HEADER MEMBRANE PROTEIN 18-JUN-24 8ZYU TITLE CRYO-EM STRUCTURE OF NEUROTENSIN RECEPTOR 1 IN COMPLEX WITH BETA- TITLE 2 ARRESTIN1 AND SBI-553 (COMPLEX 1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-ARRESTIN-1; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: ARRESTIN BETA-1,NON-VISUAL ARRESTIN-2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB30 HEAVY CHAIN; COMPND 8 CHAIN: D; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NEUROTENSIN PEPTIDE 8-13; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: FAB30 LIGHT CHAIN; COMPND 16 CHAIN: Q; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: SOLUBLE CYTOCHROME B562,NEUROTENSIN RECEPTOR TYPE 1; COMPND 20 CHAIN: R; COMPND 21 SYNONYM: CYTOCHROME B-562,NT-R-1,NTR1,HIGH-AFFINITY LEVOCABASTINE- COMPND 22 INSENSITIVE NEUROTENSIN RECEPTOR,NTRH; COMPND 23 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: ARRB1, ARR1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 MOL_ID: 3; SOURCE 15 SYNTHETIC: YES; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 562, 9606; SOURCE 29 GENE: CYBC, NTSR1, NTRR; SOURCE 30 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR FLAG-MCS-PCDNA3.1; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 2021188 KEYWDS NEUROTENSIN RECEPTOR, BETA-ARRESTIN1, PHOSPHORYLATION, INTRACELLULAR KEYWDS 2 AGONIST, SBI-553, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.SUN,X.LI,Q.YUAN,W.YIN,H.E.XU,C.TIAN REVDAT 1 16-APR-25 8ZYU 0 JRNL AUTH D.SUN,X.LI,Q.YUAN,Y.WANG,P.SHI,H.ZHANG,T.WANG,W.SUN,S.LING, JRNL AUTH 2 Y.LIU,J.LAI,W.XIE,W.YIN,L.LIU,H.E.XU,C.TIAN JRNL TITL MOLECULAR MECHANISM OF THE ARRESTIN-BIASED AGONISM OF JRNL TITL 2 NEUROTENSIN RECEPTOR 1 BY AN INTRACELLULAR ALLOSTERIC JRNL TITL 3 MODULATOR. JRNL REF CELL RES. V. 35 284 2025 JRNL REFN ISSN 1001-0602 JRNL PMID 40118988 JRNL DOI 10.1038/S41422-025-01095-7 REMARK 2 REMARK 2 RESOLUTION. 2.65 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) : 2.650 REMARK 3 NUMBER OF PARTICLES : 359739 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 8ZYU 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_1300048333. 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 : NTSR1-BETA-ARRESTIN1 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NTSR1 IN COMPLEX WITH BEAT REMARK 245 -ARRESTIN1 AND THE ARRESTIN-BIASED INTRACELLULAR AGONIST SBI-553 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 F20 REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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) : 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, L, Q, R 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 B -20 REMARK 465 GLY B -19 REMARK 465 SER B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 HIS B -10 REMARK 465 GLY B -9 REMARK 465 SER B -8 REMARK 465 LEU B -7 REMARK 465 GLU B -6 REMARK 465 VAL B -5 REMARK 465 LEU B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 PRO B 0 REMARK 465 GLY B 1 REMARK 465 ASP B 2 REMARK 465 LYS B 3 REMARK 465 GLU B 366 REMARK 465 ASN B 367 REMARK 465 GLU B 368 REMARK 465 THR B 369 REMARK 465 PRO B 370 REMARK 465 VAL B 371 REMARK 465 ASP B 372 REMARK 465 THR B 373 REMARK 465 ASN B 374 REMARK 465 LEU B 375 REMARK 465 ILE B 376 REMARK 465 GLU B 377 REMARK 465 LEU B 378 REMARK 465 ASP B 379 REMARK 465 THR B 380 REMARK 465 ASN B 381 REMARK 465 MET D 1 REMARK 465 VAL D 2 REMARK 465 SER D 3 REMARK 465 ALA D 4 REMARK 465 ILE D 5 REMARK 465 VAL D 6 REMARK 465 LEU D 7 REMARK 465 TYR D 8 REMARK 465 VAL D 9 REMARK 465 LEU D 10 REMARK 465 LEU D 11 REMARK 465 ALA D 12 REMARK 465 ALA D 13 REMARK 465 ALA D 14 REMARK 465 ALA D 15 REMARK 465 HIS D 16 REMARK 465 SER D 17 REMARK 465 ALA D 18 REMARK 465 PHE D 19 REMARK 465 ALA D 20 REMARK 465 GLU D 21 REMARK 465 ILE D 22 REMARK 465 SER D 23 REMARK 465 SER D 245 REMARK 465 CYS D 246 REMARK 465 ASP D 247 REMARK 465 LYS D 248 REMARK 465 THR D 249 REMARK 465 ALA D 250 REMARK 465 ALA D 251 REMARK 465 ALA D 252 REMARK 465 HIS D 253 REMARK 465 HIS D 254 REMARK 465 HIS D 255 REMARK 465 HIS D 256 REMARK 465 HIS D 257 REMARK 465 HIS D 258 REMARK 465 HIS D 259 REMARK 465 HIS D 260 REMARK 465 MET Q 1 REMARK 465 VAL Q 2 REMARK 465 SER Q 3 REMARK 465 ALA Q 4 REMARK 465 ILE Q 5 REMARK 465 VAL Q 6 REMARK 465 LEU Q 7 REMARK 465 TYR Q 8 REMARK 465 VAL Q 9 REMARK 465 LEU Q 10 REMARK 465 LEU Q 11 REMARK 465 ALA Q 12 REMARK 465 ALA Q 13 REMARK 465 ALA Q 14 REMARK 465 ALA Q 15 REMARK 465 HIS Q 16 REMARK 465 SER Q 17 REMARK 465 ALA Q 18 REMARK 465 PHE Q 19 REMARK 465 MET R -135 REMARK 465 LYS R -134 REMARK 465 THR R -133 REMARK 465 ILE R -132 REMARK 465 ILE R -131 REMARK 465 ALA R -130 REMARK 465 LEU R -129 REMARK 465 SER R -128 REMARK 465 TYR R -127 REMARK 465 ILE R -126 REMARK 465 PHE R -125 REMARK 465 CYS R -124 REMARK 465 LEU R -123 REMARK 465 VAL R -122 REMARK 465 PHE R -121 REMARK 465 ALA R -120 REMARK 465 GLY R -119 REMARK 465 SER R -118 REMARK 465 ALA R -117 REMARK 465 ASP R -116 REMARK 465 LEU R -115 REMARK 465 GLU R -114 REMARK 465 ASP R -113 REMARK 465 ASN R -112 REMARK 465 TRP R -111 REMARK 465 GLU R -110 REMARK 465 THR R -109 REMARK 465 LEU R -108 REMARK 465 ASN R -107 REMARK 465 ASP R -106 REMARK 465 ASN R -105 REMARK 465 LEU R -104 REMARK 465 LYS R -103 REMARK 465 VAL R -102 REMARK 465 ILE R -101 REMARK 465 GLU R -100 REMARK 465 LYS R -99 REMARK 465 ALA R -98 REMARK 465 ASP R -97 REMARK 465 ASN R -96 REMARK 465 ALA R -95 REMARK 465 ALA R -94 REMARK 465 GLN R -93 REMARK 465 VAL R -92 REMARK 465 LYS R -91 REMARK 465 ASP R -90 REMARK 465 ALA R -89 REMARK 465 LEU R -88 REMARK 465 THR R -87 REMARK 465 LYS R -86 REMARK 465 MET R -85 REMARK 465 ARG R -84 REMARK 465 ALA R -83 REMARK 465 ALA R -82 REMARK 465 ALA R -81 REMARK 465 LEU R -80 REMARK 465 ASP R -79 REMARK 465 ALA R -78 REMARK 465 GLN R -77 REMARK 465 LYS R -76 REMARK 465 ALA R -75 REMARK 465 THR R -74 REMARK 465 PRO R -73 REMARK 465 PRO R -72 REMARK 465 LYS R -71 REMARK 465 LEU R -70 REMARK 465 GLU R -69 REMARK 465 ASP R -68 REMARK 465 LYS R -67 REMARK 465 SER R -66 REMARK 465 PRO R -65 REMARK 465 ASP R -64 REMARK 465 SER R -63 REMARK 465 PRO R -62 REMARK 465 GLU R -61 REMARK 465 MET R -60 REMARK 465 LYS R -59 REMARK 465 ASP R -58 REMARK 465 PHE R -57 REMARK 465 ARG R -56 REMARK 465 HIS R -55 REMARK 465 GLY R -54 REMARK 465 PHE R -53 REMARK 465 ASP R -52 REMARK 465 ILE R -51 REMARK 465 LEU R -50 REMARK 465 VAL R -49 REMARK 465 GLY R -48 REMARK 465 GLN R -47 REMARK 465 ILE R -46 REMARK 465 ASP R -45 REMARK 465 ASP R -44 REMARK 465 ALA R -43 REMARK 465 LEU R -42 REMARK 465 LYS R -41 REMARK 465 LEU R -40 REMARK 465 ALA R -39 REMARK 465 ASN R -38 REMARK 465 GLU R -37 REMARK 465 GLY R -36 REMARK 465 LYS R -35 REMARK 465 VAL R -34 REMARK 465 LYS R -33 REMARK 465 GLU R -32 REMARK 465 ALA R -31 REMARK 465 GLN R -30 REMARK 465 ALA R -29 REMARK 465 ALA R -28 REMARK 465 ALA R -27 REMARK 465 GLU R -26 REMARK 465 GLN R -25 REMARK 465 LEU R -24 REMARK 465 LYS R -23 REMARK 465 THR R -22 REMARK 465 THR R -21 REMARK 465 ARG R -20 REMARK 465 ASN R -19 REMARK 465 ALA R -18 REMARK 465 TYR R -17 REMARK 465 ILE R -16 REMARK 465 GLN R -15 REMARK 465 LYS R -14 REMARK 465 TYR R -13 REMARK 465 LEU R -12 REMARK 465 ALA R -11 REMARK 465 SER R -10 REMARK 465 GLY R -9 REMARK 465 SER R -8 REMARK 465 LEU R -7 REMARK 465 GLU R -6 REMARK 465 VAL R -5 REMARK 465 LEU R -4 REMARK 465 PHE R -3 REMARK 465 GLN R -2 REMARK 465 GLY R -1 REMARK 465 PRO R 0 REMARK 465 MET R 1 REMARK 465 ARG R 2 REMARK 465 LEU R 3 REMARK 465 ASN R 4 REMARK 465 SER R 5 REMARK 465 SER R 6 REMARK 465 ALA R 7 REMARK 465 PRO R 8 REMARK 465 GLY R 9 REMARK 465 THR R 10 REMARK 465 PRO R 11 REMARK 465 GLY R 12 REMARK 465 THR R 13 REMARK 465 PRO R 14 REMARK 465 ALA R 15 REMARK 465 ALA R 16 REMARK 465 ASP R 17 REMARK 465 PRO R 18 REMARK 465 PHE R 19 REMARK 465 GLN R 20 REMARK 465 ARG R 21 REMARK 