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Job DescriptionP17952
Confidence96.41%DateThu Jan 5 11:36:25 GMT 2012
Rank182Aligned Residues67
% Identity18%Templated3lada2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.20

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


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Query Sequence  RHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPN. . . . . . . . . . . PVTQQLMNLGATIYFNHRPENVRD. . . . . . . . . .
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Template Sequence  GKLGVIGAGVIGLEL. GSVWARLGAEVTVLEAMDKFLPAVDEQVAKEAQKILTKQGLKILLGARVTGTEVKNKQVTVKFV
Template Known Secondary structure  S

S.TT
SSSSSSTTS
TTT

SS
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   181........190..... ....200.........210.........220.........230.........240.........250.........
 
   7980.......
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Query Sequence  . . . . . . . . . ASVVVVSSA
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Template Sequence  DAEGEKSQAFDKLIVAVG
Template Known Secondary structure  SSSS


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   260.........270.......
 
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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