Fig. 5: The L-Lys(D-iAsn) residue is necessary and sufficient for PBP5 binding. | Nature Communications

Fig. 5: The L-Lys(D-iAsn) residue is necessary and sufficient for PBP5 binding.

From: Peptidoglycan recruitment by a penicillin binding protein

Fig. 5: The L-Lys(D-iAsn) residue is necessary and sufficient for PBP5 binding.

a Overlay of 2D [1H,15N] TROSY spectrum of PBP5 (black) with SP4 (1:80 ratio; red). b 1H/15N and c 1H/13C ILV methyl CSPs vs residue number plot for PBP5:SP4 (1:80 ratio); average+1σ (red line) for the PBP5 TP domain. d SP4 CSPs mapped on PBP5 structure (gray surface, PDBid: 6MKA); orange surface: residues with significant changes (underlined residues indicate 1H/13C ILV methyl data). S422 is highlighted in red. e Molecular structure of SP4, with yellow circles indicating the 1H atoms with >50% saturation transfer difference (STD) enhancement. f Overlay of 2D [1H,15N] TROSY spectrum of PBP5 (black) with SP5 (1:80 ratio; red). g 1H/15N and h 1H/13C ILV methyl CSPs vs residue number plot for PBP5:SP5 (1:80 ratio); average+1σ (red line) for the PBP5 TP domain. i SP5 CSPs mapped on PBP5 structure (gray surface, PDBid: 6MKA); orange surface: residues with significant changes (underlined residues indicate 1H/13C ILV methyl data). S422 is highlighted in red. j Molecular structure of SP5, with yellow circles indicating the 1H atoms with >50% saturation transfer difference (STD) enhancement.

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