465 ALA R 22 REMARK 465 GLN R 23 REMARK 465 ALA R 24 REMARK 465 GLY R 25 REMARK 465 LEU R 26 REMARK 465 GLU R 27 REMARK 465 GLU R 28 REMARK 465 ALA R 29 REMARK 465 LEU R 30 REMARK 465 LEU R 31 REMARK 465 ALA R 32 REMARK 465 PRO R 33 REMARK 465 GLY R 34 REMARK 465 PHE R 35 REMARK 465 GLY R 36 REMARK 465 ASN R 37 REMARK 465 ALA R 38 REMARK 465 SER R 39 REMARK 465 GLY R 40 REMARK 465 ASN R 41 REMARK 465 ALA R 42 REMARK 465 SER R 43 REMARK 465 GLU R 44 REMARK 465 ARG R 45 REMARK 465 VAL R 46 REMARK 465 LEU R 47 REMARK 465 ALA R 48 REMARK 465 ALA R 49 REMARK 465 PRO R 50 REMARK 465 SER R 51 REMARK 465 SER R 52 REMARK 465 GLU R 53 REMARK 465 LEU R 54 REMARK 465 ASP R 55 REMARK 465 VAL R 56 REMARK 465 SER R 213 REMARK 465 ALA R 214 REMARK 465 ASP R 215 REMARK 465 GLY R 216 REMARK 465 GLN R 217 REMARK 465 HIS R 218 REMARK 465 ALA R 219 REMARK 465 ARG R 268 REMARK 465 GLN R 269 REMARK 465 ALA R 270 REMARK 465 ALA R 271 REMARK 465 GLU R 272 REMARK 465 GLN R 273 REMARK 465 GLY R 274 REMARK 465 GLN R 275 REMARK 465 VAL R 276 REMARK 465 CYS R 277 REMARK 465 THR R 278 REMARK 465 VAL R 279 REMARK 465 GLY R 280 REMARK 465 GLY R 281 REMARK 465 GLU R 282 REMARK 465 CYS R 382A REMARK 465 PRO R 382B REMARK 465 VAL R 382C REMARK 465 TRP R 382D REMARK 465 ARG R 382E REMARK 465 ARG R 382F REMARK 465 ARG R 382G REMARK 465 ARG R 382H REMARK 465 LYS R 382I REMARK 465 ARG R 382J REMARK 465 PRO R 382K REMARK 465 CYS R 382L REMARK 465 PHE R 382M REMARK 465 ASN R 382N REMARK 465 ALA R 382O REMARK 465 PHE R 382P REMARK 465 SER R 382Q REMARK 465 ARG R 382R REMARK 465 LYS R 382S REMARK 465 CYS R 382T REMARK 465 ASP R 382U REMARK 465 SEP R 382V REMARK 465 VAL R 382W REMARK 465 SEP R 382X REMARK 465 THR R 413 REMARK 465 ARG R 414 REMARK 465 GLU R 415 REMARK 465 THR R 416 REMARK 465 LEU R 417 REMARK 465 TYR R 418 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 B 45 CG CD OE1 OE2 REMARK 470 GLU B 49 CG CD OE1 OE2 REMARK 470 ASP B 68 CG OD1 OD2 REMARK 470 VAL B 69 CG1 CG2 REMARK 470 LEU B 70 CG CD1 CD2 REMARK 470 GLU B 91 CG CD OE1 OE2 REMARK 470 ASP B 92 CG OD1 OD2 REMARK 470 LYS B 93 CG CD CE NZ REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 133 CG CD OE1 OE2 REMARK 470 GLU B 154 CG CD OE1 OE2 REMARK 470 LYS B 156 CG CD CE NZ REMARK 470 GLU B 175 CG CD OE1 OE2 REMARK 470 ARG B 176 CG CD NE CZ NH1 NH2 REMARK 470 MET B 191 CG SD CE REMARK 470 ASP B 193 CG OD1 OD2 REMARK 470 GLU B 256 CG CD OE1 OE2 REMARK 470 ARG B 306 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 307 CG CD OE1 OE2 REMARK 470 ASN B 310 CG OD1 ND2 REMARK 470 ARG B 311 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 312 CG CD OE1 OE2 REMARK 470 ILE B 313 CG1 CG2 CD1 REMARK 470 LEU B 314 CG CD1 CD2 REMARK 470 ARG B 330 CG CD NE CZ NH1 NH2 REMARK 470 LEU B 333 CG CD1 CD2 REMARK 470 LEU B 334 CG CD1 CD2 REMARK 470 ASP B 336 CG OD1 OD2 REMARK 470 LEU B 337 CG CD1 CD2 REMARK 470 LYS B 356 CG CD CE NZ REMARK 470 GLU B 357 CG CD OE1 OE2 REMARK 470 GLU B 358 CG CD OE1 OE2 REMARK 470 HIS B 361 CG ND1 CD2 CE1 NE2 REMARK 470 GLU D 24 CG CD OE1 OE2 REMARK 470 GLU D 29 OE1 REMARK 470 GLU D 178 CG CD OE1 OE2 REMARK 470 SER D 216 OG REMARK 470 LEU D 219 CG CD1 CD2 REMARK 470 TYR D 224 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG Q 129 CG CD NE CZ NH1 NH2 REMARK 470 ASP Q 143 CG OD1 OD2 REMARK 470 GLN Q 145 CG CD OE1 NE2 REMARK 470 LEU Q 146 CG CD1 CD2 REMARK 470 LYS Q 147 CG CD CE NZ REMARK 470 LEU Q 156 CG CD1 CD2 REMARK 470 GLU Q 164 CG CD OE1 OE2 REMARK 470 LYS Q 166 CB CG CD CE NZ REMARK 470 GLN Q 168 CG CD OE1 NE2 REMARK 470 LYS Q 170 CG CD CE NZ REMARK 470 VAL Q 171 CG1 CG2 REMARK 470 ASP Q 172 CG OD1 OD2 REMARK 470 ASN Q 173 CG OD1 ND2 REMARK 470 LEU Q 175 CG CD1 CD2 REMARK 470 GLN Q 176 CG CD OE1 NE2 REMARK 470 ASN Q 179 CG OD1 ND2 REMARK 470 GLU Q 182 CG CD OE1 OE2 REMARK 470 LYS Q 190 CG CD CE NZ REMARK 470 LEU Q 202 CG CD1 CD2 REMARK 470 SER Q 