Coevolving residues inform protein dynamics profiles and disease susceptibility of nSNVs
Fig 2
Color-coded ribbon diagrams using experimental and theoretical B-factors obtained by Seq-GNM.
The observed crystallographic B-factors (left) and the predicted B-factors from the Seq-GNM superimposed on the structure. The three proteins selected–2JAO, 1F2J, and 1UMK–are high-resolution structures better than 2.0 Å. The B-factors are color-coded according to their B-factor profile on a spectrum of blue–white–red where blue represents the lowest B-factors (less mobility) and red represents the highest B-factors (more mobility). The B-factor scores are converted to a percentile rank so that they can be compared across different proteins. Each protein is also rotated 180° so that both sides can be visualized and compared. Moreover, the proteins are selected so that they have a variety of secondary structure components–2JAO contains primarily alpha helices, 1UMK is mainly composed of beta-sheets, and 1F2J is a combination of alpha helices and beta-sheets.