Fig. 4
Relaxation rates and backbone dynamics of Pgm(692–768)*. Plots of the 15N R1 a, R2 b relaxation and heteronuclear {1H}-15N NOE c parameters obtained at 950 MHz 1H and 20 °C, using 0.5 mM of the 13C-15N-labeled Pgm(692–768)* domain, as a function of residue number and solution secondary structure. β-sheets are represented as full arrows and α-helices as full rectangles. d Backbone order parameter S2, derived from the chemical shifts, was generated by TALOS+ [40]. e Plot of the local backbone rmsd calculated using the CcpNmr software [41] on the 15 structures (aligned on residues 685–768), as a function of residue number and solution secondary structure. Dynamic parameters were extracted from the 15N relaxation data using the model-free formalism of Lipari-Szabo with an isotropic reorientation model: f amplitude of the picosecond (ps) to nanosecond (ns) time scale motion (S2), g internal correlation time (τε) and h exchange contributions on the microsecond (μs) to millisecond (ms) timescale (Rex). i The structure of the Pgm CRD highlights residues with conformational exchange: (695–702) in pink, (741–755) in dark blue and 8 amino acids from the structured region in light blue. Zinc ions are represented as yellow spheres