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Job DescriptionQ46820
Confidence98.81%DateThu Jan 5 12:34:45 GMT 2012
Rank272Aligned Residues106
% Identity17%Templated1q1ra2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.91

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


   303......310.........320.........330.........340.........350.........360.........370.........380..
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Query Sequence  VSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCE
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Template Sequence  IRRQLIADNRLVVIGGGYIGLEVAATAIKANMHVTLLDTAAR. . . . . . . . VLERVTAPPVSAFYEHLHREAGVDIRTGTQ
Template Known Secondary structure  T

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   142.......150.........160.........170.........180... ......190.........200.........210...
 
   383......390.........400.........410.......
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Query Sequence  IGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHED
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Template Sequence  VC. GFEMSTDQQKVTAVLCEDGTRLPADLVIAGIG
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   214. ....220.........230.........240.......
 
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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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