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. 2024 Apr 24;13:RP93561. doi: 10.7554/eLife.93561

Video 1. Molecular dynamics simulations for the wild-type hsPURA I–II (chain B).

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Red color indicates the residues with significantly higher fluctuation described as p-value computed using the average position of the carbon alpha during the simulation as the reference point. 10 production runs were performed at the temperature of 310 K, resulting in 20 simulations of 100 ns each (1000 frames), or a total aggregate time of 1 µs for each protein. The systems were analyzed using root means square fluctuations (RMSF). More precisely, the RMSF was computed for each Cα atom in each simulation, leaving 10 RMSF data points per residue.