Secondary structures of EspB and its peptide fragments estimated from the results of far-UV CD or amino acid sequences.

aSum of the contents of regular and distorted α-helix estimated by CDpro [17] based on the far-UV CD spectra. bSum of the contents of regular and distorted β-sheet estimated by CDpro [17] based on the far-UV CD spectra. cContents of turns estimated by CDpro [17] based on the far-UV CD spectra. dContents of unordered structures estimated by CDpro [17] based on the far-UV CD spectra. eα-Helical propensities calculated by AGADIR algorithm [35]–[39]. fNumber of residues involved in α-helix calculated from the α-helix content estimated by CDpro [17] and the total length of each polypeptides. Total length of EspB, EspB1–176 and EspB177–312 are 332, 197 and 156 amino acids including additional sequences of N-terminal his-tag.