BMRB Entry 19362

Title:
Solution Structure of the STIM1 CC1-CC2 homodimer.
Deposition date:
2013-07-12
Original release date:
2014-01-13
Authors:
Stathopulos, Peter; Ikura, Mitsuhiko
Citation:

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).
PubMed: 24351972

Assembly members:

Assembly members:
STIM1_CC1-CC2, polymer, 82 residues, 9703.089 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: pET-28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts693
15N chemical shifts156
1H chemical shifts1076

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1STIM1_CC1-CC21
2STIM1_CC1-CC21

Entities:

Entity 1, STIM1_CC1-CC2 82 residues - 9703.089 Da.

Residues -5-0 (i.e. GSHMAS) are a cloning artifact.

1   GLYSERHISMETALASERSERARGGLNLYS
2   TYRALAGLUGLUGLULEUGLUGLNVALARG
3   GLUALALEUARGLYSALAGLULYSGLULEU
4   GLUSERHISSERSERTRPTYRALAPROGLU
5   ALALEUGLNLYSTRPLEUGLNLEUTHRHIS
6   GLUVALGLUVALGLNTYRTYRASNILELYS
7   LYSGLNASNALAGLULYSGLNLEULEUVAL
8   ALALYSGLUGLYALAGLULYSILELYSLYS
9   LYSARG

Samples:

sample_1: STIM1_CC1-CC2, [U-99% 15N], 0.5 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], 0.5 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], 0.5 mM; bis-TRIS 20 mM; TFE, [U-99% 2H], 0.175 v/v; D2O 100%

sample_4: STIM1_CC1-CC2, [U-99% 13C; U-99% 15N], 0.5 mM; STIM1_CC1-CC2 0.5 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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D C(CO)NH TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NH TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-13C-1H-12C/14N xfilt NOESYsample_4isotropicsample_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:

REF NP_003147.2 NP_001264890 XP_003910388 XP_003923449 XP_003951854 XP_004016320
BMRB 19363
PDB
GB ADO20317

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