Fig. 5: Excerpts of the MurD regions with a salient pattern of conformational exchange and fast ps-ns dynamics.

The excerpted regions are shown for the MurD_apo on the X-ray structure of open conformation (PDB 1E0D²¹) with observed conformational exchange dynamics on μs-ms time scale identified by CPMG-RD (backbone in yellow and amide nitrogen in yellow spheres) and with increased fast ps-ns dynamics assigned to G1 group (backbone in orange). Yellow spheres on orange backbone indicate the amide nitrogen of residues with identified conformational exchange on μs-ms time scale and increased fast dynamics. Residues shown in white indicate unavailable data. The closed structure (in transparent cyan, PDB 2XPC¹¹) is overlaid over CeD. Regions shown: i) β-sheet (β15-β16-β20-β17-β18-β19) in the CTD, (ii) CTD with highlighted helices (α12, α13 and α14) and loops (α12-β17, α13-β18 and α14-β19) (iii) β−meander (β12-β13-β14) in the CeD, (iv) uracil-binding pocket (β1, β2, β1-α1, β2-α2, β3-α3 and β4-α4) with a potentially bound inhibitor shown in green. Representative CPMG-RD plots are shown, illustrating μs-ms dynamics (k_ex) for residues from each region. R₂^eff represents the effective transverse relaxation rate at each refocusing pulse train frequency (ν_CPMG). The errors in the R₂^eff values were determined based on the uncertainties of the peak intensities estimated from the background noise level of the spectra.