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Job DescriptionP17952
Confidence94.16%DateThu Jan 5 11:36:25 GMT 2012
Rank469Aligned Residues78
% Identity14%Templated1mo9a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.65

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


   910......... 20.........30.........40.........50.... .....60.........70.....
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Query Sequence  LRSIVPEMRRV. . RHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPN. . . . . . . . . . . PVTQQLMNLGATIYFNHRPEN
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Template Sequence  HATLVEELDYEPGSTVVVVGGSKTAVEY. GCFFNATGRRTVMLVRTEPLKLIKDNETRAYVLDRMKEQGMEIISGSNVTR
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   202.......210.........220......... 230.........240.........250.........260.........270.........280
 
   76.. .80.......
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Query Sequence  VRD. . . . . . . . . . . . . . . . . . . . . ASVVVVSSA
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Template Sequence  IEEDANGRVQAVVAMTPNGEMRIETDFVFLGLG
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   281........290.........300.........310...
 
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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