GPRC1C, MGLUR3; 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: ARRB1, ARR1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_TAXID: 10090; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.L.WEN,M.DU,X.YANG,Y.Q.SHEN REVDAT 1 05-MAR-25 9II2 0 JRNL AUTH T.L.WEN,X.YANG,Y.Q.SHEN JRNL TITL CRYO-EM STRUCTURE OF THE 2:1 COMPLEX OF MGLU3 AND JRNL TITL 2 BETA-ARRESTIN1 JRNL REF NAT.CHEM.BIOL. 2025 JRNL REFN ESSN 1552-4469 JRNL DOI 10.1038/S41589-025-01858-8 REMARK 2 REMARK 2 RESOLUTION. 3.70 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 51324 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9II2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 20-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048807. 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 : GPCR/BETA-ARRESTIN/SCFV30 REMARK 245 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 : 7.20 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1900.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, S, B, C, D, E, 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 MET R 1 REMARK 465 LYS R 2 REMARK 465 MET R 3 REMARK 465 LEU R 4 REMARK 465 THR R 5 REMARK 465 ARG R 6 REMARK 465 LEU R 7 REMARK 465 GLN R 8 REMARK 465 VAL R 9 REMARK 465 LEU R 10 REMARK 465 THR R 11 REMARK 465 LEU R 12 REMARK 465 ALA R 13 REMARK 465 LEU R 14 REMARK 465 PHE R 15 REMARK 465 SER R 16 REMARK 465 LYS R 17 REMARK 465 GLY R 18 REMARK 465 PHE R 19 REMARK 465 LEU R 20 REMARK 465 LEU R 21 REMARK 465 SER R 22 REMARK 465 LEU R 23 REMARK 465 GLY R 24 REMARK 465 ASP R 25 REMARK 465 HIS R 26 REMARK 465 ASN R 27 REMARK 465 PHE R 28 REMARK 465 LEU R 29 REMARK 465 LYS R 50 REMARK 465 GLY R 51 REMARK 465 THR R 52 REMARK 465 GLY R 53 REMARK 465 THR R 54 REMARK 465 GLU R 55 REMARK 465 GLU R 56 REMARK 465 GLU R 122 REMARK 465 ALA R 123 REMARK 465 GLU R 124 REMARK 465 TYR R 125 REMARK 465 MET R 126 REMARK 465 CYS R 127 REMARK 465 ARG R 838 REMARK 465 LEU R 839 REMARK 465 HIS R 840 REMARK 465 LEU R 841 REMARK 465 ASN R 842 REMARK 465 ARG R 843 REMARK 465 PHE R 844 REMARK 465 SER R 845 REMARK 465 VAL R 846 REMARK 465 SER R 847 REMARK 465 GLY R 848 REMARK 465 THR R 849 REMARK 465 GLY R 850 REMARK 465 THR R 851 REMARK 465 THR R 852 REMARK 465 TYR R 853 REMARK 465 SER R 854 REMARK 465 VAL R 865 REMARK 465 CYS R 866 REMARK 465 ASN R 867 REMARK 465 GLY R 868 REMARK 465 ARG R 869 REMARK 465 GLU R 870 REMARK 465 VAL R 871 REMARK 465 LEU R 872 REMARK 465 ASP R 873 REMARK 465 SER R 874 REMARK 465 THR R 875 REMARK 465 THR R 876 REMARK 465 SER R 877 REMARK 465 SER R 878 REMARK 465 LEU R 879 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 ASP A 3 REMARK 465 LYS A 4 REMARK 465 ALA A 90 REMARK 465 PRO A 91 REMARK 465 GLU A 92 REMARK 465 ASP A 93 REMARK 465 ALA A 310 REMARK 465 ASN A 311 REMARK 465 SER A 330 REMARK 465 ARG A 331 REMARK 465 GLY A 332 REMARK 465 GLY A 333 REMARK 465 LEU A 334 REMARK 465 LEU A 335 REMARK 465 GLY A 336 REMARK 465 ASP A 337 REMARK 465 LEU A 338 REMARK 465 ALA A 339 REMARK 465 SER A 340 REMARK 465 GLU A 369 REMARK 465 THR A 370 REMARK 465 PRO A 371 REMARK 465 VAL A 372 REMARK 465 ASP A 373 REMARK 465 THR A 374 REMARK 465 ASN A 375 REMARK 465 LEU A 376 REMARK 465 ILE A 377 REMARK 465 GLU A 378 REMARK 465 LEU A 379 REMARK 465 ASP A 380 REMARK 465 THR A 381 REMARK 465 ASN A 382 REMARK 465 ASP A 383 REMARK 465 ASP A 384 REMARK 465 ASP A 385 REMARK 465 ILE A 386 REMARK 465 VAL A 387 REMARK 465 PHE A 388 REMARK 465 GLU A 389 REMARK 465 ASP A 390 REMARK 465 PHE A 391 REMARK 465 ALA A 392 REMARK 465 ARG A 393 REMARK 465 GLN A 394 REMARK 465 ARG A 395 REMARK 465 LEU A 396 REMARK 465 LYS A 397 REMARK 465 GLY A 398 REMARK 465 MET A 399 REMARK 465 LYS A 400 REMARK 465 ASP A 401 REMARK 465 ASP A 402 REMARK 465 LYS A 403 REMARK 465 GLU A 404 REMARK 465 GLU A 405 REMARK 465 GLU A 406 REMARK 465 GLU A 407 REMARK 465 ASP A 408 REMARK 465 GLY A 409 REMARK 465 THR A 410 REMARK 465 GLY A 411 REMARK 465 SER A 412 REMARK 465 PRO A 413 REMARK 465 GLN A 414 REMARK 465 LEU A 415 REMARK 465 ASN A 416 REMARK 465 ASN A 417 REMARK 465 ARG A 418 REMARK 465 SER S 1 REMARK 465 LYS S 987 REMARK 465 GLY S 988 REMARK 465 THR S 989 REMARK 465 THR S 990 REMARK 465 ALA S 991 REMARK 465 ALA S 992 REMARK 465 SER S 993 REMARK 465 GLY S 994 REMARK 465 SER S 995 REMARK 465 SER S 996 REMARK 465 GLY S 997 REMARK 465 GLY S 998 REMARK 465 SER S 999 REMARK 465 SER S 1000 REMARK 465 SER S 1001 REMARK 465 GLY S 1002 REMARK 465 ALA S 1003 REMARK 465 GLU S 1004 REMARK 465 VAL S 1005 REMARK 465 SER S 1122 REMARK 465 SER S 1123 REMARK 465 ALA S 1124 REMARK 465 HIS S 1125 REMARK 465 HIS S 1126 REMARK 465 HIS S 1127 REMARK 465 HIS S 1128 REMARK 465 HIS S 1129 REMARK 465 HIS S 1130 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 MET B 3 REMARK 465 LEU B 4 REMARK 465 THR B 5 REMARK 465 ARG B 6 REMARK 465 LEU B 7 REMARK 465 GLN B 8 REMARK 465 VAL B 9 REMARK 465 LEU B 10 REMARK 465 THR B 11 REMARK 465 LEU B 12 REMARK 465 ALA B 13 REMARK 465 LEU B 14 REMARK 465 PHE B 15 REMARK 465 SER B 16 REMARK 465 LYS B 17 REMARK 465 GLY B 18 REMARK 465 PHE B 19 REMARK 465 LEU B 20 REMARK 465 LEU B 21 REMARK 465 SER B 22 REMARK 465 LEU B 23 REMARK 465 GLY B 24 REMARK 465 ASP B 25 REMARK 465 HIS B 26 REMARK 465 ASN B 27 REMARK 465 PHE B 28 REMARK 465 LEU B 29 REMARK 465 LYS B 50 REMARK 465 GLY B 51 REMARK 465 THR B 52 REMARK 465 GLY B 53 REMARK 465 THR B 54 REMARK 465 GLU B 55 REMARK 465 GLU B 56 REMARK 465 GLU B 122 REMARK 465 ALA B 123 REMARK 465 GLU B 124 REMARK 465 TYR B 125 REMARK 465 MET B 126 REMARK 465 CYS B 127 REMARK 465 ARG B 838 REMARK 465 LEU B 839 REMARK 465 HIS B 840 REMARK 465 LEU B 841 REMARK 465 ASN B 842 REMARK 465 ARG B 843 REMARK 465 PHE B 844 REMARK 465 SER B 845 REMARK 465 VAL B 846 REMARK 465 SER B 847 REMARK 465 GLY B 848 REMARK 465 THR B 849 REMARK 465 GLY B 850 REMARK 465 THR B 851 REMARK 465 THR B 852 REMARK 465 TYR B 853 REMARK 465 SER B 854 REMARK 465 VAL B 865 REMARK 465 CYS B 866 REMARK 465 ASN B 867 REMARK 465 GLY B 868 REMARK 465 ARG B 869 REMARK 