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Job DescriptionP33898
Confidence79.67%DateThu Jan 5 11:52:40 GMT 2012
Rank493Aligned Residues81
% Identity19%Templated1xhca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   3......10.........20.........30..... ....40.........50.. ...... .60.........70.....
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Query Sequence  KVGINGFGRIGRLVLGRLLEVKSNIDVVAINDL. . . TSPKILAYLLKHDSNYG. . . PFPWSV. DFTEDSLIVDGKSIAVY
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Template Sequence  EAIIIGGGFIGLELAGNLAEAGYHVKLIHRGAMFLGLDEELSNMIKDMLEETGVKFFLNSELLEANEEGVLTNSGFIE. .
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   137..140.........150.........160.........170.........180.........190.........200.........210....
 
   76...80.........90.........
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Query Sequence  AEKEAKNIPWKAKGAEIIVECTGF
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Template Sequence  . . . . . . . . . . . . . . GKVKICAIGI
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   215....220....
 
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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