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Job DescriptionP08201
Confidence99.40%DateThu Jan 5 11:00:55 GMT 2012
Rank155Aligned Residues116
% Identity19%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


   116...120.........130.........140.........150.........160.........170.........180.........190.....
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Query Sequence  PPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLRR
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Template Sequence  PNFKFSN. . RIL. . . . . . DSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSG. FEKQMAAIIKK
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   155....160. ... .....170.........180.........190.........200.........210.... .....220.....
 
   196...200.........210.........220......... 230.........240
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Query Sequence  KIESMGVRVHTSKNTLEIVQEGVEARKTMRFADG. SELEVDFIVFS
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Template Sequence  RLKKKGVEVVTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVT
Template Known Secondary structure  TT
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   226...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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