BMRB Entry 18767

Name: Hug1: an intrinsically disordered protein involved in the DNA damage response.
Published: 2019-09-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18767

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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:

Hug1: an intrinsically disordered protein involved in the DNA damage response.

Deposition date:

2012-10-08

Original release date:

2019-09-05

Authors:

Ochsenbein, Francoise; Richet, Nicolas; Meurisse, Julie; Peyroche, Anne

Citation:

Citation: Meurisse, Julie; Bacquin, Agathe; Richet, Nicolas; Charbonnier, Jean-Baptiste; Ochsenbein, Francoise; Peyroche, Anne. "Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit" Nucleic Acids Res. 42, 13174-13185 (2014).
PubMed: 25378334

Assembly members:

Assembly members:
Hug1, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGSTbis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hug1: GAMADPMTMDQGLNPKQFFL DDVVLQDTLCSMSNRVNKSV KTGYLFPKDHVPSANIIAVE RRGGLSDIGKNTSN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	211
15N chemical shifts	70
1H chemical shifts	317

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hug1	1

Entities:

Entity 1, Hug1 74 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

ASP

PRO

MET

THR

MET

ASP

2

GLN

GLY

LEU

ASN

PRO

LYS

GLN

PHE

LEU

3

ASP

VAL

LEU

GLN

ASP

THR

LEU

CYS

4

SER

MET

SER

ASN

ARG

VAL

ASN

LYS

SER

VAL

5

LYS

THR

GLY

TYR

LEU

PHE

PRO

LYS

ASP

HIS

6

VAL

PRO

SER

ALA

ASN

ILE

ALA

VAL

GLU

7

ARG

GLY

LEU

SER

ASP

ILE

GLY

LYS

8

ASN

THR

SER

ASN

Samples:

sample_1: Hug1, [U-13C; U-15N], 60 uM; sodium phosphate 20 mM; sodium chloride 50 mM; EDTA 0.1 mM; DSS 0.1 mM; sodium azide 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 5; pressure: 1 atm; temperature: 284 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN_3.0, Bruker Biospin - collection, data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz

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