BMRB Entry 51173
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51173
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Title: Resonance assignment of STIM1 CC1 d296 R304 mutant PubMed: 36749824
Deposition date: 2021-11-10 Original release date: 2023-01-31
Authors: Rathner, Petr; Cerofolini, Linda; Grabmayr, Herwig; Ravera, Enrico; Fahrner, Marc; Luchinat, Claudio; Romanin, Christoph; Mueller, Norbert
Citation: Gamage, Thilini; Grabmayr, Herwig; Horvath, Ferdinand; Fahrner, Marc; Misceo, Doriana; Louch, William Edward; Gunnes, Gjermund; Pullisaar, Helen; Reseland, Janne Elin; Lyngstadaas, Staale Petter; Holmgren, Asbjorn; Amundsen, Silja; Rathner, Petr; Cerofolini, Linda; Ravera, Enrico; Krobath, Heinrich; Luchinat, Claudio; Renger, Thomas; Muller, Norbert; Romanin, Christoph; Frengen, Eirik. "A single amino acid deletion in STIM1 reverts the effects of the Stormorken Syndrome mutation" Sci. Signal. 16, eadd0509-eadd0509 (2023).
Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available
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 Vector: pGEX 4T-1
Entity Sequences (FASTA):
entity_1: GSPEFNRYSKEHMKKMMKDL
EGLHRAEQSLHDLQERLHKA
QEEHRTVEVEKVHLEKKLRD
EINLAKQAQRLKELWEGTEN
ERSRQKYAEEELEQVREALR
KAEKELESHSSWYA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 161 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | STIM1 CC1 R304W | 1 |
Entities:
Entity 1, STIM1 CC1 R304W 114 residues - Formula weight is not available
| 1 | GLY | SER | PRO | GLU | PHE | ASN | ARG | TYR | SER | LYS | ||||
| 2 | GLU | HIS | MET | LYS | LYS | MET | MET | LYS | ASP | LEU | ||||
| 3 | GLU | GLY | LEU | HIS | ARG | ALA | GLU | GLN | SER | LEU | ||||
| 4 | HIS | ASP | LEU | GLN | GLU | ARG | LEU | HIS | LYS | ALA | ||||
| 5 | GLN | GLU | GLU | HIS | ARG | THR | VAL | GLU | VAL | GLU | ||||
| 6 | LYS | VAL | HIS | LEU | GLU | LYS | LYS | LEU | ARG | ASP | ||||
| 7 | GLU | ILE | ASN | LEU | ALA | LYS | GLN | ALA | GLN | ARG | ||||
| 8 | LEU | LYS | GLU | LEU | TRP | GLU | GLY | THR | GLU | ASN | ||||
| 9 | GLU | ARG | SER | ARG | GLN | LYS | TYR | ALA | GLU | GLU | ||||
| 10 | GLU | LEU | GLU | GLN | VAL | ARG | GLU | ALA | LEU | ARG | ||||
| 11 | LYS | ALA | GLU | LYS | GLU | LEU | GLU | SER | HIS | SER | ||||
| 12 | SER | TRP | TYR | ALA |
Samples:
sample_1: TRIS 20 mM; SDS, [U-99% 2H], 7 mM; STIM1 CC1 R304W, [U-95% 13C; U-95% 15N], 0.3 mM; H2O, [U-99% 2H], 10 % w/v; H2O 90 % w/v
sample_conditions_1: ionic strength: 0.02 M; pH: 7.25; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| CON | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.4.2 - chemical shift assignment
TOPSPIN v3.5, 3.6 - collection
NMR spectrometers:
- Bruker Avance 950 MHz
- Bruker Avance 900 MHz
- Bruker AVANCE III 700 MHz
- Bruker AVANCE NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts