BMRB Entry 26574

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26574
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism
Deposition date:
2015-05-08
Original release date:
2015-12-22
Authors:
Xiao, Shuyan; 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:
GAT, polymer, 100 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GAT: GPLGSEQIGKLRSELEMVSG NVRVMSEMLTELVPTQAEPA DLELLQELNRTCRAMQQRVL ELIPQIANEQLTEELLIVND NLNNVFLRHERFERFRTGQT

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts88
1H chemical shifts88

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1GAT1

Entities:

Entity 1, GAT 100 residues - Formula weight is not available

1   GLYPROLEUGLYSERGLUGLNILEGLYLYS
2   LEUARGSERGLULEUGLUMETVALSERGLY
3   ASNVALARGVALMETSERGLUMETLEUTHR
4   GLULEUVALPROTHRGLNALAGLUPROALA
5   ASPLEUGLULEULEUGLNGLULEUASNARG
6   THRCYSARGALAMETGLNGLNARGVALLEU
7   GLULEUILEPROGLNILEALAASNGLUGLN
8   LEUTHRGLUGLULEULEUILEVALASNASP
9   ASNLEUASNASNVALPHELEUARGHISGLU
10   ARGPHEGLUARGPHEARGTHRGLYGLNTHR

Samples:

sample_1: GAT, [U-99% 13C; U-99% 15N], 1.0 mM; potassium chloride 50 mM; TRIS, [U-2H], 20 mM; sodium azide 1 mM; DSS 50 uM; DTT, [U-2H], 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 HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

SPARKY, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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