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The six <jats:styled-content style=\"fixed-case\">NMR<\/jats:styled-content>\u2010observable methionine methyl groups in the catalytic domain of human calcineurin A\u03b1 (<jats:styled-content style=\"fixed-case\">CNA<\/jats:styled-content>) were assigned and used as reporters of the presence of potential <jats:italic>cis\u2010trans<\/jats:italic> isomers in solution. Proline 84 is found in the <jats:italic>cis<\/jats:italic> conformation in most calcineurin X\u2010ray structures, and proline 309, which is part of a highly conserved motif in phosphoprotein phosphatases, was modeled with a <jats:italic>cis<\/jats:italic> peptide bond in one of the two molecules present in the asymmetric unit of <jats:styled-content style=\"fixed-case\">CNA<\/jats:styled-content>. We mutated each of the two prolines to alanine to force the <jats:italic>trans<\/jats:italic> conformation. 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