Sequence‐specific resonance assignments in the 1H nuclear‐magnetic‐resonance spectrum of the Lac repressor DNA‐binding domain 1–51 from Escherichia coli by two‐dimensional spectroscopy

Abstract

The assignment of the ¹H nuclear magnetic resonance (NMR) spectrum of the DNA‐binding domain 1–51 of lac repressor from Escherichia coli is described and documented. The assignments are based entirely on the amino acid sequence and on two‐dimensional NMR experiments at 360 MHz and 500 MHz. Individual assignments were obtained at 18 °C for the backbone protons of 44 out of the total of 51 amino acid residues, the exceptions being Met‐1, Lys‐2, Tyr‐7, Arg‐35, Glu‐36, Lys‐37 and Ile‐48. Complete assignments of the non‐labile hydrogen atoms of the side chain were obtained for 33 residues, and for Asn‐46 and Asn‐50 the δ amide protons were also identified. The chemical shifts for the assigned resonances at 18 °C are listed for an aqueous solution at pH 4.9 and at pH 6.8.