HEADER MEMBRANE PROTEIN 05-NOV-24 9HB3 TITLE CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE-VASOPRESSIN (AVP) V2 TITLE 2 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A (MQK39A) COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAMBAQUARETIN-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MQ-1,MQ1,UPSILON-DA2A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SYNTHETIC ANTIBODY, ANTI-BRIL FAB FRAGMENT, HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ANTI-BRIL FAB NANOBODY; COMPND 12 CHAIN: K; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: SYNTHETIC ANTIBODY, ANTI-BRIL FAB FRAGMENT, LIGHT CHAIN; COMPND 16 CHAIN: L; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: ARGININE-VASOPRESSIN (AVP) V2 RECEPTOR (V2R)-BRIL, COMPND 20 VASOPRESSIN V2 RECEPTOR,VASOPRESSIN V2 RECEPTOR; COMPND 21 CHAIN: R; COMPND 22 SYNONYM: V2R,AVPR V2,ANTIDIURETIC HORMONE RECEPTOR,RENAL-TYPE COMPND 23 ARGININE VASOPRESSIN RECEPTOR; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS; SOURCE 4 ORGANISM_COMMON: EASTERN GREEN MAMBA; SOURCE 5 ORGANISM_TAXID: 8618; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 561; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: AVPR2, ADHR, DIR, DIR3, V2R; SOURCE 26 EXPRESSION_SYSTEM: SPODOPTERA; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 7106 KEYWDS GPCR, V2R, TVP, TOLVAPTAN, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.BOUS,A.FOUILLEN,P.COUVINEAU,H.ORCEL,C.MARY,C.MENDRE,G.SCHULTE, AUTHOR 2 S.GRANIER,N.GILLES,B.MOUILLAC REVDAT 1 04-JUN-25 9HB3 0 JRNL AUTH A.FOUILLEN,J.BOUS,P.COUVINEAU,H.ORCEL,C.MARY,L.LAFLEUR, JRNL AUTH 2 T.PIERRE,C.MENDRE,N.GILLES,G.SCHULTE,S.GRANIER,B.MOUILLAC JRNL TITL INACTIVE STRUCTURES OF THE VASOPRESSIN V2 RECEPTOR REVEAL JRNL TITL 2 DISTINCT BINDING MODES FOR TOLVAPTAN AND MAMBAQUARETIN JRNL TITL 3 TOXIN. JRNL REF NAT COMMUN V. 16 3899 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40274867 JRNL DOI 10.1038/S41467-025-59114-5 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : TOPAZ, EPU, CRYOSPARC, COOT, ROSETTA, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, RELION, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 2.500 REMARK 3 NUMBER OF PARTICLES : 202513 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 9HB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1292142940. 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 : INACTIVE V2R-BRIL BOUND TO REMARK 245 TOLVAPTAN STABILLIZED WITH ANTI- REMARK 245 BRIL FAB AND ANTI-BRIL FAB REMARK 245 NANOBODY REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 22.00 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 8000.00 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, K, L, 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 ARG A 1 REMARK 465 PRO A 2 REMARK 465 SER A 3 REMARK 465 SER A 24 REMARK 465 GLN A 25 REMARK 465 LYS A 26 REMARK 465 THR A 27 REMARK 465 ASN A 28 REMARK 465 LYS A 29 REMARK 465 GLY A 57 REMARK 465 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 SER H 229 REMARK 465 CYS H 230 REMARK 465 ASP H 231 REMARK 465 ALA K -5 REMARK 465 GLN K -4 REMARK 465 PRO K -3 REMARK 465 ALA K -2 REMARK 465 MET K -1 REMARK 465 ALA K 0 REMARK 465 SER K 121 REMARK 465 LEU K 122 REMARK 465 GLU K 123 REMARK 465 ASP K 124 REMARK 465 TYR K 125 REMARK 465 LYS K 126 REMARK 465 ASP K 127 REMARK 465 ASP K 128 REMARK 465 LYS K 129 REMARK 465 HIS K 130 REMARK 465 HIS K 131 REMARK 465 HIS K 132 REMARK 465 HIS K 133 REMARK 465 HIS K 134 REMARK 465 HIS K 135 REMARK 465 GLY L 214 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 MET R -63 REMARK 465 LYS R -62 REMARK 465 THR R -61 REMARK 465 ILE R -60 REMARK 465 ILE R -59 REMARK 465 ALA R -58 REMARK 465 LEU R -57 REMARK 465 SER R -56 REMARK 465 TYR R -55 REMARK 465 ILE R -54 REMARK 465 PHE R -53 REMARK 465 CYS R -52 REMARK 465 LEU R -51 REMARK 465 VAL R -50 REMARK 465 PHE R -49 REMARK 465 ALA R -48 REMARK 465 ASP R -47 REMARK 465 TYR R -46 REMARK 465 LYS R -45 REMARK 465 ASP R -44 REMARK 465 ASP R -43 REMARK 465 ASP R -42 REMARK 465 ASP R -41 REMARK 465 ALA R -40 REMARK 465 TRP R -39 REMARK 465 SER R -38 REMARK 465 HIS R -37 REMARK 465 PRO R -36 REMARK 465 GLN R -35 REMARK 465 PHE R -34 REMARK 465 GLU R -33 REMARK 465 LYS R -32 REMARK 465 GLY R -31 REMARK 465 GLY R -30 REMARK 465 GLY R -29 REMARK 465 SER R -28 REMARK 465 GLY R -27 REMARK 465 GLY R -26 REMARK 465 GLY R -25 REMARK 465 SER R -24 REMARK 465 GLY R -23 REMARK 465 GLY R -22 REMARK 465 GLY R -21 REMARK 465 SER R -20 REMARK 465 TRP R -19 REMARK 465 SER R -18 REMARK 465 HIS R -17 REMARK 465 PRO R -16 REMARK 465 GLN R -15 REMARK 465 PHE R -14 REMARK 465 GLU R -13 REMARK 465 LYS R -12 REMARK 465 LEU R -11 REMARK 465 GLU R -10 REMARK 465 VAL R -9 REMARK 465 LEU R -8 REMARK 465 GLN R -7 REMARK 465 GLY R -6 REMARK 465 PRO R -5 REMARK 465 ASP R -4 REMARK 465 TYR R -3 REMARK 465 LYS R -2 REMARK 465 ASP R -1 REMARK 465 ASP R 0 REMARK 465 ASP R 1 REMARK 465 ASP R 2 REMARK 465 ALA R 3 REMARK 465 ALA R 4 REMARK 465 SER R 5 REMARK 465 THR R 6 REMARK 465 THR R 7 REMARK 465 SER R 8 REMARK 465 ALA R 9 REMARK 465 VAL R 10 REMARK 465 PRO R 11 REMARK 465 GLY R 12 REMARK 465 HIS R 13 REMARK 465 PRO R 14 REMARK 465 SER R 15 REMARK 465 LEU R 16 REMARK 465 PRO R 17 REMARK 465 SER R 18 REMARK 465 LEU R 19 REMARK 465 PRO R 20 REMARK 465 SER R 21 REMARK 465 GLN R 22 REMARK 465 SER R 23 REMARK 465 SER R 24 REMARK 465 GLN R 25 REMARK 465 GLU R 26 REMARK 465 ARG R 27 REMARK 465 PRO R 28 REMARK 465 LEU R 29 REMARK 465 ASP R 30 REMARK 465 THR R 31 REMARK 465 ARG R 32 REMARK 465 ASP R 33 REMARK 465 PRO R 34 REMARK 465 PRO R 108 REMARK 465 MET R 145 REMARK 465 LEU R 146 REMARK 465 ALA R 147 REMARK 465 TYR R 148 REMARK 465 ARG R 149 REMARK 465 HIS R 150 REMARK 465 GLY R 151 REMARK 465 SER R 152 REMARK 465 GLY R 153 REMARK 465 ALA R 154 REMARK 465 HIS R 155 REMARK 465 TRP R 156 REMARK 465 ARG R 181 REMARK 465 ASN R 182 REMARK 465 VAL R 183 REMARK 465 GLU R 184 REMARK 465 GLY R 185 REMARK 465 GLY R 186 REMARK 465 SER R 187 REMARK 465 GLY R 188 REMARK 465 VAL R 189 REMARK 465 ALA R 197 REMARK 465 GLU R 198 REMARK 465 PRO R 199 REMARK 465 SER R 235 REMARK 465 LEU R 236 REMARK 465 VAL R 237 REMARK 465 