BMRB Entry 34708

Name: Structure in solution of the TANGO1 cargo-binding domain (21-131)
Published: 2023-02-14

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PDB ID: 7r3m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34708
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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:

Structure in solution of the TANGO1 cargo-binding domain (21-131)

Deposition date:

2022-02-07

Original release date:

2023-02-14

Authors:

Arnolds, O.; Stoll, R.

Citation:

Citation: Arnolds, O.; Stoll, R.. "Characterization of a fold in TANGO1 evolved from SH3 domains for the export of bulky cargos" Nat. Commun. 14, 2273-2273 (2023).
PubMed: 37080980

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 12890.382 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):

Entity Sequences (FASTA):
entity_1: MPGQLDPSTGRRFSEHKLCA DDECSMLMYRGEALEDFTGP DCRFVNFKKGDPVYVYYKLA RGWPEVWAGSVGRTFGYFPK DLIQVVHEYTKEELQVPTDE TDFVCFDGGRDD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	475
15N chemical shifts	107
1H chemical shifts	733

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 112 residues - 12890.382 Da.

1

MET

PRO

GLY

GLN

LEU

ASP

PRO

SER

THR

GLY

2

ARG

PHE

SER

GLU

HIS

LYS

LEU

CYS

ALA

3

ASP

GLU

CYS

SER

MET

LEU

MET

TYR

ARG

4

GLY

GLU

ALA

LEU

GLU

ASP

PHE

THR

GLY

PRO

5

ASP

CYS

ARG

PHE

VAL

ASN

PHE

LYS

GLY

6

ASP

PRO

VAL

TYR

VAL

TYR

LYS

LEU

ALA

7

ARG

GLY

TRP

PRO

GLU

VAL

TRP

ALA

GLY

SER

8

VAL

GLY

ARG

THR

PHE

GLY

TYR

PHE

PRO

LYS

9

ASP

LEU

ILE

GLN

VAL

HIS

GLU

TYR

THR

10

LYS

GLU

LEU

GLN

VAL

PRO

THR

ASP

GLU

11

THR

ASP

PHE

VAL

CYS

PHE

ASP

GLY

ARG

12

ASP

Samples:

sample_1: TANGO1(21-131), [U-100% 13C; U-100% 15N], 1 mM; HEPES 25 mM; NaCl 150 mM; CHAPS 1%; NaN3 0.02 % (w/v)

sample_conditions_1: ionic strength: 195 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
4D 13C-1H-13C HSQCNOESYHSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker DRX600 600 MHz
Bruker AVANCE III HD 700 MHz

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