BMRB Entry 17289
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17289
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Title: NMR structure of calcium-loaded STIM2 EF-SAM. PubMed: 21217057
Deposition date: 2010-11-09 Original release date: 2011-01-18
Authors: Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko
Citation: Zheng, Le; Stathopulos, Peter; Schindl, Rainer; Li, Guang-Yao; Romanin, Christoph; Ikura, Mitsuhiko. "Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-operated calcium entry." Proc. Natl. Acad. Sci. U. S. A. 108, 1337-1342 (2011).
Assembly members:
Stromal_Interaction_Molecule_2, polymer, 150 residues, Formula weight is not available
CA, non-polymer, 40.078 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):
Stromal_Interaction_Molecule_2: GSHMASTEEDRFSLEALQTI
HKQMDDDKDGGIEVEESDEF
IREDMKYKDATNKHSHLHRE
DKHITIEDLWKRWKTSEVHN
WTLEDTLQWLIEFVELPQYE
KNFRDNNVKGTTLPRIAVHE
PSFMISQLKISDRSHRQKLQ
LKALDVVLFG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 431 |
15N chemical shifts | 141 |
1H chemical shifts | 957 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Stromal_Interaction_Molecule_2 | 1 |
2 | CALCIUM ION | 2 |
Entities:
Entity 1, Stromal_Interaction_Molecule_2 150 residues - Formula weight is not available
Residues 1 to 144 are equivalent residues 62 to 205 of the STIM2 gene. Residue 145 is Calcium ion.
1 | GLY | SER | HIS | MET | ALA | SER | THR | GLU | GLU | ASP | |
2 | ARG | PHE | SER | LEU | GLU | ALA | LEU | GLN | THR | ILE | |
3 | HIS | LYS | GLN | MET | ASP | ASP | ASP | LYS | ASP | GLY | |
4 | GLY | ILE | GLU | VAL | GLU | GLU | SER | ASP | GLU | PHE | |
5 | ILE | ARG | GLU | ASP | MET | LYS | TYR | LYS | ASP | ALA | |
6 | THR | ASN | LYS | HIS | SER | HIS | LEU | HIS | ARG | GLU | |
7 | ASP | LYS | HIS | ILE | THR | ILE | GLU | ASP | LEU | TRP | |
8 | LYS | ARG | TRP | LYS | THR | SER | GLU | VAL | HIS | ASN | |
9 | TRP | THR | LEU | GLU | ASP | THR | LEU | GLN | TRP | LEU | |
10 | ILE | GLU | PHE | VAL | GLU | LEU | PRO | GLN | TYR | GLU | |
11 | LYS | ASN | PHE | ARG | ASP | ASN | ASN | VAL | LYS | GLY | |
12 | THR | THR | LEU | PRO | ARG | ILE | ALA | VAL | HIS | GLU | |
13 | PRO | SER | PHE | MET | ILE | SER | GLN | LEU | LYS | ILE | |
14 | SER | ASP | ARG | SER | HIS | ARG | GLN | LYS | LEU | GLN | |
15 | LEU | LYS | ALA | LEU | ASP | VAL | VAL | LEU | PHE | GLY |
Entity 2, CALCIUM ION - Ca - 40.078 Da.
1 | CA |
Samples:
sample_1: PROTEIN (Stromal Interaction Molecule 2), [U-99% 15N], 0.5 0.7 mM; TRIS 20 mM; sodium chloride 100 mM; Calcium Ion 10 mM; H2O 90%; D2O 10%
sample_2: PROTEIN (Stromal Interaction Molecule 2), [U-99% 13C; U-99% 15N], 0.5 0.7 mM; TRIS 20 mM; sodium chloride 100 mM; Calcium Ion 10 mM; H2O 90%; D2O 10%
sample_3: PROTEIN (Stromal Interaction Molecule 2), [U-99% 13C; U-99% 15N], 0.5 0.7 mM; TRIS 20 mM; sodium chloride 100 mM; CALCIUM ION 10 mM; D2O 100%
sample_conditions_1: ionic strength: 105 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K
sample_conditions_2: ionic strength: 105 mM; pD: 7.9; pressure: 1 atm; temperature: 288 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_2 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_2 |
3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_2 |
3D HCCH-COSY | sample_3 | isotropic | sample_conditions_2 |
Software:
CNS vv1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA vv2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
PDB | |
DBJ | BAA96006 BAD32461 BAG10078 BAG53377 |
EMBL | CAB66512 CAN36430 |
GB | AAI36450 AAI37882 AAI45002 AAI46662 AAI52555 |
REF | NP_001074572 NP_001099220 NP_001162588 NP_001162589 NP_065911 |
SP | P83093 Q9P246 |
TPG | DAA28777 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts