BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19379

Title: NMR structures of the alpha7 nAChR transmembrane domain.   PubMed: 24384062

Authors: Bondarenko, Vasyl; Mowrey, David; Xu, Yan; Tang, Pei

Citation: Bondarenko, Vasyl; Mowrey, David; Tillman, Tommy; Seyoum, Edom; Xu, Yan; Tang, Pei. "NMR structures of the human 7 nAChR transmembrane domain and associated anesthetic binding sites."  Biochim. Biophys. Acta ., .-. (2013).

Assembly members:
entity, polymer, 137 residues, 14309.850 Da.

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

Entity Sequences (FASTA):
entity: SNAEEELYYGLNLLIPCVLI SALALLVFLLPADSGEKISL GITVLLSLTVFMLLVAEIMP STSDSSPSIAQYFASTMIIV GLSVVVTVIVLQYHHHDPDG GEGGGEGIDRLCLMAFSVFT IICTIGILMSAPNFVEE

Data sets:
Data typeCount
13C chemical shifts473
15N chemical shifts128
1H chemical shifts712

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha7 nAChR transmembrane domain1

Entities:

Entity 1, alpha7 nAChR transmembrane domain 137 residues - 14309.850 Da.

1   SERASNALAGLUGLUGLULEUTYRTYRGLY
2   LEUASNLEULEUILEPROCYSVALLEUILE
3   SERALALEUALALEULEUVALPHELEULEU
4   PROALAASPSERGLYGLULYSILESERLEU
5   GLYILETHRVALLEULEUSERLEUTHRVAL
6   PHEMETLEULEUVALALAGLUILEMETPRO
7   SERTHRSERASPSERSERPROSERILEALA
8   GLNTYRPHEALASERTHRMETILEILEVAL
9   GLYLEUSERVALVALVALTHRVALILEVAL
10   LEUGLNTYRHISHISHISASPPROASPGLY
11   GLYGLUGLYGLYGLYGLUGLYILEASPARG
12   LEUCYSLEUMETALAPHESERVALPHETHR
13   ILEILECYSTHRILEGLYILELEUMETSER
14   ALAPROASNPHEVALGLUGLU

Samples:

sample_1: alpha7 nAChR transmembrane domain, [U-100% 13C; U-100% 15N], 0.25 mM; NaCl, natural abundacne, 10 mM; sodium acetate buffer, natural abundacne, 5 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 4.7; pressure: 1 atm; temperature: 318 K

Experiments:

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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

SPARKY, Goddard - chemical shift assignment, data analysis

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

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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