BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34454

Title: A New Structural Model of Abeta(1-40) Fibrils   PubMed: 32749391

Deposition date: 2019-11-21 Original release date: 2020-07-18

Authors: Bertini, I.; Gonnelli, L.; Luchinat, C.; Mao, J.; Nesi, A.

Citation: Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Boddrich, A.; Bettina, P.; Benilova, I.; Korsak, M.; Gallo, G.; Rizzo, D.; Gonnelli, L.; Fragai, M.; De Strooper, B.; Wanker, E.; Luchinat, C.. "Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils"  Chem. Commun. (Camb.) 56, 8830-8833 (2020).

Assembly members:
entity_1, polymer, 40 residues, 4335.852 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV

Data sets:
Data typeCount
13C chemical shifts159
15N chemical shifts38

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_31
4unit_41
5unit_51
6unit_61
7unit_71
8unit_81
9unit_91
10unit_101
11unit_111
12unit_121
13unit_131
14unit_141
15unit_151
16unit_161

Entities:

Entity 1, unit_1 40 residues - 4335.852 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL

Samples:

sample_1: Amyloid beta peptide 1-40, [U-100% 13C; U-100% 15N], 100 uM; ammonium acetate 50 mM

sample_conditions_1: pH: 8.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 15N-13C NCAsample_1anisotropicsample_conditions_1
2D 15N-13C NCOsample_1anisotropicsample_conditions_1
3D NCACXsample_1anisotropicsample_conditions_1
3D NCOCXsample_1anisotropicsample_conditions_1
3D CANCOsample_1anisotropicsample_conditions_1
2D 13C-13C DARR (<100 ms)sample_1anisotropicsample_conditions_1
2D 15N-13C PAINsample_1anisotropicsample_conditions_1
2D 13C-13C DARR/PDSD (>100 ms)sample_1anisotropicsample_conditions_1
2D 13C-13C PAR (10-15 ms)sample_1anisotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CARA, Keller and Wuthrich - chemical shift assignment

Sparky, Goddard - chemical shift assignment

HADDOCK, Bonvin - structure calculation

NMR spectrometers:

  • Bruker AVANCE II 700 MHz
  • Bruker AVANCE III 850 MHz