title: Complete sequence-specific 1H nuclear magnetic resonance assignments for the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae.
abstract: The 1H nuclear magnetic resonance (n.m.r.) spectrum of the alpha-amylase inhibitor Tendamistat was completely assigned with the use of phase-sensitive homonuclear two-dimensional n.m.r. The assignments include the non-labile protons of the 74 amino acid residues as well as the labile protons which exchange sufficiently slowly to be observed in H2O solution. The proton chemical shifts are listed at 50 degrees C and pH 3.2, which coincides with the conditions used for the determination of the three-dimensional structure of Tendamistat.
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004578:Electron Spin Resonance Spectroscopy; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D013302:Streptomyces / Q000032:analysis; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate