Extended Data Table 2.

Binding affinities, molecular dimensions, and reconfiguration times of fluorescently labeled H1 and ProTα.(top left) Affinities of labeled ProTα for H1 at different ionic strength (IS) and for H1 fragments for 165 mM IS (^bsee Extended Data Table 1). Uncertainties for the IS dependence are standard errors estimated from two independent titrations (^auncertainty at 165 mM: see Methods), for fragment binding from dilution errors (see Methods). ^cApparent K_D from fraction of all bound species. (top center) Binding affinities of ProTα and H1 labeled with different dye pairs for the respective unlabeled partner. dUncertainties based on dilution errors. (top right) Transfer efficiencies and average distances of ProTα and H1 labeled with different dye pairs in the bound (R_bound) and unbound state (R_unbound). Uncertainties in distance are based on an estimated systematic error of ± 0.05 in the transfer efficiency from instrument calibration for the different dye pairs. (bottom left) Intermolecular reconfiguration times for the complex of donor-labeled H1 and acceptor-labeled ProTα and vice versa. (bottom right) Reconfiguration times of doubly labeled ProTα and H1 (unbound and bound). Uncertainties estimated by propagating the error on the transfer efficiency (± 0.05).