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Job DescriptionO05204
Confidence99.81%DateTue Jul 17 17:05:01 BST 2012
Rank115Aligned Residues125
% Identity69%Templated1fl2a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.90

  Insertion relative to template
  Deletion relative to template
  Catalytic residue from the CSA
 
Detailed help on interpreting your alignment


   316...320.........330.........340.........350.........360.........370.........380.........390.....
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Query Sequence  WRKLNIPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKADNVLQDRLRSLSN
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Template Sequence  WRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKLRSLKN
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TTTTTTBTTTS
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   326...330.........340.........350.........360.........370.........380.........390.........400.....
 
   396...400.........410 .........420.........430.........440
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Query Sequence  VDIKTNAKTTEVVGE. DHVTGIRYEDMNTGEEHLLNLDGIFVQIGL
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Template Sequence  VDIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQIGL
Template Known Secondary structure  SSSSSSTTT


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   406...410.........420.........430.........440.........450.
 
Download:Text version

No model constructed - rank, confidence too low




Phyre is for academic use only

Please cite: Protein structure prediction on the web: a case study using the Phyre server
Kelley LA and Sternberg MJE. Nature Protocols 4, 363 - 371 (2009) [pdf] [Import into BibTeX]
 
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Lawrence Kelley, Benjamin Jefferys 
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