BMRB Entry 19424

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19424

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone chemical shift assignments of delta exon 3 mouse RyR2 domain A
Deposition date:
2013-08-13
Original release date:
2014-02-12
Authors:
Amador, Fernando; Stathopulos, Peter; Seabrook, Genevieve; Ikura, Mitsuhiko
Citation:

Citation: Amador, Fernando; Kimlicka, Lynn; Stathopulos, Peter; Gasmi-Seabrook, Genevieve; Maclennan, David; Van Petegem, Filip; Ikura, Mitsuhiko. "Type 2 ryanodine receptor domain A contains a unique and dynamic -helix that transitions to a -strand in a mutant linked with a heritable cardiomyopathy."  J. Mol. Biol. 425, 4034-4046 (2013).
PubMed: 23978697

Assembly members:

Assembly members:
RyR2A, polymer, 177 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RyR2A: GSGSEIQFLRTDDEVVLQCT ATIHKEQQKLCLAAEGFGNR LCFLESTSNSKQVDVEKWKF MMKTAQGGGHRTLLYGHAIL LRHSYSGMYLCCLSTSRSST DKLAFDVGLQEDTTGEACWW TIHPASKQRSEGEKVRVGDD LILVSVSSERYLHLSYGNSS WHVDAAFQQTLWSVAPI

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts145
1H chemical shifts145

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RyR2A delta exon 31

Entities:

Entity 1, RyR2A delta exon 3 177 residues - Formula weight is not available

Residues 1-4 are a cloning artifact; residues 5-177 correspond to residues 10-217 of mouse RyR2 with the exon 3 deletion.

1   GLYSERGLYSERGLUILEGLNPHELEUARG
2   THRASPASPGLUVALVALLEUGLNCYSTHR
3   ALATHRILEHISLYSGLUGLNGLNLYSLEU
4   CYSLEUALAALAGLUGLYPHEGLYASNARG
5   LEUCYSPHELEUGLUSERTHRSERASNSER
6   LYSGLNVALASPVALGLULYSTRPLYSPHE
7   METMETLYSTHRALAGLNGLYGLYGLYHIS
8   ARGTHRLEULEUTYRGLYHISALAILELEU
9   LEUARGHISSERTYRSERGLYMETTYRLEU
10   CYSCYSLEUSERTHRSERARGSERSERTHR
11   ASPLYSLEUALAPHEASPVALGLYLEUGLN
12   GLUASPTHRTHRGLYGLUALACYSTRPTRP
13   THRILEHISPROALASERLYSGLNARGSER
14   GLUGLYGLULYSVALARGVALGLYASPASP
15   LEUILELEUVALSERVALSERSERGLUARG
16   TYRLEUHISLEUSERTYRGLYASNSERSER
17   TRPHISVALASPALAALAPHEGLNGLNTHR
18   LEUTRPSERVALALAPROILE

Samples:

sample_1: RyR2A, [U-13C; U-15N; U-2H], 0.6 mM; sodium phosphate 20 mM; sodium chloride 300 mM; DTT 5 mM; TCEP 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.328 M; pH: 7.4; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

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

XEASY, Bartels et al. - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP E9Q401
PDB
GB EGW04831
REF XP_002923703 XP_003473556 XP_003893766 XP_004028704 XP_004416638
AlphaFold Q9ERN6

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