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1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure

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Abstract

The assignment of the 1H and 15Nnuclear magnetic resonance spectra of the Src-homology region 3 domain ofchicken brain α-spectrin has been obtained. A set of solutionstructures has been determined from distance and dihedral angle restraints,which provide a reasonable representation of the protein structure insolution, as evaluated by a principal component analysis of the globalpairwise root-mean-square deviation (rmsd) in a large set of structuresconsisting of the refined and unrefined solution structures and the crystalstructure. The solution structure is well defined, with a lower degree ofconvergence between the structures in the loop regions than in the secondarystructure elements. The average pairwise rmsd between the 15 refinedsolution structures is 0.71 ± 0.13 Å for the backbone atoms and1.43 ± 0.14 Å for all heavy atoms. The solution structure isbasically the same as the crystal structure. The average rmsd between the 15refined solution structures and the crystal structure is 0.76 Å forthe backbone atoms and 1.45 ± 0.09 Å for all heavy atoms. Thereare, however, small differences probably caused by intermolecular contactsin the crystal structure.

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Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany

    Francisco J. Blanco, Ángel R. Ortiz & Luis Serrano

  2. Department of Pharmacology, University of Alcalá de Henares, E-28871, Madrid, Spain

    Ángel R. Ortiz

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  1. Francisco J. Blanco
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  2. Ángel R. Ortiz
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  3. Luis Serrano
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Blanco, F.J., Ortiz, Á.R. & Serrano, L. 1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure. J Biomol NMR 9, 347–357 (1997). https://doi.org/10.1023/A:1018330122908

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