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Job DescriptionP17109
Confidence79.24%DateThu Jan 5 11:35:57 GMT 2012
Rank138Aligned Residues162
% Identity11%Templated2ieaa1
SCOP infoThiamin diphosphate-binding fold (THDP-binding) Thiamin diphosphate-binding fold (THDP-binding) TK-like Pyr module
Resolution1.85

  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  AFNRRWAAVILEALTRHGV. . RHICIAPGSRSTPLTLAAAENSAF. . . . . . . . IHHTH. FDERGLGHLALGLAKVSKQ. .
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Template Sequence  STTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPEDEKGQILQEGINELGAGCSWLAAATSYSTNN
Template Known Secondary structure 
TT
TTTGGGSS
SGGGT

BB


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   493......500.........510.........520.........530.........540.........550.........560.........570..
 
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Query Sequence  . . . PVAVIVTSGTAVANLYPALIEAGL. TGEKLILLTADRPPELIDCG. ANQAIRQPGMFASHPTHSISLPRPTQDIPAR
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Template Sequence  LPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPN. . CISYDPAYAYEVA
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   590.........600.........610.........620.........630.........640.........650.... .....660.......
 
   147..150.........160........
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Query Sequence  WLVSTIDHALGTLHAGGVHINC
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Template Sequence  VIMHDGLERMYGEKQENVYYYI
Template Known Secondary structure  STT



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   668.670.........680.........
 
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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