BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25602

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25602
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism   PubMed: 26320582

Deposition date: 2015-05-11 Original release date: 2015-09-14

Authors: Xiao, Shuyan; Armstrong, Geoffrey; Capelluto, Daniel

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).

Assembly members:
entity, polymer, 100 residues, 11089.725 Da.

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

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

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

Data sets:
Data typeCount
13C chemical shifts263
15N chemical shifts87
1H chemical shifts87

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 100 residues - 11089.725 Da.

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

Samples:

sample_1: Tom1 GAT, [U-99% 13C; U-99% 15N], 0.9 mM; Tollip TBD 1.1 mM; DSS 50 uM; potassium chloride 50 mM; TRIS, [U-2H], 20 mM; sodium azide 1 mM; DTT, [U-2H], 1 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H- 15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian Agilent DD2 900 MHz

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