Backbone torsion angles restraints

Using 18 trNOE-derived distance restraints and 13 trCCR-derived backbone torsion angle restraints, structure calculations using distance geometry and simulated annealing [48] resulted in a well-defined structure of the IKK/1-derived peptide bound to NEMO. The backbone structure is displayed in Fig. 7B and is compared with the result of the calculation carried out using the trNOE-derived distance restraints alone. It is obvious from Eig. 7 that only the combination of the trNOE- and trCCR-derived restraints results in the structure elucidation of the bound conformation of this peptide. 

For the majority of NMR structures determined with natural abundance RNA samples, NMR-derived interproton distance information has been utilized in the form of semi-quantitative distance restraints. However, NOE-derived semi-quantitative distance information alone is not sufficient to precisely determine a high resolution structure. For most RNA structures (19), semiquantitative distance restraints are typically augmented with torsion angle information to restrain the ribose moieties and part of the backbone. However, well-defined backbone torsion angle restraints, most of which arise from correlated... 

Backbone cp/ / torsion angle restraints are derived from backbone chemical shift using the program TALOS. 

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