title: Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus.
abstract: The backbone and side chain assignments of the retroviral aspartate protease from Simian Foamy Virus from macaques (SFVmac) have been determined by triple resonance NMR techniques.
authors.affiliation: Lehrstuhl Biopolymere, Universität Bayreuth, Germany.
authors.forename: Maximilian J
authors.initials: MJ
authors.lastname: Hartl
authors.forename: Birgitta M
authors.initials: BM
authors.lastname: Wöhrl
authors.forename: Kristian
authors.initials: K
authors.lastname: Schweimer
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000648:ultrastructure*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011522:Protons; D053150:Simian foamy virus / Q000201:enzymology*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D010447:Peptide Hydrolases