1aey
From Proteopedia
(New page: 200px<br /><applet load="1aey" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aey" /> '''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTI...) |
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| - | [[Image:1aey.gif|left|200px]]<br /><applet load="1aey" size=" | + | [[Image:1aey.gif|left|200px]]<br /><applet load="1aey" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aey" /> | caption="1aey" /> | ||
'''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES'''<br /> | '''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The assignment of the 1H and 15N nuclear magnetic resonance spectra of the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1AEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | + | 1AEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blanco, F | + | [[Category: Blanco, F J.]] |
| - | [[Category: Ortiz, A | + | [[Category: Ortiz, A R.]] |
[[Category: Serrano, L.]] | [[Category: Serrano, L.]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
| Line 23: | Line 23: | ||
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:45 2008'' |
Revision as of 09:43, 21 February 2008
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ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES
Overview
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.
About this Structure
1AEY is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
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., Blanco FJ, Ortiz AR, Serrano L, J Biomol NMR. 1997 Jun;9(4):347-57. PMID:9255941
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