203 OG REMARK 470 LYS Q 204 CG CD CE NZ REMARK 470 ASP Q 206 CG OD1 OD2 REMARK 470 TYR Q 207 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU Q 208 CG CD OE1 OE2 REMARK 470 LYS Q 209 CG CD CE NZ REMARK 470 LYS Q 211 CG CD CE NZ REMARK 470 GLU Q 216 CG CD OE1 OE2 REMARK 470 GLN Q 220 CG CD OE1 NE2 REMARK 470 LEU Q 222 CG CD1 CD2 REMARK 470 ARG Q 232 CG CD NE CZ NH1 NH2 REMARK 470 GLU Q 234 CG CD OE1 OE2 REMARK 470 ASP R 59 CG OD1 OD2 REMARK 470 ILE R 60 CG1 CG2 CD1 REMARK 470 TYR R 61 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS R 63 CG CD CE NZ REMARK 470 ARG R 90 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 91 CG CD CE NZ REMARK 470 LYS R 92 CG CD CE NZ REMARK 470 SER R 93 OG REMARK 470 GLN R 95 CG CD OE1 NE2 REMARK 470 ASP R 138 CG OD1 OD2 REMARK 470 LEU R 222 CG CD1 CD2 REMARK 470 HIS R 229 CG ND1 CD2 CE1 NE2 REMARK 470 THR R 230 OG1 CG2 REMARK 470 LYS R 234 CG CD CE NZ REMARK 470 HIS R 283 CG ND1 CD2 CE1 NE2 REMARK 470 ILE R 329 CG1 CG2 CD1 REMARK 470 ASP R 331 CG OD1 OD2 REMARK 470 GLU R 332 CG CD OE1 OE2 REMARK 470 GLN R 333 CG CD OE1 NE2 REMARK 470 TRP R 334 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 334 CZ3 CH2 REMARK 470 THR R 335 OG1 CG2 REMARK 470 ASP R 340 CG OD1 OD2 REMARK 470 CYS R 381 SG REMARK 470 LEU R 382 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 OD1 ASP B 203 OH TYR B 207 2.11 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 ASP B 66 49.81 -92.22 REMARK 500 PRO B 90 78.22 -68.58 REMARK 500 ASP B 92 54.16 -93.70 REMARK 500 MET B 191 60.97 -102.12 REMARK 500 ASN B 298 -179.06 -69.71 REMARK 500 ALA B 309 -131.00 56.87 REMARK 500 SER D 76 -9.27 72.25 REMARK 500 TRP D 126 39.86 70.29 REMARK 500 TYR D 127 143.59 -171.02 REMARK 500 SER D 191 32.92 -96.47 REMARK 500 TYR L 11 -8.03 71.66 REMARK 500 ASP Q 22 116.63 -161.17 REMARK 500 SER Q 51 -139.13 59.00 REMARK 500 ALA Q 72 -10.48 71.25 REMARK 500 ALA Q 105 -168.71 -161.63 REMARK 500 ARG Q 129 -167.79 -161.98 REMARK 500 ASN Q 158 -167.42 -79.84 REMARK 500 ARG Q 163 -4.90 71.32 REMARK 500 LYS R 92 -168.85 -118.80 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 PIO R 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60579 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NEUROTENSIN RECEPTOR 1 IN COMPLEX WITH BETA- REMARK 900 ARRESTIN1 AND SBI-553 (COMPLEX 1) DBREF 8ZYU B 1 381 UNP P49407 ARRB1_HUMAN 2 382 DBREF 8ZYU D 1 260 PDB 8ZYU 8ZYU 1 260 DBREF 8ZYU L 8 13 PDB 8ZYU 8ZYU 8 13 DBREF 8ZYU Q 1 235 PDB 8ZYU 8ZYU 1 235 DBREF 8ZYU R -117 -13 UNP P0ABE7 C562_ECOLX 23 127 DBREF 8ZYU R 1 418 UNP P30989 NTR1_HUMAN 1 418 SEQADV 8ZYU MET B -20 UNP P49407 INITIATING METHIONINE SEQADV 8ZYU GLY B -19 UNP P49407 EXPRESSION TAG SEQADV 8ZYU SER B -18 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -17 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -16 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -15 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -14 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -13 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -12 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -11 UNP P49407 EXPRESSION TAG SEQADV 8ZYU HIS B -10 UNP P49407 EXPRESSION TAG SEQADV 8ZYU GLY B -9 UNP P49407 EXPRESSION TAG SEQADV 8ZYU SER B -8 UNP P49407 EXPRESSION TAG SEQADV 8ZYU LEU B -7 UNP P49407 EXPRESSION TAG SEQADV 8ZYU GLU B -6 UNP P49407 EXPRESSION TAG SEQADV 8ZYU VAL B -5 UNP P49407 EXPRESSION TAG SEQADV 8ZYU LEU B -4 UNP P49407 EXPRESSION TAG SEQADV 8ZYU PHE B -3 UNP P49407 EXPRESSION TAG SEQADV 8ZYU GLN B -2 UNP P49407 EXPRESSION TAG SEQADV 8ZYU GLY B -1 UNP P49407 EXPRESSION TAG SEQADV 8ZYU PRO B 0 UNP P49407 EXPRESSION TAG SEQADV 8ZYU MET R -135 UNP P0ABE7 INITIATING METHIONINE SEQADV 8ZYU LYS R -134 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU THR R -133 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU ILE R -132 