BMRB Entry 30072

Title:
Calcium-free EF-hand domain of L-plastin
Deposition date:
2016-05-02
Original release date:
2017-04-13
Authors:
Ishida, Hiroaki; Jensen, K.; Woodman, A.; Hyndman, Eric; Vogel, Hans
Citation:

Citation: Ishida, Hiroaki; Jensen, Katharine; Woodman, Andrew; Hyndman, M. Eric; Vogel, Hans. "The Calcium-Dependent Switch Helix of L-Plastin Regulates Actin Bundling."  Sci. Rep. 7, 40662-40662 (2017).
PubMed: 28145401

Assembly members:

Assembly members:
Plastin-2, polymer, 82 residues, 9274.443 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts80
1H chemical shifts79

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 82 residues - 9274.443 Da.

1   METALAARGGLYSERVALSERASPGLUGLU
2   METMETGLULEUARGGLUALAPHEALALYS
3   VALASPTHRASPGLYASNGLYTYRILESER
4   PHEASNGLULEUASNASPLEUPHELYSALA
5   ALACYSLEUPROLEUPROGLYTYRARGVAL
6   ARGGLUILETHRGLUASNLEUMETALATHR
7   GLYASPLEUASPGLNASPGLYARGILESER
8   PHEASPGLUPHEILELYSILEPHEHISGLY
9   LEULYS

Samples:

sample_1: EF-hand domain of L-plastin, [U-98% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: EF-hand domain of L-plastin, [U-99% 13C; U-98% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_3: EF-hand domain of L-plastin, [U-99% 13C; U-98% 15N], 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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