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Job DescriptionP08201
Confidence99.68%DateThu Jan 5 11:00:55 GMT 2012
Rank119Aligned Residues129
% Identity19%Templated1q1ra2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.91

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


   114.....120. ........130.........140.........150.........160.........170.........180.........190
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Query Sequence  WIPPIKGS. . . DTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGG
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Template Sequence  RPLPVASGAVGKANNFRYLRTLEDAECIRRQLIADNRLVVIGGGYIGLEVAATAIKANMHVTLLDTAARVLERVTAPPVS
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GGGTTSTTSSST

TT


STT

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   115....120.........130.........140.........150.........160.........170.........180.........190....
 
   191........200.........210... ......220.........230.........240..
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Query Sequence  EQLRRKIESMGVRVHTSKNTLEI. VQEGVEARKTMRFADGSELEVDFIVFSTG
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Template Sequence  AFYEHLHREAGVDIRTGTQVCGFEMSTDQQKVTAVLCEDGTRLPADLVIAGIG
Template Known Secondary structure  T

S


TTT

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   195....200.........210.........220.........230.........240.......
 
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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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