BMRB Entry 25632

Title:
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism
Deposition date:
2015-05-19
Original release date:
2015-09-14
Authors:
Xiao, Shuyan; Armstrong, Geoffrey; Capelluto, Daniel
Citation:

Citation: Xiao, Shuyan; Brannon, Mary; Zhao, Xiaolin; Fread, Kristen; Ellena, Jeffrey; Bushweller, John; Finkielstein, Carla; Armstrong, Geoffrey; Capelluto, Daniel. "Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism"  Structure 23, 1910-1920 (2015).
PubMed: 26320582

Assembly members:

Assembly members:
entity, polymer, 58 residues, 2424.767 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: PGEX-6P-1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts135
15N chemical shifts46
1H chemical shifts290

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 58 residues - 2424.767 Da.

1   GLYPROLEUGLYSERMETALATHRTHRVAL
2   SERTHRGLNARGGLYPROVALTYRILEGLY
3   GLULEUPROGLNASPPHELEUARGILETHR
4   PROTHRGLNGLNGLNARGGLNVALGLNLEU
5   ASPALAGLNALAALAGLNGLNLEUGLNTYR
6   GLYGLYALAVALGLYTHRVALGLY

Samples:

sample_1: TBD, [U-99% 13C; U-99% 15N], 0.9 mM; GAT 1.1 mM; DSS 50 uM; TRIS, [U-2H], 20 mM; potassium chloride 50 mM; DTT, [U-2H], 1 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

ROSETTA, Bhattacharya and Montelione, Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, ROSETTA - data analysis, processing, structure solution

NMR spectrometers:

  • Varian DD2 900 MHz
  • Bruker Avance 600 MHz

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