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU ILE R -131 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU ALA R -130 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU LEU R -129 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU SER R -128 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU TYR R -127 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU ILE R -126 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU PHE R -125 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU CYS R -124 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU LEU R -123 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU VAL R -122 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU PHE R -121 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU ALA R -120 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU GLY R -119 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU SER R -118 UNP P0ABE7 EXPRESSION TAG SEQADV 8ZYU TRP R -111 UNP P0ABE7 MET 29 CONFLICT SEQADV 8ZYU ILE R -16 UNP P0ABE7 HIS 124 CONFLICT SEQADV 8ZYU LEU R -12 UNP P0ABE7 LINKER SEQADV 8ZYU ALA R -11 UNP P0ABE7 LINKER SEQADV 8ZYU SER R -10 UNP P0ABE7 LINKER SEQADV 8ZYU GLY R -9 UNP P0ABE7 LINKER SEQADV 8ZYU SER R -8 UNP P0ABE7 LINKER SEQADV 8ZYU LEU R -7 UNP P0ABE7 LINKER SEQADV 8ZYU GLU R -6 UNP P0ABE7 LINKER SEQADV 8ZYU VAL R -5 UNP P0ABE7 LINKER SEQADV 8ZYU LEU R -4 UNP P0ABE7 LINKER SEQADV 8ZYU PHE R -3 UNP P0ABE7 LINKER SEQADV 8ZYU GLN R -2 UNP P0ABE7 LINKER SEQADV 8ZYU GLY R -1 UNP P0ABE7 LINKER SEQADV 8ZYU PRO R 0 UNP P0ABE7 LINKER SEQADV 8ZYU CYS R 382L UNP P30989 INSERTION SEQADV 8ZYU PHE R 382M UNP P30989 INSERTION SEQADV 8ZYU ASN R 382N UNP P30989 INSERTION SEQADV 8ZYU CYS R 382T UNP P30989 ALA 399 CONFLICT SEQRES 1 B 402 MET GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SEQRES 2 B 402 LEU GLU VAL LEU PHE GLN GLY PRO GLY ASP LYS GLY THR SEQRES 3 B 402 ARG VAL PHE LYS LYS ALA SER PRO ASN GLY LYS LEU THR SEQRES 4 B 402 VAL TYR LEU GLY LYS ARG ASP PHE VAL ASP HIS ILE ASP SEQRES 5 B 402 LEU VAL ASP PRO VAL ASP GLY VAL VAL LEU VAL ASP PRO SEQRES 6 B 402 GLU TYR LEU LYS GLU ARG ARG VAL TYR VAL THR LEU THR SEQRES 7 B 402 CYS ALA PHE ARG TYR GLY ARG GLU ASP LEU ASP VAL LEU SEQRES 8 B 402 GLY LEU THR PHE ARG LYS ASP LEU PHE VAL ALA ASN VAL SEQRES 9 B 402 GLN SER PHE PRO PRO ALA PRO GLU ASP LYS LYS PRO LEU SEQRES 10 B 402 THR ARG LEU GLN GLU ARG LEU ILE LYS LYS LEU GLY GLU SEQRES 11 B 402 HIS ALA TYR PRO PHE THR PHE GLU ILE PRO PRO ASN LEU SEQRES 12 B 402 PRO CYS SER VAL THR LEU GLN PRO GLY PRO GLU ASP THR SEQRES 13 B 402 GLY LYS ALA CYS GLY VAL ASP TYR GLU VAL LYS ALA PHE SEQRES 14 B 402 CYS ALA GLU ASN LEU GLU GLU LYS ILE HIS LYS ARG ASN SEQRES 15 B 402 SER VAL ARG LEU VAL ILE ARG LYS VAL GLN TYR ALA PRO SEQRES 16 B 402 GLU ARG PRO GLY PRO GLN PRO THR ALA GLU THR THR ARG SEQRES 17 B 402 GLN PHE LEU MET SER ASP LYS PRO LEU HIS LEU GLU ALA SEQRES 18 B 402 SER LEU ASP LYS GLU ILE TYR TYR HIS GLY GLU PRO ILE SEQRES 19 B 402 SER VAL ASN VAL HIS VAL THR ASN ASN THR ASN LYS THR SEQRES 20 B 402 VAL LYS LYS ILE LYS ILE SER VAL ARG GLN TYR ALA ASP SEQRES 21 B 402 ILE CYS LEU PHE ASN THR ALA GLN TYR LYS CYS PRO VAL SEQRES 22 B 402 ALA MET GLU GLU ALA ASP ASP THR VAL ALA PRO SER SER SEQRES 23 B 402 THR PHE CYS LYS VAL TYR THR LEU THR PRO PHE LEU ALA SEQRES 24 B 402 ASN ASN ARG GLU LYS ARG GLY LEU ALA LEU ASP GLY LYS SEQRES 25 B 402 LEU LYS HIS GLU ASP THR ASN LEU ALA SER SER THR LEU SEQRES 26 B 402 LEU ARG GLU GLY ALA ASN ARG GLU ILE LEU GLY ILE ILE SEQRES 27 B 402 VAL SER TYR LYS VAL LYS VAL LYS LEU VAL VAL SER ARG SEQRES 28 B 402 GLY GLY LEU LEU GLY ASP LEU ALA SER SER ASP VAL ALA SEQRES 29 B 402 VAL GLU LEU PRO PHE THR LEU MET HIS PRO LYS PRO LYS SEQRES 30 B 402 GLU GLU PRO PRO HIS ARG GLU VAL PRO GLU ASN GLU THR SEQRES 31 B 402 PRO VAL ASP THR ASN LEU ILE GLU LEU ASP THR ASN SEQRES 1 D 260 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 D 260 ALA ALA HIS SER ALA PHE ALA GLU ILE SER GLU VAL GLN SEQRES 3 D 260 LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 4 D 260 SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE ASN VAL SEQRES 5 D 260 TYR SER SER SER ILE HIS TRP VAL ARG GLN ALA PRO GLY SEQRES 6 D 260 LYS GLY LEU GLU TRP VAL ALA SER ILE SER SER TYR TYR SEQRES 7 D 260 GLY TYR THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE SEQRES 8 D 260 THR ILE SER ALA ASP THR SER LYS ASN THR ALA TYR LEU SEQRES 9 D 260 GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR SEQRES 10 D 260 TYR CYS ALA ARG SER ARG GLN PHE TRP TYR SER GLY LEU SEQRES 11 D 260 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 12 D 260 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 13 D 260 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 14 D 260 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 15 D 260 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 16 D 260 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 17 D 260 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 18 D 260 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 19 D 260 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 20 D 260 LYS THR ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 L 6 ARG ARG PRO TYR ILE LEU SEQRES 1 Q 235 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA SEQRES 2 Q 235 ALA ALA HIS SER ALA PHE ALA SER ASP ILE GLN MET THR SEQRES 3 Q 235 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 4 Q 235 VAL THR ILE THR CYS ARG ALA SER GLN SER VAL SER SER SEQRES 5 Q 235 ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 6 Q 235 LYS LEU LEU ILE TYR SER ALA SER SER LEU TYR SER GLY SEQRES 7 Q 235 VAL PRO SER ARG PHE SER GLY SER ARG SER GLY THR ASP SEQRES 8 Q 235 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 9 Q 235 ALA THR TYR TYR CYS GLN GLN TYR LYS TYR VAL PRO VAL SEQRES 10 Q 235 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR SEQRES 11 Q 235 VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP SEQRES 12 Q 235 SER GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU SEQRES 13 Q 235 LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP SEQRES 14 Q 235 LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SEQRES 15 Q 235 SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER SEQRES 16 Q 235 LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU SEQRES 17 Q 235 LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY SEQRES 18 Q 235 LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 19 Q 235 CYS SEQRES 1 R 557 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 557 VAL PHE ALA GLY SER ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 3 R 557 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 4 R 557 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 5 R 557 ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS SEQRES 6 R 557 LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP SEQRES 7 R 557 PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP SEQRES 8 R 557 ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU SEQRES 9 R 557 ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN SEQRES 10 R 557 ALA TYR ILE GLN LYS TYR LEU ALA SER GLY SER LEU GLU SEQRES 11 R 557 VAL LEU PHE GLN GLY PRO MET ARG LEU ASN SER SER ALA SEQRES 12 R 557 PRO GLY THR PRO GLY THR PRO ALA ALA ASP PRO PHE GLN SEQRES 13 R 557 ARG ALA GLN ALA GLY LEU GLU GLU ALA LEU LEU ALA PRO SEQRES 14 R 557 GLY PHE GLY ASN ALA SER GLY ASN ALA SER GLU ARG VAL SEQRES 15 R 557 LEU ALA ALA PRO SER SER GLU LEU ASP VAL ASN THR ASP SEQRES 16 R 557 ILE TYR SER LYS VAL LEU VAL THR ALA VAL TYR LEU ALA SEQRES 17 R 557 LEU PHE VAL VAL GLY THR VAL GLY ASN THR VAL THR ALA SEQRES 18 R 557 PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER LEU GLN SEQRES 19 R 557 SER THR VAL HIS TYR HIS LEU GLY SER LEU ALA LEU SER SEQRES 