caa a22 4500 477136524 CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970601xx s 000 0 eng 10.1023/A:1018330122908 doi (NATIONALLICENCE)springer-10.1023/A:1018330122908 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 [Elektronische Daten] [Francisco Blanco, Ángel Ortiz, Luis Serrano] 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. Kluwer Academic Publishers, 1997 Protein structure nationallicence SH3 domain nationallicence Spectrin nationallicence Principal component analysis nationallicence Blanco Francisco European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut Ortiz Ángel European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut Serrano Luis European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/4(1997-06-01), 347-357 0925-2738 9:4<347 1997 9 10858 https://doi.org/10.1023/A:1018330122908 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018330122908 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Blanco Francisco European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut NATIONALLICENCE 700 1- Ortiz Ángel European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut NATIONALLICENCE 700 1- Serrano Luis European Molecular Biology Laboratory, Meyerhofstrasse 1, D- 69012, Heidelberg, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/4(1997-06-01), 347-357 0925-2738 9:4<347 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer