<p>The computed values are from the REMD simulations (red circles) and the experimental values are from Hammoudeh et al. <a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1003249#pcbi.1003249-Hammoudeh1" target="_blank">[28]</a> (blue squares). Note that the experimental values for some residues were not available. Chemical shifts are for the atoms: <b>A</b> H<sub>α</sub>, <b>B</b> H<sub>N</sub>, <b>C</b> C<sub>α</sub>, <b>D</b> C<sub>β</sub>.</p
Figure S1. Summary of sequential backbone 1HN-1HN NOEs (dNN), secondary Cα chemical shifts at 40 mM ...
<p>(A) Amide chemical shift differences between EF4mut and Ca<sup>2+</sup>-saturated wildtype (CSD =...
The performance of fragment-based ab initio(1)H, (13)C, (15)N and (17)O chemical shift predictions i...
<p>Rmsd between calculated and experimental backbone chemical shifts are reported. In particular, ch...
<p><b>A</b> Secondary structure content. For the REMD simulations (red), the helix and sheet content...
<p>The dashed lines represent the secondary structure of the apo-EPAC (PDB ID: 2BYV). The grey highl...
a<p>Assignments of nonexchangeable protons are at 25°C. All chemical shifts are reported relative to...
The evaluation of the NMR chemical shift tensor has been implemented at the semiempirical MNDO level...
<p>A. The C<sup>α</sup> secondary shifts for free (blue) and AMA1-bound (red) R1 at pH 7 and 40°C. B...
<p>(A) Weighted chemical shift difference determined for the amide resonances between the two forms ...
<p>Backbone-RMSD clustering with a cutoff of 2.0 Å of all the conformations was performed. Represent...
Figure S1. Overlay of 800-MHz TROSY-HSQC spectra of non-acetylated (black) and acetylated (red) aS, ...
We present ProCS15: a program that computes the isotropic chemical shielding values of backbone and ...
<p>(Left panel) Proportion of NMR constraints satisfied (within a certain tolerance), as a function ...
<p>a) Root-mean-square-deviation of hβ2-AR’s backbone atoms in the MM/CG simulation of hβ2-AR.S-Car ...
Figure S1. Summary of sequential backbone 1HN-1HN NOEs (dNN), secondary Cα chemical shifts at 40 mM ...
<p>(A) Amide chemical shift differences between EF4mut and Ca<sup>2+</sup>-saturated wildtype (CSD =...
The performance of fragment-based ab initio(1)H, (13)C, (15)N and (17)O chemical shift predictions i...
<p>Rmsd between calculated and experimental backbone chemical shifts are reported. In particular, ch...
<p><b>A</b> Secondary structure content. For the REMD simulations (red), the helix and sheet content...
<p>The dashed lines represent the secondary structure of the apo-EPAC (PDB ID: 2BYV). The grey highl...
a<p>Assignments of nonexchangeable protons are at 25°C. All chemical shifts are reported relative to...
The evaluation of the NMR chemical shift tensor has been implemented at the semiempirical MNDO level...
<p>A. The C<sup>α</sup> secondary shifts for free (blue) and AMA1-bound (red) R1 at pH 7 and 40°C. B...
<p>(A) Weighted chemical shift difference determined for the amide resonances between the two forms ...
<p>Backbone-RMSD clustering with a cutoff of 2.0 Å of all the conformations was performed. Represent...
Figure S1. Overlay of 800-MHz TROSY-HSQC spectra of non-acetylated (black) and acetylated (red) aS, ...
We present ProCS15: a program that computes the isotropic chemical shielding values of backbone and ...
<p>(Left panel) Proportion of NMR constraints satisfied (within a certain tolerance), as a function ...
<p>a) Root-mean-square-deviation of hβ2-AR’s backbone atoms in the MM/CG simulation of hβ2-AR.S-Car ...
Figure S1. Summary of sequential backbone 1HN-1HN NOEs (dNN), secondary Cα chemical shifts at 40 mM ...
<p>(A) Amide chemical shift differences between EF4mut and Ca<sup>2+</sup>-saturated wildtype (CSD =...
The performance of fragment-based ab initio(1)H, (13)C, (15)N and (17)O chemical shift predictions i...