Fig. 4

NMR data define secondary structure, dynamics and conformational heterogeneity of Ps-LTP1 in solution. From top to bottom: (δΔ) Root from the sum of squared differences in ¹H^N and ¹⁵N^H chemical shifts for the two structural forms. Differences in the ¹⁵N chemical shifts were scaled by factor 0.2. The arbitrary taken cutoff value (0.25 ppm) shows residues subjected to large-amplitude motions in ms time scale. (Helix_p) Probability of helix conformation calculated in TALOS+. The secondary structure of Ps-LTP1 is shown below the protein sequence. The α- and probable 3₁₀-helical elements are shown by white and gray bars, respectively. The helices of the protein are numbered sequentially (H1-H5). The β-turns are denoted by wavy lines. The site of Met11Leu replacement is underlined. (³J_H ^N _H ^α) Large (>8 Hz), small (<6 Hz) and medium (others) J-couplings are indicated by the up pointing black-filled triangles, gray-filled squares, and down pointing open triangles, respectively. (H₂O_EX) Amide protons which demonstrate fast exchange with water protons are shown by filled circles. The corresponding cross-peaks on the water frequency were observed in the 3D 15N-TOCSY-HSQC spectrum (τ_m = 80 ms). (Δδ¹H^N/ΔT) Black-filled stars denote amide protons with temperature gradients less than −4.5 ppb/K. NOE connectivities observed in the 80 ms 3D NOESY spectra are denoted as usual. Steady-state ¹⁵N-{¹H}-NOE values are shown on the bottom of the figure. Residues displaying NOE < 0.7 are subjected to enhanced motions in ps-ns time scale