The Structure and Receptor Binding Properties of the 1918 Influenza Hemagglutinin

By S. Gamblin, L. Haire, R. Russell, D. Stevens, B. Xiao, Y. Ha, N. Vasisht, D. Steinhauer, R. Daniels, A. Elliot and 2 more. Science, 2004

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Accurate Measurement of the Effects of All Amino-Acid Mutations on Influenza Hemagglutinin (2016, methodology): “For panels B-G, tolerance is mapped onto PDB structure 1RVX [39].”
Cross-Species Virus Transmission and the Emergence of New Epidemic Diseases (2008, background): “In addition, avian and mammalian viruses infect cells of different tissues and must recognize sialic acids found on cells of the intestinal tracts of waterfowl or in the respiratory tracts of humans or other mammals (37) so that changes in the binding sites can be selected rapidly as the viruses ada”
Influenza: lessons from past pandemics, warnings from current incidents (2005, background): “The three-dimensional structure of the HA of the 1918 virus indicates that, despite retaining the residues in the host-receptor-binding site that are characteristic of an avian precursor H”
The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin (2014, background): “The structure is PDB 1RVX (Gamblin et al., 2004).”
Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses (2009, neutral): “Three-dimensional comparisons of the epitope in the five known crystal structure subtypes (three from group 1 (H1, H5 and H9) and two from group 2 (H3 and H7”
Inferring Stabilizing Mutations from Protein Phylogenies: Application to Influenza Hemagglutinin (2009, neutral): “A/PR/8/34 (H1N1) hemagglutinin (PDB code 1RVZ [107]),”