465 GLU B 870 REMARK 465 VAL B 871 REMARK 465 LEU B 872 REMARK 465 ASP B 873 REMARK 465 SER B 874 REMARK 465 THR B 875 REMARK 465 THR B 876 REMARK 465 SER B 877 REMARK 465 SER B 878 REMARK 465 LEU B 879 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 ASP C 3 REMARK 465 LYS C 4 REMARK 465 ALA C 90 REMARK 465 PRO C 91 REMARK 465 GLU C 92 REMARK 465 ASP C 93 REMARK 465 ALA C 310 REMARK 465 ASN C 311 REMARK 465 SER C 330 REMARK 465 ARG C 331 REMARK 465 GLY C 332 REMARK 465 GLY C 333 REMARK 465 LEU C 334 REMARK 465 LEU C 335 REMARK 465 GLY C 336 REMARK 465 ASP C 337 REMARK 465 LEU C 338 REMARK 465 ALA C 339 REMARK 465 SER C 340 REMARK 465 GLU C 369 REMARK 465 THR C 370 REMARK 465 PRO C 371 REMARK 465 VAL C 372 REMARK 465 ASP C 373 REMARK 465 THR C 374 REMARK 465 ASN C 375 REMARK 465 LEU C 376 REMARK 465 ILE C 377 REMARK 465 GLU C 378 REMARK 465 LEU C 379 REMARK 465 ASP C 380 REMARK 465 THR C 381 REMARK 465 ASN C 382 REMARK 465 ASP C 383 REMARK 465 ASP C 384 REMARK 465 ASP C 385 REMARK 465 ILE C 386 REMARK 465 VAL C 387 REMARK 465 PHE C 388 REMARK 465 GLU C 389 REMARK 465 ASP C 390 REMARK 465 PHE C 391 REMARK 465 ALA C 392 REMARK 465 ARG C 393 REMARK 465 GLN C 394 REMARK 465 ARG C 395 REMARK 465 LEU C 396 REMARK 465 LYS C 397 REMARK 465 GLY C 398 REMARK 465 MET C 399 REMARK 465 LYS C 400 REMARK 465 ASP C 401 REMARK 465 ASP C 402 REMARK 465 LYS C 403 REMARK 465 GLU C 404 REMARK 465 GLU C 405 REMARK 465 GLU C 406 REMARK 465 GLU C 407 REMARK 465 ASP C 408 REMARK 465 GLY C 409 REMARK 465 THR C 410 REMARK 465 GLY C 411 REMARK 465 SER C 412 REMARK 465 PRO C 413 REMARK 465 GLN C 414 REMARK 465 LEU C 415 REMARK 465 ASN C 416 REMARK 465 ASN C 417 REMARK 465 ARG C 418 REMARK 465 SER D 1 REMARK 465 LYS D 987 REMARK 465 GLY D 988 REMARK 465 THR D 989 REMARK 465 THR D 990 REMARK 465 ALA D 991 REMARK 465 ALA D 992 REMARK 465 SER D 993 REMARK 465 GLY D 994 REMARK 465 SER D 995 REMARK 465 SER D 996 REMARK 465 GLY D 997 REMARK 465 GLY D 998 REMARK 465 SER D 999 REMARK 465 SER D 1000 REMARK 465 SER D 1001 REMARK 465 GLY D 1002 REMARK 465 ALA D 1003 REMARK 465 GLU D 1004 REMARK 465 VAL D 1005 REMARK 465 SER D 1122 REMARK 465 SER D 1123 REMARK 465 ALA D 1124 REMARK 465 HIS D 1125 REMARK 465 HIS D 1126 REMARK 465 HIS D 1127 REMARK 465 HIS D 1128 REMARK 465 HIS D 1129 REMARK 465 HIS D 1130 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 ARG R 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 119 CG CD CE NZ REMARK 470 ASP R 121 CG OD1 OD2 REMARK 470 ASP R 129 CG OD1 OD2 REMARK 470 SER R 131 OG REMARK 470 TYR R 132 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE R 134 CG1 CG2 CD1 REMARK 470 GLN R 135 CG CD OE1 NE2 REMARK 470 GLU R 136 CG CD OE1 OE2 REMARK 470 ASN R 137 CG OD1 ND2 REMARK 470 ARG R 249 CG CD NE CZ NH1 NH2 REMARK 470 SER R 250 OG REMARK 470 ASN R 251 CG OD1 ND2 REMARK 470 ILE R 252 CG1 CG2 CD1 REMARK 470 ARG R 253 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 254 CG CD CE NZ REMARK 470 ASN R 268 CG OD1 ND2 REMARK 470 ARG R 352 CZ NH1 NH2 REMARK 470 GLN R 364 CG CD OE1 NE2 REMARK 470 ASN R 365 CG OD1 ND2 REMARK 470 LYS R 366 CG CD CE NZ REMARK 470 ARG R 367 CG CD NE CZ NH1 NH2 REMARK 470 ASN R 368 CG OD1 ND2 REMARK 470 HIS R 369 CG ND1 CD2 CE1 NE2 REMARK 470 ARG R 370 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 371 CG CD NE CZ NH1 NH2 REMARK 470 HIS R 376 CG ND1 CD2 CE1 NE2 REMARK 470 ASN R 414 CG OD1 ND2 REMARK 470 ASN R 447 CG OD1 ND2 REMARK 470 LYS R 448 CG CD CE NZ REMARK 470 ASP R 449 CG OD1 OD2 REMARK 470 ASP R 451 CG OD1 OD2 REMARK 470 ILE R 453 CD1 REMARK 470 LYS R 477 CG CD CE NZ REMARK 470 THR R 489 OG1 CG2 REMARK 470 ASP R 511 CG OD1 OD2 REMARK 470 MET R 518 CG SD CE REMARK 470 LEU R 540 CG CD1 CD2 REMARK 470 ASP R 542 CG OD1 OD2 REMARK 470 MET R 547 CG SD CE REMARK 470 ASP R 558 CG OD1 OD2 REMARK 470 LEU R 559 CG CD1 CD2 REMARK 470 ASP R 564 CG OD1 OD2 REMARK 470 LEU R 565 CG CD1 CD2 REMARK 470 ILE R 578 CG1 CG2 CD1 REMARK 470 MET R 589 CG SD CE REMARK 470 THR R 836 OG1 CG2 REMARK 470 HIS R 837 CG ND1 CD2 CE1 NE2 REMARK 470 GLN R 855 CG CD OE1 NE2 REMARK 470 SEP R 856 OG P O1P O2P O3P REMARK 470 THR R 864 OG1 CG2 REMARK 470 ASN A 15 CG OD1 ND2 REMARK 470 LYS A 17 CG CD CE NZ REMARK 470 ASP A 44 CG OD1 OD2 REMARK 470 LEU A 48 CG CD1 CD2 REMARK 470 LYS A 49 CG CD CE NZ REMARK 470 GLU A 50 CG CD OE1 OE2 REMARK 470 ARG A 51 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 94 CG CD CE NZ REMARK 470 LYS A 95 CG CD CE NZ REMARK 470 GLU A 134 CG CD OE1 OE2 REMARK 470 LYS A 138 CG CD CE NZ REMARK 470 LEU A 140 CG CD1 CD2 REMARK 470 VAL A 150 CG1 CG2 REMARK 470 LYS A 157 CG CD CE NZ REMARK 470 ARG A 177 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 189 CG CD OE1 NE2 REMARK 470 MET A 192 CG SD CE REMARK 470 ASP A 194 CG OD1 OD2 REMARK 470 ASP A 204 CG OD1 OD2 REMARK 470 GLU A 212 CG CD OE1 OE2 REMARK 470 SER A 215 OG REMARK 470 LYS A 230 CG CD CE NZ REMARK 470 VAL A 242 CG1 CG2 REMARK 470 VAL A 251 CG1 CG2 REMARK 470 GLU A 257 CG CD OE1 OE2 REMARK 470 ASP A 259 CG OD1 OD2 REMARK 470 SER A 269 OG REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 308 CG CD OE1 OE2 REMARK 470 ARG A 312 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 313 CG CD OE1 OE2 REMARK 470 ILE A 314 CG1 CG2 CD1 REMARK 470 GLU A 346 CG CD OE1 OE2 REMARK 470 GLU A 367 CG CD OE1 OE2 REMARK 470 ASN A 368 CG OD1 ND2 REMARK 470 ASP S 2 CG OD1 OD2 REMARK 470 GLN S 4 CG CD OE1 NE2 REMARK 470 THR S 6 OG1 CG2 REMARK 470 SER S 10 OG REMARK 470 SER S 11 OG REMARK 470 LEU S 12 CG CD1 CD2 REMARK 470 SER S 15 OG REMARK 470 VAL S 16 CG1 CG2 REMARK 470 ASP S 18 CG OD1 OD2 REMARK 470 ARG S 19 CG CD NE CZ NH1 NH2 REMARK 470 VAL S 20 CG1 CG2 REMARK 470 THR S 21 OG1 CG2 REMARK 470 THR S 23 OG1 CG2 REMARK 470 ARG S 25 CG CD NE CZ NH1 NH2 REMARK 470 SER S 27 OG REMARK 470 GLN S 28 CG CD OE1 NE2 REMARK 470 LYS S 43 CG CD CE NZ REMARK 470 LYS S 46 CG CD CE NZ REMARK 470 SER S 61 OG REMARK 470 SER S 66 OG REMARK 470 SER S 77 OG REMARK 470 GLN S 80 CG CD OE1 NE2 REMARK 470 GLU S 82 CG CD OE1 OE2 REMARK 470 THR S 98 OG1 CG2 REMARK 470 GLN S 101 CG CD OE1 NE2 REMARK 470 LYS S 104 CG CD CE NZ REMARK 470 GLU S 106 CG CD OE1 OE2 REMARK 470 GLN S1006 CG CD OE1 NE2 REMARK 470 VAL S1008 CG1 CG2 REMARK 470 GLU S1009 CG CD OE1 OE2 REMARK 470 ASN S1031 CG OD1 ND2 REMARK 470 LYS S1046 CG CD CE NZ REMARK 470 ASP S1065 CG OD1 OD2 REMARK 470 LYS S1068 CG CD CE NZ REMARK 470 ASP S1076 CG OD1 OD2 REMARK 470 SER S1078 OG REMARK 470 LYS S1079 CG CD CE NZ REMARK 470 THR S1094 OG1 CG2 REMARK 470 GLN S1115 CG CD OE1 NE2 REMARK 470 LEU S1118 CG CD1 CD2 REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 119 CG CD CE NZ REMARK 470 ASP B 121 CG OD1 OD2 REMARK 470 ASP B 129 CG OD1 OD2 REMARK 470 SER B 131 OG REMARK 470 TYR B 132 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE B 134 CG1 CG2 CD1 REMARK 470 GLN B 135 CG CD OE1 NE2 REMARK 470 GLU B 136 CG CD OE1 OE2 REMARK 470 ASN B 137 CG OD1 ND2 REMARK 470 ARG B 249 CG CD NE CZ NH1 NH2 REMARK 470 SER B 250 OG REMARK 470 ASN B 251 CG OD1 ND2 REMARK 470 ILE B 252 CG1 CG2 CD1 REMARK 470 ARG B 253 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 254 CG CD CE NZ REMARK 470 ASN B 268 CG OD1 ND2 REMARK 470 ARG B 352 CZ NH1 NH2 REMARK 470 GLN B 364 CG CD OE1 NE2 REMARK 470 ASN B 365 CG OD1 ND2 REMARK 470 LYS B 366 CG CD CE NZ REMARK 470 ARG B 367 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 368 CG OD1 ND2 REMARK 470 HIS B 369 CG ND1 CD2 CE1 NE2 REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 371 CG CD NE CZ NH1 NH2 REMARK 470 HIS B 376 CG ND1 CD2 CE1 NE2 REMARK 470 ASN B 414 CG OD1 ND2 REMARK 470 ASN B 447 CG OD1 ND2 REMARK 470 LYS B 448 CG CD CE NZ REMARK 470 ASP B 449 CG OD1 OD2 REMARK 470 ASP B 451 CG OD1 OD2 REMARK 470 ILE B 453 CD1 REMARK 470 LYS B 477 CG CD CE NZ REMARK 470 THR B 489 OG1 CG2 REMARK 470 ASP B 511 CG OD1 OD2 REMARK 470 MET B 518 CG SD CE REMARK 470 LEU B 540 CG CD1 CD2 REMARK 470 ASP B 542 CG OD1 OD2 REMARK 470 MET B 547 CG SD CE REMARK 470 ASP B 558 CG OD1 OD2 REMARK 470 LEU B 559 CG CD1 CD2 REMARK 470 ASP B 564 CG OD1 OD2 REMARK 470 LEU B 565 CG CD1 CD2 REMARK 470 ILE B 578 CG1 CG2 CD1 REMARK 470 MET B 589 CG SD CE REMARK 470 THR B 836 OG1 CG2 REMARK 470 HIS B 837 CG ND1 CD2 CE1 NE2 REMARK 470 GLN B 855 CG CD OE1 NE2 REMARK 470 SEP B 856 OG P O1P O2P O3P REMARK 470 THR B 864 OG1 CG2 REMARK 470 ASN C 15 CG OD1 ND2 REMARK 470 LYS C 17 CG CD CE NZ REMARK 470 ASP C 44 CG OD1 OD2 REMARK 470 LEU C 48 CG CD1 CD2 REMARK 470 LYS C 49 CG CD CE NZ REMARK 470 GLU C 50 CG CD OE1 OE2 REMARK 470 ARG C 51 CG CD NE CZ NH1 NH2 REMARK 470 PHE C 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 94 CG CD CE NZ REMARK 470 LYS C 95 CG CD CE NZ REMARK 470 GLU C 134 CG CD OE1 OE2 REMARK 470 LYS C 138 CG CD CE NZ REMARK 470 LEU C 140 CG CD1 CD2 REMARK 470 VAL C 150 CG1 CG2 REMARK 470 LYS C 157 CG CD CE NZ REMARK 470 ARG C 177 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 189 CG CD OE1 NE2 REMARK 470 MET C 192 CG SD CE REMARK 470 ASP C 194 CG OD1 OD2 REMARK 470 ASP C 204 CG OD1 OD2 REMARK 470 GLU C 212 CG CD OE1 OE2 REMARK 470 SER C 215 OG REMARK 470 LYS C 230 CG CD CE NZ REMARK 470 VAL C 242 CG1 CG2 REMARK 470 VAL C 251 CG1 CG2 REMARK 470 GLU C 257 CG CD OE1 OE2 REMARK 470 ASP C 259 CG OD1 OD2 REMARK 470 SER C 269 OG REMARK 470 ARG C 307 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 308 CG CD OE1 OE2 REMARK 470 ARG C 312 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 313 CG CD OE1 OE2 REMARK 470 ILE C 314 CG1 CG2 CD1 REMARK 470 GLU C 346 CG CD OE1 OE2 REMARK 470 GLU C 367 CG CD OE1 OE2 REMARK 470 ASN C 368 CG OD1 ND2 REMARK 470 ASP D 2 CG OD1 OD2 REMARK 470 GLN D 4 CG CD OE1 NE2 REMARK 470 THR D 6 OG1 CG2 REMARK 470 SER D 10 OG REMARK 470 SER D 11 OG REMARK 470 LEU D 12 CG CD1 CD2 REMARK 470 SER D 15 OG REMARK 470 VAL D 16 CG1 CG2 REMARK 470 ASP D 18 CG OD1 OD2 REMARK 470 ARG D 19 CG CD NE CZ NH1 NH2 REMARK 470 VAL D 20 CG1 CG2 REMARK 470 THR D 21 OG1 CG2 REMARK 470 THR D 23 OG1 CG2 REMARK 470 ARG D 25 CG CD NE CZ NH1 NH2 REMARK 470 SER D 27 OG REMARK 470 GLN D 28 CG CD OE1 NE2 REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 LYS D 46 CG CD CE NZ REMARK 470 SER D 61 OG REMARK 470 SER D 66 OG REMARK 470 SER D 77 OG REMARK 470 GLN D 80 CG CD OE1 NE2 REMARK 470 GLU D 82 CG CD OE1 OE2 REMARK 470 THR D 98 OG1 CG2 REMARK 470 GLN D 101 CG CD OE1 NE2 REMARK 470 LYS D 104 CG CD CE NZ REMARK 470 GLU D 106 CG CD OE1 OE2 REMARK 470 GLN D1006 CG CD OE1 NE2 REMARK 470 VAL D1008 CG1 CG2 REMARK 470 GLU D1009 CG CD OE1 OE2 REMARK 470 ASN D1031 CG OD1 ND2 REMARK 470 LYS D1046 CG CD CE NZ REMARK 470 ASP D1065 CG OD1 OD2 REMARK 470 LYS D1068 CG CD CE NZ REMARK 470 ASP D1076 CG OD1 OD2 REMARK 470 SER D1078 OG REMARK 470 LYS D1079 CG CD CE NZ REMARK 470 THR D1094 OG1 CG2 REMARK 470 GLN D1115 CG CD OE1 NE2 REMARK 470 LEU D1118 CG CD1 CD2 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 GLY B 148 OG SER B 154 2.16 REMARK 500 O GLY R 148 OG SER R 154 2.16 REMARK 500 O TYR B 212 OG SER B 507 2.19 REMARK 500 O TYR R 212 OG SER R 507 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR R 132 -98.29 55.99 REMARK 500 GLU R 136 -114.36 50.54 REMARK 500 TYR R 150 145.80 69.71 REMARK 500 PRO R 193 -175.78 -69.88 REMARK 500 CYS R 513 158.36 69.58 REMARK 500 MET R 547 -169.16 -125.67 REMARK 500 HIS R 601 33.84 -97.46 REMARK 500 ARG R 723 179.62 60.43 REMARK 500 LYS R 760 33.29 -99.73 REMARK 500 ILE A 31 -65.76 60.70 REMARK 500 LYS A 95 70.26 56.58 REMARK 500 ASN A 153 -161.93 56.46 REMARK 500 SER A 193 -144.55 59.36 REMARK 500 THR A 298 -179.92 -68.23 REMARK 500 GLU A 358 -65.48 -95.21 REMARK 500 ASP S 83 58.74 -93.49 REMARK 500 VAL S1051 -60.83 -121.92 REMARK 500 ARG S1090 -165.47 59.65 REMARK 500 TYR B 132 -98.25 55.95 REMARK 500 GLU B 136 -114.35 50.51 REMARK 500 TYR B 150 145.86 69.74 REMARK 500 PRO B 193 -175.78 -69.87 REMARK 500 CYS B 513 158.37 69.64 REMARK 500 MET B 547 -169.16 -125.64 REMARK 500 HIS B 601 33.84 -97.46 REMARK 500 ARG B 723 179.57 60.51 REMARK 500 LYS B 760 33.38 -99.81 REMARK 500 ILE