BMRB Entry 51330

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51330

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
phosphomimetic variant of the C-terminal domain of the vasopressin V2 receptor
Deposition date:
2022-02-15
Original release date:
2024-08-09
Authors:
Guillien, Myriam; Sibille, Nathalie
Citation:

Citation: Guillien, Myriam; Mouhand, Assia; Sagar, Amin; Fournet, Aurelie; Allemand, Frederic; Pereira, Glaecia; Thureau, Aurelien; Bernado, Pau; Baneres, Jean-Louis; Sibille, Nathalie. "Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction"  Structure 31, 1394-1406 (2023).
PubMed: 37669668

Assembly members:

Assembly members:
entity_1, polymer, 33 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM33

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMAARGREPPELGPQDEEC EEAEEELAKDTSS

Data sets:
Data typeCount
13C chemical shifts91
15N chemical shifts28
1H chemical shifts28

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1pm-V2R-Cter GPCR1

Entities:

Entity 1, pm-V2R-Cter GPCR 33 residues - Formula weight is not available

1   GLYPROMETALAALAARGGLYARGGLUPRO
2   PROGLULEUGLYPROGLNASPGLUGLUCYS
3   GLUGLUALAGLUGLUGLULEUALALYSASP
4   THRSERSER

Samples:

sample_1: pm-V2R-Cter, [U-13C; U-15N], 50 uM; Bis-Tris 50 mM; NaCl 150 mM; EDTA 1 mM; TCEP 0.5 mM; DSS-d6, [U-2H], 5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks