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1xnb

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[[Image:1xnb.png|left|200px]]
[[Image:1xnb.png|left|200px]]
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{{STRUCTURE_1xnb| PDB=1xnb | SCENE= }}
{{STRUCTURE_1xnb| PDB=1xnb | SCENE= }}
===HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS===
===HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS===
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{{ABSTRACT_PUBMED_008890913}}
==About this Structure==
==About this Structure==
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1XNB is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNB OCA].
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[[1xnb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNB OCA].
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==Reference==
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<ref group="xtra">PMID:008890913</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/>
[[Category: Bacillus circulans]]
[[Category: Bacillus circulans]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Campbell, R L.]]
[[Category: Campbell, R L.]]
[[Category: Glycosidase]]
[[Category: Glycosidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:14:14 2009''
 

Revision as of 13:12, 5 January 2013

Template:STRUCTURE 1xnb

HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS

Template:ABSTRACT PUBMED 008890913

About this Structure

1xnb is a 1 chain structure with sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

  • Krengel U, Dijkstra BW. Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum. J Mol Biol. 1996 Oct 18;263(1):70-8. PMID:8890913 doi:http://dx.doi.org/10.1006/jmbi.1996.0556
  • Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
  • Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1

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