BMRB Entry 51317

Name: C-terminal domain of the Growth Hormone Secretagogue Receptor type 1a
Published: 2022-06-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51317

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: C-terminal domain of the Growth Hormone Secretagogue Receptor type 1a PubMed: 35625550

Deposition date: 2022-02-09 Original release date: 2022-06-08

Authors: Guillien, Myriam; Sibille, Nathalie

Citation: Guillien, Myriam; Mouhand, Assia; Fournet, Aurelie; Gontier, Amandine; Marti Navia, Aleix; Cordeiro, Tiago; Allemand, Frederic; Thureau, Aurelien; Baneres, Jean-Louis; Bernado, Pau; Sibille, Nathalie. "Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction" Biomolecules 12, 617-617 (2022).

Assembly members:
entity_1, polymer, 32 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity_1: GPMAGFEPFSQRKLSTLKDE SSRAWTESSINT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	83
15N chemical shifts	29
1H chemical shifts	29

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GHSR-Cter GPCR	1

Entities:

Entity 1, GHSR-Cter GPCR 32 residues - Formula weight is not available

1

GLY

PRO

MET

ALA

GLY

PHE

GLU

PRO

PHE

SER

2

GLN

ARG

LYS

LEU

SER

THR

LEU

LYS

ASP

GLU

3

SER

ARG

ALA

TRP

THR

GLU

SER

ILE

4

ASN

THR

Samples:

sample_1: wt-GHSR-Cter, [U-13C; U-15N], 312 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:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 700 MHz

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