BMRB: 11056

KMTM7 a peptide derived from V-ATPase subunit a, putative TM7

Authors

Vermeer, L.S., Reat, V., Hemminga, M.A., Milon, A.

Assembly

peptide from V-ATPase

Entity

1. peptide from V-ATPase (polymer, Thiol state: not present), 25 monomers, 2825.270 Da Detail

KKSHTASYLR LWALSLAHAQ LSSKK

Formula weight

2825.27 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 96.0 %, Completeness: 91.8 %, Completeness (bb): 96.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	91.8 % (145 of 158)	91.8 % (145 of 158)
Backbone	96.0 % (48 of 50)	96.0 % (48 of 50)
Sidechain	89.8 % (97 of 108)	89.8 % (97 of 108)
Aromatic	100.0 % (14 of 14)	100.0 % (14 of 14)
Methyl	93.3 % (14 of 15)	93.3 % (14 of 15)

1. KMTM7

KKSHTASYLR LWALSLAHAQ LSSKK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 5.0

#	Name	Isotope labeling	Type	Concentration
1	KMTM7	natural abundance		1 mM
2	SDS	[U-100% 2H]		250 mM
3	sodium phosphate	natural abundance		10 mM
4	DSS	natural abundance		0.3 mM
5	H2O			90 %
6	D2O			10 %

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Protein Blocks Logo

Calculated from 20 models in PDB: 2RPW, Strand ID: X Detail

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Release date

2009-04-16

Citation

Structural properties of a peptide derived from H+ -V-ATPase subunit a
Vermeer, L.S., Reat, V., Hemminga, M.A., Milon, A.
Biochim. Biophys. Acta (2009), 1788, 1204-1212, PubMed 19249284 , DOI 10.1016/j.bbamem.2009.02.015 , Abstract

Related entities 1. peptide from V-ATPase, : 1 : 2 : 13 : 75 entities Detail

Interaction partners 1. peptide from V-ATPase, : 4 interactors Detail

Experiments performed 2 experiments Detail

Chemical shift validation 3 contents Detail