NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4
Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin.
RESIDUES 1 TO 20 OF N-TERMINUS OF HA2 SUBUNIT
NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 5
The sequence of the peptide is naturally found in INFLUENZA VIRUS strain X31.
This structure was determined using standard 2D homonuclear
The submitted conformer models are the 20 structures with the lowest energy
the structures are based on a total of 398 restraints, 135 are NOE-derived distance constraints, 58 dihedral angle restraints,
2 mM peptide in the presence of 200 mM d38-DPC in 0.05% NaN3, 5 mM DTT, 20 mM d4-acetic acid, pH 7.4