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Job DescriptionP27306
Confidence98.48%DateThu Jan 5 11:43:55 GMT 2012
Rank297Aligned Residues115
% Identity25%Templated1gera2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.86

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


   154.....160.........170.........180.........190.........200.........210.........220.........230...
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Query Sequence  TDVDFTHPRIYDSDSILSMHHEPRHVLIYGAGVIGCEYASIFRGMDVKVDLINTRDRLLAFLDQEMSDSLSYHFWNSGVV
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Template Sequence  DIPGV. . EYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQ
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   147..150. ........160.........170.........180.........190.........200.........210.........220....
 
   234.....240......... 250.........260.........270
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Query Sequence  IRHNEEYEKIEGCDDG. VIMHLKSGKKLKADCLLYANG
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Template Sequence  LHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIG
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   225....230.........240.........250.........260..
 
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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