20 R 557 ASP LEU LEU THR LEU LEU LEU ALA MET PRO VAL GLU LEU SEQRES 21 R 557 TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA PHE GLY SEQRES 22 R 557 ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG ASP ALA SEQRES 23 R 557 CYS THR TYR ALA THR ALA LEU ASN VAL ALA SER LEU SER SEQRES 24 R 557 VAL GLU ARG TYR LEU ALA ILE CYS HIS PRO PHE LYS ALA SEQRES 25 R 557 LYS THR LEU MET SER ARG SER ARG THR LYS LYS PHE ILE SEQRES 26 R 557 SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA VAL PRO SEQRES 27 R 557 MET LEU PHE THR MET GLY GLU GLN ASN ARG SER ALA ASP SEQRES 28 R 557 GLY GLN HIS ALA GLY GLY LEU VAL CYS THR PRO THR ILE SEQRES 29 R 557 HIS THR ALA THR VAL LYS VAL VAL ILE GLN VAL ASN THR SEQRES 30 R 557 PHE MET SER PHE ILE PHE PRO MET VAL VAL ILE SER VAL SEQRES 31 R 557 LEU ASN THR ILE ILE ALA ASN LYS LEU THR VAL MET VAL SEQRES 32 R 557 ARG GLN ALA ALA GLU GLN GLY GLN VAL CYS THR VAL GLY SEQRES 33 R 557 GLY GLU HIS SER THR PHE SER MET ALA ILE GLU PRO GLY SEQRES 34 R 557 ARG VAL GLN ALA LEU ARG HIS GLY VAL ARG VAL LEU ARG SEQRES 35 R 557 ALA VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR SEQRES 36 R 557 HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU SEQRES 37 R 557 GLN TRP THR PRO PHE LEU TYR ASP PHE TYR HIS TYR PHE SEQRES 38 R 557 TYR MET VAL THR ASN ALA LEU PHE TYR VAL SER SER THR SEQRES 39 R 557 ILE ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE SEQRES 40 R 557 ARG HIS ILE PHE LEU ALA THR LEU ALA CYS LEU CYS PRO SEQRES 41 R 557 VAL TRP ARG ARG ARG ARG LYS ARG PRO CYS PHE ASN ALA SEQRES 42 R 557 PHE SER ARG LYS CYS ASP SEP VAL SEP SEP ASN HIS TPO SEQRES 43 R 557 LEU SEP SEP ASN ALA THR ARG GLU THR LEU TYR MODRES 8ZYU SEP R 404 SER MODIFIED RESIDUE MODRES 8ZYU TPO R 407 THR MODIFIED RESIDUE MODRES 8ZYU SEP R 409 SER MODIFIED RESIDUE MODRES 8ZYU SEP R 410 SER MODIFIED RESIDUE HET SEP R 404 10 HET TPO R 407 11 HET SEP R 409 10 HET SEP R 410 10 HET SRW R 500 33 HET PIO R 501 40 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETNAM SRW 2-[{2-(1-FLUOROCYCLOPROPYL)-4-[4-(2-METHOXYPHENYL) HETNAM 2 SRW PIPERIDIN-1-YL]QUINAZOLIN-6-YL}(METHYL)AMINO]ETHAN-1- HETNAM 3 SRW OL HETNAM PIO [(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2, HETNAM 2 PIO 3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY- HETNAM 3 PIO PHOSPHORYL]OXY-PROPYL] OCTANOATE HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE HETSYN PIO DIOCTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5- HETSYN 2 PIO DIPHOSPHATE FORMUL 5 SEP 3(C3 H8 N O6 P) FORMUL 5 TPO C4 H10 N O6 P FORMUL 6 SRW C26 H31 F N4 O2 FORMUL 7 PIO C25 H49 O19 P3 HELIX 1 AA1 ASP B 43 LYS B 48 1 6 HELIX 2 AA2 THR B 97 GLY B 108 1 12 HELIX 3 AA3 ARG D 110 THR D 114 5 5 HELIX 4 AA4 SER D 186 ALA D 188 5 3 HELIX 5 AA5 SER D 217 LEU D 219 5 3 HELIX 6 AA6 GLN Q 100 PHE Q 104 5 5 HELIX 7 AA7 SER Q 142 GLY Q 149 1 8 HELIX 8 AA8 LYS Q 170 ALA Q 174 5 5 HELIX 9 AA9 LYS Q 204 HIS Q 210 1 7 HELIX 10 AB1 ASP R 59 ARG R 90 1 32 HELIX 11 AB2 THR R 100 PHE R 127 1 28 HELIX 12 AB3 GLY R 137 HIS R 172 1 36 HELIX 13 AB4 HIS R 172 MET R 180 1 9 HELIX 14 AB5 SER R 181 VAL R 201 1 21 HELIX 15 AB6 VAL R 201 THR R 206 1 6 HELIX 16 AB7 HIS R 229 VAL R 267 1 39 HELIX 17 AB8 HIS R 300 PHE R 326 1 27 HELIX 18 AB9 THR R 335 SER R 368 1 34 HELIX 19 AC1 SER R 368 LEU R 382 1 15 SHEET 1 AA1 5 ALA B 111 PHE B 116 0 SHEET 2 AA1 5 VAL B 36 LEU B 41 -1 N VAL B 40 O TYR B 112 SHEET 3 AA1 5 THR B 18 LEU B 21 -1 N TYR B 20 O VAL B 39 SHEET 4 AA1 5 ARG B 6 ALA B 11 -1 N PHE B 8 O LEU B 21 SHEET 5 AA1 5 LEU R 408 ASN R 411 -1 O SEP R 410 N VAL B 7 SHEET 1 AA2 6 ASP B 25 VAL B 27 0 SHEET 2 AA2 6 SER B 162 VAL B 170 1 O ARG B 168 N PHE B 26 SHEET 3 AA2 6 GLY B 140 ALA B 150 -1 N VAL B 145 O LEU B 165 SHEET 4 AA2 6 ARG B 51 ARG B 64 -1 N THR B 55 O LYS B 146 SHEET 5 AA2 6 VAL B 126 LEU B 128 0 SHEET 6 AA2 6 ALA B 287 ASP B 289 -1 O LEU B 288 N THR B 127 SHEET 1 AA3 