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Biological Magnetic Resonance Data Bank


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BMRB Entry 30121

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30121
MolProbity Validation Chart

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Title: Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils   PubMed: 27355699

Deposition date: 2016-06-20 Original release date: 2016-07-11

Authors: Colvin, M.; Silvers, R.; Zhe Ni, Q.; Can, T.; Sergeyev, I.; Rosay, M.; Donovan, K.; Michael, B.; Wall, J.; Linse, S.; Griffin, R.

Citation: Colvin, M.; Silvers, R.; Ni, Q.; Can, T.; Sergeyev, I.; Rosay, M.; Donovan, K.; Michael, B.; Wall, J.; Linse, S.; Griffin, R.; Colvin, M.; Silvers, R.; Frohm, B.; Su, Y.; Linse, S.; Griffin, R.. "Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils."  J. Am. Chem. Soc. ., .-. (2016).

Assembly members:
entity_1, polymer, 42 residues, 4520.087 Da.

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):
entity_1: DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts29

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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_1, 111
12entity_1, 121
13entity_1, 131
14entity_1, 141
15entity_1, 151
16entity_1, 161
17entity_1, 171
18entity_1, 181

Entities:

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

1   ASPALAGLUPHEARGHISASPSERGLYTYR
2   GLUVALHISHISGLNLYSLEUVALPHEPHE
3   ALAGLUASPVALGLYSERASNLYSGLYALA
4   ILEILEGLYLEUMETVALGLYGLYVALVAL
5   ILEALA

Samples:

sample_3: AB42-M01-42, [U-100% 13C; U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM

sample_4: AB42-M01-42, [U-30% 13C; U-30% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM

sample_5: AB42-M01-42, [1,6-13C-glucose, U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM

sample_6: AB42-M01-42, [2-13C-glycerol, U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 1 mM; pH: 8.0; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
PAR 5 ms mixingsample_3isotropicsample_conditions_1
PAR 10 ms mixingsample_3isotropicsample_conditions_1
PAR 20 ms mixingsample_3isotropicsample_conditions_1
PAIN 30 ms mixingsample_3isotropicsample_conditions_1
DARR 25 ms mixingsample_3isotropicsample_conditions_1
DARR 100 ms mixingsample_4isotropicsample_conditions_1
ZF-TEDOR 6.4 ms mixingsample_5isotropicsample_conditions_1
FS-REDORsample_4isotropicsample_conditions_1
FS-REDORsample_3isotropicsample_conditions_1
PAR 20 ms mixingsample_4isotropicsample_conditions_1
DARR 400 ms mixingsample_6isotropicsample_conditions_1
DARR 100 ms mixingsample_5isotropicsample_conditions_1
ZF-TEDOR 12 ms mixingsample_5isotropicsample_conditions_1
3D CONCAsample_3isotropicsample_conditions_1
3D NCOCXsample_3isotropicsample_conditions_1
3D NCACXsample_3isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Home-built RUBEN750 750 MHz
  • Bruker AvanceIII 600 MHz