Table 1 Solid-state NMR and structure refinement statistics for F₄-TPP⁺ complexed S64V-EmrE structure in lipid bilayers.

	Monomer A	Monomer B
NMR distance and dihedral constraints
Dipolar couplings	42	30
Distance constraints	120	94
Total number of dihedral-angle restraints
ϕ	99	86
ψ	99	87
χ₁	53	42
Structure refinement statistics
Violations (mean ± s.d.)
Distance constraints (Å)	0.008 ± 0.064	0.019 ± 0.114
Max. distance-constraint violation (Å)	0.96	1.48
ϕ Dihedral-angle constraints (°)	0.160 ± 1.486	0.126 ± 0.995
ψ Dihedral-angle constraints (°)	0.217 ± 2.143	0.383 ± 2.421
Max. ϕ dihedral-angle violation (°)	22.8	13.9
Max. ψ dihedral-angle violation (°)	31.4	31.5
Average pairwise r.m.s.d (Å)^a
Protein heavy atom	2.12 ± 0.23
Protein backbone	1.61 ± 0.19
Ligand heavy	1.35 ± 0.35
Ligand center^b	0.76 ± 0.32

^aPairwise r.m.s.d. was calculated among 10 lowest-violation structures between the two independent MD runs after the refinement had equilibrated.
^bLigand center is defined as phosphorus and its four directly bonded carbon atoms of F₄-TPP⁺.

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