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. 2012 Jun 18;13(6):7532–7549. doi: 10.3390/ijms13067532

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© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Distributions of the predicted ligand-interacting residues in the primary structure of ALG-2. ALG-2 amino acid residues predicted to interact with the virtual peptide N-acetyl-ProAlaProGlyPhe-amide are colored in red, cyan and purple for hydrophobic interactions, hydrogen bonds and both, respectively. Each helix-loop-helix structural motif of EF-hands is marked from EF1 to EF5. Eight α-helices (α1 to α8) and one β-sheet are indicated by orange bars and a dark orange arrow above the sequences. Calcium ions are coordinated with oxygen atoms at positions x, y, z, −y and −z from amino acid residues and with an oxygen atom at position −x from the neighboring water molecule.