4cpv
From Proteopedia
(New page: 200px<br /><applet load="4cpv" size="450" color="white" frame="true" align="right" spinBox="true" caption="4cpv, resolution 1.5Å" /> '''REFINED CRYSTAL STRUC...) |
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| - | [[Image:4cpv.gif|left|200px]]<br /><applet load="4cpv" size=" | + | [[Image:4cpv.gif|left|200px]]<br /><applet load="4cpv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4cpv, resolution 1.5Å" /> | caption="4cpv, resolution 1.5Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF CALCIUM-LIGANDED CARP PARVALBUMIN 4.25 AT 1.5-ANGSTROMS RESOLUTION'''<br /> | '''REFINED CRYSTAL STRUCTURE OF CALCIUM-LIGANDED CARP PARVALBUMIN 4.25 AT 1.5-ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of carp parvalbumin (pI = 4.25) has been refined by | + | The crystal structure of carp parvalbumin (pI = 4.25) has been refined by restrained least-squares analysis employing X-ray diffractometer data to 1.5-A resolution. The final residual for 12,653 reflections between 10 and 1.5 A with I(hkl) greater than 2 sigma(I) is 0.215. A total of 74 solvent molecules were included in the least-squares analysis. The root mean square deviation from ideality of bond lengths is 0.024 A. The model has a root mean square difference of 0.59 A from the positions of the main-chain atoms in a previously reported structure [Moews, P. C., & Kretsinger, R. H. (1975) J. Mol. Biol. 91, 201-228], which was refined by difference Fourier syntheses using data collected by film to 1.9 A. Although the overall features of the two models are very similar, there are significant differences in the amino-terminal region, which was extensively refit, and in the number of oxygen atoms liganding calcium in the CD and EF sites, which increased from six to seven in the CD site and decreased from eight to seven in the EF site. |
==About this Structure== | ==About this Structure== | ||
| - | 4CPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 4CPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CPV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cyprinus carpio]] | [[Category: Cyprinus carpio]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Edwards, B | + | [[Category: Edwards, B F.P.]] |
| - | [[Category: Kumar, V | + | [[Category: Kumar, V D.]] |
[[Category: Lee, L.]] | [[Category: Lee, L.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: calcium binding]] | [[Category: calcium binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:12:59 2008'' |
Revision as of 17:13, 21 February 2008
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REFINED CRYSTAL STRUCTURE OF CALCIUM-LIGANDED CARP PARVALBUMIN 4.25 AT 1.5-ANGSTROMS RESOLUTION
Overview
The crystal structure of carp parvalbumin (pI = 4.25) has been refined by restrained least-squares analysis employing X-ray diffractometer data to 1.5-A resolution. The final residual for 12,653 reflections between 10 and 1.5 A with I(hkl) greater than 2 sigma(I) is 0.215. A total of 74 solvent molecules were included in the least-squares analysis. The root mean square deviation from ideality of bond lengths is 0.024 A. The model has a root mean square difference of 0.59 A from the positions of the main-chain atoms in a previously reported structure [Moews, P. C., & Kretsinger, R. H. (1975) J. Mol. Biol. 91, 201-228], which was refined by difference Fourier syntheses using data collected by film to 1.9 A. Although the overall features of the two models are very similar, there are significant differences in the amino-terminal region, which was extensively refit, and in the number of oxygen atoms liganding calcium in the CD and EF sites, which increased from six to seven in the CD site and decreased from eight to seven in the EF site.
About this Structure
4CPV is a Single protein structure of sequence from Cyprinus carpio with and as ligands. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution., Kumar VD, Lee L, Edwards BF, Biochemistry. 1990 Feb 13;29(6):1404-12. PMID:2334704
Page seeded by OCA on Thu Feb 21 19:12:59 2008
Categories: Cyprinus carpio | Single protein | Edwards, B F.P. | Kumar, V D. | Lee, L. | ACE | CA | Calcium binding
