HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 15-MAY-25 9UYN TITLE CRYO-EM STRUCTURE OF THE G PROTEIN-COUPLED RECEPTOR 1 (GPR1) BOUND TO TITLE 2 BETA-ARRESTIN 1 IN LIGAND-FREE STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHEMERIN-LIKE RECEPTOR 2,VASOPRESSIN V2 RECEPTOR; COMPND 3 CHAIN: R; COMPND 4 SYNONYM: CHEMERIN CHEMOKINE-LIKE RECEPTOR 2,CHEMOKINE-LIKE RECEPTOR COMPND 5 2,G-PROTEIN COUPLED RECEPTOR 1,V2R,AVPR V2,ANTIDIURETIC HORMONE COMPND 6 RECEPTOR,RENAL-TYPE ARGININE VASOPRESSIN RECEPTOR; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: BETA-ARRESTIN-1; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: ARRESTIN BETA-1,NON-VISUAL ARRESTIN-2; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: NANOBODY 32; COMPND 17 CHAIN: B; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: SINGLE-CHAIN FRAGMENT VARIABLE 30 (SCFV30); COMPND 21 CHAIN: C; COMPND 22 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: CMKLR2, GPR1, AVPR2, ADHR, DIR, DIR3, V2R; 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: ESCHERICHIA PHAGE ECSZW-2; SOURCE 17 ORGANISM_TAXID: 2419741; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS G PROTEIN-COUPLED RECEPTOR 1, CHEMERIN, BETA-ARRESTIN1, SIGNALING KEYWDS 2 PROTEIN, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN-IMMUNE KEYWDS 3 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR H.CAI,X.LIN,L.ZHAO,M.HE,J.YU,B.ZHANG,Y.MA,C.XIE,W.SHUI,Q.ZHAO,Y.ZHU, AUTHOR 2 B.WU REVDAT 1 19-NOV-25 9UYN 0 JRNL AUTH H.CAI,X.LIN,L.ZHAO,M.HE,J.YU,B.ZHANG,Y.MA,X.CHANG,Y.TANG, JRNL AUTH 2 T.LUO,J.JIANG,M.MA,W.SONG,L.MA,X.CHU,C.YI,K.CHEN,S.HAN, JRNL AUTH 3 C.XIE,W.SHUI,Q.ZHAO,Y.ZHU,B.WU JRNL TITL NONCANONICAL AGONIST-DEPENDENT AND -INDEPENDENT ARRESTIN JRNL TITL 2 RECRUITMENT OF GPR1 JRNL REF SCIENCE 2025 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADT8794 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.900 REMARK 3 NUMBER OF PARTICLES : 413367 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 9UYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-MAY-25. REMARK 100 THE DEPOSITION ID IS D_1300059373. 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 : G PROTEIN-COUPLED RECEPTOR 1 IN REMARK 245 COMPLEX WITH BETA-ARRESTIN1 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 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) : 218.75 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, B, C 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 -62 REMARK 465 LYS R -61 REMARK 465 THR R -60 REMARK 465 ILE R -59 REMARK 465 ILE R -58 REMARK 465 ALA R -57 REMARK 465 LEU R -56 REMARK 465 SER R -55 REMARK 465 TYR R -54 REMARK 465 ILE R -53 REMARK 465 PHE R -52 REMARK 465 CYS R -51 REMARK 465 LEU R -50 REMARK 465 VAL R -49 REMARK 465 PHE R -48 REMARK 465 ALA R -47 REMARK 465 GLY R -46 REMARK 465 SER R -45 REMARK 465 TRP R -44 REMARK 465 SER R -43 REMARK 465 HIS R -42 REMARK 465 PRO R -41 REMARK 465 GLN R -40 REMARK 465 PHE R -39 REMARK 465 GLU R -38 REMARK 