Fig. 2
From: Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
P4P5 domains in liposomes compared to free solution. a Topology and secondary structural elements determined using TALOS+ (BMRB 19928) depicted above the sequence for the P4P5 domains. Upper sequence: Residues identified in 1H-detected ssNMR spectra (green and bold), those replaced with dash (-) do not appear in the spectra within 1 ppm of their solution NMR assignment. Residues replaced with asterisks (*) show weak signals. Lower sequence: Residues replaced with asterisks (*) show dynamics as judged by 15N CPMG relaxation (solution NMR). Residues replaced with a dash (-) could not be assigned in solution. b Rex plotted on the crystal structure of P4P5 (PDB 3Q6B). Box in the top left indicates the extent of chemical exchange. Adapted from Structure, 23, Sinnige, T. et al., Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA, 1317–1324, copyright (2015) with permission from Elsevier35. c P4P5 residues that are not present at the solution NMR assignment in liposomes, in both the CαNH and the CONH ssNMR spectra (red) plotted on the crystal structure (PDB 5D0O), in light red are residues with weak ssNMR intensity and in black are those which were not assigned in solution
