title: 1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain).
abstract: The backbone and side chain resonance assignments of human ACS (approximately 22 KD), apoptosis-associated speck-like protein containing a caspase recruitment domain and a pyrin domain, have been determined by triple-resonance NMR techniques.
authors.affiliation: Department of Protein Science, Center for Biological Research, CSIC, Ramiro de Maeztu 9, Madrid 28040, Spain. dealbae@cib.csic.es
authors.forename: Eva
authors.initials: E
authors.lastname: de Alba
mesh_terms: D053468:CARD Signaling Adaptor Proteins / Q000737:chemistry / Q000235:genetics; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D053468:CARD Signaling Adaptor Proteins; D003598:Cytoskeletal Proteins; C402202:PYCARD protein, human; D011994:Recombinant Proteins