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2knt

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(New page: 200px<br /> <applet load="2knt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2knt, resolution 1.20&Aring;" /> '''THE 1.2 ANGSTROM ST...)
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'''THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5'''<br />
'''THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5'''<br />
==Overview==
==Overview==
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The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain, was previously described at 1.6 A resolution at room temperature. By, changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of, the same space group at 291 K. The protein-water-ion model has been, refined anisotropically against these new data using the program SHELXL93;, the results converged to an R factor of 15.0%, with all data between 7 and, 1.2 A. The final electron-density map reveals a clear chain tracing with a, few disordered residues and five residues out of 58 that present alternate, conformations. The Cys14-Cys38 bond presents the less frequently observed, left-hand conformation (chi1 = -60 degrees). The solvent molecules and a, phosphate ion are well ordered with an average B of 38 A2. The, high-resolution structure reveals the N and C termini which were missing, from the 1.6 A structure.
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The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2KNT 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=2KNT OCA].
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2KNT 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=2KNT 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 22:58:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:53 2008''

Revision as of 16:06, 21 February 2008


2knt, resolution 1.20Å

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THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5

Contents

Overview

The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.

Disease

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

About this Structure

2KNT is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen., Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897

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