C 31 -65.73 60.70 REMARK 500 LYS C 95 70.32 56.58 REMARK 500 ASN C 153 -161.94 56.44 REMARK 500 SER C 193 -144.54 59.39 REMARK 500 THR C 298 -179.95 -68.17 REMARK 500 GLU C 358 -65.41 -95.25 REMARK 500 ASP D 83 58.77 -93.47 REMARK 500 VAL D1051 -60.83 -121.92 REMARK 500 ARG D1090 -165.44 59.66 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 GLU R 1001 REMARK 610 GLU B 1001 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60588 RELATED DB: EMDB REMARK 900 GPCR/BETA-ARRESTIN1 COMPLEX (STATE 2) REMARK 900 RELATED ID: EMD-60941 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-60942 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-60943 RELATED DB: EMDB DBREF 9II2 R 1 879 UNP Q14832 GRM3_HUMAN 1 879 DBREF 9II2 A 1 418 UNP P49407 ARRB1_HUMAN 1 418 DBREF 9II2 S 1 1130 PDB 9II2 9II2 1 1130 DBREF 9II2 B 1 879 UNP Q14832 GRM3_HUMAN 1 879 DBREF 9II2 C 1 418 UNP P49407 ARRB1_HUMAN 1 418 DBREF 9II2 D 1 1130 PDB 9II2 9II2 1 1130 SEQADV 9II2 VAL A 59 UNP P49407 CYS 59 CONFLICT SEQADV 9II2 SER A 125 UNP P49407 CYS 125 CONFLICT SEQADV 9II2 LEU A 140 UNP P49407 CYS 140 CONFLICT SEQADV 9II2 VAL A 150 UNP P49407 CYS 150 CONFLICT SEQADV 9II2 GLU A 169 UNP P49407 ARG 169 CONFLICT SEQADV 9II2 VAL A 242 UNP P49407 CYS 242 CONFLICT SEQADV 9II2 VAL A 251 UNP P49407 CYS 251 CONFLICT SEQADV 9II2 SER A 269 UNP P49407 CYS 269 CONFLICT SEQADV 9II2 VAL C 59 UNP P49407 CYS 59 CONFLICT SEQADV 9II2 SER C 125 UNP P49407 CYS 125 CONFLICT SEQADV 9II2 LEU C 140 UNP P49407 CYS 140 CONFLICT SEQADV 9II2 VAL C 150 UNP P49407 CYS 150 CONFLICT SEQADV 9II2 GLU C 169 UNP P49407 ARG 169 CONFLICT SEQADV 9II2 VAL C 242 UNP P49407 CYS 242 CONFLICT SEQADV 9II2 VAL C 251 UNP P49407 CYS 251 CONFLICT SEQADV 9II2 SER C 269 UNP P49407 CYS 269 CONFLICT SEQRES 1 R 879 MET LYS MET LEU THR ARG LEU GLN VAL LEU THR LEU ALA SEQRES 2 R 879 LEU PHE SER LYS GLY PHE LEU LEU SER LEU GLY ASP HIS SEQRES 3 R 879 ASN PHE LEU ARG ARG GLU ILE LYS ILE GLU GLY ASP LEU SEQRES 4 R 879 VAL LEU GLY GLY LEU PHE PRO ILE ASN GLU LYS GLY THR SEQRES 5 R 879 GLY THR GLU GLU CYS GLY ARG ILE ASN GLU ASP ARG GLY SEQRES 6 R 879 ILE GLN ARG LEU GLU ALA MET LEU PHE ALA ILE ASP GLU SEQRES 7 R 879 ILE ASN LYS ASP ASP TYR LEU LEU PRO GLY VAL LYS LEU SEQRES 8 R 879 GLY VAL HIS ILE LEU ASP THR CYS SER ARG ASP THR TYR SEQRES 9 R 879 ALA LEU GLU GLN SER LEU GLU PHE VAL ARG ALA SER LEU SEQRES 10 R 879 THR LYS VAL ASP GLU ALA GLU TYR MET CYS PRO ASP GLY SEQRES 11 R 879 SER TYR ALA ILE GLN GLU ASN ILE PRO LEU LEU ILE ALA SEQRES 12 R 879 GLY VAL ILE GLY GLY SER TYR SER SER VAL SER ILE GLN SEQRES 13 R 879 VAL ALA ASN LEU LEU ARG LEU PHE GLN ILE PRO GLN ILE SEQRES 14 R 879 SER TYR ALA SER THR SER ALA LYS LEU SER ASP LYS SER SEQRES 15 R 879 ARG TYR ASP TYR PHE ALA ARG THR VAL PRO PRO ASP PHE SEQRES 16 R 879 TYR GLN ALA LYS ALA MET ALA GLU ILE LEU ARG PHE PHE SEQRES 17 R 879 ASN TRP THR TYR VAL SER THR VAL ALA SER GLU GLY ASP SEQRES 18 R 879 TYR GLY GLU THR GLY ILE GLU ALA PHE GLU GLN GLU ALA SEQRES 19 R 879 ARG LEU ARG ASN ILE CYS ILE ALA THR ALA GLU LYS VAL SEQRES 20 R 879 GLY ARG SER ASN ILE ARG LYS SER TYR ASP SER VAL ILE SEQRES 21 R 879 ARG GLU LEU LEU GLN LYS PRO ASN ALA ARG VAL VAL VAL SEQRES 22 R 879 LEU PHE MET ARG SER ASP ASP SER ARG GLU LEU ILE ALA SEQRES 23 R 879 ALA ALA SER ARG ALA ASN ALA SER PHE THR TRP VAL ALA SEQRES 24 R 879 SER ASP GLY TRP GLY ALA GLN GLU SER ILE ILE LYS GLY SEQRES 25 R 879 SER GLU HIS VAL ALA TYR GLY ALA ILE THR LEU GLU LEU SEQRES 26 R 879 ALA SER GLN PRO VAL ARG GLN PHE ASP ARG TYR PHE GLN SEQRES 27 R 879 SER LEU ASN PRO TYR ASN ASN HIS ARG ASN PRO TRP PHE SEQRES 28 R 879 ARG ASP PHE TRP GLU GLN LYS PHE GLN CYS SER LEU GLN SEQRES 29 R 879 ASN LYS ARG ASN HIS ARG ARG VAL CYS ASP LYS HIS LEU SEQRES 30 R 879 ALA ILE ASP SER SER ASN TYR GLU GLN GLU SER LYS ILE SEQRES 31 R 879 MET PHE VAL VAL ASN ALA VAL TYR ALA MET ALA HIS ALA SEQRES 32 R 879 LEU HIS LYS MET GLN ARG THR LEU CYS PRO ASN THR THR SEQRES 33 R 879 LYS LEU CYS ASP ALA MET LYS ILE LEU ASP GLY LYS LYS SEQRES 34 R 879 LEU TYR LYS ASP TYR LEU LEU LYS ILE ASN PHE THR ALA SEQRES 35 R 879 PRO PHE ASN PRO ASN LYS ASP ALA ASP SER ILE VAL LYS SEQRES 36 R 879 PHE ASP THR PHE GLY ASP GLY MET GLY ARG TYR ASN VAL SEQRES 37 R 879 PHE ASN PHE GLN ASN VAL GLY GLY LYS TYR SER TYR LEU SEQRES 38 R 879 LYS VAL GLY HIS TRP ALA GLU THR LEU SER LEU ASP VAL SEQRES 39 R 879 ASN SER ILE HIS TRP SER ARG ASN SER VAL PRO THR SER SEQRES 40 R 879 GLN CYS SER ASP PRO CYS ALA PRO ASN GLU MET LYS ASN SEQRES 41 R 879 MET GLN PRO GLY ASP VAL CYS CYS TRP ILE CYS ILE PRO SEQRES 42 R 879 CYS GLU PRO TYR GLU TYR LEU ALA ASP GLU PHE THR CYS SEQRES 43 R 879 MET ASP CYS GLY SER GLY GLN TRP PRO THR ALA ASP LEU SEQRES 44 R 879 THR GLY CYS TYR ASP LEU PRO GLU ASP TYR ILE ARG TRP SEQRES 45 R 879 GLU ASP ALA TRP ALA ILE GLY PRO VAL THR ILE ALA CYS SEQRES 46 R 879 LEU GLY PHE MET CYS THR CYS MET VAL VAL THR VAL PHE SEQRES 47 R 879 ILE LYS HIS ASN ASN THR PRO LEU VAL LYS ALA SER GLY SEQRES 48 R 879 ARG GLU LEU CYS TYR ILE LEU LEU PHE GLY VAL GLY LEU SEQRES 49 R 879 SER TYR CYS MET THR PHE PHE PHE ILE ALA LYS PRO SER SEQRES 50 R 879 PRO VAL ILE CYS ALA LEU ARG ARG LEU GLY LEU GLY SER SEQRES 51 R 879 SER PHE ALA ILE CYS TYR SER ALA LEU LEU THR LYS THR SEQRES 52 R 879 ASN CYS ILE ALA ARG ILE PHE ASP GLY VAL LYS ASN GLY SEQRES 53 R 879 ALA GLN ARG PRO LYS PHE ILE SER PRO SER SER GLN VAL SEQRES 54 R 879 PHE ILE CYS LEU GLY LEU ILE LEU VAL GLN ILE VAL MET SEQRES 55 R 879 VAL SER VAL TRP LEU ILE LEU GLU ALA PRO GLY THR ARG SEQRES 56 R 879 ARG TYR THR LEU ALA GLU LYS ARG GLU THR VAL ILE LEU SEQRES 57 R 879 LYS CYS ASN VAL LYS ASP SER SER MET LEU ILE SER LEU SEQRES 58 R 879 THR TYR ASP VAL ILE LEU VAL ILE LEU CYS THR VAL TYR SEQRES 59 R 879 ALA PHE LYS THR ARG LYS CYS PRO GLU ASN PHE ASN GLU SEQRES 60 R 879 ALA LYS PHE ILE GLY PHE THR MET TYR THR THR CYS ILE SEQRES 61 R 879 ILE TRP LEU ALA PHE LEU PRO ILE PHE TYR VAL THR SER SEQRES 62 R 879 SER ASP TYR ARG VAL GLN THR THR THR MET CYS ILE SER SEQRES 63 R 879 VAL SER LEU SER GLY