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 30596

Title: S8 phosphorylated beta amyloid 40 fibrils

Deposition date: 2019-03-22 Original release date: 2019-05-31

Authors: Qiang, W.; Hu, Z.

Citation: Hu, Z.; Vugmeyster, L.; Au, D.; Ostrovsky, D.; Sun, Y.; Qiang, W.. "The molecular structure of a "seeding-prone" N-terminal phosphorylated b-amyloid fibril."  . ., .-..

Assembly members:
entity_1, polymer, 40 residues, 4335.852 Da.
entity_2PO, non-polymer, 79.980 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV

Data sets:
Data typeCount
13C chemical shifts123

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31
4entity_1, 41
5entity_1, 51
6entity_1, 61
7entity_1, 71
8entity_1, 81
9entity_1, 91
10entity_1, 101
11entity_2, 12
12entity_2, 22
13entity_2, 32
14entity_2, 42
15entity_2, 52
16entity_2, 62
17entity_2, 72
18entity_2, 82
19entity_2, 92
20entity_2, 102

Entities:

Entity 1, entity_1, 1 40 residues - 4335.852 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL

Entity 2, entity_2, 1 - H O3 P - 79.980 Da.

1   2PO

Samples:

sample_1: beta amyloid peptide, E3, G9, V18, F20, D23, S26, K28, 50 uM; beta amyloid peptide, A2, F4, D7, Y10, V24, G25, 50 uM; beta amyloid peptide, Q15, F19, A21, I31, L34, V36, G37, 50 uM; beta amyloid peptide, V12, E22, G29, A30, M35, 50 uM; beta amyloid peptide, E11, L17, N27, I32, G33, G38, V39, 50 uM; beta amyloid peptide, F19, L34, 50 uM; beta amyloid peptide, E3, F4, V24, G25, S26, 50 uM; beta amyloid peptide, V12, F20, E22, 50 uM; beta amyloid peptide, I31, G33, V39, 50 uM

sample_2: beta amyloid peptide, L17, 2H-CD3, 50 uM; beta amyloid peptide, F19, 2H-ring-D5, 50 uM; beta amyloid peptide, L34, 2H-CD3, 50 uM; beta amyloid peptide, M35, 2H-CD3, 50 uM; beta amyloid peptide, V36, 2H-CD3, 50 uM

sample_3: beta amyloid peptide, A2-CH3, V12-CO, 50 uM; beta amyloid peptide, V18-CO, A21-CH3, 50 uM; beta amyloid peptide, V24-CO, A30-CH3, 50 uM; beta amyloid peptide, G33-CO, V39-Ca, 50 uM; beta amyloid peptide, V36-Ca, G38-CO, 50 uM; beta amyloid peptide, G9-CO, 50 uM

sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D spin diffusionsample_1anisotropicsample_conditions_1
1D PITHIRDs-CTsample_3anisotropicsample_conditions_1
1D 13C-31P REDORsample_3anisotropicsample_conditions_1
2H relaxationsample_2anisotropicsample_conditions_1
2H staticsample_2anisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 750 MHz