BMRB Entry 19363
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19363
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Title: Solution structure of the STIM1 CC1-CC2 homodimer in complex with two Orai1 C-terminal domains. PubMed: 24351972
Deposition date: 2013-07-12 Original release date: 2014-01-13
Authors: Stathopulos, Peter; Ikura, Mitsuhiko
Citation: Stathopulos, Peter; Schindl, Rainer; Fahrner, Marc; Zheng, Le; Gasmi-Seabrook, Genevieve; Muik, Martin; Romanin, Christoph; Ikura, Mitsuhiko. "STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry" Nat. Commun. 4, 2963-2963 (2013).
Assembly members:
STIM1_CC1-CC2, polymer, 82 residues, 9703.089 Da.
Orai1, polymer, 23 residues, 2654.828 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):
STIM1_CC1-CC2: GSHMASSRQKYAEEELEQVR
EALRKAEKELESHSSWYAPE
ALQKWLQLTHEVEVQYYNIK
KQNAEKQLLVAKEGAEKIKK
KR
Orai1: GSELNELAEFARLQDQLDHR
GDH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 425 |
15N chemical shifts | 105 |
1H chemical shifts | 715 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | STIM1_CC1-CC2_1 | 1 |
2 | Orai1_1 | 2 |
3 | STIM1 | 1 |
4 | Orai1_2 | 2 |
Entities:
Entity 1, STIM1_CC1-CC2_1 82 residues - 9703.089 Da.
Residues -5-0 (i.e. GSHMAS) are a cloning artifact.
1 | GLY | SER | HIS | MET | ALA | SER | SER | ARG | GLN | LYS | ||||
2 | TYR | ALA | GLU | GLU | GLU | LEU | GLU | GLN | VAL | ARG | ||||
3 | GLU | ALA | LEU | ARG | LYS | ALA | GLU | LYS | GLU | LEU | ||||
4 | GLU | SER | HIS | SER | SER | TRP | TYR | ALA | PRO | GLU | ||||
5 | ALA | LEU | GLN | LYS | TRP | LEU | GLN | LEU | THR | HIS | ||||
6 | GLU | VAL | GLU | VAL | GLN | TYR | TYR | ASN | ILE | LYS | ||||
7 | LYS | GLN | ASN | ALA | GLU | LYS | GLN | LEU | LEU | VAL | ||||
8 | ALA | LYS | GLU | GLY | ALA | GLU | LYS | ILE | LYS | LYS | ||||
9 | LYS | ARG |
Entity 2, Orai1_1 23 residues - 2654.828 Da.
Residues -1-0 (i.e. GS) are a cloning artifact.
1 | GLY | SER | GLU | LEU | ASN | GLU | LEU | ALA | GLU | PHE | ||||
2 | ALA | ARG | LEU | GLN | ASP | GLN | LEU | ASP | HIS | ARG | ||||
3 | GLY | ASP | HIS |
Samples:
sample_1: STIM1_CC1-CC2, [U-100% 15N], 0.25 mM; Orai1 3.0 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; H2O 90%; D2O 10%
sample_2: STIM1_CC1-CC2, [U-99% 13C; U-99% 15N], 0.25 mM; Orai1 3.0 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; H2O 90%; D2O 10%
sample_3: STIM1_CC1-CC2, [U-99% 13C; U-99% 15N], 0.25 mM; Orai1 3.0 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; D2O 100%
sample_4: STIM1_CC1-CC2 2.5 mM; Orai1, [U-99% 15N], 0.25 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; H2O 90%; D2O 10%
sample_5: STIM1_CC1-CC2 2.5 mM; Orai1, [U-99% 13C; U-99% 15N], 0.25 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; D2O 100%
sample_conditions_1: ionic strength: 0.02 M; pH: 5.5; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_5 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_5 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
BMRB | 19362 |
PDB | |
GB | ADO20317 AAH13386 AAH15369 AAH23149 AAH75831 AAH88225 |
REF | NP_001264890 XP_003910388 XP_003923449 XP_003951854 XP_004016320 NP_001014004 NP_001092472 NP_001166990 NP_116179 NP_780632 |
DBJ | BAB55068 BAC35045 BAC39533 BAF47905 |
EMBL | CAN36426 |
SP | Q5M848 Q8BWG9 Q96D31 |
TPG | DAA20623 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts