BMRB Entry 17289

Title:
NMR structure of calcium-loaded STIM2 EF-SAM.
Deposition date:
2010-11-09
Original release date:
2011-01-18
Authors:
Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko
Citation:

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).
PubMed: 21217057

Assembly members:

Assembly members:
Stromal_Interaction_Molecule_2, polymer, 150 residues, Formula weight is not available
CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts141
1H chemical shifts957

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Stromal_Interaction_Molecule_21
2CALCIUM ION2

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   GLYSERHISMETALASERTHRGLUGLUASP
2   ARGPHESERLEUGLUALALEUGLNTHRILE
3   HISLYSGLNMETASPASPASPLYSASPGLY
4   GLYILEGLUVALGLUGLUSERASPGLUPHE
5   ILEARGGLUASPMETLYSTYRLYSASPALA
6   THRASNLYSHISSERHISLEUHISARGGLU
7   ASPLYSHISILETHRILEGLUASPLEUTRP
8   LYSARGTRPLYSTHRSERGLUVALHISASN
9   TRPTHRLEUGLUASPTHRLEUGLNTRPLEU
10   ILEGLUPHEVALGLULEUPROGLNTYRGLU
11   LYSASNPHEARGASPASNASNVALLYSGLY
12   THRTHRLEUPROARGILEALAVALHISGLU
13   PROSERPHEMETILESERGLNLEULYSILE
14   SERASPARGSERHISARGGLNLYSLEUGLN
15   LEULYSALALEUASPVALVALLEUPHEGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_2
3D HCCH-COSYsample_3isotropicsample_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
AlphaFold Q9P246 P83093

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