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Job DescriptionP08201
Confidence99.42%DateThu Jan 5 11:00:55 GMT 2012
Rank153Aligned Residues117
% Identity22%Templated1v59a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.20

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


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Query Sequence  PPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLRR
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Template Sequence  PGIE. IDEEKIVSSTGALSLKEI. . . . . . PKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGAS. MDGEVAKATQK
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   161... .....170.........180.. .......190.........200.........210.........220. ........230..
 
   196...200.........210.........220......... 230.........240
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Query Sequence  KIESMGVRVHTSKNTLEIVQEGVEARKTMRFADG. . . . . SELEVDFIVFS
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Template Sequence  FLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVA
Template Known Secondary structure  TT

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   233......240.........250.........260.........270.........280..
 
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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