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Job DescriptionP00393
Confidence99.20%DateThu Jan 5 10:56:36 GMT 2012
Rank165Aligned Residues178
% Identity18%Templated1trba1
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


   166...170.........180.........190.........200.........210.........220.... .....230.........240....
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Query Sequence  GANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPAL. PPRISAAAHNELTKLGVRVL
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Template Sequence  GTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEII
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SSTTGGGGG
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   245....250....... ..260.........270.........280.........290 ......... 300.........310....
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Query Sequence  TQTMVTSADEGGL. . HTKDGEYIEADLMVWAAGIKAPDFLKDIGGLET. . . NRINQLVVE. . . . . PTLQTTRDPDIYAIG
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Template Sequence  FDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYHSPNTAIFEGQLELENGYIKVQSGIHGNATQT. SIPGVFAAG
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GGGTTTS
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   81........90.........100.........110.........120.........130.........140.........150 .........
 
   315....320.........330.........340.........350.
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Query Sequence  DCASCPRPEGGFVPPRAQAAHQMATCAMNNILAQMNG
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Template Sequence  DVMD. . . . . . . HIYRQAITSAGTGCMAALDAERYLDG
Template Known Secondary structure  GGG
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   286... 290.........300.........310.....
 
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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