Abstract

In the crystal structure of the penta­peptide Boc0—Gly1–ΔZPhe2—Gly3–ΔZPhe4—Gly5—OMe, C30H35N5O8, the values of torsion angles Φ and Ψ show the presence of two type III′ β-turns, at the ΔZPhe2 and Gly3 residues, and Gly3 and ΔZPhe4 residues. All amino acids in the peptide are linked trans to each other. Two intra­molecular N—H⋯O hydrogen bonds, between CO and NH groups, stabilize β-turns present in the peptide.

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