Table 5. Dynamics, structural and line width parameters obtained from nonlinear least-squares fits to the ESR spectra of TOAC-labeled Ctx(Ile²¹)-Ha analogues acquired at 22°C.

Peptide	Rx (τx)	Ry (τy)	Rz (τz)	<τ>	Δ	W0	c 20	S 0
Buffer
TOAC0	110.0 (0.15)	110.0 (0.15)	110.0 (0.15)	0.15	0.7	1.1	–	–
TOAC2	47.8 (0.35)	47.8 (0.35)	47.8 (0.35)	0.35	0.7	1.2	–	–
TOAC13	21.4 (0.78)	21.4 (0.78)	21.4 (0.78)	0.78	0.7	1.9	–	–
LPC
TOAC0	16.2 (1.02)4.1 (4.1)	16.2 (1.02)6.5 (2.6)	29.5 (0.56)5.1 (3.3)	0.843.3	––	2.0	0.350.64	0.070.14
TOAC2	2.19 (7.7)	1.51 (10.9)	0.81 (20.6)	12.0	1.8	5.1	1.72	0.38
TOAC13	0.51 (32.7)	0.51 (32.7)	0.19 (85.5)	45.0	4.6	6.8	6.46	0.83
Observations•Δ and W0 are, respectively, the calculated Gaussian line width and the experimental peak-to-peak width of the central line, and are given in Gauss units;•R-component and τ-component values are given in 107 s −1 and ns, respectively;•TOAC0 derivative incorporated into LPC micelles presented two components. Populations: site 1 (40%), site 2 (60%). Uncertainty: 2%.•Uncertainty of the R-tensor values from nonlinear least-squares simulations:
	Buffer TOACx (x = 0, 2) TOAC13	Rx (5%), Ry (5%), Rz (5%) Rx (5%), Ry (2%), Rz (5%);
	LPC micelles TOAC0 TOACx (x = 2, 13)	Site 1: Rx (5%), Ry (5%), Rz (10%) Site 2: Rx (10%), Ry (2%), Rz (10%) Rx (5%), Ry (5%), Rz (10%);