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. Author manuscript; available in PMC: 2019 Apr 1.
Published in final edited form as: J Thromb Haemost. 2018 Mar 12;16(4):734–748. doi: 10.1111/jth.13968

Fig. 7. Conservation in TF-induced changes in the residue-residue covariance matrix for FVIIa serine protease during MD simulation.

Fig. 7

Maps of the dynamic cross-correlation matrices (DCCM) show the extent of correlation for all residue Cα pairs of human (A) free FVIIa and (B) sTF-bound FVIIa, and lamprey (C) free FVIIa and (D) sTf-bound FVIIa. FVIIa residues along the axes of each DCCM map are represented by FVIIa domain schematics. The DCCM diagonal represents the correlations between covalently bonded residues, while off-diagonal regions provide information of correlations across non-covalently bonded residues. Motion occurring along the same direction is represented by positive correlation (blue, +1.0), whereas anti-correlated motion is represented by negative correlation (red, -1.0).