1H, 13C and 15N resonance assignment of the oxidized form (Cys(67)-Cys (70)) of the N-terminal domain of PilB from Neisseria meningitidis.
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.
Quinternet
Marc
M
Laboratoire de Chimie-Physique Macromoléculaire, UMR 7568 CNRS-INPL, Nancy Université, 1 rue Grandville, B.P. 451, 54001 Nancy Cedex, France.
Beaufils
Chrystel
C
Neiers
Fabrice
F
Tsan
Pascale
P
Boschi-Muller
Sandrine
S
Averlant-Petit
Marie-Christine
MC
Branlant
Guy
G
Cung
Manh-Thong
MT
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003553:Cystine / Q000737:chemistry; D015394:Molecular Structure; D009345:Neisseria meningitidis / Q000737:chemistry* / Q000235:genetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D003553:Cystine; D010088:Oxidoreductases; C068255:pilB protein, Bacteria