BMRB Entry 51175

Title:
NMR assignments for the C-terminal domain of human RIPK3
Deposition date:
2021-11-10
Original release date:
2022-11-10
Authors:
Titaux Delgado, Gustavo Alfredo; Pham, Chi; Sunde, Margaret; Mompean, Miguel
Citation:

Citation: Pham, ChiL; Titaux-Delgado, GustavoA; Varghese, NikhilR; Polonio, Paula; Wilde, KarynL; Sunde, Margaret; Mompean, Miguel. "NMR characterization of an assembling RHIM (RIP Homotypic Interaction Motif) amyloid reveals a cryptic region for self-recognition"  J. Biol. Chem. 299, 104568-104568 (2023).
PubMed: 36870681

Assembly members:

Assembly members:
entity_1, polymer, 133 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: pMAL

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts126
1H chemical shifts428
T1 relaxation values112
T1rho relaxation values112
coupling constants84

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of RIPK31

Entities:

Entity 1, C-terminal domain of RIPK3 133 residues - Formula weight is not available

1   GLYSERSERSERASPSERMETALAGLNPRO
2   PROGLNTHRPROGLUTHRSERTHRPHEARG
3   ASNGLNMETPROSERPROTHRSERTHRGLY
4   THRPROSERPROGLYPROARGGLYASNGLN
5   GLYALAGLUARGGLNGLYMETASNTRPSER
6   CYSARGTHRPROGLUPROASNPROVALTHR
7   GLYARGPROLEUVALASNILETYRASNCYS
8   SERGLYVALGLNVALGLYASPASNASNTYR
9   LEUTHRMETGLNGLNTHRTHRALALEUPRO
10   THRTRPGLYLEUALAPROSERGLYLYSGLY
11   ARGGLYLEUGLNHISPROPROPROVALGLY
12   SERGLNGLUGLYPROLYSASPPROGLUALA
13   TRPSERARGPROGLNGLYTRPTYRASNHIS
14   SERGLYLYS

Samples:

sample_1: C-terminal domain of RIPK3, [U-100% 13C; U-100% 15N], 18 uM; C-terminal domain of RIPK3, [U-100% 13C; U-100% 15N], 180 uM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHA gpsample_1isotropicsample_conditions_1
HSQC T1 etf 3gpsisample_1isotropicsample_conditions_1
HSQC T ref 3gpsisample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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