BMRB: 5972

Proton Chemical Shifts for E coli ProP 468-497 peptide

Authors

Zoetewey, D.L., Tripet, B.P., Kutateladze, T.G., Overduin, M.J., Wood, J.M., Hodges, R.S.

Assembly

ProP antiparallel coiled-coil

Entity

1. ProP antiparallel coiled-coil (polymer, Thiol state: all other bound), 36 monomers, 3971.438 × 2 Da Detail

XXCGGDNIEQ KIDDIDHEIA DLQAKRTRLV QQHPRX

Total weight

7942.876 Da

Max. entity weight

3971.438 Da

Source organism

Escherichia coli

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.7 %, Completeness: 98.5 %, Completeness (bb): 97.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	98.5 % (200 of 203)	98.5 % (200 of 203)
Backbone	97.0 % (65 of 67)	97.0 % (65 of 67)
Sidechain	99.3 % (135 of 136)	99.3 % (135 of 136)
Aromatic	100.0 % (4 of 4)	100.0 % (4 of 4)
Methyl	100.0 % (17 of 17)	100.0 % (17 of 17)

1. ProP

XXCGGDNIEQ KIDDIDHEIA DLQAKRTRLV QQHPRX

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Sample

Temperature 298 (±1) K, pH 5.0 (±0.3)

#	Name	Isotope labeling	Type	Concentration
1	ProP			3.0 mM
2	potassium phosphate			50 mM
3	KCl			100 mM
4	D2O			10 %
5	H2O			90 %

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Calculated from 51 models in PDB: 1R48, Strand ID: A, B Detail

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Release date

2003-12-18

Citation

Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP
Zoetewey, D.L., Tripet, B.P., Kutateladze, T.G., Overduin, M.J., Wood, J.M., Hodges, R.S.
J. Mol. Biol. (2003), 334, 1063-1076, PubMed 14643666 , DOI: , Abstract

Related entities 1. ProP antiparallel coiled-coil, : 1 : 2 : 2 entities Detail

Experiments performed 3 experiments Detail