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Job DescriptionP0A786
Confidence87.62%DateThu Jan 5 11:05:04 GMT 2012
Rank220Aligned Residues93
% Identity13%Templated1nhpa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

  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...... .
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Query Sequence  LNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMP. . . . . . . . Q
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Template Sequence  IPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGS. . . GYIGIEAAEAFAKA. GKKVTVIDILDRPLGVYLDKEFTD
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TTTTSBS


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   120.........130.........140.........150....... ..160.........170. ........180.........190.....
 
   198.200.........210.........220..
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Query Sequence  YILDMLDEKGIAWSLHSSIEEVMAE
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Template Sequence  VLTEEMEANNITIATGETVERYEGD
Template Known Secondary structure  TTTS


S
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   196...200.........210.........220
 
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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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Lawrence Kelley, Benjamin Jefferys 
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