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Job DescriptionO05204
Confidence99.19%DateTue Jul 17 17:05:01 BST 2012
Rank201Aligned Residues111
% Identity18%Templated1lpfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.80

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


   327..330.........340.........350.........360.........370.........380... ......390.........400.
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Query Sequence  LINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKAD. . . . . NVLQDRLRSLSNVDIKTN
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Template Sequence  LSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLG
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   162.......170.........180.........190.........200.........210.........220.........230.........240.
 
   402.......410.........420.........430.........
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Query Sequence  AKTTEVVGEDHVTGIRYEDMNTGEEHLLNLDGIFVQIG
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Template Sequence  ARVTASEVKKKQVTVTFT. . DANGEQKETFDKLIVAVG
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   242.......250......... 260.........270.......
 
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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