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Job DescriptionP77650
Confidence98.89%DateThu Jan 5 12:31:22 GMT 2012
Rank258Aligned Residues110
% Identity20%Templated1v59a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.20

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


   126...130.........140.........150.........160.........170.........180.........190.........200.....
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Query Sequence  FTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILL
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Template Sequence  IDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQ. IGASMDGEVAKATQKFLKKQGLDFKL
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   165....170.........180.........190.........200.........210....... ..220.........230.........240...
 
   206...210.........220. ........230......
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Query Sequence  NNAIEHVVDGEKVELT. . . . . . . . LQSGETLQADVVIYG
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Template Sequence  STKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVA
Template Known Secondary structure  STTTTTTTTS
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   244.....250.........260.........270.........280..
 
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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