PHE VAL VAL LEU GLY CYS LEU PHE SEQRES 64 R 879 ALA PRO LYS VAL HIS ILE ILE LEU PHE GLN PRO GLN LYS SEQRES 65 R 879 ASN VAL VAL THR HIS ARG LEU HIS LEU ASN ARG PHE SER SEQRES 66 R 879 VAL SER GLY THR GLY THR THR TYR SER GLN SEP SEP ALA SEQRES 67 R 879 SEP TPO TYR VAL PRO THR VAL CYS ASN GLY ARG GLU VAL SEQRES 68 R 879 LEU ASP SER THR THR SER SER LEU SEQRES 1 A 418 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER SEQRES 2 A 418 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP SEQRES 3 A 418 PHE VAL ASP HIS ILE ASP LEU VAL ASP PRO VAL ASP GLY SEQRES 4 A 418 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG SEQRES 5 A 418 VAL TYR VAL THR LEU THR VAL ALA PHE ARG TYR GLY ARG SEQRES 6 A 418 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP SEQRES 7 A 418 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO SEQRES 8 A 418 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU SEQRES 9 A 418 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE SEQRES 10 A 418 GLU ILE PRO PRO ASN LEU PRO SER SER VAL THR LEU GLN SEQRES 11 A 418 PRO GLY PRO GLU ASP THR GLY LYS ALA LEU GLY VAL ASP SEQRES 12 A 418 TYR GLU VAL LYS ALA PHE VAL ALA GLU ASN LEU GLU GLU SEQRES 13 A 418 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE GLU SEQRES 14 A 418 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO SEQRES 15 A 418 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS SEQRES 16 A 418 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR SEQRES 17 A 418 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR SEQRES 18 A 418 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER SEQRES 19 A 418 VAL ARG GLN TYR ALA ASP ILE VAL LEU PHE ASN THR ALA SEQRES 20 A 418 GLN TYR LYS VAL PRO VAL ALA MET GLU GLU ALA ASP ASP SEQRES 21 A 418 THR VAL ALA PRO SER SER THR PHE SER LYS VAL TYR THR SEQRES 22 A 418 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY SEQRES 23 A 418 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN SEQRES 24 A 418 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG SEQRES 25 A 418 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL SEQRES 26 A 418 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU SEQRES 27 A 418 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU SEQRES 28 A 418 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU SEQRES 29 A 418 VAL PRO GLU ASN GLU THR PRO VAL ASP THR ASN LEU ILE SEQRES 30 A 418 GLU LEU ASP THR ASN ASP ASP ASP ILE VAL PHE GLU ASP SEQRES 31 A 418 PHE ALA ARG GLN ARG LEU LYS GLY MET LYS ASP ASP LYS SEQRES 32 A 418 GLU GLU GLU GLU ASP GLY THR GLY SER PRO GLN LEU ASN SEQRES 33 A 418 ASN ARG SEQRES 1 S 251 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 S 251 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 S 251 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 S 251 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 S 251 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 S 251 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 S 251 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 S 251 TYR LYS TYR VAL PRO VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 S 251 VAL GLU ILE LYS GLY THR THR ALA ALA SER GLY SER SER SEQRES 10 S 251 GLY GLY SER SER SER GLY ALA GLU VAL GLN LEU VAL GLU SEQRES 11 S 251 SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG SEQRES 12 S 251 LEU SER CYS ALA ALA SER GLY PHE ASN VAL TYR SER SER SEQRES 13 S 251 SER ILE HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU SEQRES 14 S 251 GLU TRP VAL ALA SER ILE SER SER TYR TYR GLY TYR THR SEQRES 15 S 251 TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER SEQRES 16 S 251 ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET ASN SEQRES 17 S 251 SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 18 S 251 ARG SER ARG GLN PHE TRP TYR SER GLY LEU ASP TYR TRP SEQRES 19 S 251 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA HIS HIS SEQRES 20 S 251 HIS HIS HIS HIS SEQRES 1 B 879 MET LYS MET LEU THR ARG LEU GLN VAL LEU THR LEU ALA SEQRES 2 B 879 LEU PHE SER LYS GLY PHE LEU LEU SER LEU GLY ASP HIS SEQRES 3 B 879 ASN PHE LEU ARG ARG GLU ILE LYS ILE GLU GLY ASP LEU SEQRES 4 B 879 VAL LEU GLY GLY LEU PHE PRO ILE ASN GLU LYS GLY THR SEQRES 5 B 879 GLY THR GLU GLU CYS GLY ARG ILE ASN GLU ASP ARG GLY SEQRES 6 B 879 ILE GLN ARG LEU GLU ALA MET LEU PHE ALA ILE ASP GLU SEQRES 7 B 879 ILE ASN LYS ASP ASP TYR LEU LEU PRO GLY VAL LYS LEU SEQRES 8 B 879 GLY VAL HIS ILE LEU ASP THR CYS SER ARG ASP THR TYR SEQRES 9 B 879 ALA LEU GLU GLN SER LEU GLU PHE VAL ARG ALA SER LEU SEQRES 10 B 879 THR LYS VAL ASP GLU ALA GLU TYR MET CYS PRO ASP GLY SEQRES 11 B 879 SER TYR ALA ILE GLN GLU ASN ILE PRO LEU LEU ILE ALA SEQRES 12 B 879 GLY VAL ILE GLY GLY SER TYR SER SER VAL SER ILE GLN SEQRES 13 B 879 VAL ALA ASN LEU LEU ARG LEU PHE GLN ILE PRO GLN ILE SEQRES 14 B 879 SER TYR ALA SER THR SER ALA LYS LEU SER ASP LYS SER SEQRES 15 B 879 ARG TYR ASP TYR PHE ALA ARG THR VAL PRO PRO ASP PHE SEQRES 16 B 879 TYR GLN ALA LYS ALA MET ALA GLU ILE LEU ARG PHE PHE SEQRES 17 B 879 ASN TRP THR TYR VAL SER THR VAL ALA SER GLU GLY ASP SEQRES 18 B 879 TYR GLY GLU THR GLY ILE GLU ALA PHE GLU GLN GLU ALA SEQRES 19 B 879 ARG LEU ARG ASN ILE CYS ILE ALA THR ALA GLU LYS VAL SEQRES 20 B 879 GLY ARG SER ASN ILE ARG LYS SER TYR ASP SER VAL ILE SEQRES 21 B 879 ARG GLU LEU LEU GLN LYS PRO ASN ALA ARG VAL VAL VAL SEQRES 22 B 879 LEU PHE MET ARG SER ASP ASP SER ARG GLU LEU ILE ALA SEQRES 23 B 879 ALA ALA SER ARG ALA ASN ALA SER PHE THR TRP VAL ALA SEQRES 24 B 879 SER ASP GLY TRP GLY ALA GLN GLU SER ILE ILE LYS GLY SEQRES 25 B 879 SER GLU HIS VAL ALA TYR GLY ALA ILE THR LEU GLU LEU SEQRES 26 B 879 ALA SER GLN PRO VAL ARG GLN PHE ASP ARG TYR PHE GLN SEQRES 27 B 879 SER LEU ASN PRO TYR ASN ASN HIS ARG ASN PRO TRP PHE SEQRES 28 B 879 ARG ASP PHE TRP GLU GLN LYS PHE GLN CYS SER LEU GLN SEQRES 29 B 879 ASN LYS ARG ASN HIS ARG ARG VAL CYS ASP LYS HIS LEU SEQRES 30 B 879 ALA ILE ASP SER SER ASN TYR GLU GLN GLU SER LYS ILE SEQRES 31 B 879 MET PHE VAL VAL ASN