PRO R 238 REMARK 465 GLY R 239 REMARK 465 PRO R 240 REMARK 465 SER R 241 REMARK 465 GLU R 242 REMARK 465 ARG R 243 REMARK 465 PRO R 244 REMARK 465 GLY R 245 REMARK 465 GLY R 246 REMARK 465 ARG R 247 REMARK 465 ARG R 248 REMARK 465 ARG R 249 REMARK 465 GLY R 250 REMARK 465 ARG R 251 REMARK 465 ARG R 252 REMARK 465 THR R 253 REMARK 465 GLY R 254 REMARK 465 SER R 255 REMARK 465 PRO R 256 REMARK 465 GLY R 257 REMARK 465 GLU R 258 REMARK 465 GLY R 259 REMARK 465 ALA R 260 REMARK 465 HIS R 261 REMARK 465 VAL R 262 REMARK 465 SER R 263 REMARK 465 GLU R 299 REMARK 465 ALA R 300 REMARK 465 PRO R 301 REMARK 465 LEU R 302 REMARK 465 GLU R 303 REMARK 465 GLY R 304 REMARK 465 ALA R 305 REMARK 465 SER R 466 REMARK 465 LEU R 467 REMARK 465 LEU R 468 REMARK 465 CYS R 469 REMARK 465 CYS R 470 REMARK 465 ALA R 471 REMARK 465 ARG R 472 REMARK 465 GLY R 473 REMARK 465 ARG R 474 REMARK 465 THR R 475 REMARK 465 PRO R 476 REMARK 465 PRO R 477 REMARK 465 SER R 478 REMARK 465 LEU R 479 REMARK 465 GLY R 480 REMARK 465 PRO R 481 REMARK 465 GLN R 482 REMARK 465 ASP R 483 REMARK 465 GLU R 484 REMARK 465 SER R 485 REMARK 465 CYS R 486 REMARK 465 THR R 487 REMARK 465 THR R 488 REMARK 465 ALA R 489 REMARK 465 SER R 490 REMARK 465 SER R 491 REMARK 465 SER R 492 REMARK 465 LEU R 493 REMARK 465 ALA R 494 REMARK 465 LYS R 495 REMARK 465 ASP R 496 REMARK 465 THR R 497 REMARK 465 SER R 498 REMARK 465 SER R 499 REMARK 465 PRO R 550 REMARK 465 LYS R 551 REMARK 465 LEU R 552 REMARK 465 GLU R 553 REMARK 465 ASP R 554 REMARK 465 LYS R 555 REMARK 465 SER R 556 REMARK 465 PRO R 557 REMARK 465 ASP R 558 REMARK 465 SER R 559 REMARK 465 PRO R 560 REMARK 465 GLU R 561 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 TYR A 22 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS A 30 SG REMARK 470 SER A 32 OG REMARK 470 ASN A 43 CG OD1 ND2 REMARK 470 GLU A 49 CG CD OE1 OE2 REMARK 470 LYS A 50 CG CD CE NZ REMARK 470 CYS A 51 SG REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2 REMARK 470 THR A 54 OG1 CG2 REMARK 470 CYS A 55 SG REMARK 470 VAL A 56 CG1 CG2 REMARK 470 ARG R 38 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 64 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 65 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 67 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 68 CG CD NE CZ NH1 NH2 REMARK 470 HIS R 70 CG ND1 CD2 CE1 NE2 REMARK 470 PHE R 77 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU R 90 CG CD1 CD2 REMARK 470 VAL R 93 CG1 CG2 REMARK 470 LYS R 100 CG CD CE NZ REMARK 470 PHE R 105 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG R 106 CG CD NE CZ NH1 NH2 REMARK 470 ASP R 109 CG OD1 OD2 REMARK 470 LEU R 111 CG CD1 CD2 REMARK 470 ARG R 113 CG CD NE CZ NH1 NH2 REMARK 470 VAL R 115 CG1 CG2 REMARK 470 MET R 129 CG SD CE REMARK 470 MET R 133 CG SD CE REMARK 470 LEU R 135 CG CD1 CD2 REMARK 470 ILE R 141 CG1 CG2 CD1 REMARK 470 ARG R 143 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 158 CG CD NE CZ NH1 NH2 REMARK 470 LEU R 168 CG CD1 CD2 REMARK 470 LEU R 169 CG CD1 CD2 REMARK 470 LEU R 172 CG CD1 CD2 REMARK 470 LEU