<p>Supplementary Materials.</p><p>Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA. </p><p>Caroline Smet-Nocca,1* Hélène Launay1, Jean-Michel Wieruszeski,1 Guy Lippens,1 and Isabelle Landrieu1*.</p><p>1 Université de Lille-Nord de France - CNRS UMR 8576, Institut Fédératif de Recherches 147, Villeneuve d'Ascq, France. </p><p>Figure S1</p><p>Figure S1: K values comparison of the exchangeable amide (HN) and the arginine side chain (Hε) protons for the WW (light grey) and the phospho-WW (dark grey).</p><p>1 Figure S2</p><p>Figure S2: Comparison of the modeled phospho-WW structure (blue) and the structure of the WW domain bound to a phospho-peptide substrate (grey). Only the residues of the phospho-binding loop are shown. A pairwise alignment was done based on the Cα atoms of residues S16 to G20.</p><p>2 3</p>