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Job DescriptionP30844
Confidence97.00%DateThu Jan 5 11:46:28 GMT 2012
Rank51Aligned Residues100
% Identity18%Templatec1y4sA_
PDB info PDB header:chaperoneChain: A: PDB Molecule:chaperone protein htpg; PDBTitle: conformation rearrangement of heat shock protein 90 upon2 adp binding
Resolution2.90 Å

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


   254.....260.... .....270.........280.........290.........300.........310.....
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Query Sequence  LRMLLRNLVEN. . . . . . . . . . . AHRYSPQGSNIMIKLQEDDGAVMAVEDEGPGIDESKCGELSKAFVRMDSRY. . . . . . .
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Template Sequence  LRELISNASDAADKLRFRALSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKSGTKSFLESSQL
Template Known Secondary structure 
GGGG
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TTTT
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TT




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   32.......40.........50.........60.........70.........80.........90.........100.........110.
 
   316...320.........330... ......340..... ....350...
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Query Sequence  . GGIGLGLSIVSRITQLHH. . . . . . . . . . . . . . . . . . . . . GQFFLQNRQETS. GTRAWVRL
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Template Sequence  IGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAGEGEYTVADITKEDRGTEITLHL
Template Known Secondary structure 
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SGGG
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   120.........130.........140.........150.........160.........170.........180
 
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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