Data were processed automatically using Mascot Distiller software (version 2.5.1, Matrix Science) followed by Mascot (version 2.6) searches using the sequences of the different peptides of interest as database. None was chosen as enzyme, and the precisions were set at 10 ppm for the peptide precursor and 20 milli mass unit for the fragments. At first instance, many different possibilities of variable modifications were tested to find out on which amino acid was observed in the dehydramino modification (−2H) (36). Manual annotations were performed in parallel to Mascot searches to assess the positions of thioether linkages. For final searches, dehydramino (A, N, R, and K), deamidation (NQ), and ammonia loss (N) were set as variable modifications. Qual Browser and Xtract (Thermo Fisher Scientific) were used for the display and the deconvolution of the spectra. All considered experimental masses were monoisotopic and nonprotonated masses.

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