title: A new approach for applying residual dipolar couplings as restraints in structure elucidation.
abstract: Residual dipolar couplings are useful global structural restraints. The dipolar couplings define the orientation of a vector with respect to the alignment tensor. Although the size of the alignment tensor can be derived from the distribution of the experimental dipolar couplings, its orientation with respect to the coordinate system of the molecule is unknown at the beginning of structure determination. This causes convergence problems in the simulated annealing process. We therefore propose a protocol that translates dipolar couplings into intervector projection angles, which are independent of the orientation of the alignment tensor with respect to the molecule. These restraints can be used during the whole simulated annealing protocol.
authors.affiliation: Universität Frankfurt, Institut für Organische Chemie, Frankfurt am Main, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Meiler
authors.forename: N
authors.initials: N
authors.lastname: Blomberg
authors.forename: M
authors.initials: M
authors.lastname: Nilges
authors.forename: C
authors.initials: C
authors.lastname: Griesinger
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry; D029742:Caenorhabditis elegans Proteins; D004926:Escherichia coli / Q000378:metabolism; D015801:Helminth Proteins / Q000737:chemistry / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry; D008958:Models, Molecular; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017434:Protein Structure, Tertiary
chemical_list: D000596:Amino Acids; D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; D019476:Insect Proteins; D009124:Muscle Proteins; C098932:Unc-89 protein, C elegans; C082506:rhodniin protein, Rhodnius