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Job DescriptionP37127
Confidence98.96%DateThu Jan 5 11:54:48 GMT 2012
Rank228Aligned Residues118
% Identity20%Templated1nhpa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

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


   430.........440.........450.........460.........470.........480.........490.........500.........
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Query Sequence  LPNEDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGS
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Template Sequence  IPGKDLDNIYLMRGRQWAIKLK. . . . . . . . . QKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGK. KVTVIDILDRPLGVYL
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TTTTSBS


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   120.........130.........140. ........150.........160.........170... ......180.........
 
   510... ......520.........530.........540.........550.........560.........570.........580
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Query Sequence  KKEV. . . . . KNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAF
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Template Sequence  DKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKV. . . . . . . . . . . . . . . . . . . . . . . VTDKNAYDADLVVVAV
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   190.........200.........210.........220...... ...230.........240..
 
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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