Protein 3D structure determination using computational/experimental hybrid methods allows smart information usage by combining molecular modelling with minimal sets of structural data from a range of biochemical and biophysical experiments. Paramagnetic lanthanide ions are particularly attractive probes to generate such data by NMR spectroscopy, because they provide structural restraints which are orientation dependent and long-range (up to 40 Angstrom from the metal centre) due to the strong interaction of the unpaired electron(s) with nuclei in the protein.
The focus of this talk will be on protein 3D structure determination by assembling super-secondary structure motifs with the help of pseudocontact shift (PCS) restraints for backbone amide protons, where the PCSs are produced from different metal centres. I will show successes and pitfalls of the new assembly algorithm, and discuss how the sparsity of data affects model quality.