1kth

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(New page: 200px<br /> <applet load="1kth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kth, resolution 0.95&Aring;" /> '''The Anisotropic Ref...)
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'''The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom'''<br />
'''The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom'''<br />
==Overview==
==Overview==
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The C-terminal Kunitz-type domain from the alpha3 chain of human type VI, collagen (C5), a single amino-acid residue chain with three disulfide, bridges, was refined at 0.9 A resolution in a monoclinic form, space group, P2(1) with one molecule per asymmetric unit, using data collected at, cryogenic temperature (110 K). The average protein factor decreases from, 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The, different structural motifs of C5 were analyzed in terms of rigid-body, displacement (TLS analyses) and show dominant libration motion for the, secondary structure.
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The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1KTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KTH OCA].
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1KTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTH OCA].
==Reference==
==Reference==
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[[Category: kunitz inhibitor]]
[[Category: kunitz inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:54:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:45 2008''

Revision as of 11:37, 21 February 2008


1kth, resolution 0.95Å

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The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom

Contents

Overview

The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.

Disease

Known diseases associated with this structure: Bethlem myopathy OMIM:[120250], Ullrich congenital muscular dystrophy OMIM:[120250]

About this Structure

1KTH is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A)., Arnoux B, Ducruix A, Prange T, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1252-4. Epub 2002, Jun 20. PMID:12077460

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