title: Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints.
abstract: We report the determination of the global fold of human ubiquitin using protein backbone NMR residual dipolar coupling and long-range nuclear Overhauser effect (NOE) data as conformational restraints. Specifically, by use of a maximum of three backbone residual dipolar couplings per residue (Ni-H N i, Ni-C'(i-1), H N i - C'(i-1)) in two tensor frames and only backbone H N -H N NOEs, a global fold of ubiquitin can be derived with a backbone root-mean-square deviation of 1.4 A with respect to the crystal structure. This degree of accuracy is more than adequate for use in databases of structural motifs, and suggests a general approach for the determination of protein global folds using conformational restraints derived only from backbone atoms.
authors.affiliation: Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology University of Leeds, LS2 9JT UK.
authors.forename: Alexander W
authors.initials: AW
authors.lastname: Giesen
authors.forename: Steve W
authors.initials: SW
authors.lastname: Homans
authors.forename: Jonathan Miles
authors.initials: JM
authors.lastname: Brown
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008280:Magnetics; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D011506:Proteins; D025801:Ubiquitin