3D Ramachandran histograms for the backbone torsion angles φ and ψ (A) andtwo dimensional plots of the secondary structure analysis (B).

<p>In <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0038967#pone-0038967-g005" target="_blank">Fig 5A</a> the analysis was performed for the residues that were predicted to from the transmembrane helix: 221–238 for the TM 3 helix and 220–238 for the TM 3A helix. Each exported conformation of the peptide in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0038967#pone-0038967-g005" target="_blank">Fig 5B</a>, generated by the 20 ns MD simulation was analyzed for is the secondary structure. Purple colour depicts the alpha helix structure, green indicates the turn structure and blue depicts the 3–10 helical structure. Selected residue numbers on the y-axis corresponds to the residues numbers of the BTL sequence.