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Job DescriptionP13033
Confidence97.35%DateThu Jan 5 11:33:29 GMT 2012
Rank285Aligned Residues105
% Identity11%Templated1trba2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

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


   204.....210.........220.........230.........240.........250.........260.........270.........280...
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Query Sequence  LLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGVWMPGDEVKKVT
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Template Sequence  ATSDGFFYRNQKVAVIGGGNTAVEEALYLS. . . . NIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVT
Template Known Secondary structure  GGGGTTS
SST....TTSS
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   136...140.........150.........160..... ....170.........180.........190.........200.........210.
 
   284.....290......... 300.........310..
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Query Sequence  CKNGVVNEIWTRNHAD. . . . IPLRPRFAVLASG
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Template Sequence  GDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIG
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   212.......220.........230.........240....
 
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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