465 LYS R -37 REMARK 465 GLY R -36 REMARK 465 SER R -35 REMARK 465 GLY R -34 REMARK 465 ALA R -33 REMARK 465 GLY R -32 REMARK 465 ALA R -31 REMARK 465 SER R -30 REMARK 465 ALA R -29 REMARK 465 GLY R -28 REMARK 465 SER R -27 REMARK 465 TRP R -26 REMARK 465 SER R -25 REMARK 465 HIS R -24 REMARK 465 PRO R -23 REMARK 465 GLN R -22 REMARK 465 PHE R -21 REMARK 465 GLU R -20 REMARK 465 LYS R -19 REMARK 465 GLY R -18 REMARK 465 SER R -17 REMARK 465 ASP R -16 REMARK 465 TYR R -15 REMARK 465 LYS R -14 REMARK 465 ASP R -13 REMARK 465 ASP R -12 REMARK 465 ASP R -11 REMARK 465 ASP R -10 REMARK 465 LYS R -9 REMARK 465 GLU R -8 REMARK 465 PHE R -7 REMARK 465 LEU R -6 REMARK 465 GLU R -5 REMARK 465 VAL R -4 REMARK 465 LEU R -3 REMARK 465 PHE R -2 REMARK 465 GLN R -1 REMARK 465 GLY R 0 REMARK 465 PRO R 1 REMARK 465 GLU R 2 REMARK 465 ASP R 3 REMARK 465 LEU R 4 REMARK 465 GLU R 5 REMARK 465 GLU R 6 REMARK 465 THR R 7 REMARK 465 LEU R 8 REMARK 465 PHE R 9 REMARK 465 GLU R 10 REMARK 465 GLU R 11 REMARK 465 PHE R 12 REMARK 465 GLU R 13 REMARK 465 ASN R 14 REMARK 465 TYR R 15 REMARK 465 SER R 16 REMARK 465 TYR R 17 REMARK 465 ASP R 18 REMARK 465 LEU R 19 REMARK 465 ASP R 20 REMARK 465 TYR R 21 REMARK 465 TYR R 22 REMARK 465 SER R 23 REMARK 465 LEU R 24 REMARK 465 GLU R 25 REMARK 465 SER R 26 REMARK 465 ASP R 27 REMARK 465 LEU R 28 REMARK 465 GLU R 29 REMARK 465 GLU R 30 REMARK 465 LYS R 31 REMARK 465 VAL R 32 REMARK 465 GLN R 33 REMARK 465 LEU R 34 REMARK 465 GLY R 35 REMARK 465 SER R 1338 REMARK 465 VAL R 1339 REMARK 465 ALA R 1340 REMARK 465 GLU R 1341 REMARK 465 ILE R 1342 REMARK 465 ALA R 1343 REMARK 465 ARG R 1344 REMARK 465 GLY R 1345 REMARK 465 ARG R 1346 REMARK 465 THR R 1347 REMARK 465 PRO R 1348 REMARK 465 PRO R 1349 REMARK 465 SER R 1350 REMARK 465 LEU R 1351 REMARK 465 GLY R 1352 REMARK 465 PRO R 1353 REMARK 465 GLN R 1354 REMARK 465 ASP R 1355 REMARK 465 GLU R 1356 REMARK 465 ASP R 1368 REMARK 465 THR R 1369 REMARK 465 SER R 1370 REMARK 465 SER R 1371 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 ASP A 3 REMARK 465 LYS A 4 REMARK 465 GLY A 5 REMARK 465 ALA A 90 REMARK 465 PRO A 91 REMARK 465 GLU A 92 REMARK 465 ASP A 93 REMARK 465 LYS A 94 REMARK 465 PHE A 190 REMARK 465 LEU A 191 REMARK 465 MET A 192 REMARK 465 SER A 193 REMARK 465 ASP A 194 REMARK 465 LYS A 195 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 SER A 341 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 GLN B 1 REMARK 465 SER B 113 REMARK 465 SER B 114 REMARK 465 HIS B 115 REMARK 465 HIS B 116 REMARK 465 HIS B 117 REMARK 465 HIS B 118 REMARK 465 HIS B 119 REMARK 465 HIS B 120 REMARK 465 SER C 1 REMARK 465 ILE C 107 REMARK 465 LYS C 108 REMARK 465 GLY C 109 REMARK 465 THR C 110 REMARK 465 THR C 111 REMARK 465 ALA C 112 REMARK 465 ALA C 113 REMARK 465 SER C 114 REMARK 465 GLY C 115 REMARK 465 SER C 116 REMARK 465 SER C 117 REMARK 465 GLY C 118 REMARK 465 GLY C 119 REMARK 465 SER C 120 REMARK 465 SER C 121 REMARK 465 SER C 122 REMARK 465 GLY C 123 REMARK 465 ALA C 124 REMARK 465 GLU C 125 REMARK 465 SER C 243 REMARK 465 SER C 244 REMARK 465 ALA C 245 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 GLU R 180 CG CD OE1 OE2 REMARK 470 ASN R 182 CG OD1 ND2 REMARK 470 ASN R 183 CG OD1 ND2 REMARK 470 GLN R 192 CG CD OE1 NE2 REMARK 470 HIS R 194 CG ND1 CD2 CE1 NE2 REMARK 470 ASP R 195 CG OD1 OD2 REMARK 470 ASP R 197 CG OD1 OD2 REMARK 470 LEU R 198 CG CD1 CD2 REMARK 470 THR R 199 OG1 CG2 REMARK 470 LEU R 200 CG CD1 CD2 REMARK 470 HIS R 273 CG ND1 CD2 CE1 NE2 REMARK 470 HIS R 274 CG ND1 CD2 CE1 NE2 REMARK 470 ASN R 275 CG OD1 ND2 REMARK 470 TYR R 277 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN R 283 CG CD OE1 NE2 REMARK 470 LYS R 309 CG CD CE NZ REMARK 470 PHE R 315 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG R 316 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 49 CG CD CE NZ REMARK 470 GLU A 50 CG CD OE1 OE2 REMARK 470 ASP A 69 CG OD1 OD2 REMARK 470 GLU A 134 CG CD OE1 OE2 REMARK 470 THR A 136 OG1 CG2 REMARK 470 ASN A 153 CG OD1 ND2 REMARK 470 GLU A 155 CG CD OE1 OE2 REMARK 470 LYS A 157 CG CD CE NZ REMARK 470 HIS A 159 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 160 CG CD CE NZ REMARK 470 GLU A 176 CG CD OE1 OE2 REMARK 470 ARG A 177 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 185 CG CD OE1 OE2 REMARK 470 GLN A 189 CG CD OE1 NE2 REMARK 470 HIS A 219 CG ND1 CD2 CE1 NE2 REMARK 470 ASN A 225 CG OD1 ND2 REMARK 470 LYS A 229 CG CD CE NZ REMARK 470 HIS A 295 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 308 CG CD OE1 OE2 REMARK 470 ASN A 311 CG OD1 ND2 REMARK 470 ARG A 312 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 357 CG CD CE NZ REMARK 470 GLU A 359 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 PHE B 28 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 64 CG CD CE NZ REMARK 470 ASP B 65 CG OD1 OD2 REMARK 470 LYS B 75 CG CD CE NZ REMARK 470 LYS B 86 CG CD CE NZ REMARK 470 ARG C 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 GLU C 82 CG CD OE1 OE2 REMARK 470 GLU C 106 CG CD OE1 OE2 REMARK 470 GLN C 137 CG CD OE1 NE2 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 OD1 ASP A 204 OH TYR A 208 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR R 72 -23.82 -140.24 REMARK 500 HIS R 141 66.87 60.25 REMARK 500 ARG R 149 54.94 -91.37 REMARK 500 GLN R 192 36.19 -96.14 REMARK 500 LEU R 200 -1.63 71.10 REMARK 500 PHE R 231 -4.02 69.68 REMARK 500 ALA R1361 -152.11 -109.19 REMARK 500 TYR A 47 -0.23 66.31 REMARK 500 ARG A 65 52.38 -93.36 REMARK 500 ASP A 69 59.03 -90.73 REMARK 500 LEU A 73 52.29 -91.51 REMARK 500 HIS A 111 52.11 -90.40 REMARK 500 ASN A 162 51.56 -92.77 REMARK 500 ASN A 281 52.66 -91.22 REMARK 500 HIS A 295 4.72 -69.93 REMARK 500 GLU A 358 -63.64 -96.62 REMARK 500 GLU A 359 148.76 -175.75 REMARK 500 SER B 62 50.02 -92.42 REMARK 500 SER C 32 6.96 -68.60 REMARK 500 ALA C 52 -8.83 70.42 REMARK 500 ASP C 71 44.38 -141.99 REMARK 500 GLU C 82 49.98 -92.