Conformational analysis of the SF region. (A) Distances between opposing Cα atoms of SF-forming amino acids (combined data of all 14 × 1-µs runs). (B) Left plot: Comparison of distance data of opposing Y157 Cα atoms between clusters of MD runs with high (magenta, 1µs_run1 + 1µs_run5 [40 mV nm⁻¹]; orange, 1µs_run12 + 1µs_run13 [20 mV nm⁻¹]) or low (green, 1µs_run2 + 1µs_run4 [40 mV nm⁻¹]; blue, 1µs_run11 + 1µs_run14 [20 mV nm⁻¹]) conductance. Right plot: To analyze temporary conductance fluctuations, snippets of phases with high (orange) or low (blue) conductance of the MD runs 1µs_run5 (0.2–0.5 µs = high; 0.7–1 µs = low) and 1µs_run8 (0–0.4 µs = high; 0.6–1 µs = low) are clustered. See also Fig. S9. (C) Distances between opposing Cα atoms of residues at the HBC gate (F192 and V193). The runs were clustered and colored the same way as in the left plot of B. (D) Analysis of hydrogen bonds in the SF area (combined data of all 14 × 1-µs runs). (E) Visualization of the hydrogen bonds in the SF area. The front subunit is hidden for better visibility. (F) Psi angles of residue Y157 as a function of time for two MD runs with phases of high and low conductance. Each plot shows the psi angles of all four subunits (colored in black, blue, green, and orange).