. 2017 Aug 10;114(35):9343–9348. doi: 10.1073/pnas.1702201114

Table S4.

FRET efficiencies and distances determined from SecY292 FRET pairs on SecA–PhoA–SecYEG complex

Labeled site on SecYEG	Labeled site on PhoA peptide portion of SecA–PhoA chimera
SecA–PhoA, SecYEG–SecY292–AF488	PhoA2–AF647		PhoA22–AF647		PhoA37–AF647		PhoA45–AF647
	R₀^*: 57		R₀^*: 50		R₀^*: 53		R₀^*: 54
	f_D = 1.00, f_A = 0.61^†		f_D = 1.00, f_A = 0.56^†		f_D = 1.00, f_A = 0.51^†		f_D = 1.00, f_A = 0.61^†
	E_FRET^‡	Distance^†	E_FRET^‡	Distance^†	E_FRET^‡	Distance^†	E_FRET^‡	Distance^†
ADP	0.25 ± 0.06	68 ± 15	0.46 ± 0.06	51.3 ± 9.2	0.24 ± 0.05	64 ± 14	0.30 ± 0.01	62 ± 13
ATP-γS	0.19 ± 0.03	72 ± 17	0.71 ± 0.01	42.9 ± 8.6	0.30 ± 0.03	61 ± 13	0.27 ± 0.01	63 ± 13

R₀ values given in angstroms were calculated as previously described (20).

^{^†}

The donor−acceptor distances (R) given in angstroms were calculated as described in SI Materials and Methods and consider the fractional labeling of the donor (f_D) and acceptor (f_A) in the doubly labeled complex. The larger error in the distances results from a consideration of the steady-state fluorescence anisotropy values of the dyes.

^{^‡}

The FRET efficiency (E_FRET) was calculated from the decrease of donor fluorescence intensity in the presence of the acceptor as described in SI Materials and Methods. The indicated error is determined from three independent measurements.