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   <subfield code="a">The three-dimensional structure of a complex of cinnamycin, a 19-amino acid residue immunopotentiator peptide, and lysophosphatidylethanolamine was determined by 1H-NMR. The complex was cylindrical in shape, 11 Å in diameter and 26 Å in length, excluding the acyl chain of the phospholipid. The peptide had a hydrophobic pocket surrounded by . residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanol-amine head group would be unable to fit the pocket. The goodness of the fitting is compatible with the strict specificity of ligand binding of the peptide.</subfield>
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