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Job DescriptionO05204
Confidence98.88%DateTue Jul 17 17:05:01 BST 2012
Rank259Aligned Residues108
% Identity21%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


   321........330.........340.........350.........360...... ...370.........380... ......390..
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Query Sequence  IPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAG. . . IVNHVTLFEFASELKAD. . . . . NVLQDRLRS
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Template Sequence  IPGIE. . . . . HCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELTKQLT
Template Known Secondary structure 
TTGG.....G
B
TT
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S
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TT
SSSSSSTTS
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   170.... .....180.........190.........200.........210.........220.........230.........240....
 
   393......400.........410 .........420.........430........
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Query Sequence  LSNVDIKTNAKTTEVVGE. DHVTGIRYEDMNTGEEHLLNLDGIFVQI
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Template Sequence  ANGIQILTKENPAKVELNADGSKSVTFESG. . . . . KKMDFDLVMMAI
Template Known Secondary structure  TT
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TTS
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   245....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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