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224 Skillssecondary

tooluniverse-protein-structural-annotation-pdb

tooluniverse-protein-structural-annotation-pdb

Given a PDB structure, produce a per-residue annotation table: which residues sit at a binding interface (vs a partner chain), which line a ligand pocket, which are buried (core) vs solvent-exposed (surface), and optionally secondary structure. This is the structural track drawn under a DMS heatmap and the structural prior SAE feature drops are read against…

Données et rechercheSKILL.mdZIP complet

tooluniverse-residue-functional-mechanism-interpretation

tooluniverse-residue-functional-mechanism-interpretation

Given a set of residues in a protein, explain WHY they are functionally critical by combining structural context (binding interface, ligand pocket, core, secondary structure), UniProt features (active sites, binding sites, PTM sites, disulfides), optional SAE feature evidence, and optional DMS data. Accepts residues from any source: DMS hotspots (top-K by m…

Données et rechercheSKILL.mdZIP complet

tooluniverse-protein-structural-annotation-pdb

tooluniverse-protein-structural-annotation-pdb

Given a PDB structure, produce a per-residue annotation table: which residues sit at a binding interface (vs a partner chain), which line a ligand pocket, which are buried (core) vs solvent-exposed (surface), and optionally secondary structure. This is the structural track drawn under a DMS heatmap and the structural prior SAE feature drops are read against…

Données et rechercheSKILL.mdZIP complet

tooluniverse-residue-functional-mechanism-interpretation

tooluniverse-residue-functional-mechanism-interpretation

Given a set of residues in a protein, explain WHY they are functionally critical by combining structural context (binding interface, ligand pocket, core, secondary structure), UniProt features (active sites, binding sites, PTM sites, disulfides), optional SAE feature evidence, and optional DMS data. Accepts residues from any source: DMS hotspots (top-K by m…

Données et rechercheSKILL.mdZIP complet
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