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 34456

Title: Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils   PubMed: 32749391

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

Authors: Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Boddrich, A.; Purfurst, B.; Benilova, A.; Korsak, M.; Gallo, G.; Rizzo, D.; Gonnelli, L.; Fragai, M.; De Strooper, B.; Wanker, E.; Luchinat, C.

Citation: Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Boddrich, A.; Purfurst, B.; Benilova, A.; 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.
entity_2, polymer, 42 residues, 4520.087 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
entity_2: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts82

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_31
4unit_41
5unit_51
6unit_61
7unit_71
8unit_81
9unit_92
10unit_102
11unit_112
12unit_122
13unit_132
14unit_142
15unit_152
16unit_162

Entities:

Entity 1, unit_1 40 residues - 4335.852 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL

Entity 2, unit_9 42 residues - 4520.087 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL
5   ILEALA

Samples:

sample_1: Amyloid-beta peptide 1-40, [U-100% 13C; U-100% 15N], 50 uM; Amyloid-beta peptide 1-42 50 uM; ammonium acetate 50 mM

sample_2: Amyloid-beta peptide 1-40, [U-100% 13C; U-100% 15N], 70 uM; Amyloid-beta peptide 1-42 30 uM; ammonium acetate 50 mM

sample_3: Amyloid-beta peptide 1-40 50 uM; Amyloid-beta peptide 1-42, [U-100% 13C; U-100% 15N], 50 uM; ammonium acetate 50 mM

sample_4: Amyloid-beta peptide 1-40, [U-100% 13C], 50 uM; Amyloid-beta peptide 1-42, [U-100% 15N], 50 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 NCACBsample_1anisotropicsample_conditions_1
3D N(CO)CACBsample_1anisotropicsample_conditions_1
3D CANCOsample_1anisotropicsample_conditions_1
2D 13C-13C SHANGHAI (15-300 ms)sample_1anisotropicsample_conditions_1
2D 13C-13C PDSD (400, 800 ms)sample_1anisotropicsample_conditions_1
2D 13C-15N PAIN (10 ms)sample_1anisotropicsample_conditions_1
2D 15N-13C NCAsample_2anisotropicsample_conditions_1
2D 13C-13C DARR (100 ms)sample_2anisotropicsample_conditions_1
2D 15N-13C NCAsample_3anisotropicsample_conditions_1
2D 15N-13C NCOsample_3anisotropicsample_conditions_1
2D 13C-13C SHANGHAI (15-300 ms)sample_3anisotropicsample_conditions_1
2D 15N-13C hNhhCsample_4anisotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CARA, Keller and Wuthrich - chemical shift assignment

HADDOCK v2.2, Bonvin - structure calculation

MODELLER, Fiser and Sali - structure calculation

NMR spectrometers:

  • Bruker AVANCE II 700 MHz
  • Bruker AVANCE III 850 MHz
  • Bruker AVANCE III 800 MHz