The folder contains all the raw data files utilised in this study.

The files are grouped into 15 files. 
1 Figure 1 data	The tripartite ß-lactamase assay (TPBLA)
2 Figure 2 data	Comparison of the structure, stability and amyloid propensity of WT- and D76N-ß2m
3 Figure 3 data	Saturation mutagenesis of ß2m at positions 76, 53 or 98.
4 Figure 4 data	Stability, aggregation and crystal structures of the D76X-ß2m variants.
5 Figure 5 data	Evolving D76N-ß2m to improve its properties.
6 Supplementary Figure 1 data	Antibiotic survival curves for each of the twenty variants of D53X-, D76X-, and D98X-ß2m
7 Supplementary Figure 2 data	Comparison of the effect of Asp to Asn substitutions at residues 53, 76 or 98 in the TPBLA.
8 Supplementary Figure 6 data	Thermal stability and aggregation rates of the twenty D76X-ß2m variants
9 Supplementary Figure 9 data	Residues altered in the D76N-ß2m* library that give rise to enhanced antibiotic resistance in the TPBLA
10 Supplementary Figure 10 data	Unique sequences obtained during D76N-ß2m evolution and selection using the TPBLA.
11 Supplementary Figure 11 data	Prediction of the behaviour of the evolved D76N_X-ß2m variants.
12 Supplementary Figure 12 data	Saturation mutagenesis of D76N-ß2m using Solubis
13 Supplementary Figure 13 data	Characterisation of different D76N_X-ß2m variants.
14 Supplementary Figure 14 data	Comparison of the effect of single point substitutions in the APR for WT- and D76N-ß2m.
15 Supplementary Figure 15 data	Natural evolution of ß2m sequences.