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Job DescriptionP37127
Confidence98.43%DateThu Jan 5 11:54:48 GMT 2012
Rank314Aligned Residues125
% Identity14%Templated1gv4a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.0

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


   434.....440.........450.........460.........470.........480.........490... ......500.........510
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Query Sequence  DAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGAS. . . NVTCAYRRDEANMPGSK
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Template Sequence  SLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGRKSQASGIEVIQLFPEKGNMGKILP
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   265....270.........280.........290.........300.........310.........320.........330.........340....
 
   511.. ......520.........530.........540.........550.........560.........570.........580
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Query Sequence  KEV. . . . . KNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAF
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Template Sequence  QYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKL. . . . . . . . . . . . . . . . . . . . . . KDGRKVETDHIVTAV
Template Known Secondary structure  TTT

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   345....350.........360.........370.........380.. .......390.......
 
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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