ALA VAL TYR ALA MET ALA HIS ALA SEQRES 32 B 879 LEU HIS LYS MET GLN ARG THR LEU CYS PRO ASN THR THR SEQRES 33 B 879 LYS LEU CYS ASP ALA MET LYS ILE LEU ASP GLY LYS LYS SEQRES 34 B 879 LEU TYR LYS ASP TYR LEU LEU LYS ILE ASN PHE THR ALA SEQRES 35 B 879 PRO PHE ASN PRO ASN LYS ASP ALA ASP SER ILE VAL LYS SEQRES 36 B 879 PHE ASP THR PHE GLY ASP GLY MET GLY ARG TYR ASN VAL SEQRES 37 B 879 PHE ASN PHE GLN ASN VAL GLY GLY LYS TYR SER TYR LEU SEQRES 38 B 879 LYS VAL GLY HIS TRP ALA GLU THR LEU SER LEU ASP VAL SEQRES 39 B 879 ASN SER ILE HIS TRP SER ARG ASN SER VAL PRO THR SER SEQRES 40 B 879 GLN CYS SER ASP PRO CYS ALA PRO ASN GLU MET LYS ASN SEQRES 41 B 879 MET GLN PRO GLY ASP VAL CYS CYS TRP ILE CYS ILE PRO SEQRES 42 B 879 CYS GLU PRO TYR GLU TYR LEU ALA ASP GLU PHE THR CYS SEQRES 43 B 879 MET ASP CYS GLY SER GLY GLN TRP PRO THR ALA ASP LEU SEQRES 44 B 879 THR GLY CYS TYR ASP LEU PRO GLU ASP TYR ILE ARG TRP SEQRES 45 B 879 GLU ASP ALA TRP ALA ILE GLY PRO VAL THR ILE ALA CYS SEQRES 46 B 879 LEU GLY PHE MET CYS THR CYS MET VAL VAL THR VAL PHE SEQRES 47 B 879 ILE LYS HIS ASN ASN THR PRO LEU VAL LYS ALA SER GLY SEQRES 48 B 879 ARG GLU LEU CYS TYR ILE LEU LEU PHE GLY VAL GLY LEU SEQRES 49 B 879 SER TYR CYS MET THR PHE PHE PHE ILE ALA LYS PRO SER SEQRES 50 B 879 PRO VAL ILE CYS ALA LEU ARG ARG LEU GLY LEU GLY SER SEQRES 51 B 879 SER PHE ALA ILE CYS TYR SER ALA LEU LEU THR LYS THR SEQRES 52 B 879 ASN CYS ILE ALA ARG ILE PHE ASP GLY VAL LYS ASN GLY SEQRES 53 B 879 ALA GLN ARG PRO LYS PHE ILE SER PRO SER SER GLN VAL SEQRES 54 B 879 PHE ILE CYS LEU GLY LEU ILE LEU VAL GLN ILE VAL MET SEQRES 55 B 879 VAL SER VAL TRP LEU ILE LEU GLU ALA PRO GLY THR ARG SEQRES 56 B 879 ARG TYR THR LEU ALA GLU LYS ARG GLU THR VAL ILE LEU SEQRES 57 B 879 LYS CYS ASN VAL LYS ASP SER SER MET LEU ILE SER LEU SEQRES 58 B 879 THR TYR ASP VAL ILE LEU VAL ILE LEU CYS THR VAL TYR SEQRES 59 B 879 ALA PHE LYS THR ARG LYS CYS PRO GLU ASN PHE ASN GLU SEQRES 60 B 879 ALA LYS PHE ILE GLY PHE THR MET TYR THR THR CYS ILE SEQRES 61 B 879 ILE TRP LEU ALA PHE LEU PRO ILE PHE TYR VAL THR SER SEQRES 62 B 879 SER ASP TYR ARG VAL GLN THR THR THR MET CYS ILE SER SEQRES 63 B 879 VAL SER LEU SER GLY PHE VAL VAL LEU GLY CYS LEU PHE SEQRES 64 B 879 ALA PRO LYS VAL HIS ILE ILE LEU PHE GLN PRO GLN LYS SEQRES 65 B 879 ASN VAL VAL THR HIS ARG LEU HIS LEU ASN ARG PHE SER SEQRES 66 B 879 VAL SER GLY THR GLY THR THR TYR SER GLN SEP SEP ALA SEQRES 67 B 879 SEP TPO TYR VAL PRO THR VAL CYS ASN GLY ARG GLU VAL SEQRES 68 B 879 LEU ASP SER THR THR SER SER LEU SEQRES 1 C 418 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER SEQRES 2 C 418 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP SEQRES 3 C 418 PHE VAL ASP HIS ILE ASP LEU VAL ASP PRO VAL ASP GLY SEQRES 4 C 418 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG SEQRES 5 C 418 VAL TYR VAL THR LEU THR VAL ALA PHE ARG TYR GLY ARG SEQRES 6 C 418 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP SEQRES 7 C 418 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO SEQRES 8 C 418 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU SEQRES 9 C 418 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE SEQRES 10 C 418 GLU ILE PRO PRO ASN LEU PRO SER SER VAL THR LEU GLN SEQRES 11 C 418 PRO GLY PRO GLU ASP THR GLY LYS ALA LEU GLY VAL ASP SEQRES 12 C 418 TYR GLU VAL LYS ALA PHE VAL ALA GLU ASN LEU GLU GLU SEQRES 13 C 418 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE GLU SEQRES 14 C 418 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO SEQRES 15 C 418 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS SEQRES 16 C 418 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR SEQRES 17 C 418 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR SEQRES 18 C 418 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER SEQRES 19 C 418 VAL ARG GLN TYR ALA ASP ILE VAL LEU PHE ASN THR ALA SEQRES 20 C 418 GLN TYR LYS VAL PRO VAL ALA MET GLU GLU ALA ASP ASP SEQRES 21 C 418 THR VAL ALA PRO SER SER THR PHE SER LYS VAL TYR THR SEQRES 22 C 418 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY SEQRES 23 C 418 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN SEQRES 24 C 418 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG SEQRES 25 C 418 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL SEQRES 26 C 418 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU SEQRES 27 C 418 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU SEQRES 28 C 418 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU SEQRES 29 C 418 VAL PRO GLU ASN GLU THR PRO VAL ASP THR ASN LEU ILE SEQRES 30 C 418 GLU LEU ASP THR ASN ASP ASP ASP ILE VAL PHE GLU ASP SEQRES 31 C 418 PHE ALA ARG GLN ARG LEU LYS GLY MET LYS ASP ASP LYS SEQRES 32 C 418 GLU GLU GLU GLU ASP GLY THR GLY SER PRO GLN LEU ASN SEQRES 33 C 418 ASN ARG SEQRES 1 D 251 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 D 251 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 D 251 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 D 251 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 D 251 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 D 251 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 D 251 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 D 251 TYR LYS TYR VAL PRO VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 D 251 VAL GLU ILE LYS GLY THR THR ALA ALA SER GLY SER SER SEQRES 10 D 251 GLY GLY SER SER SER GLY ALA GLU VAL GLN LEU VAL GLU SEQRES 11 D 251 SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG SEQRES 12 D 251 LEU SER CYS ALA ALA SER GLY PHE ASN VAL TYR SER SER SEQRES 13 D 251 SER ILE HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU SEQRES 14 D 251 GLU TRP VAL ALA SER ILE SER SER TYR TYR GLY TYR THR SEQRES 15 D 251 TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER SEQRES 16 D 251 ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET ASN SEQRES 17 D 251 SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 18 D 251 ARG SER ARG GLN PHE TRP TYR SER GLY LEU ASP TYR TRP