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Job DescriptionP37596
Confidence99.07%DateThu Jan 5 11:55:42 GMT 2012
Rank187Aligned Residues120
% Identity21%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
 
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   115....120.........130...... ...140.........150.........160.........170.........180.........190..
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Query Sequence  PVPGRELMLTLNSQQEYRACET. . QLRDARRVLIVGGGLIGSELAMDFCRAGKAVTLIDNAASILASLMPPEVSSRLQHR
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Template Sequence  PGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEE
Template Known Secondary structure  TTTTSBS


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   121........130.........140.........150.........160.........170.........180.........190.........200
 
   193......200.........210.........220.........230.....
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Query Sequence  LTEMGVHLLLKSQLQGLEKTDSGIQATLDRQRNIEVDAVIAAT
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Template Sequence  MEANNITIATGETVERYEGDGRVQKV. VTDKNAYDADLVVVAV
Template Known Secondary structure  TTTS


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   201........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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