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Job DescriptionO05204
Confidence99.40%DateTue Jul 17 17:05:01 BST 2012
Rank167Aligned Residues119
% Identity18%Templated1ojta2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.75

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


   316...320.........330.........340.........350.........360.........370.........380... ......390
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Query Sequence  WRKLNIPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKAD. . . . . NVLQDRL
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Template Sequence  TKLPFIPEDP. . . . . RIIDSSGALALKEVPGKLLIIGGGIIGLEMGTVYSTLGSRLDVVEMMDGLMQGADRDLVKVWQKQ
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   277..280...... ...290.........300.........310.........320.........330.........340.........350.
 
   391........400.........410.........420.........430.........440
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Query Sequence  RSLSNVDIKTNAKTTEVVGEDHVTGIRYEDMNTGEEHLLNLDGIFVQIGL
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Template Sequence  NEYRFDNIMVNTKTVAVEPKEDGVYVTFEG. ANAPKEPQRYDAVLVAAGR
Template Known Secondary structure  GGG
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   352.......360.........370.........380. ........390.........400
 
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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