1aey: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1aey.gif|left|200px]]<br /><applet load="1aey" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1aey" />
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'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEY OCA].  
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.J.]]
[[Category: Blanco, F J.]]
[[Category: Ortiz, A.R.]]
[[Category: Ortiz, A R.]]
[[Category: Serrano, L.]]
[[Category: Serrano, L.]]
[[Category: calcium-binding]]
[[Category: calcium-binding]]
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[[Category: sh3 domain]]
[[Category: sh3 domain]]


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