BMRB: 441

NMR studies of the Escherichia coli trp aporepressor Sequence-specific assignment of the aromatic proton residues

Authors

Hyde, E.I., Ramesh, V., Roberts, G.C.K., Arrowsmith, C.H., Treat-Clemons, L., Klaic, B., Jardetzky, O.

Assembly

trp repressor

Entity

1. trp repressor (polymer), 107 monomers, 12223.81 Da Detail

AQQSPYSAAM AEQRHQEWLR FVDLLKNAYQ NDLHLPLLNL MLTPDEREAL GTRVRIVEEL LRGEMSQREL KNELGAGIAT ITRGSNSLKA APVELRQWLE EVLLKSD

Formula weight

12223.81 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.7 %, Completeness: 0.9 %, Completeness (bb): 0.5 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	0.9 % (6 of 665)	0.9 % (6 of 665)
Backbone	0.5 % (1 of 215)	0.5 % (1 of 215)
Sidechain	1.1 % (5 of 450)	1.1 % (5 of 450)
Aromatic	6.9 % (2 of 29)	6.9 % (2 of 29)
Methyl	0.0 % (0 of 68)	0.0 % (0 of 68)

1. trp repressor

AQQSPYSAAM AEQRHQEWLR FVDLLKNAYQ NDLHLPLLNL MLTPDEREAL GTRVRIVEEL LRGEMSQREL KNELGAGIAT ITRGSNSLKA APVELRQWLE EVLLKSD

Show sample condition

Sample

Temperature 318 K, pH 5.6

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Release date

1995-07-30

Citation

NMR studies of the Escherichia coli trp aporepressor. Sequence-specific assignment of the aromatic proton resonances
Hyde, E.I., Ramesh, V., Roberts, G.C.K., Arrowsmith, C.H., Treat-Clemons, L., Klaic, B., Jardetzky, O.
Eur. J. Biochem. (1989), 183, 545-553, PubMed 2673778 , DOI: , Abstract

Related entities 1. trp repressor, : 1 : 12 : 3 : 16 : 36 entities Detail

Interaction partners 1. trp repressor, : 2 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail