BMRB Entry 25632

Name: Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism
Published: 2015-09-14

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PDB ID: 2n31
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25632
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2015-05-19

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):

Entity Sequences (FASTA):
entity: GPLGSMATTVSTQRGPVYIG ELPQDFLRITPTQQQRQVQL DAQAAQQLQYGGAVGTVG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	135
15N chemical shifts	46
1H chemical shifts	290

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 58 residues - 2424.767 Da.

1

GLY

PRO

LEU

GLY

SER

MET

ALA

THR

VAL

2

SER

THR

GLN

ARG

GLY

PRO

VAL

TYR

ILE

GLY

3

GLU

LEU

PRO

GLN

ASP

PHE

LEU

ARG

ILE

THR

4

PRO

THR

GLN

ARG

GLN

VAL

GLN

LEU

5

ASP

ALA

GLN

ALA

GLN

LEU

GLN

TYR

6

GLY

ALA

VAL

GLY

THR

VAL

GLY

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_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