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Job DescriptionP77212
Confidence98.38%DateThu Jan 5 12:26:22 GMT 2012
Rank303Aligned Residues114
% Identity26%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


   135....140.........150.........160.........170.........180.........190.........200.........210....
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Query Sequence  PIPGITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGV
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Template Sequence  DIPGVEYG. . . IDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGP
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TTGGGS...B
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   147..150.... .....160.........170.........180.........190.........200.........210.........220...
 
   215....220.........230... ......240.........250.
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Query Sequence  DIILNAHVERISHHENQVQ. . VHSEHAQLAVDALLIASG
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Template Sequence  QLHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIG
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   224.....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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