BMRB Entry 25289

Title:
Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation
Deposition date:
2014-10-17
Original release date:
2014-11-24
Authors:
Schuetz, Anne; Vagt, Toni; Huber, Matthias; Ovchinnikova, Oxana; Cadalbert, Riccardo; Wall, Joseph; Guentert, Peter; Bockmann, Anja; Glockshuber, Rudi; Meier, Beat
Citation:

Citation: Schuetz, Anne; Vagt, Toni; Huber, Matthias; Ovchinnikova, Oxana; Cadalbert, Riccardo; Wall, Joseph; Guentert, Peter; Bockmann, Anja; Glockshuber, Rudi; Meier, Beat. "Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation"  Angew. Chem. Int. Ed. Engl. 54, 331-335 (2015).
PubMed: 25395337

Assembly members:

Assembly members:
amyloid_beta, polymer, 39 residues, 4206.777 Da.

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: pET T7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
amyloid_beta: DAEFRHDSGYEVHHQKLVFF ADVGSNKGAIIGLMVGGVV

Data typeCount
13C chemical shifts477
15N chemical shifts91

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41
5entity_51
6entity_61
7entity_71
8entity_81
9entity_91
10entity_101

Entities:

Entity 1, entity_1 39 residues - 4206.777 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAASPVALGLYSERASNLYSGLYALAILE
4   ILEGLYLEUMETVALGLYGLYVALVAL

Samples:

uniform_13C15N: amyloid beta, [U-100% 13C; U-100% 15N], 15 mg

uniform_13C: amyloid beta, [U-100% 13C], 15 mg

mixed_13C-15N: amyloid beta, [U-100% 13C; U-100% 15N], 15 mg

2-13C-glucose: amyloid beta, [U-100% 2-13C-glucose; U-100% 15N], 15 mg

diluted: amyloid beta, [U-100% 13C; U-100% 15N]/natural abundance, 15 mg

sample_conditions_1: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
NCAuniform_13C15Nsolidsample_conditions_1
NCOuniform_13C15Nsolidsample_conditions_1
DARR 15 msuniform_13Csolidsample_conditions_1
PAIN 6 msuniform_13C15Nsolidsample_conditions_1
PAIN 6 msmixed_13C-15Nsolidsample_conditions_1
DARR 400 msuniform_13Csolidsample_conditions_1
DARR 400 msdilutedsolidsample_conditions_1
PAR 8 msuniform_13Csolidsample_conditions_1
PAR 8 msdilutedsolidsample_conditions_1
CHHC 500 usuniform_13Csolidsample_conditions_1
CHHC 500 usdilutedsolidsample_conditions_1
PDSD 4 s2-13C-glucosesolidsample_conditions_1

Software:

CYANA v3.9.6, Guntert, Mumenthaler and Wuthrich - structure solution

CcpNMR v2.2.2, CCPN - chemical shift assignment, data analysis, peak picking

TALOS+ v2.1, Cornilescu, Delaglio and Bax - dihedral angle prediction

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

BMRB 11435 15775 17159 17186 17764 17793 17794 17795 17796 18052 18127 18128 18129 18131 19009 19309 19393 25218 25429 26508 26516
PDB
DBJ BAA22264 BAA84580 BAD51938 BAE01907 BAG10647
EMBL CAA30050 CAA31830 CAA39589 CAA39590 CAA39591
GB AAA35540 AAA36829 AAA51722 AAA51726 AAA51727
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 Q28053 Q28280
TPG DAA33655
AlphaFold P53601 P79307 Q28280 Q28053 P05067