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Job DescriptionP13033
Confidence98.07%DateThu Jan 5 11:33:29 GMT 2012
Rank272Aligned Residues114
% Identity15%Templated1lpfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.80

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


   195....200.........210.........220.........230.........240.........250.... .....260.........270..
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Query Sequence  LDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . GIRLQNQLQRQFVRQGGV
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Template Sequence  LSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARL. . . . GAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLN
Template Known Secondary structure 

TTT
TT
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S

ST....T

SSSSSSTTS
T
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   162.......170.........180.........190.........200.. .......210.........220.........230.......
 
   273......280.........290.........300.........310..
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Query Sequence  WMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASG
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Template Sequence  IRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVG
Template Known Secondary structure  TT


TT
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   238.240.........250.........260.........270.......
 
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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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