<p>(A) RMSF values calculated for each residue of the L33 (blue line) and the P33 (red line) forms of β3. Both structures show high flexibility. (B) Atom movements analyzed by PCA are projected on the first two modes. The P33 structure movements (red cloud of dots) are higher than that measured for the L33 structure (blue cloud of dots) for the first mode. No significant differences were observed for the second mode. The proline increased the structural flexibility of the PSI, I-EGF-1 and I-EGF-2 domains. The first and second modes represent 45% and 13% of the informativeness of the data.</p
<p>(a–b). Structure snapshots (one structure for 1-ns interval) for two independent MD simulations f...
<p>For each graph, an experimental measure (grey) is compared to the flexibility calculated from a s...
<p>(<b>A</b>) Conformer plot: projection of all kinesin X-ray structures onto the principal planes d...
<p>Three structure snapshots of L33 (a, b, and c) and of P33 (e, f, and d) β3 were chosen among the ...
<p><i>N<sub>eq</sub></i> values (average number of PBs weighted by their frequencies, see <a href="h...
<p>Backbone RMSF per residue reported for n-HRP (black) and p-HRP (red) along the analyzed time fram...
<p>Positive values for ΔRMSF correlate to atoms of increased flexibility while negative values for Δ...
The RMSF analysis of all-atom simulations exhibit similar atomic flexibilities of AWSEM- and AlphaFo...
<p>Projection of structures onto the first two PCs obtained using A) 46 structure dataset and B) 71 ...
<p>A) Representative structures of the conformational sub-states of the C-terminal stretch (marked i...
<p>(a) RMSF values for backbone atoms in first and second eigenvectors of Apo (black), ES (red), ET ...
<p>(A) RMSD<sub>Cα</sub> of sampled conformations during five cMD simulations with different atomic ...
<p>The degree of structural variation of the framework residues were measured as the standard deviat...
<p>a) Histogram showing change in local flexibility of each residue going from the apo to the ATP bo...
<p>The number of available structures, the length of connecting helices (number of residues), and th...
<p>(a–b). Structure snapshots (one structure for 1-ns interval) for two independent MD simulations f...
<p>For each graph, an experimental measure (grey) is compared to the flexibility calculated from a s...
<p>(<b>A</b>) Conformer plot: projection of all kinesin X-ray structures onto the principal planes d...
<p>Three structure snapshots of L33 (a, b, and c) and of P33 (e, f, and d) β3 were chosen among the ...
<p><i>N<sub>eq</sub></i> values (average number of PBs weighted by their frequencies, see <a href="h...
<p>Backbone RMSF per residue reported for n-HRP (black) and p-HRP (red) along the analyzed time fram...
<p>Positive values for ΔRMSF correlate to atoms of increased flexibility while negative values for Δ...
The RMSF analysis of all-atom simulations exhibit similar atomic flexibilities of AWSEM- and AlphaFo...
<p>Projection of structures onto the first two PCs obtained using A) 46 structure dataset and B) 71 ...
<p>A) Representative structures of the conformational sub-states of the C-terminal stretch (marked i...
<p>(a) RMSF values for backbone atoms in first and second eigenvectors of Apo (black), ES (red), ET ...
<p>(A) RMSD<sub>Cα</sub> of sampled conformations during five cMD simulations with different atomic ...
<p>The degree of structural variation of the framework residues were measured as the standard deviat...
<p>a) Histogram showing change in local flexibility of each residue going from the apo to the ATP bo...
<p>The number of available structures, the length of connecting helices (number of residues), and th...
<p>(a–b). Structure snapshots (one structure for 1-ns interval) for two independent MD simulations f...
<p>For each graph, an experimental measure (grey) is compared to the flexibility calculated from a s...
<p>(<b>A</b>) Conformer plot: projection of all kinesin X-ray structures onto the principal planes d...