Site entropy mapped to PB1 structure

The influenza virus polymerase is central to influenza virus evolution. Adaptive mutations within the polymerase are often a prerequisite for efficient spread of novel animal-derived viruses in human populations. The polymerase also determines fidelity, and therefore the rate at which the virus will acquire mutations that lead to host range expansion, drug resistance, or antigenic drift. Despite its importance to viral replication and evolution, our understanding of the mutational effects and associated constraints on the influenza RNA-dependent RNA polymerase (RdRp) is relatively limited. We performed deep mutational scanning of the A/WSN/1933(H1N1) PB1, generating a library of 95.4% of amino acid substitutions at 757 sites. After accuracy filters, we were able to measure replicative fitness for 13,354 (84%) of all possible amino acid substitutions, and 13 were validated by results from pairwise competition assays. Functional and structural constraints were better revealed by individua..., The deposited data is a .cxs file, which can be viewed on the UCSF Chimera structural analysis program. Details of the data and analysis are in the manuscript linked to this data., , # Site Entropy Mapped to PB1 Structure

[https://doi.org/10.5061/dryad.p2ngf1vxm](https://doi.org/10.5061/dryad.p2ngf1vxm)

This is a file that allow visualization of site entropy values on the PB1 structure in UCSF Chimera, as described in the accompanying paper