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-64619 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE G PROTEIN-COUPLED RECEPTOR 1 (GPR1) BOUND REMARK 900 TO BETA-ARRESTIN 1 IN LIGAND-FREE STATE DBREF 9UYN R 2 1342 UNP P46091 CML2_HUMAN 2 322 DBREF 9UYN R 1343 1371 UNP P30518 V2R_HUMAN 343 371 DBREF 9UYN A 1 376 UNP P49407 ARRB1_HUMAN 1 376 DBREF 9UYN B 1 120 PDB 9UYN 9UYN 1 120 DBREF 9UYN C 1 245 PDB 9UYN 9UYN 1 245 SEQADV 9UYN MET R -62 UNP P46091 INITIATING METHIONINE SEQADV 9UYN LYS R -61 UNP P46091 EXPRESSION TAG SEQADV 9UYN THR R -60 UNP P46091 EXPRESSION TAG SEQADV 9UYN ILE R -59 UNP P46091 EXPRESSION TAG SEQADV 9UYN ILE R -58 UNP P46091 EXPRESSION TAG SEQADV 9UYN ALA R -57 UNP P46091 EXPRESSION TAG SEQADV 9UYN LEU R -56 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -55 UNP P46091 EXPRESSION TAG SEQADV 9UYN TYR R -54 UNP P46091 EXPRESSION TAG SEQADV 9UYN ILE R -53 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -52 UNP P46091 EXPRESSION TAG SEQADV 9UYN CYS R -51 UNP P46091 EXPRESSION TAG SEQADV 9UYN LEU R -50 UNP P46091 EXPRESSION TAG SEQADV 9UYN VAL R -49 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -48 UNP P46091 EXPRESSION TAG SEQADV 9UYN ALA R -47 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -46 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -45 UNP P46091 EXPRESSION TAG SEQADV 9UYN TRP R -44 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -43 UNP P46091 EXPRESSION TAG SEQADV 9UYN HIS R -42 UNP P46091 EXPRESSION TAG SEQADV 9UYN PRO R -41 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLN R -40 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -39 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLU R -38 UNP P46091 EXPRESSION TAG SEQADV 9UYN LYS R -37 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -36 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -35 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -34 UNP P46091 EXPRESSION TAG SEQADV 9UYN ALA R -33 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -32 UNP P46091 EXPRESSION TAG SEQADV 9UYN ALA R -31 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -30 UNP P46091 EXPRESSION TAG SEQADV 9UYN ALA R -29 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -28 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -27 UNP P46091 EXPRESSION TAG SEQADV 9UYN TRP R -26 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -25 UNP P46091 EXPRESSION TAG SEQADV 9UYN HIS R -24 UNP P46091 EXPRESSION TAG SEQADV 9UYN PRO R -23 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLN R -22 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -21 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLU R -20 UNP P46091 EXPRESSION TAG SEQADV 9UYN LYS R -19 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R -18 UNP P46091 EXPRESSION TAG SEQADV 9UYN SER R -17 UNP P46091 EXPRESSION TAG SEQADV 9UYN ASP R -16 UNP P46091 EXPRESSION TAG SEQADV 9UYN TYR R -15 UNP P46091 EXPRESSION TAG SEQADV 9UYN LYS R -14 UNP P46091 EXPRESSION TAG SEQADV 9UYN ASP R -13 UNP P46091 EXPRESSION TAG SEQADV 9UYN ASP R -12 UNP P46091 EXPRESSION TAG SEQADV 9UYN ASP R -11 UNP P46091 EXPRESSION TAG SEQADV 9UYN ASP R -10 UNP P46091 EXPRESSION TAG SEQADV 9UYN LYS R -9 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLU R -8 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -7 UNP P46091 EXPRESSION TAG SEQADV 9UYN LEU R -6 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLU R -5 UNP P46091 EXPRESSION TAG SEQADV 9UYN VAL R -4 UNP P46091 EXPRESSION TAG SEQADV 9UYN LEU R -3 UNP P46091 EXPRESSION TAG SEQADV 9UYN PHE R -2 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLN R -1 UNP P46091 EXPRESSION TAG SEQADV 9UYN GLY R 0 UNP P46091 EXPRESSION TAG SEQADV 9UYN PRO R 1 UNP P46091 EXPRESSION TAG SEQADV 9UYN CYS R 143 UNP P46091 VAL 143 ENGINEERED MUTATION SEQADV 9UYN ALA A 59 UNP P49407 CYS 59 ENGINEERED MUTATION SEQADV 9UYN SER A 125 UNP P49407 CYS 125 ENGINEERED MUTATION SEQADV 9UYN ILE A 140 UNP P49407 CYS 140 ENGINEERED MUTATION SEQADV 9UYN VAL A 150 UNP P49407 CYS 150 ENGINEERED MUTATION SEQADV 9UYN GLU A 169 UNP P49407 ARG 169 ENGINEERED MUTATION SEQADV 9UYN VAL A 242 UNP P49407 CYS 242 ENGINEERED MUTATION SEQADV 9UYN CYS A 249 UNP P49407 TYR 249 ENGINEERED MUTATION SEQADV 9UYN VAL A 251 UNP P49407 CYS 251 ENGINEERED MUTATION SEQADV 9UYN SER A 269 UNP P49407 CYS 269 ENGINEERED MUTATION SEQRES 1 R 414 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 414 VAL PHE ALA GLY SER TRP SER HIS PRO GLN PHE GLU LYS SEQRES 3 R 414 GLY SER GLY ALA GLY ALA SER ALA GLY SER TRP SER HIS SEQRES 4 R 414 PRO GLN PHE GLU LYS GLY SER ASP TYR LYS ASP ASP ASP SEQRES 5 R 414 ASP LYS GLU PHE LEU GLU VAL LEU PHE GLN GLY PRO GLU SEQRES 6 R 414 ASP LEU GLU GLU THR LEU PHE GLU GLU PHE GLU ASN TYR SEQRES 7 R 414 SER TYR ASP LEU ASP TYR TYR SER LEU GLU SER ASP LEU SEQRES 8 R 414 GLU GLU LYS VAL GLN LEU GLY VAL VAL HIS TRP VAL SER SEQRES 9 R 414 LEU VAL LEU TYR CYS LEU ALA PHE VAL LEU GLY ILE PRO SEQRES 10 R 414 GLY ASN ALA ILE VAL ILE TRP PHE THR GLY PHE LYS TRP SEQRES 11 R 414 LYS LYS THR VAL THR THR LEU TRP PHE LEU ASN LEU ALA SEQRES 12 R 414 ILE ALA ASP PHE ILE PHE LEU LEU PHE LEU PRO LEU TYR SEQRES 13 R 414 ILE SER TYR VAL ALA MET ASN PHE HIS TRP PRO PHE GLY SEQRES 14 R 414 ILE TRP LEU CYS LYS ALA ASN SER PHE THR ALA GLN LEU SEQRES 15 R 414 ASN MET PHE ALA SER VAL PHE PHE LEU THR VAL ILE SER SEQRES 16 R 414 LEU ASP HIS TYR ILE HIS LEU ILE HIS PRO CYS LEU SER SEQRES 17 R 414 HIS ARG HIS ARG THR LEU LYS ASN SER LEU ILE VAL ILE SEQRES 18 R 414 ILE PHE ILE TRP LEU LEU ALA SER LEU ILE GLY GLY PRO SEQRES 19 R 414 ALA LEU TYR PHE ARG ASP THR VAL GLU PHE ASN ASN HIS SEQRES 20 R 414 THR LEU CYS TYR ASN ASN PHE GLN LYS HIS ASP PRO ASP SEQRES 21 R 414 LEU THR LEU ILE ARG HIS HIS VAL LEU THR TRP VAL LYS SEQRES 22 R 414 PHE ILE ILE GLY TYR LEU PHE PRO LEU LEU THR MET SER SEQRES 23 R 414 ILE CYS TYR LEU CYS LEU ILE PHE LYS VAL LYS LYS ARG SEQRES 24 R 414 SER ILE LEU ILE SER SER ARG HIS PHE TRP THR ILE LEU SEQRES 25 R 414 VAL VAL VAL