BMRB: 15025

Backbone 1H Chemical Shift Assignments for peptide sMTM7 from subunit a of proton V-ATPase

Authors

Duarte, A.M.S., Hemminga, M.A., de Jong, E.R., van Mierlo, C.P.M., Wechselberger, R.

Assembly

sMTM7

Entity

1. sMTM7 (polymer, Thiol state: all disulfide bound), 25 monomers, 2834.233 Da Detail

EFCLNCVSHT ASYLRLWALS LAHAQ

Formula weight

2834.233 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 92.4 %, Completeness (bb): 94.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	92.4 % (133 of 144)	92.4 % (133 of 144)
Backbone	94.0 % (47 of 50)	94.0 % (47 of 50)
Sidechain	91.5 % (86 of 94)	91.5 % (86 of 94)
Aromatic	94.7 % (18 of 19)	94.7 % (18 of 19)
Methyl	88.2 % (15 of 17)	88.2 % (15 of 17)

1. sMTM7

EFCLNCVSHT ASYLRLWALS LAHAQ

Show sample condition

Sample

Solvent system DMSO, Temperature 303 K, Details Peptide dissolved in 100% d6-DMSO

#	Name	Isotope labeling	Type	Concentration
1	sMTM7	natural abundance		2 mM
2	DMSO	[U-100% 2H]		100 %

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Protein Blocks Logo

Calculated from 20 models in PDB: 2NVJ, Strand ID: A Detail

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Release date

2008-02-03

Citation

Segment TM7 from the cytoplasmic hemi-channel from VO-H+-V-ATPase includes a flexible region that has a potential role in proton translocation
Duarte, A.M.S., de Jong, E.R., Wechselberger, R., van Mierlo, C.P.M., Hemminga, M.A.
Biochim. Biophys. Acta (2007), 1768, 2263-2270, PubMed 17573038 , DOI 10.1016/j.bbamem.2007.05.014 , Abstract

Related entities 1. sMTM7, : 1 : 13 : 2 : 7 : 66 entities Detail

Interaction partners 1. sMTM7, : 28 interactors Detail

Experiments performed 2 experiments Detail