1AEY
ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES
Summary for 1AEY
| Entry DOI | 10.2210/pdb1aey/pdb |
| Descriptor | ALPHA-SPECTRIN (1 entity in total) |
| Functional Keywords | cytoskeleton, capping protein, calcium-binding, duplication, sh3 domain |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cytoplasm, cytoskeleton: P07751 |
| Total number of polymer chains | 1 |
| Total formula weight | 7229.24 |
| Authors | Blanco, F.J.,Ortiz, A.R.,Serrano, L. (deposition date: 1997-03-02, release date: 1997-05-15, Last modification date: 2024-05-22) |
| Primary citation | Blanco, F.J.,Ortiz, A.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 Cited by PubMed Abstract: 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. PubMed: 9255941DOI: 10.1023/A:1018330122908 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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