HEADER SIGNALING PROTEIN 20-SEP-24 9JMD TITLE CRYO-EM STRUCTURE OF THE AZITHROMYCIN-MOTILIN RECEPTOR-GQ PROTEIN TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 7 BETA-1; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: SCFV16; COMPND 13 CHAIN: E; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 17 GAMMA-2; COMPND 18 CHAIN: G; COMPND 19 SYNONYM: G GAMMA-I; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: MOTILIN RECEPTOR; COMPND 23 CHAIN: R; COMPND 24 SYNONYM: G-PROTEIN COUPLED RECEPTOR 38; COMPND 25 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: GNB1; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 GENE: GNG2; SOURCE 23 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 GENE: MLNR, GPR38, MTLR, MTLR1; SOURCE 30 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS CRYO-EM, GPCR, MOTILIN RECEPTOR, AZITHROMYCIN, MACROLIDE ANTIBIOTICS, KEYWDS 2 GQ, COMPLEX, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.E.XU,C.YOU,Y.JIANG REVDAT 1 28-MAY-25 9JMD 0 JRNL AUTH C.YOU,M.JIANG,T.GAO,Z.ZHU,X.HE,Y.XU,Y.GAO,Y.JIANG,H.E.XU JRNL TITL DECODING THE STRUCTURAL BASIS OF LIGAND RECOGNITION AND JRNL TITL 2 BIASED SIGNALING IN THE MOTILIN RECEPTOR. JRNL REF CELL REP V. 44 15329 2025 JRNL REFN ESSN 2211-1247 JRNL PMID 39987561 JRNL DOI 10.1016/J.CELREP.2025.115329 REMARK 2 REMARK 2 RESOLUTION. 2.74 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) : 2.740 REMARK 3 NUMBER OF PARTICLES : 559995 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 9JMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300049686. 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 : THE AZITHROMYCIN-MOTILIN REMARK 245 RECEPTOR-GQ PROTEIN 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 5000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 20000.00 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: A, B, E, G, 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 A 1 REMARK 465 GLY A 2 REMARK 465 HIS A 57 REMARK 465 VAL A 58 REMARK 465 ASN A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 SER B 3 REMARK 465 LEU B 4 REMARK 465 LEU B 5 REMARK 465 GLN B 6 REMARK 465 SER B 7 REMARK 465 ALA E 120 REMARK 465 GLY E 121 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 SER E 125 REMARK 465 GLY E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 SER E 130 REMARK 465 GLY E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 ALA G 1 REMARK 465 SER G 2 REMARK 465 ASN G 3 REMARK 465 ASN G 4 REMARK 465 LYS G 63 REMARK 465 LYS G 64 REMARK 465 PHE G 65 REMARK 465 PHE G 66 REMARK 465 CYS G 67 REMARK 465 ALA G 68 REMARK 465 ILE G 69 REMARK 465 LEU G 70 REMARK 465 MET R 1 REMARK 465 GLY R 2 REMARK 465 SER R 3 REMARK 465 PRO R 4 REMARK 465 TRP R 5 REMARK 465 ASN R 6 REMARK 465 GLY R 7 REMARK 465 SER R 8 REMARK 465 ASP R 9 REMARK 465 GLY R 10 REMARK 465 PRO R 11 REMARK 465 GLU R 12 REMARK 465 GLY R 13 REMARK 465 ALA R 14 REMARK 465 ARG R 15 REMARK 465 GLU R 16 REMARK 465 PRO R 17 REMARK 465 PRO R 18 REMARK 465 TRP R 19 REMARK 465 PRO R 20 REMARK 465 ALA R 21 REMARK 465 LEU R 22 REMARK 465 PRO R 23 REMARK 465 PRO R 24 REMARK 465 CYS R 25 REMARK 465 ASP R 26 REMARK 465 GLU R 27 REMARK 465 ARG R 28 REMARK 465 ARG R 29 REMARK 465 CYS R 30 REMARK 465 GLY R 184 REMARK 465 ILE R 185 REMARK 465 SER R 186 REMARK 465 VAL R 187 REMARK 465 VAL R 188 REMARK 465 PRO R 189 REMARK 465 GLY R 190 REMARK 465 LEU R 191 REMARK 465 ASN R 192 REMARK 465 GLY R 193 REMARK 465 THR R 194 REMARK 465 ALA R 195 REMARK 465 ARG R 196 REMARK 465 ILE