Determination of the secondary structure of the DNA binding protein Ner from phage Mu using 1H homonuclear and 15N-1H heteronuclear NMR spectroscopy

Biochemistry. 1989 Jun 13;28(12):5081-9. doi: 10.1021/bi00438a027.


The sequential resonance assignment of the 1H and 15N NMR spectra of the DNA binding protein Ner from phage Mu is presented. This is carried out by using a combination of 1H-1H and 1H-15N two-dimensional experiments. The availability of completely labeled 15N protein enabled us to record a variety of relayed heteronuclear multiple quantum coherence experiments, thereby enabling the correlation of proton-proton through-space and through-bond connectivities with the chemical shift of the directly bonded 15N atom. These heteronuclear experiments were crucial for the sequential assignment as the proton chemical shift dispersion of the Ner protein is limited and substantial overlap precluded unambiguous assignment of the homonuclear spectra in several cases. From a qualitative interpretation of the NOE data involving the NH, C alpha H, and C beta H protons, it is shown that Ner is composed of five helices extending from residues 11 to 22, 27 to 34, 38 to 45, 50 to 60, and 63 to 73.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage mu / analysis
  • Bacteriophage mu / genetics*
  • DNA-Binding Proteins / analysis*
  • Energy Transfer
  • Escherichia coli / analysis
  • Escherichia coli / genetics*
  • Genes, Regulator
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Structure
  • Protein Conformation
  • Repressor Proteins / analysis*
  • Transcription Factors / analysis*
  • Viral Proteins / analysis*
  • Viral Regulatory and Accessory Proteins


  • DNA-Binding Proteins
  • Repressor Proteins
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins