title: NMR assignment of the Rhodobacter sphaeroides fasciclin-1 domain protein (Fdp).
abstract: We report the almost complete assignment of 1H, 13C and 15N nuclei in the 137-residue his-tagged fasciclin domain protein (Fdp) from Rhodobacter sphaeroides. Fdp is homologous to fasciclin I domains, including Drosophila FAS1 and M. tuberculosis MPB70 and plays a role in cell adhesion.
authors.affiliation: Astbury Centre for Structural Molecular Biology, Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
authors.forename: Robert G
authors.initials: RG
authors.lastname: Moody
authors.forename: Mary K
authors.initials: MK
authors.lastname: Phillips-Jones
authors.forename: Mike P
authors.initials: MP
authors.lastname: Williamson
mesh_terms: D000818:Animals; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D015816:Cell Adhesion Molecules, Neuronal / Q000737:chemistry* / Q000235:genetics; D029721:Drosophila Proteins / Q000737:chemistry; D005798:Genes, Bacterial; D009169:Mycobacterium tuberculosis / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D015816:Cell Adhesion Molecules, Neuronal; D029721:Drosophila Proteins; C051641:fasciclin I