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![[Figure 5]](ba5251fig5mag.jpg)
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Figure 5
A peptide molecule that appears to be projected from the binding site of a noncrystallographic symmetry (NCS)-related copy. Shown are electron-density maps from the 1.9 Å resolution structure of concanavalin A in complex with a glycomimetic peptide (PDB entry 4czs). Two peptide molecules (chains E and F; ranks 3105 and 2528) are well traceable in electron density [chain E is shown in (a)], while chains G and H (rank 254 and 99, respectively) are only partly visible in electron density [chain H is shown in (b)] (Ng et al., 2015  ). The original publication shows only a surface rendering with a ball-and-stick model of the glycopeptide (unspecified chain ID, without electron density). |
![[Figure 5]](ba5251fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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