title: Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor.
abstract: The sequence specific (1)H, (13)C, and (15)N resonance assignments for stromelysin, a Matrix metalloproteinase, are reported in this article. Almost 70% of assignable backbone and side-chain atoms were assigned in this highly dynamic protein.
authors.affiliation: Exploratory Medicinal Sciences, Pfizer Global Research & Development, MS 8118A-2024, Eastern Point Road, Groton, CT 06340, USA. Parag.sahasrabudhe@pfizer.com
authors.forename: Parag V
authors.initials: PV
authors.lastname: Sahasrabudhe
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Stockman
mesh_terms: D004791:Enzyme Inhibitors / Q000378:metabolism* / Q000494:pharmacology; D006877:Hydroxamic Acids / Q000378:metabolism* / Q000494:pharmacology; D019278:Matrix Metalloproteinase 3 / Q000737:chemistry* / Q000378:metabolism*; D061965:Matrix Metalloproteinase Inhibitors; D019906:Nuclear Magnetic Resonance, Biomolecular; D012984:Software; D013450:Sulfones / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D006877:Hydroxamic Acids; D061965:Matrix Metalloproteinase Inhibitors; C546397:N-hydroxy-3-((4-methoxyphenyl)sulfonyl)-2-(((4-methoxyphenyl)sulfonyl)methyl)propanamide; D013450:Sulfones; D019278:Matrix Metalloproteinase 3