1fia

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[[Image:1fia.png|left|200px]]
[[Image:1fia.png|left|200px]]
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{{STRUCTURE_1fia| PDB=1fia | SCENE= }}
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===CRYSTAL STRUCTURE OF THE FACTOR FOR INVERSION STIMULATION FIS AT 2.0 ANGSTROMS RESOLUTION===
===CRYSTAL STRUCTURE OF THE FACTOR FOR INVERSION STIMULATION FIS AT 2.0 ANGSTROMS RESOLUTION===
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{{ABSTRACT_PUBMED_1619650}}
{{ABSTRACT_PUBMED_1619650}}
==About this Structure==
==About this Structure==
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1FIA is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIA OCA].
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[[1fia]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIA OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:1619650</ref><references group="xtra"/>
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<ref group="xtra">PMID:001619650</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Choe, H W.]]
[[Category: Choe, H W.]]
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[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
[[Category: Dna-binding protein]]
[[Category: Dna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:16:47 2009''
 

Revision as of 10:12, 21 November 2012

Template:STRUCTURE 1fia

CRYSTAL STRUCTURE OF THE FACTOR FOR INVERSION STIMULATION FIS AT 2.0 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1619650

About this Structure

1fia is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Kostrewa D, Granzin J, Stock D, Choe HW, Labahn J, Saenger W. Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. J Mol Biol. 1992 Jul 5;226(1):209-26. PMID:1619650
  • Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid-binding motif. Proteins. 2004 May 1;55(2):330-8. PMID:15048824 doi:10.1002/prot.10630

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