VAL ALA PHE VAL VAL CYS TRP THR PRO TYR SEQRES 26 R 414 HIS LEU PHE SER ILE TRP GLU LEU THR ILE HIS HIS ASN SEQRES 27 R 414 SER TYR SER HIS HIS VAL MET GLN ALA GLY ILE PRO LEU SEQRES 28 R 414 SER THR GLY LEU ALA PHE LEU ASN SER CYS LEU ASN PRO SEQRES 29 R 414 ILE LEU TYR VAL LEU ILE SER LYS LYS PHE GLN ALA ARG SEQRES 30 R 414 PHE ARG SER SER VAL ALA GLU ILE ALA ARG GLY ARG THR SEQRES 31 R 414 PRO PRO SER LEU GLY PRO GLN ASP GLU SEP CYS TPO TPO SEQRES 32 R 414 ALA SEP SEP SEP LEU ALA LYS ASP THR SER SER SEQRES 1 A 376 MET GLY ASP LYS GLY THR ARG VAL PHE LYS LYS ALA SER SEQRES 2 A 376 PRO ASN GLY LYS LEU THR VAL TYR LEU GLY LYS ARG ASP SEQRES 3 A 376 PHE VAL ASP HIS ILE ASP LEU VAL ASP PRO VAL ASP GLY SEQRES 4 A 376 VAL VAL LEU VAL ASP PRO GLU TYR LEU LYS GLU ARG ARG SEQRES 5 A 376 VAL TYR VAL THR LEU THR ALA ALA PHE ARG TYR GLY ARG SEQRES 6 A 376 GLU ASP LEU ASP VAL LEU GLY LEU THR PHE ARG LYS ASP SEQRES 7 A 376 LEU PHE VAL ALA ASN VAL GLN SER PHE PRO PRO ALA PRO SEQRES 8 A 376 GLU ASP LYS LYS PRO LEU THR ARG LEU GLN GLU ARG LEU SEQRES 9 A 376 ILE LYS LYS LEU GLY GLU HIS ALA TYR PRO PHE THR PHE SEQRES 10 A 376 GLU ILE PRO PRO ASN LEU PRO SER SER VAL THR LEU GLN SEQRES 11 A 376 PRO GLY PRO GLU ASP THR GLY LYS ALA ILE GLY VAL ASP SEQRES 12 A 376 TYR GLU VAL LYS ALA PHE VAL ALA GLU ASN LEU GLU GLU SEQRES 13 A 376 LYS ILE HIS LYS ARG ASN SER VAL ARG LEU VAL ILE GLU SEQRES 14 A 376 LYS VAL GLN TYR ALA PRO GLU ARG PRO GLY PRO GLN PRO SEQRES 15 A 376 THR ALA GLU THR THR ARG GLN PHE LEU MET SER ASP LYS SEQRES 16 A 376 PRO LEU HIS LEU GLU ALA SER LEU ASP LYS GLU ILE TYR SEQRES 17 A 376 TYR HIS GLY GLU PRO ILE SER VAL ASN VAL HIS VAL THR SEQRES 18 A 376 ASN ASN THR ASN LYS THR VAL LYS LYS ILE LYS ILE SER SEQRES 19 A 376 VAL ARG GLN TYR ALA ASP ILE VAL LEU PHE ASN THR ALA SEQRES 20 A 376 GLN CYS LYS VAL PRO VAL ALA MET GLU GLU ALA ASP ASP SEQRES 21 A 376 THR VAL ALA PRO SER SER THR PHE SER LYS VAL TYR THR SEQRES 22 A 376 LEU THR PRO PHE LEU ALA ASN ASN ARG GLU LYS ARG GLY SEQRES 23 A 376 LEU ALA LEU ASP GLY LYS LEU LYS HIS GLU ASP THR ASN SEQRES 24 A 376 LEU ALA SER SER THR LEU LEU ARG GLU GLY ALA ASN ARG SEQRES 25 A 376 GLU ILE LEU GLY ILE ILE VAL SER TYR LYS VAL LYS VAL SEQRES 26 A 376 LYS LEU VAL VAL SER ARG GLY GLY LEU LEU GLY ASP LEU SEQRES 27 A 376 ALA SER SER ASP VAL ALA VAL GLU LEU PRO PHE THR LEU SEQRES 28 A 376 MET HIS PRO LYS PRO LYS GLU GLU PRO PRO HIS ARG GLU SEQRES 29 A 376 VAL PRO GLU ASN GLU THR PRO VAL ASP THR ASN LEU SEQRES 1 B 120 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 120 ALA GLY GLY SER LEU ARG LEU SER CYS VAL VAL SER GLY SEQRES 3 B 120 PHE PHE PHE ASP THR VAL THR MET ALA TRP TYR ARG ARG SEQRES 4 B 120 ALA PRO GLY LYS HIS ARG GLU LEU VAL ALA SER ALA THR SEQRES 5 B 120 ALA GLY GLY THR THR THR TYR ALA ASP SER VAL LYS ASP SEQRES 6 B 120 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 B 120 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 B 120 VAL TYR TYR CYS ASN THR PHE VAL ARG SER LEU SER TRP