Return to main results Retrieve Phyre Job Id

Job DescriptionP30011
Confidence47.70%DateThu Jan 5 11:45:42 GMT 2012
Rank390Aligned Residues148
% Identity11%Templatec1ydnA_
PDB info PDB header:lyaseChain: A: PDB Molecule:hydroxymethylglutaryl-coa lyase; PDBTitle: crystal structure of the hmg-coa lyase from brucella melitensis,2 northeast structural genomics target lr35.
Resolution2.30 Å

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


   134.....140.........150.........160.........170.........180.........190.........200.........210...
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Query Sequence  KVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKASWLHPDAPVE
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Template Sequence  SREVXAGIRRADGVRYSVLVPNXKGYEAAAAAHADEIAVFISASEGFSKANINCTIAESIERLSPVIGAAINDGLAIRGY
Template Known Secondary structure  S


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   60.........70.........80.........90.........100.........110.........120.........130.........
 
   214.. ...220.........230...... ...240.........250. ........260 .........
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Query Sequence  VEV. . . . . . . . . . . . . ENLEELDEALKAGADIIMLD. . . . NFETEQMREAVKRTN. . . GKALLEVSG. . . . NVTDKTLRE
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Template Sequence  VSCVVECPYDGPVTPQAVASVTEQLFSLGCHEVSLGDTIGRGTPDTVAAXLDAVLAIAPAHSLAGHYHDTGGRALDNIRV
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   140.........150.........160.........170.........180.........190.........200.........210.........
 
   270.........280.
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Query Sequence  FAETGVDFISVG
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Template Sequence  SLEKGLRVFDAS
Template Known Secondary structure  T

B
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   220.........230.
 
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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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