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Job DescriptionP17109
Confidence88.62%DateThu Jan 5 11:35:57 GMT 2012
Rank123Aligned Residues112
% Identity12%Templated1efva2
SCOP infoDHS-like NAD/FAD-binding domain DHS-like NAD/FAD-binding domain C-terminal domain of the electron transfer flavoprotein alpha subunit
Resolution2.10

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


   221........ 230.........240.........250. ........260.........270.........280.........290......
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Query Sequence  RGVVVAGRM. . SAEEGKKVALWAQTLGWPLIGD. . VLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQ
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Template Sequence  KVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKI. . . . . . VAPELYIAVG. . . ISGAIQH
Template Known Secondary structure  S
GGG
STGGGT

TTSS
GGGBBSTTSB
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   216...220.........230.........240.........250.........260......... 270......... 280......
 
   297..300.........310.........320.........330.........340..
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Query Sequence  WQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKR
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Template Sequence  LAGMKDSKTIVAINKDPEAP. IFQVADYGIVADLFKVVPEMTEILK
Template Known Secondary structure  TTTTT
SS
TT
G.GGGT
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T
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   287..290.........300...... ...310.........320.........330.
 
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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