BMRB Entry 11435

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11435

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Title:
1H, 13C, and 15N Chemical Shift Assignments for amyloid-beta-(1-40)
Deposition date:
2011-03-16
Original release date:
2011-06-07
Authors:
Yamaguchi, Takahiro; Matsuzaki, Katsumi; Hoshino, Masaru
Citation:

Citation: Yamaguchi, Takahiro; Matsuzaki, Katsumi; Hoshino, Masaru. "Transient formation of intermediate conformational states of amyloid-beta peptide revealed by heteronuclear magnetic resonance spectroscopy"  FEBS Lett. 585, 1097-1102 (2011).
PubMed: 21402073

Assembly members:

Assembly members:
Amyloid-beta-(1-40), polymer, 40 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Amyloid-beta-(1-40): DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV

Data sets:
Data typeCount
13C chemical shifts107
15N chemical shifts39
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Amyloid beta-(1-40)1

Entities:

Entity 1, Amyloid beta-(1-40) 40 residues - Formula weight is not available

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL

Samples:

sample_1: Amyloid-beta-(1-40), [U-15N], 50 uM; sodium phosphate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: Amyloid-beta-(1-40), [U-13C; U-15N], 50 uM; sodium phosphate 50 mM; sodium chloride 100 mM; D2O 100%

sample_3: Amyloid-beta-(1-40), [U-13C; U-15N], 150 uM; sodium phosphate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 15775 17159 17186 17764 17793 17794 17795 17796 18052 18127 18128 18129 18131 19009 19309 19393 25218 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
AlphaFold P05067 P53601 P79307 P86906 Q28053

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks