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. Author manuscript; available in PMC: 2020 May 7.
Published in final edited form as: Nature. 2019 Nov 7;577(7789):275–279. doi: 10.1038/s41586-019-1759-1

Extended Data Fig. 8 |. MS2 spectrum of the Ser148 P phosphopeptide.

Extended Data Fig. 8 |

(a) One MS2 spectrum used for identification of the phosphorylated P peptide 142DALDLLS#DNEEEDAESSILTFEER is displayed. Tandem mass spectrum (top) and deviation (bottom) allowed detection of phosphorylation (symbol #) at site Ser148. Peptides fragmented from the N-terminus (b-fragments) and C-terminus (y-fragments) are colored in blue and red, respectively. (b) y and b ion series m/z identified in the spectrum (a) and their deviation from theoretical m/z are displayed in the Table. The present pattern of phosphorylation agrees with observations showing that phosphorylation of the peptide comprising residues 100–120 (ref 44) of RSV-P - in particular phosphorylation of Thr108 (ref 45) corresponding to Ser148 of HMPV-P (Extended Data Fig. 9)) - controls its interaction with the M2–1 protein.