R 197 REMARK 465 ALA R 198 REMARK 465 SER R 199 REMARK 465 SER R 200 REMARK 465 PRO R 201 REMARK 465 LEU R 202 REMARK 465 ALA R 203 REMARK 465 SER R 204 REMARK 465 SER R 205 REMARK 465 PRO R 206 REMARK 465 PRO R 207 REMARK 465 LEU R 208 REMARK 465 TRP R 209 REMARK 465 LEU R 210 REMARK 465 SER R 211 REMARK 465 ARG R 212 REMARK 465 ALA R 213 REMARK 465 PRO R 214 REMARK 465 PRO R 215 REMARK 465 PRO R 216 REMARK 465 SER R 217 REMARK 465 PRO R 218 REMARK 465 PRO R 219 REMARK 465 SER R 220 REMARK 465 GLY R 221 REMARK 465 PRO R 222 REMARK 465 GLU R 223 REMARK 465 THR R 224 REMARK 465 ALA R 225 REMARK 465 SER R 277 REMARK 465 ARG R 278 REMARK 465 ARG R 279 REMARK 465 PRO R 280 REMARK 465 LEU R 281 REMARK 465 ARG R 282 REMARK 465 GLY R 283 REMARK 465 PRO R 284 REMARK 465 ALA R 285 REMARK 465 ALA R 286 REMARK 465 SER R 287 REMARK 465 GLY R 288 REMARK 465 ARG R 289 REMARK 465 GLU R 290 REMARK 465 ALA R 372 REMARK 465 ARG R 373 REMARK 465 LYS R 374 REMARK 465 SER R 375 REMARK 465 ARG R 376 REMARK 465 PRO R 377 REMARK 465 ARG R 378 REMARK 465 GLY R 379 REMARK 465 PHE R 380 REMARK 465 HIS R 381 REMARK 465 ARG R 382 REMARK 465 SER R 383 REMARK 465 ARG R 384 REMARK 465 ASP R 385 REMARK 465 THR R 386 REMARK 465 ALA R 387 REMARK 465 GLY R 388 REMARK 465 GLU R 389 REMARK 465 VAL R 390 REMARK 465 ALA R 391 REMARK 465 GLY R 392 REMARK 465 ASP R 393 REMARK 465 THR R 394 REMARK 465 GLY R 395 REMARK 465 GLY R 396 REMARK 465 ASP R 397 REMARK 465 THR R 398 REMARK 465 VAL R 399 REMARK 465 GLY R 400 REMARK 465 TYR R 401 REMARK 465 THR R 402 REMARK 465 GLU R 403 REMARK 465 THR R 404 REMARK 465 SER R 405 REMARK 465 ALA R 406 REMARK 465 ASN R 407 REMARK 465 VAL R 408 REMARK 465 LYS R 409 REMARK 465 THR R 410 REMARK 465 MET R 411 REMARK 465 GLY R 412 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 ASP B 295 CG OD1 OD2 REMARK 470 SER E 135 CB OG 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 VAL R 165 OG SER R 169 2.14 REMARK 500 OE2 GLU A 8 OH TYR E 175 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO R 313 N - CA - CB ANGL. DEV. = -8.2 DEGREES 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 SER B 72 33.51 -97.28 REMARK 500 THR B 169 33.57 70.08 REMARK 500 MET B 267 149.14 -171.99 REMARK 500 VAL E 47 -62.82 -97.06 REMARK 500 SER E 135 -148.98 77.72 REMARK 500 MET E 192 -14.19 62.65 REMARK 500 SER E 193 -15.14 -143.52 REMARK 500 PRO E 236 70.73 -66.47 REMARK 500 ARG R 102 43.65 -143.53 REMARK 500 TYR R 116 -48.22 -133.84 REMARK 500 SER R 232 -139.21 50.50 REMARK 500 ARG R 236 148.27 177.35 REMARK 500 SER R 238 150.79 -45.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG R 97 0.14 SIDE CHAIN REMARK 500 ARG R 236 0.11 SIDE CHAIN REMARK 500 ARG R 318 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61598 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE AZITHROMYCIN-MOTILIN RECEPTOR-GQ PROTEIN REMARK 900 COMPLEX DBREF 9JMD A 1 361 PDB 9JMD 9JMD 1 361 DBREF 9JMD B 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 9JMD E 1 247 PDB 9JMD 9JMD 1 247 DBREF 9JMD G 1 70 UNP P59768 GBG2_HUMAN 2 71 DBREF 9JMD R 1 412 UNP O43193 MTLR_HUMAN 1 412 SEQADV 9JMD MET B 1 UNP P62873 INITIATING METHIONINE SEQADV 9JMD GLY B 2 UNP P62873 EXPRESSION TAG SEQADV 9JMD SER B 3 UNP P62873 EXPRESSION TAG SEQADV 9JMD LEU B 4 UNP P62873 EXPRESSION TAG SEQADV 9JMD LEU B 5 UNP P62873 EXPRESSION TAG SEQADV 9JMD GLN B 6 UNP P62873 EXPRESSION TAG SEQRES 1 A 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 A 361 LYS GLN VAL TYR ARG ARG THR LEU ARG LEU LEU