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Job DescriptionO52582
Confidence98.98%DateTue Jul 17 17:05:03 BST 2012
Rank205Aligned Residues119
% Identity19%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


   119120.........130.........140.........150.........160.........170.........180.... .....190.......
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Query Sequence  SLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLNERGLHPTLIHRSDKIN. KLMDADMNQPILD
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Template Sequence  IPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTE
Template Known Secondary structure 
TTTTSBS


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STT
SSSSTTTTT

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   120.........130.........140.........150.........160.........170.........180.........190.........
 
   198.200.........210........ .220.........230.......
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Query Sequence  ELDKREIPYRLNEEINAINGN. . . EITFKSGKVEHYDMIIEGV
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Template Sequence  EMEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVVAV
Template Known Secondary structure  TTTS


SSB

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   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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