BMRB Entry 17289

Name: NMR structure of calcium-loaded STIM2 EF-SAM.
Published: 2011-01-18

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PDB ID: 2l5y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17289
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	141
1H chemical shifts	957

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

PDB	2L5Y
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

Biological Magnetic Resonance Data Bank