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Job DescriptionP18392
Confidence98.23%DateThu Jan 5 11:36:55 GMT 2012
Rank42Aligned Residues99
% Identity20%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


   323......330.... .....340.........350.........360........ .370.........380..
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Query Sequence  VLDNLLNNALRY. . . . . . . . . . . . . . . . CHSTVETSLLLSGNRATLIVEDDGPGIAPENREH. . . . IFEPFVRLDPSRDR
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Template Sequence  FLRELISNASDAADKLRFRALSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKSGTKSFLESSQ
Template Known Secondary structure 
GGGG
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TTTT
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   31........40.........50.........60.........70.........80.........90.........100.........110
 
   383......390......... 400. ........ 410.........420.
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Query Sequence  STGGCGLGLAIVHSIAL. . . . . . . . . . . . . . . AM. . . . . . GGTVNCDT. . SELGGARFSFSW
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Template Sequence  LIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAGEGEYTVADITKEDRGTEITLHL
Template Known Secondary structure 

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SGGG
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   119120.........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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