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. 2021 Mar 16;12:1693. doi: 10.1038/s41467-021-21754-8

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Positional substrate preferences of coagulation proteases from the chymotrypsin-like family (Chymotrypsin, activated α-, β-, γ-Thrombin, aFVII, aFIX, aFX, aFXI, aPC and PLG). The heat map includes positions P4-P4’. The AAs are grouped according to their physicochemical properties. The enrichments are reported as log₂ FC compared to a random AA distribution generated from HTPS database. b Peptides generated by the coagulation proteases included in the study; each protease is characterized by the average number of peptides identified from three independent replicate experiments (n = 3). Data are presented as mean values±SD. c Unsupervised hierarchical cluster of coagulation proteases. The color scale describes the Pearson correlation coefficient value calculated for the respective protease samples. d Unsupervised hierarchical cluster of coagulation proteases according to the positional cleavage entropy. The color scale describes the cleavage entropy (S) values for positions P8-P8’ for all respective proteases included in the assay. Source data are provided as a Source Data file.