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. 2016 Dec 27;3:85. doi: 10.3389/fmolb.2016.00085

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Copyright © 2016 Hsieh, Poitevin, Delarue and Koehl.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Correlated motions in the DENV E protein. Cross Correlation Matrices (CCM) obtained from the 94 first non-zero modes for the E protein alone (MONO, A), the E protein in the asymmetric unit (UNIT, B), and the E protein in the whole capsid (FULL, C). Those plot show correlations between the motions of Cα atoms in each complex considered. Both axes of a matrix are the amino acid residue index. Each cell in a matrix shows the correlation between the motions of two residues (Cα atoms) in the protein on a range from −1 (anticorrelated, blue) to 1 (correlated, red), with 0 conferring no correlation. (D) The E protein is shown in cartoon mode. The color code for the structure in (C) as well as for the X and Y axes of the CCM plots in (A) to follows the standard designation of the E protein domains I (red), II (yellow), and III (blue). The transmembrane domain is shown in purple. Panel (D) was generated using Pymol.