Fig. 4

Analyses of tr-NOESY spectrum and three-dimensional solution structure of HVF18 in LPS micelles. a Diagram summarising the sequential and medium range NOE contacts identified in HVF18. b Bar diagram showing number and type of NOEs observed for HVF18 in complex with LPS as a function of amino acids. c Superposition of backbone atoms (N, Cα, C’) for the 20 lowest energy conformers of LPS-bound HVF18. d A representative structure of LPS-bound HVF18 showing backbone topology and side-chain dispositions and (e) plausible hydrogen bond formation between K6 and I9 in the β-turn region. Ribbon representation of peptide backbone showing amphipathic disposition of (f) hydrophilic residues along the convex side (g) and the hydrophobic residues on the concave side of a curved backbone fold of HVF18 in complex with LPS. Figures were generated using MolMol v2K.2 and Pymol v1.7.4.0