BMRB: 34622

NMR structure of the Bak transmembrane helix in lipid nanodiscs

Authors

Sperl, L.E., Hagn, F.

Assembly

Bcl-2 homologous antagonist/killer

Entity

1. Bcl-2 homologous antagonist/killer (polymer, Thiol state: not present), 30 monomers, 3241.910 Da Detail

SLGNGPILNV LVVLGVVLLG QFVVRRFFKS

Formula weight

3241.91 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 80.0 %, Completeness: 21.8 %, Completeness (bb): 52.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	21.8 % (48 of 220)	12.9 % (24 of 186)	70.6 % (24 of 34)
Backbone	52.2 % (48 of 92)	38.1 % (24 of 63)	82.8 % (24 of 29)
Sidechain	0.0 % (0 of 128)	0.0 % (0 of 123)	0.0 % (0 of 5)
Aromatic	0.0 % (0 of 15)	0.0 % (0 of 15)
Methyl	0.0 % (0 of 28)	0.0 % (0 of 28)

1. entity 1

SLGNGPILNV LVVLGVVLLG QFVVRRFFKS

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 315 K, pH 7.0, Details 400 uM [U-13C; U-15N; U-2H] Bak transmembrane helix, 20 mM sodium phosphate, 50 mM sodium chloride, 1 mM EDTA, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	Bak transmembrane helix	[U-13C; U-15N; U-2H]		400 uM
2	sodium phosphate	natural abundance		20 mM
3	sodium chloride	natural abundance		50 mM
4	EDTA	natural abundance		1 mM

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Release date

2021-06-10

Citation

High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane
Sperl, L.E., Ruhrnossl, F., Schiller, A., Haslbeck, M., Hagn, F.
EMBO J. (2021), 40, e107159-e107159, PubMed 34523144 , DOI 10.15252/embj.2020107159 , Abstract

Related entities 1. Bcl-2 homologous antagonist/killer, : 1 : 1 : 2 : 4 entities Detail

Interaction partners 1. Bcl-2 homologous antagonist/killer, : 43 interactors Detail

Experiments performed 3 experiments Detail

Chemical shift validation 3 contents Detail