Primary information |
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Hemolytik ID | 4167 |
PMID | 19111524 |
YEAR | 2009 |
SEQUENCE | X-NH-GDATQLLAAYILLFDEYNEKKASAQKDILIKVL |
LENGTH | 21 |
NAME | Mu1-H88 |
C-ter Modification | Amidation |
N-ter Modification | X=H, NBD, Rhodamine |
Linear/Cyclic | Linear |
Stereochemistry | L |
Modified Residues | None |
FUNCTION | Cytotoxic |
ACTIVITY | 0% hemolysis at 0.8μM |
RBCs SOURCE | Human |
Secondary information |
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Properties | Physico-Chemical details |
STRUCTURE | |
DSSP states | CCHHHHHHHHHHHCGGGCGGGTCSSCCSSSCCC |
SMILES | NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O |
External Links |
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PDB exact | PDB partial | SP exact | SP partial | TrEMBL exact | TrEMBL partial | IEDB exact | IEDB partial |
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Reference Informaiton |
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ARTICLE | A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: plausible implications in the toxic activity of the protein. |
AUTHORS | Yadav SP,Ahmad A,Pandey BK,Singh D,Asthana N,Verma R,Tripathi RK |
JOURNAL | Biochim Biophys Acta. 2009 Feb;1788(2):538-50. doi: 10.1016/j.bbamem.2008.11.013. Epub 2008 Nov 28. |