Residue burial encodes a protein’s fold

contact map, and 1.5 times more efficient than the machine-learned embeddings from FoldSeek's 3Di. Even when the folded structure is unavailable, predicting each residue's burial from sequence yields a more accurate estimate of fold quality than predicting pairwise contacts from the same sequence information. Thus, this work emphasizes that the problem of determining a protein's native fold can be re-framed as predicting each residue's core identity.