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Job DescriptionP27306
Confidence98.60%DateThu Jan 5 11:43:55 GMT 2012
Rank288Aligned Residues113
% Identity27%Templated1aoga2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.30

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


   155....160.........170.........180.........190....... ..200.........210.........220.........230.
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Query Sequence  DVDFTHPRIYDSDSILSMHHEPRHVLIYGAGVIGCEYASIFRG. . . MDVKVDLINTRDRLLAFLDQEMSDSLSYHFWNSG
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Template Sequence  IPGIE. . HCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELTKQLTANG
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TTGG..G
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   170.... .....180.........190.........200.........210.........220.........230.........240.......
 
   232.......240.........250. ........260.........
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Query Sequence  VVIRHNEEYEKIEGCDDGVI. MHLKSGKKLKADCLLYAN
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Template Sequence  IQILTKENPAKVELNADGSKSVTFESGKKMDFDLVMMAI
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   248.250.........260.........270.........280......
 
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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