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Job DescriptionO05204
Confidence98.98%DateTue Jul 17 17:05:01 BST 2012
Rank243Aligned Residues110
% Identity25%Templated1gera2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.86

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


   320.........330.........340.........350.........360.........370.........380... ......390....
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Query Sequence  NIPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKAD. . . . . NVLQDRLRSLS
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Template Sequence  DIPGVEY. . . . . GIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAE
Template Known Secondary structure 

TTGGG.....SB
T
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S

STT

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   147..150... ......160.........170.........180.........190.........200.........210.........220.
 
   395....400.........410 .........420.........430.........
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Query Sequence  NVDIKTNAKTTEVVGE. DHVTGIRYEDMNTGEEHLLNLDGIFVQIG
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Template Sequence  GPQLHTNAIPKAVVKNTDGSLTLELEDG. . . . . RSETVDCLIWAIG
Template Known Secondary structure  S

S


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   222.......230.........240......... 250.........260..
 
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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