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Job DescriptionP37596
Confidence99.14%DateThu Jan 5 11:55:42 GMT 2012
Rank182Aligned Residues122
% Identity32%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


   110.........120.........130.........140.........150.........160.........170.........180.........
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Query Sequence  SAFVPPVPGRELMLTLNSQQEYRACETQLRDARRVLIVGGGLIGSELAMDFCRAGKAVTLIDNAASILASLMPPEVSSRL
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Template Sequence  RAREPQIKGKEYLLTLRTIFDADRIKESIENSGEAIIIGGGFIGLELAGNLAEAGYHVKLIHRGAMFLG. . LDEELSNMI
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B



SBTGGG


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   104.....110.........120.........130.........140.........150.........160.........170.. .......180.
 
   190.........200.........210.........220.........230........
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Query Sequence  QHRLTEMGVHLLLKSQLQGLEKTDSGIQATLDRQRNIEVDAVIAATGLR
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Template Sequence  KDMLEETGVKFFLNSELLEANEEG. . . . . VLTNSGFIEGKVKICAIGIV
Template Known Secondary structure  TT
S


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   182.......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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