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Job DescriptionP77212
Confidence98.40%DateThu Jan 5 12:26:22 GMT 2012
Rank302Aligned Residues116
% Identity30%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


   133......140.........150.........160.........170.........180.........190.........200.........210..
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Query Sequence  VPPIPGITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQ
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Template Sequence  LPGVT. . IDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIGSEVTVVEFASEIVPTMDAEIRKQFQRSLEKQ
Template Known Secondary structure  BTTB
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SSS
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S
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   154.... .160.........170.........180.........190.........200.........210.........220.........230.
 
   213......220.........230..... ....240.........250
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Query Sequence  GVDIILNAHVERISHHENQVQVH. . . . . . SEHAQLAVDALLIAS
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Template Sequence  GMKFKLKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSA
Template Known Secondary structure  S


S
SSSSSSS


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   232.......240.........250.........260.........270.....
 
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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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