BMRB: 1136

15N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: Sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobin G

Authors

Torigoe, H., Shimada, I., Waelchli, M., Saito, A., Sato, M., Arata, Y.

Assembly

IgG Fc region-binding protein

Entity

1. IgG Fc region-binding protein (polymer), 60 monomers, 6770.353 Da Detail

TADNKFNKEQ QNAFYEILHL PNLNEEQRNG FIQSLKDDPS QSANLLAEAK KLNDAQAPKA

Formula weight

6770.353 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.3 %, Completeness: 2.8 %, Completeness (bb): 3.5 % Detail

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Polymer type: polypeptide(L)

	Total	15N
All	2.8 % (2 of 71)	2.8 % (2 of 71)
Backbone	3.5 % (2 of 57)	3.5 % (2 of 57)
Sidechain	0.0 % (0 of 14)	0.0 % (0 of 14)

1. IgG Fc region-binding protein

TADNKFNKEQ QNAFYEILHL PNLNEEQRNG FIQSLKDDPS QSANLLAEAK KLNDAQAPKA

Show sample condition

Sample

Temperature 303 K, pH 5

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Release date

1995-07-30

Citation

15N nuclear magnetic resonance studies of the B domain of staphylococcal protein A: sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobulin G
Torigoe, H., Shimada, I., Waelchli, M., Saito, A., Sato, M., Arata, Y.
FEBS Lett. (1990), 269, 174-176, PubMed 2387398 , Abstract

Related entities 1. IgG Fc region-binding protein, : 1 : 1 : 1 : 101 : 73 entities Detail

Interaction partners 1. IgG Fc region-binding protein, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail