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Solid State NMR sequential assignment of Amyloid b(1-42) fibrils
Authors
Ravotti, F., Waelti, M.A., Guentert, P., Meier, B.H., Riek, R., Boeckmann, A.
Assembly
Amyloid Beta fibril
Entity
1. Amyloid Beta fibril (polymer, Thiol state: not present), 42 monomers, 4514.037 Da Detail

DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IA


Formula weight
4514.037 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 90.5 %, Completeness: 84.8 %, Completeness (bb): 90.1 % Detail

Polymer type: polypeptide(L)

Total13C15N
All84.8 % (195 of 230)83.3 % (155 of 186)90.9 % (40 of 44)
Backbone90.1 % (146 of 162)90.0 % (108 of 120)90.5 % (38 of 42)
Sidechain77.9 % (81 of 104)77.5 % (79 of 102)100.0 % (2 of 2)
Aromatic48.0 % (12 of 25)48.0 % (12 of 25)
Methyl92.3 % (24 of 26)92.3 % (24 of 26)

1. Amyloid Beta

DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IA

Sample

Solvent system Sodium phosphate, Pressure 1 atm, Temperature 273 K, pH 7.4


#NameIsotope labelingTypeConcentration
1Amyloid Beta[U-13C]20 mg

Protein Blocks Logo
Calculated from 10 models in PDB: 2NAO, Strand ID: A, B, C, D, E, F Detail


Release date
2016-05-23
Citation
Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph
Ravotti, F., Waelti, M.A., Guentert, P., Meier, B.H., Riek, R., Boeckmann, A.
Biomol. NMR Assign. (2016), 10, 269-276, PubMed 27165577 , DOI 10.1007/s12104-016-9682-y ,
Related entities 1. Amyloid Beta fibril, : 1 : 51 : 3 : 59 : 17 entities Detail
Interaction partners 1. Amyloid Beta fibril, : 96 interactors Detail
Experiments performed 8 experiments Detail
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