Table 1. Parameters of spatial orientations in the lipid bilayer of antimicrobial peptides.

Peptide	Deptha (Å)	Tilt angleb (°)	ΔGtransfer (kcal/mol)	ΔGfolding (kcal/mol)	ΔGbinding c (kcal/mol)
RTA3	6.8±1.1.	82±9	−8.0	3.8	−4.2
CA-MA	8.2±3.6	85±2	−12.0	4.2	−7.8
BMAP-18	5.1±0.5	87±2	−12.3	0.4	−11.9
Bactenecin monomer	3.8±0.7	72±4	−5.7	0	−5.7
Bactenecin dimer, ↓↑	8.7±0.9	30±5	−6.6	0	−6.6
Bactenecin dimer ↑↑	8.9±0.4	59±7	−8.0	0	−8.0

The parameters were calculated by the PPM server.

^aDepth of the deepest non-hydrogen atom relative to position of membrane boundary located at the level of lipid carbonyl group.

^bAngle between membrane normal and main inertia axis of the molecule.

^cBinding energy (ΔG_binding) was calculated as the sum of the energy of peptide transfer from water to the lipid bilayer (ΔG_transfer) estimated by PPM and the folding energy (ΔG_folding) of an α-helix estimated by Framework; the folding energy of a β-hairpin stabilized by the disulfide was assumed to be zero.