Fig. 2
From: Two novel variants in DYRK1B causative of AOMS3: expanding the clinical spectrum
![Fig. 2](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs13023-021-01924-z/MediaObjects/13023_2021_1924_Fig2_HTML.png)
Molecular dynamic analysis of DYRK1B-252His. a Root mean square deviation (RMSD) of atomic positions, analysis of wild-type protein (black line), and DYR1B-252His (red line). b Root mean square fluctuation (RMSF) of the wild-type protein (black line) and DYR1B-252His (red line). c Wild-type structure. d Structure of DYRK1B-252His. The protein structure colors are the same as previously described. e Region of interest zoomed-in for Arg252. The hydrogen bonds are depicted by the blue dots. f Same region of interest with the His252 variant