Nuclear magnetic resonance (NMR) chemical shifts are experimental observables that are available during the first stage of the protein structure determination process. Recently, some methodologies for building structural models of proteins using only these experimental data have been implemented. To assess the potential of these methods for modeling metalloproteins (generally considered a challenging benchmark), we determined the structures of the yeast copper chaperone Atx1 and the CuA domain of Thermus thermophilus cytochrome c oxidase starting from the available chemical shift data. The metal centers were modeled using molecular dynamics simulations with molecular mechanics potentials. The results obtained are evaluated and discussed.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|