Blanco F J, Ortiz A R, Serrano L
European Molecular Biology Laboratory, Heidelberg, Germany.
J Biomol NMR. 1997 Jun;9(4):347-57. doi: 10.1023/a:1018330122908.
The assignment of the 1H and 15N nuclear magnetic resonance spectra of the Src-homology region 3 domain of chicken brain alpha-spectrin has been obtained. A set of solution structures has been determined from distance and dihedral angle restraints, which provide a reasonable representation of the protein structure in solution, as evaluated by a principal component analysis of the global pairwise root-mean-square deviation (rmsd) in a large set of structures consisting of the refined and unrefined solution structures and the crystal structure. The solution structure is well defined, with a lower degree of convergence between the structures in the loop regions than in the secondary structure elements. The average pairwise rmsd between the 15 refined solution structures is 0.71 +/- 0.13 A for the backbone atoms and 1.43 +/- 0.14 A for all heavy atoms. The solution structure is basically the same as the crystal structure. The average rmsd between the 15 refined solution structures and the crystal structure is 0.76 A for the backbone atoms and 1.45 +/- 0.09 A for all heavy atoms. There are, however, small differences probably caused by intermolecular contacts in the crystal structure.
已完成鸡脑α-血影蛋白Src同源区域3结构域的1H和15N核磁共振谱的归属。通过距离和二面角约束确定了一组溶液结构，通过对由精制和未精制的溶液结构以及晶体结构组成的大量结构中的全局成对均方根偏差（rmsd）进行主成分分析评估，这些结构为溶液中蛋白质结构提供了合理的表征。溶液结构定义明确，环区域结构之间的收敛程度低于二级结构元件。15个精制溶液结构之间主链原子的平均成对rmsd为0.71±0.13 Å，所有重原子的平均成对rmsd为1.43±0.14 Å。溶液结构与晶体结构基本相同。15个精制溶液结构与晶体结构之间主链原子的平均rmsd为0.76 Å，所有重原子的平均rmsd为1.45±0.09 Å。然而，可能是由晶体结构中的分子间接触引起的微小差异。
