The crystal structure of the tBuCO‐d,l‐Ala‐Δz‐Phe‐NHiPr dipeptide has been solved by X‐ray diffraction. The peptide crystallizes in monoclinic space group P2JC with a = 13.445 (3) Å, b = 35.088 (4) Å, c = 14.755(3) Å, β= 116.73(1)°, Z = 12 and dc= 1.151 g.cm−3. The three independent molecules per asymmetric unit accommodate a βII‐folded conformation, but only one of them contains the typical i + 3 → i interaction characterizing a β‐turn. In the other two molecules, the N…O distance exceeds 3.2 Å, a value generally considered the upper limit for hydrogen bonds in peptides. In solution, the βII‐turn co