As the virus will continue to evolve, new mutations will become available and the best way we have found to allow quick mapping and update of new sequence variation in respect to drug and antibody binding sites is to give full access to users/readers via a 3D structure visualization tool at the supplementary webpage http://mendel.bii.astar.edu.sg/SEQUENCES/H1N1/ (instructions to map new mutations are given, including an example). The key finding in the paper is that the binding cavity for neuraminidase inhibitors is unaffected as suggested by molecular modeling. This finding is of significance in the current situation of an outbreak with pandemic potential. However, one issue needs to be highlighted in this regard -mutations far away from the binding site can potentially affect the shape and or binding affinity of the binding pocket. These are not always captured by homology models, especially the issue of affinity. In principle, authors could use a conservation patterns or co-evolution measures (e.g. as in PMID: 10514373) to determine if there are interaction chains that might connect distant residues to the active site. In the least it would be useful to provide the caveat of distant changes affecting affinity in the current paper.