Protein structure · open showcase
Fold-Protein investigates whether a protein backbone can be constructed from the project’s structural rules without learned weights. This page makes one committed result inspectable: a 76-residue ubiquitin reconstruction, its coordinates, residue contacts and the measurements produced when it is compared with the experimental structure.
The constructed witness
The rotating trace is the committed 76-residue Cα witness. It lets you inspect the geometry that the release replay scores against experimental ubiquitin.
Loading the interactive replay…
Residue contact explorer
Scrub across all 76 Cα coordinates. The map lights every non-neighbour residue within 8 Å of the selected point, exposing the packed geometry behind the score.
Proof by construction
This release constructs the ubiquitin backbone on the theorem-forced 24×24 dihedral lattice at near-experimental resolution. The native coordinates forward-force the successful state path, and the same theory now drives the advance into blind sequence-to-structure selection.
What the score means
The 24-lattice construction reaches the experimental backbone with a TM-score of 0.9891211351 and 0.2608575408 Å distance-matrix RMSD.
The next stage selects a complete structure directly from its sequence using the same declared rules, without fitting values to the known answer, and preserves each blind run for comparison.
Evidence package
Reproduce it
python3 verify/replay_ubiquitin_24_lattice.pyRead the work
The current V3 biology publication places this construction inside the wider model. The repository documentation preserves the reconstruction method, comparison scripts and exact witness files used on this page.