SEQRES 19 D 251 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA HIS HIS SEQRES 20 D 251 HIS HIS HIS HIS MODRES 9II2 SEP R 856 SER MODIFIED RESIDUE MODRES 9II2 SEP R 857 SER MODIFIED RESIDUE MODRES 9II2 SEP R 859 SER MODIFIED RESIDUE MODRES 9II2 TPO R 860 THR MODIFIED RESIDUE MODRES 9II2 SEP B 856 SER MODIFIED RESIDUE MODRES 9II2 SEP B 857 SER MODIFIED RESIDUE MODRES 9II2 SEP B 859 SER MODIFIED RESIDUE MODRES 9II2 TPO B 860 THR MODIFIED RESIDUE HET SEP R 856 5 HET SEP R 857 10 HET SEP R 859 10 HET TPO R 860 11 HET SEP B 856 5 HET SEP B 857 10 HET SEP B 859 10 HET TPO B 860 11 HET NAG E 1 14 HET NAG E 2 14 HET NAG F 1 14 HET NAG F 2 14 HET GLU R1001 9 HET CLR R1002 28 HET CLR R1003 28 HET CLR R1004 28 HET GLU B1001 9 HET CLR B1002 28 HET CLR B1003 28 HET CLR B1004 28 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GLU GLUTAMIC ACID HETNAM CLR CHOLESTEROL HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE 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 1 SEP 6(C3 H8 N O6 P) FORMUL 1 TPO 2(C4 H10 N O6 P) FORMUL 7 NAG 4(C8 H15 N O6) FORMUL 9 GLU 2(C5 H9 N O4) FORMUL 10 CLR 6(C27 H46 O) HELIX 1 AA1 ARG R 64 ASP R 82 1 19 HELIX 2 AA2 ARG R 101 ARG R 114 1 14 HELIX 3 AA3 ALA R 115 ASP R 121 1 7 HELIX 4 AA4 TYR R 150 ARG R 162 1 13 HELIX 5 AA5 SER R 175 SER R 179 5 5 HELIX 6 AA6 PRO R 193 PHE R 208 1 16 HELIX 7 AA7 ASP R 221 ARG R 237 1 17 HELIX 8 AA8 ILE R 252 GLN R 265 1 14 HELIX 9 AA9 ARG R 277 ALA R 291 1 15 HELIX 10 AB1 GLN R 306 SER R 313 1 8 HELIX 11 AB2 VAL R 330 SER R 339 1 10 HELIX 12 AB3 TRP R 350 GLN R 360 1 11 HELIX 13 AB4 LYS R 389 CYS R 412 1 24 HELIX 14 AB5 CYS R 419 ILE R 424 1 6 HELIX 15 AB6 ASP R 426 LEU R 435 1 10 HELIX 16 AB7 VAL R 494 ILE R 497 5 4 HELIX 17 AB8 TRP R 499 SER R 503 5 5 HELIX 18 AB9 ALA R 577 HIS R 601 1 25 HELIX 19 AC1 THR R 604 GLY R 611 1 8 HELIX 20 AC2 GLY R 611 ILE R 633 1 23 HELIX 21 AC3 SER R 637 GLY R 672 1 36 HELIX 22 AC4 SER R 686 GLU R 710 1 25 HELIX 23 AC5 LYS R 733 THR R 758 1 26 HELIX 24 AC6 PRO R 762 THR R 792 1 31 HELIX 25 AC7 ASP R 795 PHE R 828 1 34 HELIX 26 AC8 ARG A 65 GLY A 72 1 8 HELIX 27 AC9 THR A 98 GLY A 109 1 12 HELIX 28 AD1 LEU A 243 THR A 246 5 4 HELIX 29 AD2 ASN S 1031 TYR S 1033 5 3 HELIX 30 AD3 ARG B 64 ASP B 82 1 19 HELIX 31 AD4 ARG B 101 ARG B 114 1 14 HELIX 32 AD5 ALA B 115 ASP B 121 1 7 HELIX 33 AD6 TYR B 150 ARG B 162 1 13 HELIX 34 AD7 SER B 175 SER B 179 5 5 HELIX 35 AD8 PRO B 193 PHE B 208 1 16 HELIX 36 AD9 ASP B 221 ARG B 237 1 17 HELIX 37 AE1 ILE B 252 GLN B 265 1 14 HELIX 38 AE2 ARG B 277 ALA B 291 1 15 HELIX 39 AE3 GLN B 306 SER B 313 1 8 HELIX 40 AE4 VAL B 330 SER B 339 1 10 HELIX 41 AE5 TRP B 350 GLN B 360 1 11 HELIX 42 AE6 LYS B 389 CYS B 412 1 24 HELIX 43 AE7 CYS B 419 ILE B 424 1 6 HELIX 44 AE8 ASP B 426 LEU B 435 1 10 HELIX 45 AE9 VAL B 494 ILE B 497 5 4 HELIX 46 AF1 TRP B 499 SER B 503 5 5 HELIX 47 AF2 ALA B 577 HIS B 601 1 25 HELIX 48 AF3 THR B 604 GLY B 611 1 8 HELIX 49 AF4 GLY B 611 ILE B 633 1 23 HELIX 50 AF5 SER B 637 GLY B 672 1 36 HELIX 51 AF6 SER B 686 GLU B 710 1 25 HELIX 52 AF7 LYS B 733 THR B 758 1 26 HELIX 53 AF8 PRO B 762 THR B 792 1 31 HELIX 54 AF9 ASP B 795 PHE B 828 1 34 HELIX 55 AG1 ARG C 65 GLY C 72 1 8 HELIX 56 AG2 THR C 98 GLY C 109 1 12 HELIX 57 AG3 LEU C 243 THR C 246 5 4 HELIX 58 AG4 ASN D 1031 TYR D 1033 5 3 SHEET 1 AA1 6 ILE R 33 LYS R 34 0 SHEET 2 AA1 6 LEU R 91 ASP R 97 -1 O ILE R 95 N ILE R 33 SHEET 3 AA1 6 LEU R 39 PHE R 45 1 N GLY R 43 O LEU R 96 SHEET 4 AA1 6 ILE R 142 GLY R 147 1 O ILE R 146 N GLY R 42 SHEET 5 AA1 6 GLN R 168 SER R 170 1 O ILE R 169 N VAL R 145 SHEET 6 AA1 6 PHE R 187 ARG R 189 1 O ALA R 188 N SER R 170 SHEET 1 AA2 4 CYS R 240 VAL R 247 0 SHEET 2 AA2 4 TYR R 212 SER R 218 1 N VAL R 213 O ALA R 242 SHEET 3 AA2 4 VAL R 271 PHE R 275 1 O VAL R 271 N SER R 214 SHEET 4 AA2 4 THR R 296 VAL R 298 1 O VAL R 298 N VAL R 272 SHEET 1 AA3 4 ILE R 321 LEU R 325 0 SHEET 2 AA3 4 TYR R 466 ASN R 470 -1 O ASN R 467 N GLU R 324 SHEET 3 AA3 4 LEU R 481 TRP R 486 -1 O VAL R 483 N VAL R 468 SHEET 4 AA3 4 LEU R 490 LEU R 492 -1 O SER R 491 N HIS R 485 SHEET 1 AA4 2 ASN R 439 THR R 441 0 SHEET 2 AA4 2 ILE R 453 LYS R 455 -1 O VAL R 454 N PHE R 440 SHEET 1 AA5 2 GLU R 538 TYR R 539 0 SHEET 2 AA5 2 MET R 547 ASP R 548 -1 O MET R 547 N TYR R 539 SHEET 1 AA6 2 GLN R 553 PRO R 555 0 SHEET 2 AA6 2 CYS R 562 ASP R 564 -1 O TYR R 563 N TRP R 554 SHEET 1 AA7 3 GLU R 567 ASP R 568 0 SHEET 2 AA7 3 VAL R 726 CYS R 730 1 O VAL R 726 N ASP R 568 SHEET 3 AA7 3 THR R 714 TYR R 717 -1 N ARG R 715 O LYS R 729 SHEET 1 AA8 5 SEP R 857 VAL R 862 0 SHEET 2 AA8 5 THR A 6 ALA A 12 -1 O LYS A 10 N ALA R 858 SHEET 3 AA8 5 LEU A 18 LEU A 22 -1 O LEU A 22 N PHE A 9 SHEET 4 AA8 5 VAL A 37 VAL A 43 -1 O VAL A 40 N TYR A 21 SHEET 5 AA8 5 TYR A 113 PHE A 117 -1 O TYR A 113 N VAL A 41 SHEET 1 AA9 4 PHE A 75 GLN A 85 0 SHEET 2 AA9 4 TYR A 54 TYR A 63 -1 N PHE A 61 O LYS A 77 SHEET 3 AA9 4 LEU A 140 PHE A 149 -1 O GLY A 141 N ARG A 62 SHEET 4 AA9 4 VAL A 164 ILE A 168 -1 O LEU A 166 N VAL A 146 SHEET 1 AB1 5 PHE A 75 GLN A 85 0 SHEET 2 AB1 5 TYR A 54 TYR A 63 -1 N PHE A 61 O LYS A 77 SHEET 3 AB1 5 LEU A 140 PHE A 149 -1 O GLY A 141 N ARG A 62 SHEET 4 AB1 5 VAL A 127 LEU A 129 -1 N LEU A 129 O LEU A 140 SHEET 5 AB1 5 ALA A 288 ASP A 290 -1 O LEU A 289 N THR A 128 SHEET 1 AB2 4 THR A 183 GLN A 189 0 SHEET 2 AB2 4 PRO A 196 LEU A 203 -1 O LEU A 197 N ARG A 188 SHEET 3 AB2 4 ILE A 214 ASN A 222 -1 O THR A 221 N HIS A 198 SHEET 4 AB2 4 SER A 266 LEU A 274 -1 O SER A 266 N ASN A 222 SHEET 1 AB3 5 ILE A 207 TYR A 208 0 SHEET 2 AB3 5 VAL A 343 LEU A 351 1 O THR A 350 N TYR A 208 SHEET 3 AB3 5 ILE A 317 LEU A 327 -1 N TYR A 321 O PHE A 349 SHEET 4 AB3 5 ILE A 231 ILE A 241 -1 N LYS A 232 O LYS A 326 SHEET 5 AB3 5 TYR A 249 ALA A 258 -1 O GLU A 256 N ILE A 233 SHEET 1 AB4 4 THR S 6 SER S 8 0 SHEET 2 AB4 4 VAL S 20 ARG S 25 -1 O ARG S 25 N THR S 6 SHEET 3 AB4 4 ASP S 71 ILE S 76 -1 O LEU S 74 N ILE S 22 SHEET 4 AB4 4 PHE S 63 SER S 68 -1 N SER S 66 O THR S 73 SHEET 1 AB5 6 SER S 11 SER S 13 0 SHEET 