title: Protein structure determination from pseudocontact shifts using ROSETTA.
abstract: Paramagnetic metal ions generate pseudocontact shifts (PCSs) in nuclear magnetic resonance spectra that are manifested as easily measurable changes in chemical shifts. Metals can be incorporated into proteins through metal binding tags, and PCS data constitute powerful long-range restraints on the positions of nuclear spins relative to the coordinate system of the magnetic susceptibility anisotropy tensor (Δχ-tensor) of the metal ion. We show that three-dimensional structures of proteins can reliably be determined using PCS data from a single metal binding site combined with backbone chemical shifts. The program PCS-ROSETTA automatically determines the Δχ-tensor and metal position from the PCS data during the structure calculations, without any prior knowledge of the protein structure. The program can determine structures accurately for proteins of up to 150 residues, offering a powerful new approach to protein structure determination that relies exclusively on readily measurable backbone chemical shifts and easily discriminates between correctly and incorrectly folded conformations.
authors.affiliation: School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD 4072, Australia.
authors.forename: Christophe
authors.initials: C
authors.lastname: Schmitz
authors.forename: Robert
authors.initials: R
authors.lastname: Vernon
authors.forename: Gottfried
authors.initials: G
authors.lastname: Otting
authors.forename: David
authors.initials: D
authors.lastname: Baker
authors.forename: Thomas
authors.initials: T
authors.lastname: Huber
mesh_terms: D016880:Anisotropy; D008280:Magnetics / Q000379:methods; D008670:Metals / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D008670:Metals; D011506:Proteins