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Job DescriptionP35340
Confidence99.19%DateWed Jan 25 15:20:51 GMT 2012
Rank200Aligned Residues112
% Identity23%Templated1ebda2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.60

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


   329330.........340.........350.........360.........370.........380.........390... ......400...
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Query Sequence  MNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKAD. . . . . QVLQDKLRSL
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Template Sequence  PNFKFSNR. . . . . ILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKK
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T
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   155....160.. .......170.........180.........190.........200.........210.........220.........
 
   404.....410.........420.........430.........440........
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Query Sequence  KNVDIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQ
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Template Sequence  KGVEVVTNALAKGAEERED. . . GVTVTYEANGETKTIDADYVLVT
Template Known Secondary structure  TT
STT...TTS
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   230.........240........ .250.........260.........270.
 
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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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