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. 2021 Aug 14;50(D1):D488–D496. doi: 10.1093/nar/gkab651

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Screenshots taken from the page of entry DRAMP21495. (A) Enclosed alphanumeric in the sequence is 2-(4′-pentenyl) alanine in the S configuration according to the description, which is the stapling amino acid. Such two amino acids are bridged by hydrocarbon stapling. In the red box is the discrepant part comparing with general entries. (B) Helical wheel diagrams of stapled peptides in DRAMP3.0. The ‘X’ represents stapling amino acid and the black fold line is the staple connecting them. (C) Visualization of 3D predicted structure of stapled peptides in DRAMP 3.0. The green ribbons represent the stapling amino acids, and the green bond is the bridge linking two residues of stapling amino acids.

Inline graphic — Screenshots taken from the page of entry DRAMP21495. (A) Enclosed alphanumeric in the sequence is 2-(4′-pentenyl) alanine in the S configuration according to the description, which is the stapling amino acid. Such two amino acids are bridged by hydrocarbon stapling. In the red box is the discrepant part comparing with general entries. (B) Helical wheel diagrams of stapled peptides in DRAMP3.0. The ‘X’ represents stapling amino acid and the black fold line is the staple connecting them. (C) Visualization of 3D predicted structure of stapled peptides in DRAMP 3.0. The green ribbons represent the stapling amino acids, and the green bond is the bridge linking two residues of stapling amino acids.