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1H, 13C and 15N resonance assignment of the oxidized form (Cys(67)-Cys (70)) of the N-terminal domain of PilB from Neisseria meningitidis.

Titre1H, 13C and 15N resonance assignment of the oxidized form (Cys(67)-Cys (70)) of the N-terminal domain of PilB from Neisseria meningitidis.
Publication TypeJournal Article
Year of Publication2007
AuthorsQuinternet, M, Beaufils, C, Neiers, F, Tsan, P, Boschi-Muller, S, Averlant-Petit, M-C, Branlant, G, Cung, M-T
JournalBiomol NMR Assign
Volume1
Issue1
Pagination143-5
Date Published2007 Jul
ISSN1874-270X
Mots-clésBacterial Proteins, Cystine, Molecular Structure, Neisseria meningitidis, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Oxidoreductases, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins
Abstract

We report the nearly complete 1H, 13C and 15N resonance assignments of the oxidized form (Cys(67)-Cys(70)) of the N-terminal domain of PilB from Neisseria meningitidis. Secondary structure determination using CSI method and TALOS leads mainly to the prediction of 7 alpha-helical and 5 beta-sheet parts.

DOI10.1007/s12104-007-9038-8
Alternate JournalBiomol NMR Assign
PubMed ID19636850