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Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its reduced state
Authors
Schwalbe, H., Schlepckow, K.
Assembly
human prion protein (residues 121-230)
Entity
1. human prion protein (residues 121-230) (polymer, Thiol state: all other bound), 113 monomers, 13354.78 Da Detail

GHMVVGGLGG YMLGSAMSRP IIHFGSDYED RYYRENMHRY PNQVYYRPMD EYSNQNNFVH DXVNITIKQH TVTTTTKGEN FTETDVKMME RVVEQMXITQ YERESQAYYQ RGS


Formula weight
13354.78 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 94.7 %, Completeness: 38.2 %, Completeness (bb): 78.3 % Detail

Polymer type: polypeptide(L)

Total1H13C
All38.2 % (454 of 1187)28.6 % (195 of 683)51.4 % (259 of 504)
Backbone78.3 % (432 of 552)78.1 % (178 of 228)78.4 % (254 of 324)
Sidechain14.0 % (103 of 737) 4.0 % (18 of 455)30.1 % (85 of 282)
Aromatic 0.0 % (0 of 138) 0.0 % (0 of 69) 0.0 % (0 of 69)
Methyl 9.3 % (8 of 86) 9.3 % (4 of 43) 9.3 % (4 of 43)

1. hPrP(121-230)

GHMVVGGLGG YMLGSAMSRP IIHFGSDYED RYYRENMHRY PNQVYYRPMD EYSNQNNFVH DXVNITIKQH TVTTTTKGEN FTETDVKMME RVVEQMXITQ YERESQAYYQ RGS

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 2.0, Details 8M urea pH 2


#NameIsotope labelingTypeConcentration
1hPrP(121-230)[U-13C; U-15N]0.2 ~ 0.5 mM
2TSPnatural abundance1 mM
3ureanatural abundance8 M
4H2Onatural abundance90 %
5D2Onatural abundance10 %

LACS Plot; CA
Referencing offset: -0.12 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.12 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.01 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.26 ppm, Outliers: 3 Detail
Release date
2011-07-04
Citation
Unfolded-state structure and dynamics influence the fibril formation of human prion protein
Gerum, C., Silvers, R., Wirmer-Bartoschek, J., Schwalbe, H.
Angew. Chem Int Ed Engl. (2009), 48, 9452-9456, PubMed 19882604 , DOI 10.1002/anie.200903771 ,
Entries sharing articles BMRB: 1 entries Detail
  BMRB: 17756 released on 2011-07-17
    Title Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its oxidized state
Related entities 1. human prion protein (residues 121-230), : 1 : 25 : 131 entities Detail
Interaction partners 1. human prion protein (residues 121-230), : 70 interactors Detail
Experiments performed 6 experiments Detail
Chemical shift validation 3 contents Detail
Keywords prion protein, unfolded state