BMRB Entry 18225

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18225
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
AR55 solubilised in DPC micelles
Deposition date:
2012-01-27
Original release date:
2013-01-14
Authors:
Langelaan, David; Rainey, Jan
Citation:

Citation: Langelaan, David; Reddy, Tyler; Banks, Aaron; Dellaire, Graham; Dupre, Denis; Rainey, Jan. "Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking"  Biochim. Biophys. Acta 1828, 1471-1483 (2013).
PubMed: 23438363

Assembly members:

Assembly members:
AR55, polymer, 64 residues, 7298.1072 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: recombinant technology   Host organism: Escherichia coli   Vector: pEXP5-CT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AR55: MEEGGDFDNYYGADNQSECE YTDWKSSGALIPAIYMLVFL LGTTGNGLVLWTVFRKKGHH HHHH

Data typeCount
13C chemical shifts281
15N chemical shifts70
1H chemical shifts404

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AR551

Entities:

Entity 1, AR55 64 residues - 7298.1072 Da.

1   METGLUGLUGLYGLYASPPHEASPASNTYR
2   TYRGLYALAASPASNGLNSERGLUCYSGLU
3   TYRTHRASPTRPLYSSERSERGLYALALEU
4   ILEPROALAILETYRMETLEUVALPHELEU
5   LEUGLYTHRTHRGLYASNGLYLEUVALLEU
6   TRPTHRVALPHEARGLYSLYSGLYHISHIS
7   HISHISHISHIS

Samples:

sample_1: AR55, [U-99% 13C; U-99% 15N], 1 mM; DPC, [U-99% 2H], 150 mM; sodium acetate 20 mM; sodium azide 1 mM; DSS 1 mM; DTT, [U-99% 2H], 10 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 4; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
13Cfilt_NOESY (H[{N|C}]_H.NOESY)sample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
13CHSQC_arom*800 (H[C[caro]])sample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ANALYSIS v2.1, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz
  • 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