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Job DescriptionP77650
Confidence98.98%DateThu Jan 5 12:31:22 GMT 2012
Rank245Aligned Residues111
% Identity14%Templated1feca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.70

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


   129130.........140.........150.........160........ .170.........180.........190.........200......
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Query Sequence  RHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRC. . KVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLN
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Template Sequence  DLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTH
Template Known Secondary structure  GG
B
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   172.......180.........190.........200.........210.........220.........230.........240.........250.
 
   207..210.... .....220.........230.........
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Query Sequence  NAIEHVVD. . GEKVELTLQSGETLQADVVIYGIGI
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Template Sequence  ENPAKVTKNADGTRHVVFESGAEADYDVVMLAIGR
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   252.......260.........270.........280......
 
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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