Fig. 3: Chimeric bWNVKUN recapitulates the structure of wild-type WNVKUN. | Nature Communications

Fig. 3: Chimeric bWNVKUN recapitulates the structure of wild-type WNVKUN.

From: A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses

Fig. 3

a FSC of the masked maps of bWNVKUN and WNVKUN. b Plot of the root-mean-squared deviation (RMSD) between pairs of main-chain atoms for equivalent residues of the automated build of bWNVKUN and WNVKUN (red), and the best refined models (blue). The corresponding domain organization of WNVKUN is shown as in Fig. 2e. c A ribbon representation of the three copies of E within the asymmetric unit of bWNVKUN coloured as in b. The ribbon thickness is proportional to the local RMSD differences between bWNVKUN and WNVKUN including all equivalent atoms. Differences are very small with an RMSD per residue range of 0.02–1.36 Å and an average of 0.41 Å, and primarily located in exposed loops. Selected zoom panels show a close agreement even in regions of maximal RMSD. Side chains are shown as sticks for bWNVKUN (same colouring as ribbon) and WNVKUN (white).

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