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Job DescriptionP0A836
Confidence68.85%DateThu Jan 5 11:06:47 GMT 2012
Rank123Aligned Residues100
% Identity17%Templated1oi7a1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains CoA-binding domain
Resolution1.23

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


   258.260.........270.........280.........290 .........300.........310.........320.........330....
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Query Sequence  NIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVG. . . GGATKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIG
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Template Sequence  RVLVQGITGREGQFHTKQMLTYGTKIVAGVTPGKGGMEVLGVPVYDTVKEAVAHHEVDASII. . . . . FVPAPAAADAALE
Template Known Secondary structure  TTTST

TT
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   910.........20.........30.........40.........50.........60.........70 .........80...
 
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Query Sequence  AVAEVGVNVPVVVRLEGNNAELGAKKLADS
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Template Sequence  AAHAG. . IPLIVLITEGIPTLDMVRAVEEI
Template Known Secondary structure  TT..
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   84.... .90.........100.........110.
 
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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