In addition to the extended SAS map, we explore the anti-MRSA peptide landscape using a TMAP (Figure ). A TMAP shows the -nearest neighbors of each peptide (represented with a sphere) using as distance metric the MAP fingerprint and the MinHashed algorithm. Namely, the TMAP facilitates the identification and intuitive visualization of compounds (e.g., peptides) structurally related. For example, the pair of peptides AP02565 and AP02566 (pair 1 in Figure ) have a 100% of AA sequence identity and are plotted close to each other. Note, however, that the pair of peptides do not have exactly the same coordinates since the distance that is measured in a TMAP does not depend on the % identity of AA but on an alternative representation that depends on structural fingerprints (vide supra). In contrast, the pair of peptides AP02565 and AP02567 (pair 2 in Figure ) are structurally different e.g., 69% of AA sequence identity and 0.43 fingerprint-based similarity, and are plotted farthest apart as compared to the peptide pair 1. Interestingly, the peptide pairs 1 -5 have a medium-to-high structural similarity (AA sequence identity between 52% -100%) but are associated with a large change in their pMIC 50 values. However, the fingerprint-based similarity values (as measured with MAP4) do have positive correlations with identity values (R 2 = 0.66, Figure in the Supplementary material). This observation suggests that fingerprintbased similarity measures complement the insights derived from sequence alignments, but do not replace them. Namely, it is possible to use the small structural/sequence changes in peptides to help rationalize the P-SPR.