R 175 CG CD1 CD2 REMARK 470 PHE R 176 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN R 180 CG CD OE1 NE2 REMARK 470 CYS R 195 SG REMARK 470 PHE R 196 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG R 203 CG CD NE CZ NH1 NH2 REMARK 470 HIS R 233 CG ND1 CD2 CE1 NE2 REMARK 470 LYS R 268 CG CD CE NZ REMARK 470 CYS R 283 SG REMARK 470 LEU R 310 CG CD1 CD2 REMARK 470 LEU R 312 CG CD1 CD2 REMARK 470 ASN R 321 CG OD1 ND2 REMARK 470 GLU R 335 CG CD OE1 OE2 REMARK 470 LEU R 336 CG CD1 CD2 REMARK 470 ARG R 337 CG CD NE CZ NH1 NH2 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 LYS A 10 103.96 -169.98 REMARK 500 VAL H 51 -60.21 -108.90 REMARK 500 ASP H 158 66.96 60.96 REMARK 500 PRO H 161 -157.08 -74.20 REMARK 500 SER H 200 -160.04 -78.14 REMARK 500 SER H 201 66.50 66.40 REMARK 500 SER K 54 117.36 -161.69 REMARK 500 SER L 51 18.12 57.79 REMARK 500 ALA L 52 -0.70 60.86 REMARK 500 SER L 53 -12.71 -142.65 REMARK 500 ASN L 140 60.12 64.13 REMARK 500 THR R 102 -131.39 53.95 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-52011 RELATED DB: EMDB REMARK 900 CONSENSUS REFINEMENT (CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE- REMARK 900 VASOPRESSIN (AVP) V2 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A REMARK 900 (MQK39A)) REMARK 900 RELATED ID: EMD-52008 RELATED DB: EMDB REMARK 900 V2R-MQ39A (CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE-VASOPRESSIN REMARK 900 (AVP) V2 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A (MQK39A)) REMARK 900 RELATED ID: EMD-52009 RELATED DB: EMDB REMARK 900 MQ39A (CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE-VASOPRESSIN REMARK 900 (AVP) V2 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A (MQK39A)) REMARK 900 RELATED ID: EMD-52010 RELATED DB: EMDB REMARK 900 FAB-NB (CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE-VASOPRESSIN REMARK 900 (AVP) V2 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A (MQK39A)) REMARK 900 RELATED ID: EMD-52012 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF INACTIVE HUMAN ARGININE-VASOPRESSIN (AVP) V2 REMARK 900 RECEPTOR (V2R) WITH MAMBAQUARETIN1 K39A (MQK39A) DBREF1 9HB3 A 1 57 UNP MAMB1_DENAN DBREF2 9HB3 A A0A1Z0YU59 1 57 DBREF 9HB3 H 1 231 PDB 9HB3 9HB3 1 231 DBREF 9HB3 K -5 135 PDB 9HB3 9HB3 -5 135 DBREF 9HB3 L 2 216 PDB 9HB3 9HB3 2 216 DBREF 9HB3 R -63 3 PDB 9HB3 9HB3 -63 3 DBREF 9HB3 R 4 470 UNP P30518 V2R_HUMAN 4 342 DBREF 9HB3 R 471 616 PDB 9HB3 9HB3 471 616 SEQADV 9HB3 ALA A 39 UNP A0A1Z0YU5 LYS 39 VARIANT SEQADV 9HB3 GLN R 22 UNP P30518 ASN 22 CONFLICT SEQRES 1 A 57 ARG PRO SER PHE CYS ASN LEU PRO VAL LYS PRO GLY PRO SEQRES 2 A 57 CYS ASN GLY PHE PHE SER ALA PHE TYR TYR SER GLN LYS SEQRES 3 A 57 THR ASN LYS CYS HIS SER PHE THR TYR GLY GLY CYS ALA SEQRES 4 A 57 GLY ASN ALA ASN ARG PHE SER THR ILE GLU LYS CYS ARG SEQRES 5 A 57 ARG THR CYS VAL GLY SEQRES 1 H 231 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 231 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 231 ALA SER GLY PHE ASN VAL VAL ASP PHE SER LEU HIS TRP SEQRES 4 H 231 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 