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Job DescriptionP35340
Confidence98.75%DateWed Jan 25 15:20:51 GMT 2012
Rank277Aligned Residues105
% Identity12%Templated1feca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.70

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


   342.......350.........360.........370......... 380.........390... ......400.........410...
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Query Sequence  VTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVE. . . HVTLLEFAPEMKAD. . . . . QVLQDKLRSLKNVDIILNAQ
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Template Sequence  CITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTHEN
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   174.....180.........190.........200.........210.........220.........230.........240.........250...
 
   414.....420.........430.........440.........450.
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Query Sequence  TTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQIGL
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Template Sequence  PAKVTKNADGTRHVVF. . . . . ESGAEADYDVVMLAIGR
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   254.....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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