BMRB Entry 34396

Title:
Structure of pore-forming amyloid-beta tetramers
Deposition date:
2019-04-23
Original release date:
2019-09-30
Authors:
Bardiaux, B.; Ciudad, S.; Carulla, N.
Citation:

Citation: Ciudad, Sonia; Puig, Eduard; Botzanowski, Thomas; Meigooni, Moeen; Arango, Andres; Do, Jimmy; Mayzel, Maxim; Bayoumi, Mariam; Chaignepain, Stephane; Maglia, Giovanni; Cianferani, Sarah; Orekhov, Vladislav; Tajkhorshid, Emad; Bardiaux, Benjamin; Carulla, Natalia. "Abeta(1-42) Tetramer and Octamer Structures Reveal Edge Conductivity Pores as a Mechanism for Membrane Damage"  Nat. Commun. 11, 3014-3014 (2020).
PubMed: 32541820

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4520.087 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts132
1H chemical shifts132

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

Entities:

Entity 1, entity_1, 1 42 residues - 4520.087 Da.

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL
5   ILEALA

Samples:

sample_1: Amyloid-beta A4 protein, [U-15N], 1 mM; TRIS-d11, [U-2H], 10 mM; DPC-d38, [U-2H], 28.5 mM

sample_2: Amyloid-beta A4 protein, [U-13C; U-15N; U-2H], 1 mM; TRIS-d11, [U-2H], 10 mM; DPC-d38, [U-2H], 28.5 mM

sample_3: Amyloid-beta A4 protein, [U-2H,13C,15N]-Ile-[13CH3]d1, Ala-[13CH3], Leu/Val-[13CH3]proR, 1 mM; TRIS-d11, [U-2H], 10 mM; DPC-d38, [U-2H], 28.5 mM

sample_4: Amyloid-beta A4 protein, [U-2H,15N]-Ile-[13CH3]d1, Ala-[13CH3], Leu/Val-[13CH3]proR, 1 mM; TRIS-d11, [U-2H], 10 mM; DPC-d38, [U-2H], 28.5 mM

sample_conditions_1: pH: 8.5; pressure: 1 atm; temperature: 310.15 K

sample_conditions_2: pH: 9.5; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D 13C-HMQC-[1H,1H]-NOESY-13C-HMQCsample_2isotropicsample_conditions_1
3D (Hme)Cme([C]CA)COsample_3isotropicsample_conditions_1
3D (Hme)Cme([C]CA)NHsample_3isotropicsample_conditions_1
3D Hme(Cme[C]CA)NHsample_3isotropicsample_conditions_1
3D (H)C-TOCSY-C-TOCSY-(C)Hsample_3isotropicsample_conditions_1
3D Hm-CmHm NOESYsample_4isotropicsample_conditions_1
3D Cm-CmHm NOESYsample_4isotropicsample_conditions_1
3D Hm-NH NOESYsample_4isotropicsample_conditions_1
3D Cm-NH NOESYsample_4isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 13C-HMQC-[1H,1H]-NOESY-13C-HMQCsample_2isotropicsample_conditions_2
3D Hm-CmHm NOESYsample_4isotropicsample_conditions_2
3D Cm-CmHm NOESYsample_4isotropicsample_conditions_2
3D Hm-NH NOESYsample_4isotropicsample_conditions_2
3D Cm-NH NOESYsample_4isotropicsample_conditions_2

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS, Cornilescu, Delaglio and Bax - data analysis

TopSpin, Bruker Biospin - processing

CcpNmr Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 900 MHz
  • Bruker AVANCE 800 MHz

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