231 TYR ILE SER SER SER SER GLY SER THR SER TYR ALA ASP SEQRES 6 H 231 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 231 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 231 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TRP GLY TYR SEQRES 9 H 231 TRP PRO GLY GLU PRO TRP TRP LYS ALA PHE ASP TYR TRP SEQRES 10 H 231 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 H 231 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 231 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 231 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 231 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 231 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 231 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 231 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 231 ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 1 K 141 ALA GLN PRO ALA MET ALA GLN VAL GLN LEU GLN GLU SER SEQRES 2 K 141 GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SEQRES 3 K 141 SER CYS ALA ALA SER GLY ARG THR ILE SER ARG TYR ALA SEQRES 4 K 141 MET SER TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 K 141 PHE VAL ALA VAL ALA ARG ARG SER GLY ASP GLY ALA PHE SEQRES 6 K 141 TYR ALA ASP SER VAL GLN GLY ARG PHE THR VAL SER ARG SEQRES 7 K 141 ASP ASP ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 K 141 LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ILE SEQRES 9 K 141 ASP SER ASP THR PHE TYR SER GLY SER TYR ASP TYR TRP SEQRES 10 K 141 GLY GLN GLY THR GLN VAL THR VAL SER SER LEU GLU ASP SEQRES 11 K 141 TYR LYS ASP ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 215 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 215 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 215 LEU TYR TYR SER LEU VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 R 552 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 552 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA TRP SER SEQRES 3 R 552 HIS PRO GLN PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SEQRES 4 R 552 SER GLY GLY GLY SER TRP SER HIS PRO GLN PHE GLU LYS SEQRES 5 R 552 LEU GLU VAL LEU GLN GLY PRO ASP TYR LYS ASP ASP ASP SEQRES 6 R 552 ASP ALA ALA SER THR THR SER ALA VAL PRO GLY HIS PRO SEQRES 7 R 552 SER LEU PRO SER LEU PRO SER GLN SER SER GLN GLU ARG SEQRES 8 R 552 PRO LEU ASP THR ARG ASP PRO LEU LEU ALA ARG ALA GLU SEQRES 9 R 552 LEU ALA LEU LEU SER ILE VAL PHE VAL ALA VAL ALA LEU SEQRES 10 R 552 SER ASN GLY LEU VAL LEU ALA ALA LEU ALA ARG ARG GLY SEQRES 11 R 552 ARG ARG GLY HIS TRP ALA PRO ILE HIS VAL PHE ILE GLY SEQRES 12 R 552 HIS LEU CYS LEU ALA ASP LEU ALA VAL ALA LEU PHE GLN SEQRES 13 R 552 VAL LEU PRO GLN LEU ALA TRP LYS ALA THR ASP ARG PHE SEQRES 14 R 552 ARG GLY PRO ASP ALA LEU CYS ARG ALA VAL LYS TYR LEU SEQRES 15 R 552 GLN MET VAL GLY MET TYR ALA SER SER TYR MET ILE LEU SEQRES 16 R 552 ALA MET THR LEU ASP ARG HIS ARG ALA ILE CYS ARG PRO SEQRES 17 R 552 MET LEU ALA TYR ARG HIS GLY SER GLY ALA HIS TRP ASN SEQRES 18 R 552 ARG PRO VAL LEU VAL ALA TRP ALA PHE SER LEU LEU LEU SEQRES 19 R 552 SER LEU PRO GLN LEU PHE ILE PHE