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Mouse prion protein (121-231) with the mutation Y169A
Authors
Christen, B., Damberger, F.F., Perez, D.R., Hornemann, S., Wuthrich, K.
Assembly
Mouse prion protein (121-231) with the mutation Y169A
Entity
1. Mouse prion protein (121-231) with the mutation Y169A (polymer, Thiol state: all disulfide bound), 114 monomers, 13301.65 Da Detail

GSVVGGLGGY MLGSAMSRPM IHFGNDWEDR YYRENMYRYP NQVYYRPVDQ ASNQNNFVHD CVNITIKQHT VTTTTKGENF TETDVKMMER VVEQMCVTQY QKESQAYYDG RRSS


Formula weight
13301.65 Da
Entity Connection
disulfide 1 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:CYS61:SG1:CYS96:SG

Source organism
Mus musculus
Exptl. method
solution NMR
Refine. method
TORSION ANGLE DYNAMICS
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 89.5 %, Completeness (bb): 83.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All89.5 % (1189 of 1329)98.6 % (683 of 693)75.0 % (381 of 508)97.7 % (125 of 128)
Backbone83.2 % (564 of 678)95.7 % (224 of 234)69.4 % (231 of 333)98.2 % (109 of 111)
Sidechain95.0 % (718 of 756)98.3 % (451 of 459)89.6 % (251 of 280)94.1 % (16 of 17)
Aromatic79.1 % (106 of 134)98.5 % (66 of 67)59.1 % (39 of 66)100.0 % (1 of 1)
Methyl100.0 % (88 of 88)100.0 % (44 of 44)100.0 % (44 of 44)

1. entity

GSVVGGLGGY MLGSAMSRPM IHFGNDWEDR YYRENMYRYP NQVYYRPVDQ ASNQNNFVHD CVNITIKQHT VTTTTKGENF TETDVKMMER VVEQMCVTQY QKESQAYYDG RRSS

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293.2 K, pH 4.5


#NameIsotope labelingTypeConcentration
1entity[U-99% 13C; U-99% 15N]1.4 mM
2sodium acetate[U-2H]10 mM
3sodium azidenatural abundance0.02 %
4H2Onatural abundance90 %
5D2Onatural abundance10 %

LACS Plot; CA
Referencing offset: 0.4 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: 0.4 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.06 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2L40, Strand ID: A Detail


Release date
2012-07-31
Citation
Temperature-Induced Misfolding in Prion Protein: Evidence of Multiple Partially Disordered States Stabilized by Non-Native Hydrogen Bonds
Christen, B., Damberger, F.F., Perez, D.R., Hornemann, S., Wuthrich, K.
Biochemistry (2017), 56, 833-844, PubMed 28102071 , DOI 10.1021/acs.biochem.6b01042 ,
Related entities 1. Mouse prion protein (121-231) with the mutation Y169A, : 1 : 13 : 142 entities Detail
Interaction partners 1. Mouse prion protein (121-231) with the mutation Y169A, : 36 interactors Detail
Experiments performed 3 experiments Detail
nullKeywords mouse, mutation, NMR, prion, temperature