LEU LEU SEQRES 4 A 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 A 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 A 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 A 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 A 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 A 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 A 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 A 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 A 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 A 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 A 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 A 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS GLU PHE SEQRES 25 A 361 VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG HIS ILE SEQRES 26 A 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 A 361 ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE ILE LEU SEQRES 28 A 361 GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 345 MET GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 B 345 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 B 345 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 B 345 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 B 345 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 B 345 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 B 345 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 B 345 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 B 345 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 B 345 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 B 345 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 B 345 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 B 345 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 B 345 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 B 345 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 B 345 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 B 345 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 B 345 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 B 345 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 B 345 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 B 345 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 B 345 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 B 345 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 B 345 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 B 345 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 B 345 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 B 345 SER PHE LEU LYS ILE TRP ASN SEQRES 1 E 247 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 E 247 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 3 E 247 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 E 247 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 E 247 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY SEQRES 6 E 247 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU SEQRES 7 E 247 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA SEQRES 8 E 247 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SEQRES 9 E 247 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR SEQRES 10 E 247 VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 E 247 GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA SEQRES 12 E 247 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 E 247 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 E 247 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 E 247 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 E 247 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 E 247 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 E 247 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 E 247 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 1 G 70 ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG LYS SEQRES 2 G 70 LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP ARG SEQRES 3 G 70 ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA TYR SEQRES 4 G 70 CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR PRO SEQRES 5 G 70 VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS PHE SEQRES 6 G 70 PHE CYS ALA ILE LEU SEQRES 1 R 412 MET GLY SER PRO TRP ASN GLY SER ASP GLY PRO GLU GLY SEQRES 2 R 412 ALA ARG GLU PRO PRO TRP PRO ALA LEU PRO PRO CYS ASP SEQRES 3 R 412 GLU ARG ARG CYS SER PRO PHE PRO LEU GLY ALA LEU VAL SEQRES 4 R 412 PRO VAL THR ALA VAL CYS LEU CYS LEU PHE VAL VAL GLY SEQRES 5 R 412 VAL SER GLY ASN VAL VAL THR VAL MET LEU ILE GLY ARG SEQRES 6 R 412 TYR ARG ASP MET ARG THR THR THR ASN LEU TYR LEU GLY SEQRES 7 R 412 SER MET ALA VAL SER ASP LEU LEU ILE LEU LEU GLY LEU SEQRES 8 R 412 PRO PHE ASP LEU TYR ARG LEU TRP ARG SER ARG PRO TRP SEQRES 9 R 412 VAL PHE GLY PRO LEU LEU CYS ARG LEU SER LEU TYR VAL SEQRES 10 R 412 GLY GLU GLY CYS THR TYR ALA THR LEU LEU HIS MET THR SEQRES 11 R 412 ALA LEU SER VAL GLU ARG TYR LEU ALA ILE CYS ARG PRO SEQRES 12 R 412 LEU ARG ALA ARG VAL LEU VAL THR ARG ARG ARG VAL ARG SEQRES 13 R 412 ALA LEU ILE ALA VAL LEU TRP ALA VAL ALA LEU LEU SER SEQRES 14 R 412 ALA GLY PRO PHE LEU PHE LEU VAL GLY VAL GLU GLN ASP SEQRES 15 R 412 PRO GLY ILE SER VAL VAL PRO GLY LEU ASN GLY THR ALA SEQRES 16 R 412 ARG ILE ALA SER SER PRO LEU ALA SER SER PRO PRO LEU SEQRES 17 R 412 TRP LEU SER ARG ALA PRO PRO PRO SER PRO PRO SER GLY SEQRES 18 R 412 PRO GLU THR ALA GLU ALA ALA ALA LEU PHE SER ARG GLU SEQRES 19 R 412 CYS ARG PRO SER PRO ALA GLN LEU GLY ALA LEU ARG VAL SEQRES 20 R 412 MET LEU TRP VAL THR THR ALA TYR PHE PHE LEU PRO PHE SEQRES 21 R 412 LEU CYS LEU SER ILE LEU TYR GLY LEU ILE GLY ARG GLU SEQRES 22 R 412 LEU TRP SER SER ARG ARG PRO LEU ARG GLY PRO ALA ALA SEQRES 23 R 412 SER GLY ARG GLU ARG GLY HIS ARG GLN THR VAL ARG VAL SEQRES 24 R 412 LEU LEU VAL VAL VAL LEU ALA PHE ILE ILE CYS TRP LEU SEQRES 25 R 412 PRO PHE HIS VAL GLY ARG ILE ILE TYR ILE ASN THR GLU SEQRES 26 R 412 ASP SER ARG MET MET TYR PHE SER GLN TYR PHE ASN ILE SEQRES 27 R 412 VAL ALA LEU GLN LEU PHE TYR LEU SER ALA SER ILE ASN SEQRES 28 R 412 PRO ILE LEU TYR ASN LEU ILE SER LYS LYS TYR ARG ALA SEQRES 29 R 412 ALA ALA PHE LYS LEU LEU LEU ALA ARG LYS SER ARG PRO SEQRES 30 R 412 ARG GLY PHE HIS ARG SER ARG ASP THR ALA GLY GLU VAL SEQRES 31 R 412 ALA GLY ASP THR GLY GLY ASP THR VAL GLY TYR THR GLU SEQRES 32 R 412 THR SER ALA ASN VAL LYS THR MET GLY HET CLR R 501 74 HET CLR R 502 74 HET ZIT R 503 124 HETNAM CLR CHOLESTEROL HETNAM ZIT AZITHROMYCIN FORMUL 6 CLR 2(C27 H46 O) FORMUL 8 ZIT C38 H72 N2 O12 FORMUL 9 HOH *2(H2 O) HELIX 1 AA1 SER A 6 THR A 33 1 28 HELIX 2 AA2 GLY A 45 ILE A 55 1 11 HELIX 3 AA3 ILE A 212 ASN A 216 5 5 HELIX 4 AA4 ARG A 232 ASN A 245 1 14 HELIX 5 AA5 LYS A 260 ALA A 270 1 11 HELIX 6 AA6 LYS A 274 PHE A 279 1 6 HELIX 7 AA7 PRO A 280 ARG A 284 5 5 HELIX 8 AA8 ASP A 298 ALA A 318 1 21 HELIX 9 AA9 GLU A 337 TYR A 358 1 22 HELIX 10 AB1 LEU B 9 ALA B 31 1 23 HELIX 11 AB2 THR B 34 THR B 39 1 6 HELIX 12 AB3 SER E 52 GLY E 55 5 4 HELIX 13 AB4 ARG E 86 THR E 90 5 5 HELIX 14 