SEQRES 9 B 120 GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS SEQRES 10 B 120 HIS HIS HIS SEQRES 1 C 245 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 C 245 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 C 245 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 C 245 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 C 245 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 C 245 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 C 245 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 C 245 TYR LYS TYR VAL PRO VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 C 245 VAL GLU ILE LYS GLY THR THR ALA ALA SER GLY SER SER SEQRES 10 C 245 GLY GLY SER SER SER GLY ALA GLU VAL GLN LEU VAL GLU SEQRES 11 C 245 SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG SEQRES 12 C 245 LEU SER CYS ALA ALA SER GLY PHE ASN VAL TYR SER SER SEQRES 13 C 245 SER ILE HIS TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU SEQRES 14 C 245 GLU TRP VAL ALA SER ILE SER SER TYR TYR GLY TYR THR SEQRES 15 C 245 TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR ILE SER SEQRES 16 C 245 ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN MET ASN SEQRES 17 C 245 SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 18 C 245 ARG SER ARG GLN PHE TRP TYR SER GLY LEU ASP TYR TRP SEQRES 19 C 245 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA MODRES 9UYN SEP R 1357 SER MODIFIED RESIDUE MODRES 9UYN TPO R 1359 THR MODIFIED RESIDUE MODRES 9UYN TPO R 1360 THR MODIFIED RESIDUE MODRES 9UYN SEP R 1362 SER MODIFIED RESIDUE MODRES 9UYN SEP R 1363 SER MODIFIED RESIDUE MODRES 9UYN SEP R 1364 SER MODIFIED RESIDUE HET SEP R1357 10 HET TPO R1359 11 HET TPO R1360 11 HET SEP R1362 10 HET SEP R1363 10 HET SEP R1364 10 HET PAM R1401 18 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETNAM PAM PALMITOLEIC ACID HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 SEP 4(C3 H8 N O6 P) FORMUL 1 TPO 2(C4 H10 N O6 P) FORMUL 5 PAM C16 H30 O2 HELIX 1 AA1 VAL R 36 PHE R 65 1 30 HELIX 2 AA2 THR R 73 MET R 99 1 27 HELIX 3 AA3 GLY R 106 ILE R 140 1 35 HELIX 4 AA4 HIS R 141 HIS R 146 1 6 HELIX 5 AA5 THR R 150 PHE R 175 1 26 HELIX 6 AA6 ILE R 201 ILE R 230 1 30 HELIX 7 AA7 HIS R 244 HIS R 274 1 31 HELIX 8 AA8 HIS R 280 ILE R 307 1 28 HELIX 9 AA9 SER R 308 SER R 317 1 10 HELIX 10 AB1 THR A 98 GLY A 109 1 12 HELIX 11 AB2 ASP B 61 LYS B 64 5 4 HELIX 12 AB3 GLN C 80 PHE C 84 5 5 SHEET 1 AA1 2 ARG R 176 PHE R 181 0 SHEET 2 AA1 2 HIS R 184 ASN R 189 -1 O TYR R 188 N ASP R 177 SHEET 1 AA2 5 ALA R1361 SEP R1364 0 SHEET 2 AA2 5 ARG A 7 ALA A 12 -1 O LYS A 10 N ALA R1361 SHEET 3 AA2 5 LEU A 18 LEU A 22 -1 O LEU A 22 N PHE A 9 SHEET 4 AA2 5 VAL A 37 VAL A 43 -1 O VAL A 40 N TYR A 21 SHEET 5 AA2 5 ALA A 112 PHE A 117 -1 O PHE A 115 N GLY A 39 SHEET 1 AA3 6 LEU A 33 VAL A 34 0 SHEET 2 AA3 6 ASP A 26 HIS A 30 -1 N HIS A 30 O LEU A 33 SHEET 3 AA3 6 SER A 163 VAL A 171 1 O VAL A 171 N ASP A 29 SHEET 4 AA3 6 GLY A 141 ALA A 151 -1 N VAL A 146 O LEU