Updated project metadata. Proteomic analysis of integrin activation-state-dependent adhesion complexes. Adhesion complexes were isolated from K562 cells using activation-state-specific monoclonal antibodies coupled to magnetic beads.Tandem mass spectra were extracted using extract_msn (Thermo Fisher Scientific) executed in Mascot Daemon (version 2.2.2; Matrix Science). Peak list files were searched against the IPI Human database (version 3.70) modified to contain ten additional contaminants and reagent sequences of non-human origin. Searches were submitted to an in-house Mascot server (version 2.2.03; Matrix Science). Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine was allowed as a variable modification. Only tryptic peptides were considered, with up to one missed cleavage permitted. Monoisotopic precursor mass values were used, and only doubly and triply charged precursor ions were considered. Mass tolerances for precursor and fragment ions were 0.4 Da and 0.5 Da, respectively.