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Job DescriptionP13033
Confidence97.09%DateThu Jan 5 11:33:29 GMT 2012
Rank292Aligned Residues94
% Identity7%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


   213......220.........230.........240.........250.... .....260.........270.........280.........290
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Query Sequence  NTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . GIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNGVVN
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Template Sequence  SKKIGIVGSGYIAVELINVIKRL. . . . GIDSYIFARGNRILRKFDESVINVLENDMKKNNINIVTFADVVEIKKVSDKNL
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   175....180.........190....... ..200.........210.........220.........230.........240.........250
 
   291........300.........310.
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Query Sequence  EIWTRNHADIPLRPRFAVLAS
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Template Sequence  SIHLSDGRIYE. HFDHVIYCV
Template Known Secondary structure  TTS
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   251........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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