2 AB5 6 THR S 103 GLU S 106 1 O LYS S 104 N LEU S 12 SHEET 3 AB5 6 THR S 86 GLN S 91 -1 N TYR S 87 O THR S 103 SHEET 4 AB5 6 VAL S 34 GLN S 39 -1 N GLN S 39 O THR S 86 SHEET 5 AB5 6 LYS S 46 TYR S 50 -1 O LYS S 46 N GLN S 38 SHEET 6 AB5 6 SER S 54 LEU S 55 -1 O SER S 54 N TYR S 50 SHEET 1 AB6 4 LEU S1007 SER S1010 0 SHEET 2 AB6 4 GLY S1018 ALA S1027 -1 O SER S1024 N SER S1010 SHEET 3 AB6 4 THR S1081 LEU S1089 -1 O ALA S1082 N CYS S1025 SHEET 4 AB6 4 PHE S1071 ASP S1076 -1 N THR S1072 O GLN S1085 SHEET 1 AB7 2 GLY S1013 LEU S1014 0 SHEET 2 AB7 2 VAL S1119 THR S1120 1 O THR S1120 N GLY S1013 SHEET 1 AB8 4 TYR S1060 TYR S1063 0 SHEET 2 AB8 4 LEU S1048 SER S1055 -1 N SER S1055 O TYR S1060 SHEET 3 AB8 4 SER S1035 GLN S1042 -1 N TRP S1039 O ALA S1052 SHEET 4 AB8 4 VAL S1096 ARG S1103 -1 O TYR S1098 N VAL S1040 SHEET 1 AB9 6 ILE B 33 LYS B 34 0 SHEET 2 AB9 6 LEU B 91 ASP B 97 -1 O ILE B 95 N ILE B 33 SHEET 3 AB9 6 LEU B 39 PHE B 45 1 N GLY B 43 O LEU B 96 SHEET 4 AB9 6 ILE B 142 GLY B 147 1 O ILE B 146 N GLY B 42 SHEET 5 AB9 6 GLN B 168 SER B 170 1 O ILE B 169 N VAL B 145 SHEET 6 AB9 6 PHE B 187 ARG B 189 1 O ALA B 188 N SER B 170 SHEET 1 AC1 4 CYS B 240 VAL B 247 0 SHEET 2 AC1 4 TYR B 212 SER B 218 1 N VAL B 213 O ALA B 242 SHEET 3 AC1 4 VAL B 271 PHE B 275 1 O VAL B 271 N SER B 214 SHEET 4 AC1 4 THR B 296 VAL B 298 1 O VAL B 298 N VAL B 272 SHEET 1 AC2 4 ILE B 321 LEU B 325 0 SHEET 2 AC2 4 TYR B 466 ASN B 470 -1 O ASN B 467 N GLU B 324 SHEET 3 AC2 4 LEU B 481 TRP B 486 -1 O VAL B 483 N VAL B 468 SHEET 4 AC2 4 LEU B 490 LEU B 492 -1 O SER B 491 N HIS B 485 SHEET 1 AC3 2 ASN B 439 THR B 441 0 SHEET 2 AC3 2 ILE B 453 LYS B 455 -1 O VAL B 454 N PHE B 440 SHEET 1 AC4 2 GLU B 538 TYR B 539 0 SHEET 2 AC4 2 MET B 547 ASP B 548 -1 O MET B 547 N TYR B 539 SHEET 1 AC5 2 GLN B 553 PRO B 555 0 SHEET 2 AC5 2 CYS B 562 ASP B 564 -1 O TYR B 563 N TRP B 554 SHEET 1 AC6 3 GLU B 567 ASP B 568 0 SHEET 2 AC6 3 VAL B 726 CYS B 730 1 O VAL B 726 N ASP B 568 SHEET 3 AC6 3 THR B 714 TYR B 717 -1 N ARG B 715 O LYS B 729 SHEET 1 AC7 5 SEP B 857 VAL B 862 0 SHEET 2 AC7 5 THR C 6 ALA C 12 -1 O LYS C 10 N ALA B 858 SHEET 3 AC7 5 LEU C 18 LEU C 22 -1 O LEU C 22 N PHE C 9 SHEET 4 AC7 5 VAL C 37 VAL C 43 -1 O VAL C 40 N TYR C 21 SHEET 5 AC7 5 TYR C 113 PHE C 117 -1 O TYR C 113 N VAL C 41 SHEET 1 AC8 4 PHE C 75 GLN C 85 0 SHEET 2 AC8 4 TYR C 54 TYR C 63 -1 N PHE C 61 O LYS C 77 SHEET 3 AC8 4 LEU C 140 PHE C 149 -1 O GLY C 141 N ARG C 62 SHEET 4 AC8 4 VAL C 164 ILE C 168 -1 O LEU C 166 N VAL C 146 SHEET 1 AC9 5 PHE C 75 GLN C 85 0 SHEET 2 AC9 5 TYR C 54 TYR C 63 -1 N PHE C 61 O LYS C 77 SHEET 3 AC9 5 LEU C 140 PHE C 149 -1 O GLY C 141 N ARG C 62 SHEET 4 AC9 5 VAL C 127 LEU C 129 -1 N LEU C 129 O LEU C 140 SHEET 5 AC9 5 ALA C 288 ASP C 290 -1 O LEU C 289 N THR C 128 SHEET 1 AD1 4 THR C 183 GLN C 189 0 SHEET 2 AD1 4 PRO C 196 LEU C 203 -1 O LEU C 197 N ARG C 188 SHEET 3 AD1 4 ILE C 214 ASN C 222 -1 O THR C 221 N HIS C 198 SHEET 4 AD1 4 SER C 266 LEU C 274 -1 O SER C 266 N ASN C 222 SHEET 1 AD2 5 ILE C 207 TYR C 208 0 SHEET 2 AD2 5 VAL C 343 LEU C 351 1 O THR C 350 N TYR C 208 SHEET 3 AD2 5 ILE C 317 LEU C 327 -1 N TYR C 321 O PHE C 349 SHEET 4 AD2 5 ILE C 231 ILE C 241 -1 N LYS C 232 O LYS C 326 SHEET 5 AD2 5 TYR C 249 ALA C 258 -1 O GLU C 256 N ILE C 233 SHEET 1 AD3 4 THR D 6 SER D 8 0 SHEET 2 AD3 4 VAL D 20 ARG D 25 -1 O ARG D 25 N THR D 6 SHEET 3 AD3 4 ASP D 71 ILE D 76 -1 O LEU D 74 N ILE D 22 SHEET 4 AD3 4 PHE D 63 SER D 68 -1 N SER D 66 O THR D 73 SHEET 1 AD4 6 SER D 11 SER D 13 0 SHEET 2 AD4 6 THR D 103 GLU D 106 1 O LYS D 104 N LEU D 12 SHEET 3 AD4 6 THR D 86 GLN D 91 -1 N TYR D 87 O THR D 103 SHEET 4 AD4 6 VAL D 34 GLN D 39 -1 N GLN D 39 O THR D 86 SHEET 5 AD4 6 LYS D 46 TYR D 50 -1 O LYS D 46 N GLN D 38 SHEET 6 AD4 6 SER D 54 LEU D 55 -1 O SER D 54 N TYR D 50 SHEET 1 AD5 4 LEU D1007 SER D1010 0 SHEET 2 AD5 4 GLY D1018 ALA D1027 -1 O SER D1024 N SER D1010 SHEET 3 AD5 4 THR D1081 LEU D1089 -1 O ALA D1082 N CYS D1025 SHEET 4 AD5 4 PHE D1071 ASP D1076 -1 N THR D1072 O GLN D1085 SHEET 1 AD6 2 GLY D1013 LEU D1014 0 SHEET 2 AD6 2 VAL D1119 THR D1120 1 O THR D1120 N GLY D1013 SHEET 1 AD7 4 TYR D1060 TYR D1063 0 SHEET 2 AD7 4 LEU D1048 SER D1055 -1 N SER D1055 O TYR D1060 SHEET 3 AD7 4 SER D1035 GLN D1042 -1 N TRP D1039 O ALA D1052 SHEET 4 AD7 4 VAL D1096 ARG D1103 -1 O TYR D1098 N VAL D1040 SSBOND 1 CYS R 57 CYS R 99 1555 1555 2.03 SSBOND 2 CYS R 361 CYS R 373 1555 1555 2.03 SSBOND 3 CYS R 412 CYS R 419 1555 1555 2.03 SSBOND 4 CYS R 509 CYS R 528 1555 1555 2.03 SSBOND 5 CYS R 513 CYS R 531 1555 1555 2.03 SSBOND 6 CYS R 549 CYS R 562 1555 1555 2.03 SSBOND 7 CYS R 641 CYS R 730 1555 1555 2.03 SSBOND 8 CYS S 24 CYS S 89 1555 1555 2.03 SSBOND 9 CYS S 1025 CYS S 1099 1555 1555 2.03 SSBOND 10 CYS B 57 CYS B 99 1555 1555 2.03 SSBOND 11 CYS B 361 CYS B 373 1555 1555 2.03 SSBOND 12 CYS B 412 CYS B 419 1555 1555 2.03 SSBOND 13 CYS B 509 CYS B 528 1555 1555 2.03 SSBOND 14 CYS B 513 CYS B 531 1555 1555 2.03 SSBOND 15 CYS B 549 CYS B 562 1555 1555 2.03 SSBOND 16 CYS B 641 CYS B 730 1555 1555 2.03 SSBOND 17 CYS D 24 CYS D 89 1555 1555 2.03 SSBOND 18 CYS D 1025 CYS D 1099 1555 1555 2.03 LINK ND2 ASN R 209 C1 NAG E 1 1555 1555 1.44 LINK C GLN R 855 N SEP R 856 1555 1555 1.33 LINK C SEP R 856 N SEP R 857 1555 1555 1.33 LINK C SEP R 857 N ALA R 858 1555 1555 1.33 LINK C ALA R 858 N SEP R 859 1555 1555 1.33 LINK C SEP R 859 N TPO R 860 1555 1555 1.33 LINK C TPO R 860 N TYR R 861 1555 1555 1.33 LINK ND2 ASN B 209 C1 NAG F 1 1555 1555 1.44 LINK C GLN B 855 N SEP B 856 1555 1555 1.33 LINK C SEP B 856 N SEP B 857 1555 1555 1.33 LINK C SEP B 857 N ALA B 858 1555 1555 1.33 LINK C ALA B 858 N SEP B 859 1555 1555 1.33 LINK C SEP B 859 N TPO B 860 1555 1555 1.33 LINK C TPO B 860 N TYR B 861 1555 1555 1.33 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 CISPEP 1 SER S 8 PRO S 9 0 -3.54 CISPEP 2 VAL S 95 PRO S 96 0 4.50 CISPEP 3 SER D 8 PRO D 9 0 -3.54 CISPEP 4 VAL D 95 PRO D 96 0 4.58 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