BMRB Entry 18093

Title:
NMR structures of the transmembrane domains of the nAChR a4 subunit
Deposition date:
2011-11-18
Original release date:
2012-03-02
Authors:
Bondarenko, Vasyl; Mowrey, David; Tillman, Tommy; Cui, Tanxing; Liu, Lu; Xu, Yan; Tang, Pei
Citation:

Citation: Bondarenko, Vasyl; Mowrey, David; Tillman, Tommy; Cui, Tanxing; Liu, Lu Tian; Xu, Yan; Tang, Pei. "NMR structures of the transmembrane domains of the 42 nAChR."  Biochim. Biophys. Acta 1818, 1261-1268 (2012).
PubMed: 22361591

Assembly members:

Assembly members:
transmembrane domains of the a4b2 nAChR, polymer, 137 residues, 14748.773 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: pTBSG1

Data sets:
Data typeCount
13C chemical shifts567
15N chemical shifts127
1H chemical shifts869

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1transmembrane domains of the a4b2 nAChR1

Entities:

Entity 1, transmembrane domains of the a4b2 nAChR 137 residues - 14748.773 Da.

1   SERASNALAGLUGLULEUPROLEUPHETYR
2   THRILEASNLEUILEILEPROCYSLEULEU
3   ILESERCYSLEUTHRVALLEUVALPHETYR
4   LEUPROSERGLUCYSGLYGLULYSILETHR
5   LEUCYSILESERVALLEULEUSERLEUTHR
6   VALPHELEULEULEUILETHRGLUILEILE
7   PROSERTHRSERSERVALSERPROSERILE
8   GLYGLUTYRLEULEUPHETHRMETILEPHE
9   VALTHRLEUSERILEVALILETHRVALPHE
10   VALLEUASNVALHISHISARGSERPROGLU
11   THRHISTHRGLYGLYGLYGLYGLYILEASP
12   ARGILEPHELEUTRPMETPHEILEILEVAL
13   CYSLEULEUGLYTHRVALGLYLEUPHELEU
14   PROPROTRPLEUALAGLYGLU

Samples:

sample_1: a4b2_nAchR, [U-100% 13C; U-100% 15N], 0.25 mM; sodium acetate 5 mM; LDAO 1.5%; sodium chloride 10 mM; D2O, [U-100% 2H], 5%; DSS 0.1 mM; sodium chloride 10 mM; beta-mercaptoethanol 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 4.65; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB

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