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Specific recognition between surface loop 2 (132-143) and helix 1 (144-154) within sheep prion protein from in vitro studies of synthetic peptides
Authors
Kozin, S.A., Lepage, C., Hui Bon Hoa, G., Rabesona, H., Mazur, A.K., Blond, A., Cheminant, M., Haertle, T., Debey, P., Rebuffat, S.
Assembly
SheepPrP(135-155)
Entity
1. SheepPrP(135-155) (polymer, Thiol state: not present), 21 monomers, 2738.944 Da Detail

SRPLIHFGND YEDRYYRENM Y


Formula weight
2738.944 Da
Source organism
Ovis aries
Exptl. method
NMR
Refine. method
Molecular dynamics with AMBER99 all-atom force field parameters by using the variable target function approach in the torsion angle space with the standard geometry of amino acids and peptide bonds.
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 94.3 %, Completeness (bb): 97.6 % Detail

Polymer type: polypeptide(L)

Total1H
All94.3 % (133 of 141)94.3 % (133 of 141)
Backbone97.6 % (41 of 42)97.6 % (41 of 42)
Sidechain92.9 % (92 of 99)92.9 % (92 of 99)
Aromatic95.7 % (22 of 23)95.7 % (22 of 23)
Methyl100.0 % (4 of 4)100.0 % (4 of 4)

1. Sheep prion protein peptide 135-155 (in human numbering)

SRPLIHFGND YEDRYYRENM Y

Sample
#NameIsotope labelingTypeConcentration
1Sheep prion protein peptide 135-155 (in human numbering)5.0 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 1S4T, Strand ID: A Detail


Release date
2004-03-06
Citation
Specific recognition between surface loop 2 (132-143) and helix 1 (144-154) within sheep prion protein from in vitro studies of synthetic peptides
Kozin, S.A., Lepage, C., Hui Bon Hoa, G., Rabesona, H., Mazur, A.K., Blond, A., Cheminant, M., Haertle, T., Debey, P., Rebuffat, S.
J. Biol. Chem. (2004), PubMed , DOI:
Related entities 1. SheepPrP(135-155), : 1 : 49 : 85 : 1 : 11 entities Detail
Interaction partners 1. SheepPrP(135-155), : 1 interactors Detail
nullKeywords interaction, NMR, peptide, prion, protein, recognition, solution, structure