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Job DescriptionP52131
Confidence98.77%DateThu Jan 5 12:05:36 GMT 2012
Rank255Aligned Residues139
% Identity14%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


   6970.........80.........90.........100.........110.........120.........130.........140.......
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Query Sequence  ACTRDPLRFRLQIGEHFMTIVDLPGVGESGVRDTEYAALYREQLPRLDLILWLIKADDRALATDEHFYRQVIGEAYRHK.
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Template Sequence  GITINTSHVEYDTPTRHYAHVDCPG. . . . . . . HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVG. . VPY
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   5960.........70.........80... ......90.........100.........110.........120...... ...
 
   148.150.........160.........170.........180.........190.........200.........210.........220.
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Query Sequence  MLFVISQSDKAEPTSGGNILSTEQKQNISRKICLLHELFQPVHPVCAVSVRLQWGLRVMAERMIKCLPREASSP
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Template Sequence  IIVFLNKCDMVDDEELLEL. . . . . VEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSY
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   130.........140........ .150.........160.........170.........180.........190........
 
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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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