BMRB Entry 36243

Title:
Mouse receptor-interacting protein kinase 3 (RIP3) amyloid structure by solid-state NMR
Deposition date:
2019-03-26
Original release date:
2023-02-23
Authors:
Wu, X.; Hu, H.; Zhang, J.; Dong, X.; Wang, J.; Schwieters, C.; Wang, H.; Lu, J.
Citation:

Citation: Wu, Xia-Lian; Hu, Hong; Dong, Xing-Qi; Zhang, Jing; Wang, Jian; Schwieters, Charles; Liu, Jing; Wu, Guo-Xiang; Li, Bing; Lin, Jing-Yu; Wang, Hua-Yi; Lu, Jun-Xia. "The amyloid structure of mouse RIPK3 (receptor interacting protein kinase 3) in cell necroptosis."  Nat. Commun. 12, 1627-1627 (2021).
PubMed: 33712586

Assembly members:

Assembly members:
Receptor-interacting serine/threonine-protein kinase 3, polymer, 84 residues, 9454.359 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Receptor-interacting serine/threonine-protein kinase 3: HHHHHHGPHPQRNQGDGRHG TPWYPWTPPNPMTGPPALVF NNCSEVQIGNYNSLVAPPRT TASSSAKYDQAQFGRGRGWQ PFHK

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts22

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21
3entity_1, chain 31
4entity_1, chain 41
5entity_1, chain 51

Entities:

Entity 1, entity_1, chain 1 84 residues - 9454.359 Da.

1   HISHISHISHISHISHISGLYPROHISPRO
2   GLNARGASNGLNGLYASPGLYARGHISGLY
3   THRPROTRPTYRPROTRPTHRPROPROASN
4   PROMETTHRGLYPROPROALALEUVALPHE
5   ASNASNCYSSERGLUVALGLNILEGLYASN
6   TYRASNSERLEUVALALAPROPROARGTHR
7   THRALASERSERSERALALYSTYRASPGLN
8   ALAGLNPHEGLYARGGLYARGGLYTRPGLN
9   PROPHEHISLYS

Samples:

sample_1: mouse rip3 fibril, [U-99% 13C; U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%

sample_2: mouse rip3 fibril, [99% 2-13C Glycerol, U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%

sample_3: mouse rip3 fibril, [99% 1,3-13C Glycerol; U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%

sample_4: mouse rip3 fibril, [U-50% 13C; natural abundance N][natural abundance C13, U-50% N15], 0.95 – 1.05 mg/mL; H2O 100%

sample_conditions_1: ionic strength: 0 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D CC DARRsample_1anisotropicsample_conditions_1
2D NCaCXsample_1anisotropicsample_conditions_1
2D NCoCXsample_1anisotropicsample_conditions_1
3D NCACXsample_1anisotropicsample_conditions_1
3D NCOCXsample_1anisotropicsample_conditions_1
2D CC DARRsample_4anisotropicsample_conditions_1
2D NC TEDORsample_4anisotropicsample_conditions_1
2D NCoCXsample_3anisotropicsample_conditions_1
2D NCaCXsample_3anisotropicsample_conditions_1
2D CC DARRsample_3anisotropicsample_conditions_1
2D NCoCXsample_2anisotropicsample_conditions_1
2D NCaCXsample_2anisotropicsample_conditions_1
2D CC DARRsample_2anisotropicsample_conditions_1
2D NC TEDORsample_2anisotropicsample_conditions_1
2D NC TEDORsample_1anisotropicsample_conditions_1
2D NC TEDORsample_3anisotropicsample_conditions_1
2D ChhCsample_4anisotropicsample_conditions_1
2D NCaCXsample_1anisotropicsample_conditions_1
2D CC DARRsample_1anisotropicsample_conditions_1
2D NCoCXsample_1anisotropicsample_conditions_1
3D NCACXsample_1anisotropicsample_conditions_1
3D NCOCXsample_1anisotropicsample_conditions_1

Software:

Sparky, Goddard - peak picking

TopSpin, Bruker Biospin - collection

X-PLOR NIH v2.50, Schwieters, Kuszewski, Tjandra and Clore - refinement

xplor-nih v2.48, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 700 MHz
  • Agilent DD2 700 MHz