Erratum: Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains (J. Am. Chem. Soc. (2022) 144:31 (14150−14160) DOI: 10.1021/jacs.2c03819)

The Precursor-Arg (PA) dimer model shown in Figure 1 of the main text, which was used for predicting distance distributions (Figure 2, main text) and as a starting point for molecular dynamics simulations (Figure S6), was not generated by the ColabFold implementation of AlphaFold2,1 as stated in the text, but by the SWISS-MODEL2 server (swissmodel.expasy.org). The input sequence was that of Primordial-(HhH)2- Arg,3 and the template structure was the C-terminal (HhH)2- Fold domain from PDB ID 2nrv chain A. To generate a symmetric dimer structure, the first HhH motif of the homology model, which adopts a canonical conformation, was extracted and overlaid onto the second half of the structure. The N-terminal a-helix of each monomer was extended by two residues (Arg1 and Ile2) because these residues were absent from the homology model obtained from the output of SWISS-MODEL. We thank Lars Eicholt for alerting us to the mistake and apologize for the error.