Extended Data Fig. 6: Single-molecule FRET characterization of the effects of the A577I mutation on the conformation of yeast Hsp 90.

a–c, The 2D UMAP projections of trace embeddings from the different experimental conditions in Atlas coordinates (a) and system-specific coordinates (b) and (c). d, FRET histograms of all traces from the different experimental conditions. e, 2D UMAP projections of the 20% of traces with lowest LSE under the different experimental conditions in system-specific coordinates. f, FRET histograms of the 20% of traces with lowest LSE from the different experimental conditions, more strongly highlighting the conclusion from the original study⁴⁴ that, in the presence of ATP, both the A577I/A577I homodimer (5^th column) and the A577I/wild-type (wt) hetero-dimer (6^th column) lead to a shift toward closed conformations, corresponding to high-FRET states.