A 166 SHEET 5 AA3 6 ARG A 52 ARG A 62 -1 N THR A 56 O LYS A 147 SHEET 6 AA3 6 ASP A 78 GLN A 85 -1 O LEU A 79 N ALA A 59 SHEET 1 AA4 2 VAL A 127 LEU A 129 0 SHEET 2 AA4 2 ALA A 288 ASP A 290 -1 O LEU A 289 N THR A 128 SHEET 1 AA5 4 THR A 183 THR A 186 0 SHEET 2 AA5 4 HIS A 198 LEU A 203 -1 O ALA A 201 N ALA A 184 SHEET 3 AA5 4 VAL A 220 ASN A 222 -1 O THR A 221 N HIS A 198 SHEET 4 AA5 4 SER A 266 PHE A 268 -1 O PHE A 268 N VAL A 220 SHEET 1 AA6 4 THR A 183 THR A 186 0 SHEET 2 AA6 4 HIS A 198 LEU A 203 -1 O ALA A 201 N ALA A 184 SHEET 3 AA6 4 ILE A 214 ASN A 217 -1 O ASN A 217 N SER A 202 SHEET 4 AA6 4 VAL A 271 LEU A 274 -1 O LEU A 274 N ILE A 214 SHEET 1 AA7 5 ILE A 207 TYR A 209 0 SHEET 2 AA7 5 VAL A 343 MET A 352 1 O THR A 350 N TYR A 208 SHEET 3 AA7 5 ILE A 317 VAL A 329 -1 N LEU A 327 O VAL A 343 SHEET 4 AA7 5 VAL A 228 VAL A 242 -1 N TYR A 238 O SER A 320 SHEET 5 AA7 5 THR A 246 ALA A 258 -1 O VAL A 251 N GLN A 237 SHEET 1 AA8 4 GLN B 3 SER B 7 0 SHEET 2 AA8 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA8 4 THR B 77 MET B 82 -1 O LEU B 80 N LEU B 20 SHEET 4 AA8 4 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA9 5 THR B 57 TYR B 59 0 SHEET 2 AA9 5 ARG B 45 ALA B 51 -1 N SER B 50 O THR B 58 SHEET 3 AA9 5 MET B 34 ARG B 39 -1 N TRP B 36 O ALA B 49 SHEET 4 AA9 5 ALA B 91 THR B 97 -1 O TYR B 94 N TYR B 37 SHEET 5 AA9 5 THR B 108 VAL B 110 -1 O VAL B 110 N ALA B 91 SHEET 1 AB1 4 MET C 5 GLN C 7 0 SHEET 2 AB1 4 VAL C 20 ALA C 26 -1 O ARG C 25 N THR C 6 SHEET 3 AB1 4 THR C 73 ILE C 76 -1 O LEU C 74 N ILE C 22 SHEET 4 AB1 4 PHE C 63 SER C 66 -1 N SER C 64 O THR C 75 SHEET 1 AB2 5 SER C 11 LEU C 12 0 SHEET 2 AB2 5 THR C 103 VAL C 105 1 O LYS C 104 N LEU C 12 SHEET 3 AB2 5 THR C 86 GLN C 91 -1 N TYR C 87 O THR C 103 SHEET 4 AB2 5 VAL C 34 GLN C 39 -1 N ALA C 35 O GLN C 90 SHEET 5 AB2 5 LYS C 46 ILE C 49 -1 O LYS C 46 N GLN C 38 SHEET 1 AB3 4 LEU C 128 SER C 131 0 SHEET 2 AB3 4 LEU C 142 ALA C 148 -1 O SER C 145 N SER C 131 SHEET 3 AB3 4 THR C 202 MET C 207 -1 O ALA C 203 N CYS C 146 SHEET 4 AB3 4 PHE C 192 ASP C 197 -1 N ASP C 197 O THR C 202 SHEET 1 AB4 5 TYR C 181 TYR C 184 0 SHEET 2 AB4 5 LEU C 169 SER C 176 -1 N SER C 176 O TYR C 181 SHEET 3 AB4 5 SER C 156 GLN C 163 -1 N ARG C 162 O GLU C 170 SHEET 4 AB4 5 VAL C 217 ARG C 224 -1 O SER C 223 N SER C 157 SHEET 5 AB4 5 LEU C 231 TYR C 233 -1 O TYR C 233 N ARG C 222 SSBOND 1 CYS R 110 CYS R 187 1555 1555 2.03 SSBOND 2 CYS R 143 CYS A 249 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 4 CYS C 24 CYS C 89 1555 1555 2.03 SSBOND 5 CYS C 146 CYS C 220 1555 1555 2.03 LINK C SEP R1357 N CYS R1358 1555 1555 1.33 LINK C CYS R1358 N TPO R1359 1555 1555 1.33 LINK C TPO R1359 N TPO R1360 1555 1555 1.33 LINK C TPO R1360 N ALA R1361 1555 1555 1.33 LINK C ALA R1361 N SEP R1362 1555 1555 1.33 LINK C SEP R1362 N SEP R1363 1555 1555 1.33 LINK C SEP R1363 N SEP R1364 1555 1555 1.33 LINK C SEP R1364 N LEU R1365 1555 1555 1.33 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