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Job DescriptionP77212
Confidence98.70%DateThu Jan 5 12:26:22 GMT 2012
Rank283Aligned Residues119
% Identity25%Templated1xhca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   130.........140.........150...... ...160.........170.........180.........190.........200......
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Query Sequence  QTVVPPIPGITTTPGVYDSTGLLNLKE. . . LPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIA
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Template Sequence  RAREPQIKGKEYLLTLRTIFDADRIKESIENSGEAIIIGGGFIGLELAGNLAEAGYHVKLIHRGAMFLG. LDEELSNMIK
Template Known Secondary structure 
B



SBTGGG


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TT.

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   104.....110.........120.........130.........140.........150.........160.........170.. .......180..
 
   207..210.........220.........230.........240.........250...
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Query Sequence  TILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIASGRQ
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Template Sequence  DMLEETGVKFFLNSELLEANEEG. . . . VLTNSGFIEGKVKICAIGIV
Template Known Secondary structure  TT
S


SS....TT
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B
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   183......190.........200..... ....210.........220.....
 
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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