Fig. 6: Structure and stability of H3N2 neuraminidase.
From: Prevalence and mechanisms of evolutionary contingency in human influenza H3N2 neuraminidase
a The effects of different Mos99, SD93, and Bil69 NA mutants on protein melting temperature (Tm) were measured by thermal shift assay. Each bar represents the mean of six independent biological replicates. Each datapoint represents one biological replicate. Jittering was added to avoid overlap of datapoints. b The locations of the residues of interest on Mos99 NA are shown. c–e The local structure around residue 387 of Mos99 NA (white) is compared with that of c Bil69 NA (gray) and SD93 NA (wheat), d H3N2 A/Perth/16/2009 (Perth09) NA (pink, PDB 6BR5)22, and e H3N2 A/Tanzania/205/2010 (Tan10) NA (blue, PDB 4GZO)23. f Natural occurrence frequencies of the amino acid variants that have a natural occurrence at >50% in any given year at the residues of interest are shown. Source data are provided as a Source data file.
