title: ¹H, ¹³C and ¹⁵N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis.
abstract: Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition.
authors.affiliation: Institute of Chemical and Engineering Sciences, Agency for Science, Technology and Research, Singapore, Singapore.
authors.forename: Qingxin
authors.initials: Q
authors.lastname: Li
authors.forename: Angela Shuyi
authors.initials: AS
authors.lastname: Chen
authors.forename: Shovanlal
authors.initials: S
authors.lastname: Gayen
authors.forename: Congbao
authors.initials: C
authors.lastname: Kang
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D042541:Intracellular Space / Q000378:metabolism*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011480:Protease Inhibitors / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011480:Protease Inhibitors; D011522:Protons