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Job DescriptionP00393
Confidence98.62%DateThu Jan 5 10:56:36 GMT 2012
Rank234Aligned Residues104
% Identity17%Templated1trba2
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


   155....160.........170.........180.........190.........200.........210.........220.........230....
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Query Sequence  LNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPALPPRISAAAHN
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Template Sequence  RGVSACATSDGFFYRNQKVAVIGGGNTAVEEALYLSNI. . . . . . . . . . . . . . . ASEVHLIHRRDGF. . RAEKILIKRLMD
Template Known Secondary structure  TTS
GGGGTTS
SSTTT...............SS
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   130.........140.........150.........160....... ..170.........180 .........190..
 
   235....240.........250..... ....260.... .....270.....
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Query Sequence  ELTKLGVRVLTQTMVTSADEG. . . . . GLHTKDGEY. . . . . . IEADLMVWAAG
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Template Sequence  KVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIG
Template Known Secondary structure  TSS
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   193......200.........210.........220.........230.........240....
 
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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