5 THR B 73 GLN B 84 0 SHEET 2 AA3 5 ARG B 51 ARG B 64 -1 N CYS B 58 O LEU B 78 SHEET 3 AA3 5 GLY B 140 ALA B 150 -1 O LYS B 146 N THR B 55 SHEET 4 AA3 5 ARG R 294 GLN R 296 0 SHEET 5 AA3 5 MET R 288 GLU R 291 -1 N GLU R 291 O ARG R 294 SHEET 1 AA4 4 THR B 182 ARG B 187 0 SHEET 2 AA4 4 LEU B 196 LEU B 202 -1 O ALA B 200 N ALA B 183 SHEET 3 AA4 4 ILE B 213 ASN B 221 -1 O HIS B 218 N GLU B 199 SHEET 4 AA4 4 SER B 265 LEU B 273 -1 O PHE B 267 N VAL B 219 SHEET 1 AA5 6 ILE B 206 TYR B 207 0 SHEET 2 AA5 6 SER B 339 LEU B 350 1 O THR B 349 N TYR B 207 SHEET 3 AA5 6 ILE B 316 SER B 329 -1 N LEU B 326 O VAL B 342 SHEET 4 AA5 6 VAL B 227 CYS B 241 -1 N LYS B 231 O LYS B 325 SHEET 5 AA5 6 THR B 245 ALA B 257 -1 O CYS B 250 N GLN B 236 SHEET 6 AA5 6 GLN R 95 SER R 96 -1 O GLN R 95 N LYS B 249 SHEET 1 AA6 4 GLN D 26 SER D 30 0 SHEET 2 AA6 4 LEU D 41 SER D 48 -1 O ALA D 46 N VAL D 28 SHEET 3 AA6 4 THR D 101 MET D 106 -1 O MET D 106 N LEU D 41 SHEET 4 AA6 4 PHE D 91 ASP D 96 -1 N SER D 94 O TYR D 103 SHEET 1 AA7 6 LEU D 34 VAL D 35 0 SHEET 2 AA7 6 THR D 137 VAL D 141 1 O THR D 140 N VAL D 35 SHEET 3 AA7 6 ALA D 115 ARG D 123 -1 N ALA D 115 O VAL D 139 SHEET 4 AA7 6 SER D 55 GLN D 62 -1 N VAL D 60 O TYR D 118 SHEET 5 AA7 6 LEU D 68 ILE D 74 -1 O VAL D 71 N TRP D 59 SHEET 6 AA7 6 THR D 81 TYR D 83 -1 O TYR D 82 N SER D 73 SHEET 1 AA8 4 LEU D 34 VAL D 35 0 SHEET 2 AA8 4 THR D 137 VAL D 141 1 O THR D 140 N VAL D 35 SHEET 3 AA8 4 ALA D 115 ARG D 123 -1 N ALA D 115 O VAL D 139 SHEET 4 AA8 4 TYR D 132 TRP D 133 -1 O TYR D 132 N ARG D 121 SHEET 1 AA9 4 SER D 150 LEU D 154 0 SHEET 2 AA9 4 THR D 165 TYR D 175 -1 O LEU D 171 N PHE D 152 SHEET 3 AA9 4 TYR D 206 PRO D 215 -1 O VAL D 214 N ALA D 166 SHEET 4 AA9 4 HIS D 194 THR D 195 -1 N HIS D 194 O VAL D 211 SHEET 1 AB1 4 SER D 150 LEU D 154 0 SHEET 2 AB1 4 THR D 165 TYR D 175 -1 O LEU D 171 N PHE D 152 SHEET 3 AB1 4 TYR D 206 PRO D 215 -1 O VAL D 214 N ALA D 166 SHEET 4 AB1 4 VAL D 199 LEU D 200 -1 N VAL D 199 O SER D 207 SHEET 1 AB2 3 THR D 181 TRP D 184 0 SHEET 2 AB2 3 TYR D 224 HIS D 230 -1 O ASN D 227 N SER D 183 SHEET 3 AB2 3 THR D 235 VAL D 241 -1 O VAL D 237 N VAL D 228 SHEET 1 AB3 4 MET Q 25 GLN Q 27 0 SHEET 2 AB3 4 VAL Q 40 ALA Q 46 -1 O ARG Q 45 N THR Q 26 SHEET 3 AB3 4 ASP Q 91 ILE Q 96 -1 O PHE Q 92 N CYS Q 44 SHEET 4 AB3 4 PHE Q 83 ARG Q 87 -1 N SER Q 84 O THR Q 95 SHEET 1 AB4 6 SER Q 31 SER Q 33 0 SHEET 2 AB4 6 THR Q 123 GLU Q 126 1 O GLU Q 126 N LEU Q 32 SHEET 3 AB4 6 THR Q 106 GLN Q 111 -1 N TYR Q 107 O THR Q 123 SHEET 4 AB4 6 VAL Q 54 GLN Q 59 -1 N ALA Q 55 O GLN Q 110 SHEET 5 AB4 6 LYS Q 66 TYR Q 70 -1 O LYS Q 66 N GLN Q 58 SHEET 6 AB4 6 SER Q 74 LEU Q 75 -1 O SER Q 74 N TYR Q 70 SHEET 1 AB5 4 SER Q 31 SER Q 33 0 SHEET 2 AB5 4 THR Q 123 GLU Q 126 1 O GLU Q 126 N LEU Q 32 SHEET 3 AB5 4 THR Q 106 GLN Q 111 -1 N TYR Q 107 O THR Q 123 SHEET 4 AB5 4 THR Q 118 PHE Q 119 -1 O THR Q 118 N GLN Q 111 SHEET 1 AB6 4 VAL Q 136 PHE Q 139 0 SHEET 2 AB6 4 THR Q 150 PHE Q 160 -1 O LEU Q 156 N PHE Q 137 SHEET 3 AB6 4 TYR Q 194 SER Q 203 -1 O LEU Q 196 N LEU Q 157 SHEET 4 AB6 4 GLN Q 181 VAL Q 184 -1 N GLN Q 181 O THR Q 199 SHEET 1 AB7 3 VAL Q 167 GLN Q 168 0 SHEET 2 AB7 3 VAL Q 212 VAL Q 217 -1 O GLU Q 216 N GLN Q 168 SHEET 3 AB7 3 VAL Q 226 ASN Q 231 -1 O PHE Q 230 N TYR Q 213 SHEET 1 AB8 2 MET R 207 GLN R 210 0 SHEET 2 AB8 2 VAL R 223 PRO R 226 -1 O VAL R 223 N GLN R 210 SSBOND 1 CYS D 45 CYS D 119 1555 1555 2.03 SSBOND 2 CYS D 170 CYS D 226 1555 1555 2.03 SSBOND 3 CYS Q 44 CYS Q 109 1555 1555 2.04 SSBOND 4 CYS Q 155 CYS Q 215 1555 1555 2.03 SSBOND 5 CYS R 141 CYS R 224 1555 1555 2.03 LINK C SEP R 404 N ASN R 405 1555 1555 1.33 LINK C HIS R 406 N TPO R 407 1555 1555 1.33 LINK C TPO R 407 N LEU R 408 1555 1555 1.33 LINK C LEU R 408 N SEP R 409 1555 1555 1.33 LINK C SEP R 409 N SEP R 410 1555 1555 1.33 LINK C SEP R 410 N ASN R 411 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