BMRB: 18659

NMR solution structure of peptide epsilon(103-120) from Mycobacterium tuberculosis F-ATPsynthase

Authors

Basak, S., Rishikesan, S., Gruber, G.

Assembly

peptide epsilon(103-120)

Entity

1. peptide epsilon(103-120) (polymer, Thiol state: not present), 18 monomers, 1919.243 Da Detail

DPRIAARGRA RLRAVGAI

Formula weight

1919.243 Da

Source organism

Mycobacterium tuberculosis

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 89.3 %, Completeness (bb): 94.6 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	89.3 % (92 of 103)	89.3 % (92 of 103)
Backbone	94.6 % (35 of 37)	94.6 % (35 of 37)
Sidechain	86.4 % (57 of 66)	86.4 % (57 of 66)
Methyl	92.3 % (12 of 13)	92.3 % (12 of 13)

1. epsilon 103-120

DPRIAARGRA RLRAVGAI

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	epsilon103-120	natural abundance		2 mM
2	TFE	[U-99% 2H]		50 %
3	sodium phosphate	natural abundance		25 mM
4	sodium chloride	natural abundance		300 mM

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Calculated from 20 models in PDB: 2LX5, Strand ID: A Detail

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Release date

2013-08-11

Citation

Variations of subunit {varepsilon} of the Mycobacterium tuberculosis F1Fo ATP synthase and a novel model for mechanism of action of the tuberculosis drug TMC207
Biukovic, G., Basak, S., Manimekalai, M., Rishikesan, S., Roessle, M., Dick, T., Rao, S.P.S., Hunke, C., Gruber, G.
Antimicrob. Agents Chemother. (2013), 57, 168-176, PubMed 23089752 , DOI 10.1128/AAC.01039-12 , Abstract

Related entities 1. peptide epsilon(103-120), : 1 : 3 : 4 entities Detail

Experiments performed 2 experiments Detail