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Job DescriptionP17952
Confidence96.60%DateThu Jan 5 11:36:25 GMT 2012
Rank157Aligned Residues84
% Identity18%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


   4.....10.........20.........30.........40.........50.... .....60.........70...
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Query Sequence  QQLAKLRSIVPEMRRVRHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPN. . . . . . . . . . PVTQQLMNLGATIYFNHRP
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Template Sequence  RTIFDADRIKESIENSGEAIIIGGGFIGLEL. AGNLAEAGYHVKLIHRGAMFLGLDEELSNMIKDMLEETGVKFFLNSEL
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   120.........130.........140.........150 .........160.........170.........180.........190........
 
   74.... .80........
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Query Sequence  ENVRD. . . . . . . . . . . ASVVVVSSAI
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Template Sequence  LEANEEGVLTNSGFIEGKVKICAIGI
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   199200.........210.........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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