AB5 ALA G 6 ASN G 23 1 18 HELIX 15 AB6 LYS G 28 HIS G 43 1 16 HELIX 16 AB7 PRO R 34 TYR R 66 1 33 HELIX 17 AB8 ARG R 67 ARG R 70 5 4 HELIX 18 AB9 THR R 71 LEU R 89 1 19 HELIX 19 AC1 GLY R 90 ARG R 100 1 11 HELIX 20 AC2 GLY R 107 ARG R 142 1 36 HELIX 21 AC3 THR R 151 LEU R 168 1 18 HELIX 22 AC4 ALA R 170 VAL R 177 1 8 HELIX 23 AC5 ALA R 227 PHE R 231 5 5 HELIX 24 AC6 GLN R 241 THR R 252 1 12 HELIX 25 AC7 THR R 253 SER R 276 1 24 HELIX 26 AC8 GLY R 292 ASN R 323 1 32 HELIX 27 AC9 ASP R 326 LEU R 357 1 32 HELIX 28 AD1 SER R 359 LEU R 371 1 13 SHEET 1 AA1 6 ILE A 184 VAL A 191 0 SHEET 2 AA1 6 VAL A 194 VAL A 201 -1 O PHE A 196 N PHE A 189 SHEET 3 AA1 6 LEU A 34 GLY A 40 1 N LEU A 36 O PHE A 199 SHEET 4 AA1 6 ALA A 220 ASP A 226 1 O VAL A 224 N LEU A 39 SHEET 5 AA1 6 SER A 253 ASN A 259 1 O PHE A 257 N PHE A 223 SHEET 6 AA1 6 HIS A 329 PHE A 330 1 O HIS A 329 N LEU A 256 SHEET 1 AA2 4 THR B 52 LEU B 56 0 SHEET 2 AA2 4 LEU B 341 TRP B 344 -1 O LEU B 341 N LEU B 56 SHEET 3 AA2 4 VAL B 332 SER B 336 -1 N THR B 334 O LYS B 342 SHEET 4 AA2 4 VAL B 320 VAL B 325 -1 N SER B 321 O GLY B 335 SHEET 1 AA3 4 ILE B 63 TRP B 68 0 SHEET 2 AA3 4 LEU B 74 SER B 79 -1 O ALA B 78 N TYR B 64 SHEET 3 AA3 4 LYS B 83 ASP B 88 -1 O ILE B 85 N SER B 77 SHEET 4 AA3 4 ASN B 93 PRO B 99 -1 O ILE B 98 N LEU B 84 SHEET 1 AA4 4 THR B 107 TYR B 110 0 SHEET 2 AA4 4 TYR B 116 GLY B 120 -1 O GLY B 120 N THR B 107 SHEET 3 AA4 4 CYS B 126 ASN B 130 -1 O TYR B 129 N VAL B 117 SHEET 4 AA4 4 ARG B 139 LEU B 144 -1 O LEU B 144 N CYS B 126 SHEET 1 AA5 4 LEU B 151 PHE B 156 0 SHEET 2 AA5 4 GLN B 161 SER B 166 -1 O SER B 165 N CYS B 153 SHEET 3 AA5 4 THR B 170 ASP B 175 -1 O TRP B 174 N ILE B 162 SHEET 4 AA5 4 GLN B 180 THR B 186 -1 O PHE B 185 N CYS B 171 SHEET 1 AA6 4 SER B 194 LEU B 197 0 SHEET 2 AA6 4 LEU B 203 ALA B 208 -1 O VAL B 205 N SER B 196 SHEET 3 AA6 4 SER B 212 ASP B 217 -1 O TRP B 216 N PHE B 204 SHEET 4 AA6 4 CYS B 223 PHE B 227 -1 O PHE B 227 N ALA B 213 SHEET 1 AA7 4 ILE B 234 PHE B 239 0 SHEET 2 AA7 4 ALA B 245 SER B 250 -1 O ALA B 247 N CYS B 238 SHEET 3 AA7 4 CYS B 255 ASP B 259 -1 O PHE B 258 N PHE B 246 SHEET 4 AA7 4 GLN B 264 TYR B 269 -1 O LEU B 266 N LEU B 257 SHEET 1 AA8 4 ILE B 278 PHE B 283 0 SHEET 2 AA8 4 LEU B 289 TYR B 294 -1 O GLY B 293 N THR B 279 SHEET 3 AA8 4 CYS B 299 ASP B 303 -1 O TRP B 302 N LEU B 290 SHEET 4 AA8 4 ARG B 309 LEU B 313 -1 O GLY B 311 N VAL B 301 SHEET 1 AA9 4 GLN E 2 SER E 6 0 SHEET 2 AA9 4 LYS E 18 SER E 24 -1 O SER E 20 N SER E 6 SHEET 3 AA9 4 THR E 77 GLN E 81 -1 O LEU E 78 N CYS E 21 SHEET 4 AA9 4 THR E 68 ASP E 72 -1 N SER E 70 O PHE E 79 SHEET 1 AB1 6 LEU E 10 VAL E 11 0 SHEET 2 AB1 6 THR E 114 VAL E 118 1 O THR E 117 N VAL E 11 SHEET 3 AB1 6 ALA E 91 SER E 98 -1 N TYR E 93 O THR E 114 SHEET 4 AB1 6 GLY E 32 GLN E 38 -1 N VAL E 36 O TYR E 94 SHEET 5 AB1 6 LEU E 44 ILE E 50 -1 O VAL E 47 N TRP E 35 SHEET 6 AB1 6 ILE E 57 TYR E 59 -1 O TYR E 58 N TYR E 49 SHEET 1 AB2 4 MET E 140 THR E 141 0 SHEET 2 AB2 4 VAL E 155 SER E 161 -1 O ARG E 160 N THR E 141 SHEET 3 AB2 4 ALA E 211 ILE E 216 -1 O ILE E 216 N VAL E 155 SHEET 4 AB2 4 PHE E 203 GLY E 207 -1 N SER E 206 O THR E 213 SHEET 1 AB3 4 PRO E 185 ILE E 189 0 SHEET 2 AB3 4 LEU E 174 GLN E 179 -1 N TRP E 176 O LEU E 188 SHEET 3 AB3 4 GLY E 225 GLN E 231 -1 O VAL E 226 N GLN E 179 SHEET 4 AB3 4 THR E 243 LEU E 245 -1 O THR E 243 N TYR E 227 SSBOND 1 CYS E 21 CYS E 95 1555 1555 2.03 SSBOND 2 CYS R 111 CYS R 235 1555 1555 2.02 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