BMRB Entry 27983

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27983

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Title:
Backbone 1H, 13C, and 15N chemical shift assignments for C. elegans STIM EF-SAM (form 2) in the absence of calcium.
Deposition date:
2019-07-22
Original release date:
2019-11-07
Authors:
Enomoto, Masahiro; Nishikawa, Tadateru; Back, Sung-In; Ishiyama, Noboru; Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko
Citation:

Citation: Enomoto, Masahiro; Nishikawa, Tadateru; Back, Sung-In; Ishiyama, Noboru; Zheng, Le; Stathopulos, Peter; Ikura, Mitsuhiko. "Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain"  J. Mol. Biol. 432, 367-383 (2020).
PubMed: 31626806

Assembly members:

Assembly members:
stromal_interaction_molecule, polymer, 176 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: roundworm   Taxonomy ID: 6293   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
stromal_interaction_molecule: GSHMASDRVTRNVEVTAEEE KIRDKLGYEAIRDIHRDMDD DHSGSIDRNESTGFMKEDMQ MRGSERTRRENKFHGDDDAI TVDDLWEAWFESIERTWTNE RLVEWLINDVNLPSIVEAVK AKKIDGKILPRFASPNSDFL NKELGIKSSVYRQKLRLNSL DVVLFGYKDNNNRTKD

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts107
1H chemical shifts107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ca2+ depleted form 21

Entities:

Entity 1, Ca2+ depleted form 2 176 residues - Formula weight is not available

Residues -5 to 0 are residual cloning artifact residues. Residues 23 to 192 are native protein residues.

1   GLYSERHISMETALASERASPARGVALTHR
2   ARGASNVALGLUVALTHRALAGLUGLUGLU
3   LYSILEARGASPLYSLEUGLYTYRGLUALA
4   ILEARGASPILEHISARGASPMETASPASP
5   ASPHISSERGLYSERILEASPARGASNGLU
6   SERTHRGLYPHEMETLYSGLUASPMETGLN
7   METARGGLYSERGLUARGTHRARGARGGLU
8   ASNLYSPHEHISGLYASPASPASPALAILE
9   THRVALASPASPLEUTRPGLUALATRPPHE
10   GLUSERILEGLUARGTHRTRPTHRASNGLU
11   ARGLEUVALGLUTRPLEUILEASNASPVAL
12   ASNLEUPROSERILEVALGLUALAVALLYS
13   ALALYSLYSILEASPGLYLYSILELEUPRO
14   ARGPHEALASERPROASNSERASPPHELEU
15   ASNLYSGLULEUGLYILELYSSERSERVAL
16   TYRARGGLNLYSLEUARGLEUASNSERLEU
17   ASPVALVALLEUPHEGLYTYRLYSASPASN
18   ASNASNARGTHRLYSASP

Samples:

sample_1: stromal interaction molecule, [U-99% 15N], 0.2 mM; TRIS 20 mM; potassium chloride 100 mM

sample_2: stromal interaction molecule, [U-99% 13C; U-99% 15N], 0.2 mM; TRIS 20 mM; potassium chloride 100 mM

sample_3: stromal interaction molecule, [U-99% 13C; U-99% 15N], 0.2 mM; TRIS 20 mM; potassium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

sample_conditions_2: ionic strength: 100 mM; pD: 7.5 pD; 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 HNCOsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_2

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMRDraw, Delaglio, Zhengrong and Bax - processing

NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

NCBI ABG89384.1
UNP G5EF60
AlphaFold H2L0R5

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