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Job DescriptionP17952
Confidence96.06%DateThu Jan 5 11:36:25 GMT 2012
Rank263Aligned Residues78
% Identity13%Templated1onfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.60

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


   910.........20.........30.........40.........50.... .....60.........70.......
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Query Sequence  LRSIVPEMRRVRHIHFVGIGGAGMGGIAEVLANEGYQISGSDLAPN. . . . . . . . . . . PVTQQLMNLGATIYFNHRPENVR
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Template Sequence  SSDEFFNIKESKKIGIVGSGYIAVEL. INVIKRLGIDSYIFARGNRILRKFDESVINVLENDMKKNNINIVTFADVVEIK
Template Known Secondary structure  TT



S

S.TTT

SSSSS
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TT

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   165....170.........180.........190 .........200.........210.........220.........230.........240...
 
   78.80 .......
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Query Sequence  DAS. . . . VVVVSSA
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Template Sequence  KVSDKNLSIHLSDG
Template Known Secondary structure  SSTT
TTS
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   244.....250.......
 
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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