BMRB Entry 51523

Name: Backbone assignments of BARD1 Ser-141-216
Published: 2023-04-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51523

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

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone assignments of BARD1 Ser-141-216

Deposition date:

2022-07-20

Original release date:

2023-04-17

Authors:

Witus, Samuel; Tuttle, Lisa; Zelter, Alex; Kermoade, Klaiten; Wilburn, Damien; Zhao, Weixing; Davis, Trisha; Brzovic, Peter; Klevit, Rachel

Citation:

Citation: Witus, Samuel; Tuttle, Lisa; Li, Wenjing; Zelter, Alex; Wang, Meiling; Kermoade, Klaiten; Wilburn, Damien; Davis, Trisha; Brzovic, Peter; Zhao, Weixing; Klevit, Rachel. "BRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation" EMBO J. 42, e113565-e113565 (2023).
PubMed: 37305927

Assembly members:

Assembly members:
entity_1, polymer, 77 residues, Formula weight is not available

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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNSIKMWFSPRSKKVRYVVS KASVQTQPAIKKDASAQQDS YEFVSPSPPADVSERAKKAS ARSGKKQKKKTLAEINQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	63
1H chemical shifts	120

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BARD1 Ser-141-216	1

Entities:

Entity 1, BARD1 Ser-141-216 77 residues - Formula weight is not available

1

SER

ASN

SER

ILE

LYS

MET

TRP

PHE

SER

PRO

2

ARG

SER

LYS

VAL

ARG

TYR

VAL

SER

3

LYS

ALA

SER

VAL

GLN

THR

GLN

PRO

ALA

ILE

4

LYS

ASP

ALA

SER

ALA

GLN

ASP

SER

5

TYR

GLU

PHE

VAL

SER

PRO

SER

PRO

ALA

6

ASP

VAL

SER

GLU

ARG

ALA

LYS

ALA

SER

7

ALA

ARG

SER

GLY

LYS

GLN

LYS

8

THR

LEU

ALA

GLU

ILE

ASN

GLN

Samples:

sample_1: BARD1 Ser-141-216, [U-100% 13C; U-100% 15N], 500 uM; D2O, [U-100% 2H], 7%; MOPS-NaOH 25 mM; sodium chloride 100 mM; EDTA 1 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 100 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.4 - collection

NMRPipe v9.6 rev 2018.143.16.03 - processing

NMRViewJ v9.2.0-b20 - chemical shift assignment

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