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 25218

Title: Chemical shifts of amyloid beta (1-42) peptide in aqueous solution   PubMed: 25676345

Deposition date: 2014-09-11 Original release date: 2015-03-17

Authors: Walti, Marielle; Orts, Julien; Vogeli, Beat; Campioni, Silvia; Riek, Roland

Citation: Walti, Marielle; Orts, Julien; Vogeli, Beat; Campioni, Silvia; Riek, Roland. "Solution NMR Studies of Recombinant Abeta(1-42): From the Presence of a Micellar Entity to Residual Beta-Sheet Structure in the Soluble Species"  Chembiochem. 16, 659-669 (2015).

Assembly members:
amyloid_peptide, polymer, 42 residues, Formula weight is not available

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):
amyloid_peptide: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA

Data sets:
Data typeCount
13C chemical shifts78
15N chemical shifts42
1H chemical shifts242

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 42 residues - Formula weight is not available

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL
5   ILEALA

Samples:

sample_1: amyloid_peptide, [U-13C; U-15N], 0.5 – 0.7 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 273 K; pH: 7.4; pressure: 1 atm; ionic strength: 20 mM

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

ccpNMR, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 11435 15775 17159 17186 17764 17793 17794 17795 17796 18052 18127 18128 18129 18131 19009 19309 19393 25289 25429 26508 26516
PDB
DBJ BAA22264 BAA84580 BAB71958 BAD51938 BAE01907
EMBL CAA30050 CAA31830 CAA39589 CAA39590 CAA39591
GB AAA35540 AAA36829 AAA51564 AAA51722 AAA51726
PIR A60045 D60045 E60045 G60045 PQ0438
PRF 1303338A 1403400A 1405204A 1507304A 1507304B
REF NP_000475 NP_001006601 NP_001013036 NP_001070264 NP_001127014
SP P05067 P53601 P79307 P86906 Q28053
TPG DAA33655

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts