BMRB Entry 34303

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34303
MolProbity Validation Chart

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Title:
Receptor-bound Ghrelin conformation
Deposition date:
2018-07-18
Original release date:
2019-07-15
Authors:
Ferre, G.; Damian, M.; M'Kadmi, C.; Saurel, O.; Czaplicki, G.; Demange, P.; Marie, J.; Fehrentz, J.; Baneres, J.; Milon, A.
Citation:

Citation: Ferre, Guillaume; Louet, Maxime; Saurel, Oliver; Delort, Bartholome; Czaplicki, Georges; M'Kadmi, Celine; Damian, Marjorie; Renault, Pedro; Cantel, Sonia; Gavara, Laurent; Demange, Pascal; Marie, Jacky; Fehrentz, Jean-Alain; Floquet, Nicolas; Milon, Alain; Baneres, Jean-Louis. "Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain"  Proc. Natl. Acad. Sci. U.S.A. 116, 17525-17530 (2019).
PubMed: 31416915

Assembly members:

Assembly members:
entity_1, polymer, 19 residues, 2130.301 Da.
entity_FKZ, non-polymer, 129.243 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDFLSPEHQRVQQRKESX

Data sets:
Data typeCount
15N chemical shifts9
1H chemical shifts141

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 19 residues - 2130.301 Da.

1   GLYSERASPPHELEUSERPROGLUHISGLN
2   ARGVALGLNGLNARGLYSGLUSERNH2

Entity 2, entity_2 - C8 H19 N - 129.243 Da.

1   FKZ

Samples:

sample_1: Ghrelin 1-18, [U-15N]-Phe-Leu-Val, 1.37 ± 0.1 mM; Ghrelin receptor, [U-2H], 2.05 ± 0.5 uM; KCl 100 mM

sample_2: Ghrelin 1-18, [U-15N]-Phe-Leu-Val, 1.37 ± 0.1 mM; Ghrelin receptor, [U-2H], 2.05 ± 0.5 uM; JMV5327 2.05 ± 0.5 uM; KCl 100 mM

sample_3: Ghrelin 1-18, [U-15N]-Phe-Leu-Val-Ser-Gln-Glu, 1.15 ± 0.1 mM; Ghrelin receptor, [U-2H], 1.72 ± 0.5 uM; KCl 100 mM

sample_4: Ghrelin 1-18, [U-15N]-Phe-Leu-Val-Ser-Gln-Glu, 1.15 ± 0.1 mM; Ghrelin receptor, [U-2H], 1.72 ± 0.5 uM; JMV5327 1.72 ± 0.5 uM; KCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-1H-15N NOESY-HMQCsample_3isotropicsample_conditions_1
3D 1H-1H-15N NOESY-HMQCsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N SOFAST-HMQCsample_3isotropicsample_conditions_1
2D 1H-15N SOFAST-HMQCsample_4isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection

TOPSPIN v3.2, Bruker Biospin - processing

SPARKY v1.2, T. D. Goddard and D. G. Kneller, SPARKY 3, UCSF - peak picking

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 700 MHz

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