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. 2020 Nov 24;11:598789. doi: 10.3389/fmicb.2020.598789

FIGURE 5.

FIGURE 5

(A) Summary of inter-residue Nuclear Overhauser Effects (NOEs) and prediction of secondary structure of CMB001 using 1Hα chemical shifts. The sequence of CMB001 is depicted on top of the graphics with thioether links in brackets and the lanthionine ring topology is labeled by the capital letters (A–E). dA stands for 2,3-didehydroalanine, dB stands for (Z)-2,3-didehydobutyrine, and Ab stands for α-aminobutyric acid. Legend labels are as follows: dαN indicates residues with Hα (i) to HN (i + 1) NOE connections, dNN indicates residues with HN (i) to HN (i + 1) NOE connections, dβN indicates residues with Hβ (i) to HN (i + 1) NOE connections, dαN (i,i + 3) indicates residues with Hα (i) to HN (i + 3) NOE connections, dαβ (i,i + 3) indicates residues with Hα (i) to Hβ (i + 3) NOE connections, dαN (i,i + 4) indicates residues with Hα (i) to HN (i + 4) NOE connections, dNN indicates residues with HN (i) to HN (i + 2) NOE connections, dαN (i,i + 2) indicates residues with Hα (i) to HN (i + 2) NOE connections, Δδ(1Hα) indicates 1Hα difference in chemical shift to sequence adjusted random coil chemical shift for residue type, Chemical Shift Index (CSI) indicates CSI values for residues where −1 indicates α-helix, and +1 indicates β-sheet. For the (i,i + 1) NOE connections, the thickness of the bar indicates the intensity of the NOE cross peak. At the bottom of the graphics, the secondary structure for the peptide is shown. (B) Amino acid sequence alignments between CMB001 and two closest lantibiotics, subtilin and nisin. Amino acids unique for CMB001 are shown in bold text.