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. 2019 Aug 9;19:59. doi: 10.1186/s12896-019-0553-3

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Structural sequence alignment of Bt-HepI and Ph-HepI. Residues forming the secondary structures are highlighted in the Bt-HepI sequence. Identical and similar amino acid residues are shown by white letters on a red background and black letters on a yellow background, respectively. Two different amino acids that are not conserved in Ph-HepI and Bt-HepI are indicated by black stars