Using Tite-Seq, we measured the KD (equilibrium binding dissociation constant) of a combinatorial library based on an anti-influenza broadly neutralizing antibody, CR-9114, to three distinct influenza antigens. This library contains all possible combinations of 16 mutations present in the somatic CR-9114 sequence. The KD for each antigen were measured in biological triplicate. Here the average KD are displayed in a force-directed graph, where each variant (node) is connected to its 16 single-mutation neighbors, with edge weight inversely proportional to change in binding affinity to H1 (edges not shown for clarity) such that variants with similar genotypes and KD will tend to cluster. See below for a video demo of this data browser. See the preprint describing this research here (Research conducted by Angela M Phillips, Katherine R Lawrence, Alief Moulana, Thomas Dupic, Jeffrey Chang, Ivana Cvijovic, Thierry Mora, Aleksandra M Walczak, and Michael M. Desai in the Desai Lab, browser created by Milo Johnson (milo.s.johnson.13 [at] gmail.com)).