Fig. 2

Assessment of secondary structure and prediction of protein conformation of ligA. The secondary structural content is shown in the (a-I) and (a-II). In (a-I), the blue color regions correspond to helix and sheets are represented by pink color. Helix (H) is represented in pink and extended strand (E) in yellow in (a-II). Sterically hindrance in dihedral angles and conformational permitted regions are presented in the form of Ramachandran’s plot (b). The predicted three-dimensional structure of protein is presented before (c) and after (d) chain/fold refinement. The circular dichroism of the protein as a function of wave length is presented graphically in e-I, while the secondary structural content in terms of α-helix and β-sheet is presented in e-II. The later x-axis represents helix content and y-axis represents sheets. The star mark indicates the LigA. The structural co-ordinates of LigA from L. interorgans and E. faecalis were overlapped and analyzed for similarities. The output of analyzed results are presented in f-I where the blue color chain corresponds to the protein backbone of LigA of Leptospira and red chain refers to Eneterococcus. The most overlapped regions between both the proteins are highlighted residue-wise in f-II, where black color indicates most similar and green/yellow color represents the distant amino acids. The distance between the aligned sequences is given amino acid–wise in f-III, where the red color states a distance below 3A^°. (g) and (h) show the superposed structure of Thermus filiformis (red chain) and adenylation domain of H. Influenza (red chain) respectively with LigA (blue chain) of Leptospira