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Job DescriptionP13033
Confidence97.47%DateThu Jan 5 11:33:29 GMT 2012
Rank283Aligned Residues115
% Identity10%Templated1dxla2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution3.15

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


   195....200.........210.........220.........230.........240.........250.........260.........270....
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Query Sequence  LDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGVWM
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Template Sequence  IDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIG. . SEVTVVEFASEIVPTMDAEIRKQFQRSLEKQGMKFK
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   159160.........170.........180.........190.........200 .........210.........220.........230......
 
   275....280.........290.... .....300.........310.
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Query Sequence  PGDEVKKVTCKNGVVNEIWT. . RNHADIPLRPRFAVLAS
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Template Sequence  LKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSA
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   237..240.........250.........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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