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Job DescriptionQ46820
Confidence96.65%DateThu Jan 5 12:34:45 GMT 2012
Rank415Aligned Residues85
% Identity19%Templated1hyha1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains LDH N-terminal domain-like
Resolution2.20

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


   310.........320.........330.........340.........350.........360.........370.........380.........
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Query Sequence  SEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITF
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Template Sequence  ARKIGIIGLGNVGAAVAHGLIAQGVADDYVFIDA. . . . . . . . . . . . . . . NEAKVKADQIDFQDAMANLEAHGNI. . VIND
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ST

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S...............SGGGSSS

..S
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   21........30.........40.........50.... .....60.........70......... 80...
 
   390.........400.........410.
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Query Sequence  SDLTSEYDAVFIGVGTYGMMRA
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Template Sequence  WAALADADVVISTLGNIKLQQF
Template Known Secondary structure  GGGGTT
S

S
GGGT

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   84.....90.........100.....
 
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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