ALA GLN ARG ASN VAL SEQRES 20 R 552 GLU GLY GLY SER GLY VAL THR ASP CYS TRP ALA CYS PHE SEQRES 21 R 552 ALA GLU PRO TRP GLY ARG ARG THR TYR VAL THR TRP ILE SEQRES 22 R 552 ALA LEU MET VAL PHE VAL ALA PRO THR LEU GLY ILE ALA SEQRES 23 R 552 ALA CYS GLN VAL LEU ILE PHE ARG GLU ILE HIS ALA SER SEQRES 24 R 552 LEU VAL PRO GLY PRO SER GLU ARG PRO GLY GLY ARG ARG SEQRES 25 R 552 ARG GLY ARG ARG THR GLY SER PRO GLY GLU GLY ALA HIS SEQRES 26 R 552 VAL SER ALA ALA VAL ALA LYS THR VAL ARG MET THR LEU SEQRES 27 R 552 VAL ILE VAL VAL VAL TYR VAL LEU CYS TRP ALA PRO PHE SEQRES 28 R 552 PHE LEU VAL GLN LEU TRP ALA ALA TRP ASP PRO GLU ALA SEQRES 29 R 552 PRO LEU GLU GLY ALA PRO PHE VAL LEU LEU MET LEU LEU SEQRES 30 R 552 ALA SER LEU ASN SER CYS THR ASN PRO TRP ILE TYR ALA SEQRES 31 R 552 SER PHE SER SER SER VAL SER SER GLU LEU ARG SER LEU SEQRES 32 R 552 LEU CYS CYS ALA ARG GLY ARG THR PRO PRO SER LEU GLY SEQRES 33 R 552 PRO GLN ASP GLU SER CYS THR THR ALA SER SER SER LEU SEQRES 34 R 552 ALA LYS ASP THR SER SER ALA ARG ARG GLN LEU ALA ASP SEQRES 35 R 552 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 36 R 552 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 37 R 552 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 38 R 552 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 39 R 552 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 40 R 552 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 41 R 552 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 42 R 552 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 43 R 552 ARG ALA ARG SER THR LEU HELIX 1 AA1 THR A 47 VAL A 56 1 10 HELIX 2 AA2 ARG H 90 THR H 94 5 5 HELIX 3 AA3 GLY H 107 LYS H 112 1 6 HELIX 4 AA4 SER H 170 ALA H 172 5 3 HELIX 5 AA5 SER H 200 THR H 205 1 6 HELIX 6 AA6 PRO H 216 ASN H 218 5 3 HELIX 7 AA7 ASP K 74 LYS K 76 5 3 HELIX 8 AA8 LYS K 87 THR K 91 5 5 HELIX 9 AA9 GLN L 80 PHE L 84 5 5 HELIX 10 AB1 TYR L 94 VAL L 98 5 5 HELIX 11 AB2 SER L 123 SER L 129 1 7 HELIX 12 AB3 LYS L 185 HIS L 191 1 7 HELIX 13 AB4 LEU R 36 GLY R 66 1 31 HELIX 14 AB5 ARG R 67 GLY R 69 5 3 HELIX 15 AB6 ALA R 72 ALA R 101 1 30 HELIX 16 AB7 ALA R 110 ILE R 141 1 32 HELIX 17 AB8 ARG R 158 LEU R 170 1 13 HELIX 18 AB9 PRO R 173 PHE R 178 1 6 HELIX 19 AC1 GLY R 201 PHE R 214 1 14 HELIX 20 AC2 PHE R 214 ALA R 234 1 21 HELIX 21 AC3 ALA R 265 ASP R 297 1 33 HELIX 22 AC4 PHE R 307 LEU R 316 1 10 HELIX 23 AC5 LEU R 316 SER R 329 1 14 HELIX 24 AC6 SER R 329 LEU R 336 1 8 HELIX 25 AC7 ARG R 501 ALA R 524 1 24 HELIX 26 AC8 ASN R 526 ALA R 547 1 22 HELIX 27 AC9 LYS R 563 GLU R 585 1 23 HELIX 28 AD1 LYS R 587 ARG R 611 1 25 HELIX 29 AD2 ALA R 612 THR R 615 5 4 SHEET 1 AA1 2 PHE A 18 TYR A 22 0 SHEET 2 AA1 2 HIS A 31 TYR A 35 -1 O HIS A 31 N TYR A 22 SHEET 1 AA2 4 GLN H 6 SER H 10 0 SHEET 2 AA2 4 GLY H 19 SER H 28 -1 O ALA H 26 N VAL H 8 SHEET 3 AA2 4 THR H 81 ASN H 87 -1 O MET H 86 N LEU H 21 SHEET 4 AA2 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA3 6 GLY H 13 VAL H 15 0 SHEET 2 AA3 6 GLY H 120 VAL H 125 1 O THR H 124 N GLY H 13 SHEET 3 AA3 6 ALA H 95 TRP H 102 -1 N TYR H 97 O THR