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Job DescriptionP27254
Confidence98.24%DateThu Jan 5 11:43:35 GMT 2012
Rank304Aligned Residues114
% Identity18%Templatec2hdnJ_
PDB info PDB header:translationChain: J: PDB Molecule:elongation factor ef-tu; PDBTitle: trypsin-modified elongation factor tu in complex with2 tetracycline at 2.8 angstrom resolution
Resolution2.80 Å

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


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Query Sequence  EAAGYDVVIVETVGVGQ. . . SETEVARMVDCFISLQIAGGGDDLQ. . . . GIKKGLMEVA. DLIVINKDDGDNHTNVAIAR
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Template Sequence  DTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELV
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   70.........80.........90.........100.........110.........120.........130.........140.........
 
   215....220.........230.........240.........250.......
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Query Sequence  HMYESALHILRRKYDEWQPRVLTCSALEKRGIDEIWHAIIDFK
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Template Sequence  EMEVREL. LSQYDFPGDDTPIVRGSALKALEGDAEWEAKILEL
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   150...... ...160.........170.........180.........190.
 
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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