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Job DescriptionP08201
Confidence99.65%DateThu Jan 5 11:00:55 GMT 2012
Rank122Aligned Residues122
% Identity28%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


   112.......120.........130.........140.........150.........160.........170.........180.........190.
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Query Sequence  YPWIPPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGE
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Template Sequence  RAREPQIKGKE. . YLLTLRTIFDADRIKESIENSGEAIIIGGGFIGLELAGNLAEAGYHVKLIHRGAMFLG. . LDEELSN
Template Known Secondary structure 
B



SBTGG..G


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   104.....110.... .....120.........130.........140.........150.........160.........170.. .......
 
   192.......200.........210.........220.........230.........240....
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Query Sequence  QLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIVFSTGIR
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Template Sequence  MIKDMLEETGVKFFLNSELLEANEE. . . . . . . GVLTNSGFIEGKVKICAIGIV
Template Known Secondary structure  TT
S


SS.......TT
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   180.........190.........200.... .....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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