H 121 SHEET 4 AA3 6 SER H 36 GLN H 42 -1 N GLN H 42 O VAL H 96 SHEET 5 AA3 6 LEU H 48 ILE H 54 -1 O GLU H 49 N ARG H 41 SHEET 6 AA3 6 THR H 61 TYR H 63 -1 O SER H 62 N TYR H 53 SHEET 1 AA4 4 SER H 134 PHE H 136 0 SHEET 2 AA4 4 LEU H 155 TYR H 159 -1 O LYS H 157 N SER H 134 SHEET 3 AA4 4 TYR H 190 VAL H 195 -1 O LEU H 192 N VAL H 156 SHEET 4 AA4 4 HIS H 178 THR H 179 -1 N HIS H 178 O VAL H 195 SHEET 1 AA5 4 SER H 134 PHE H 136 0 SHEET 2 AA5 4 LEU H 155 TYR H 159 -1 O LYS H 157 N SER H 134 SHEET 3 AA5 4 TYR H 190 VAL H 195 -1 O LEU H 192 N VAL H 156 SHEET 4 AA5 4 VAL H 183 LEU H 184 -1 N VAL H 183 O SER H 191 SHEET 1 AA6 2 THR H 149 ALA H 151 0 SHEET 2 AA6 2 THR H 197 PRO H 199 -1 O VAL H 198 N ALA H 150 SHEET 1 AA7 3 VAL H 164 TRP H 168 0 SHEET 2 AA7 3 TYR H 208 HIS H 214 -1 O ASN H 211 N SER H 167 SHEET 3 AA7 3 THR H 219 VAL H 225 -1 O LYS H 223 N CYS H 210 SHEET 1 AA8 4 GLN K 3 SER K 7 0 SHEET 2 AA8 4 LEU K 18 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AA8 4 THR K 78 MET K 83 -1 O LEU K 81 N LEU K 20 SHEET 4 AA8 4 PHE K 68 ASP K 73 -1 N THR K 69 O GLN K 82 SHEET 1 AA9 6 LEU K 11 VAL K 12 0 SHEET 2 AA9 6 THR K 115 VAL K 119 1 O THR K 118 N VAL K 12 SHEET 3 AA9 6 ALA K 92 ASP K 99 -1 N TYR K 94 O THR K 115 SHEET 4 AA9 6 ALA K 33 GLN K 39 -1 N ALA K 33 O ASP K 99 SHEET 5 AA9 6 GLU K 46 ALA K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AA9 6 ALA K 58 TYR K 60 -1 O PHE K 59 N VAL K 50 SHEET 1 AB1 4 MET L 5 THR L 6 0 SHEET 2 AB1 4 VAL L 20 ALA L 26 -1 O ARG L 25 N THR L 6 SHEET 3 AB1 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AB1 4 PHE L 63 SER L 68 -1 N SER L 68 O ASP L 71 SHEET 1 AB2 6 SER L 11 ALA L 14 0 SHEET 2 AB2 6 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 12 SHEET 3 AB2 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 104 SHEET 4 AB2 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AB2 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AB2 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AB3 4 SER L 11 ALA L 14 0 SHEET 2 AB3 4 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 12 SHEET 3 AB3 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 104 SHEET 4 AB3 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 91 SHEET 1 AB4 4 SER L 116 PHE L 120 0 SHEET 2 AB4 4 THR L 131 PHE L 141 -1 O ASN L 139 N SER L 116 SHEET 3 AB4 4 TYR L 175 SER L 184 -1 O TYR L 175 N PHE L 141 SHEET 4 AB4 4 SER L 161 VAL L 165 -1 N GLN L 162 O THR L 180 SHEET 1 AB5 4 ALA L 155 LEU L 156 0 SHEET 2 AB5 4 LYS L 147 VAL L 152 -1 N VAL L 152 O ALA L 155 SHEET 3 AB5 4 VAL L 193 THR L 199 -1 O ALA L 195 N LYS L 151 SHEET 4 AB5 4 VAL L 207 ASN L 212 -1 O VAL L 207 N VAL L 198 SSBOND 1 CYS A 14 CYS A 38 1555 1555 2.03 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 3 CYS H 154 CYS H 210 1555 1555 2.03 SSBOND 4 CYS K 22 CYS K 96 1555 1555 2.04 SSBOND 5 CYS L 24 CYS L 89 1555 1555 2.03 SSBOND 6 CYS L 136 CYS L 196 1555 1555 2.03 SSBOND 7 CYS R 112 CYS R 192 1555 1555 2.03 CISPEP 1 TRP H 105 PRO H 106 0 -4.42 CISPEP 2 PHE H 160 PRO H 161 0 -3.57 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