<p>The RMSDs (in Å) per residue were calculated from trajectories 1 (red) and 2 (green) of MD simulations of KIT<sup>D816Y</sup>, KIT<sup>D816N</sup>, KIT<sup>D816H</sup>, KIT<sup>V560G</sup> and KIT<sup>V560G</sup>. Horizontal doted lines indicate the RMSDs mean values.</p
<p>Gray line: RMSD evaluated along the 250 ns of the MD-XR trajectory. Orange: RMSD evaluated along ...
<p>Structure snapshots (one structure for 2-ns interval) of the first MD simulations respectively fo...
<p>MD simulations were carried out using a truncated lid form (residues 16–24). The RMSD fluctuation...
<p>(<b>A</b>) MD conformations taken at 14, 26, 38 and 50 ns of two 50-ns MD simulations of KIT D816...
<p>(a–b). Root-mean-square deviations (RMSD) of the backbone atoms for two independent MD simulation...
<p>Blue: RMSD values of the 20 homology models versus each other; Green: RMSD values of the 20 NMR s...
<p>Calculation was performed on the backbone atoms of KIT<sup>WT</sup> and mutants, KIT<sup>D816H/Y/...
<p>In (A), RMSD values from the whole construct (NS3<sub>PRO</sub> F, black line) were compared with...
<p>(a) Time course of root mean square deviations (RMSDs) of wild-type CycT1 (left) and CycT1 mutant...
<p>Residual RMSD (A) and wavelet (C) analysis for each amino acid residue as function of MD simulati...
<p>(A) The MD simulations of 1-17-2 Fab and the 30 mutants. The curves indicate the RMSD value chang...
<p>Partial RMSD evaluated after structure alignment over the backbone atoms of protein core residues...
<p>Proteins Cα (A), heavy atoms of NADPH cofactor (B) and substrate cortisone (C) are plotted as fun...
<p>Root-mean-square fluctuations (RMSF) of the Cα atoms for three independent MD simulations of the ...
<p>(a–b). Structure snapshots (one structure for 1-ns interval) for two independent MD simulations f...
<p>Gray line: RMSD evaluated along the 250 ns of the MD-XR trajectory. Orange: RMSD evaluated along ...
<p>Structure snapshots (one structure for 2-ns interval) of the first MD simulations respectively fo...
<p>MD simulations were carried out using a truncated lid form (residues 16–24). The RMSD fluctuation...
<p>(<b>A</b>) MD conformations taken at 14, 26, 38 and 50 ns of two 50-ns MD simulations of KIT D816...
<p>(a–b). Root-mean-square deviations (RMSD) of the backbone atoms for two independent MD simulation...
<p>Blue: RMSD values of the 20 homology models versus each other; Green: RMSD values of the 20 NMR s...
<p>Calculation was performed on the backbone atoms of KIT<sup>WT</sup> and mutants, KIT<sup>D816H/Y/...
<p>In (A), RMSD values from the whole construct (NS3<sub>PRO</sub> F, black line) were compared with...
<p>(a) Time course of root mean square deviations (RMSDs) of wild-type CycT1 (left) and CycT1 mutant...
<p>Residual RMSD (A) and wavelet (C) analysis for each amino acid residue as function of MD simulati...
<p>(A) The MD simulations of 1-17-2 Fab and the 30 mutants. The curves indicate the RMSD value chang...
<p>Partial RMSD evaluated after structure alignment over the backbone atoms of protein core residues...
<p>Proteins Cα (A), heavy atoms of NADPH cofactor (B) and substrate cortisone (C) are plotted as fun...
<p>Root-mean-square fluctuations (RMSF) of the Cα atoms for three independent MD simulations of the ...
<p>(a–b). Structure snapshots (one structure for 1-ns interval) for two independent MD simulations f...
<p>Gray line: RMSD evaluated along the 250 ns of the MD-XR trajectory. Orange: RMSD evaluated along ...
<p>Structure snapshots (one structure for 2-ns interval) of the first MD simulations respectively fo...
<p>MD simulations were carried out using a truncated lid form (residues 16–24). The RMSD fluctuation...