Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53586

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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:

Assignment of 1H, 13C, 15N backbone chemical shifts of BARD1 124-270

Deposition date:

2026-02-25

Original release date:

2026-09-02

Authors:

Dinh, Hoang; Jasper, Angela; Baudin, Antoine; Sung, Patrick; Libich, David

Citation:

Citation: Dinh, Hoang; Jasper, Angela; Baudin, Antoine; Sung, Patrick; Libich, David. "The1H, 15N and13C backbone resonance assignments of an intrinsically disordered region (124-270) of BRCA1 associated RING domain 1 (BARD1) " Biomol. NMR Assign. 20, 26-26 (2026).
PubMed: 42678585

Assembly members:

Assembly members:
entity_1, polymer, 147 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: pAT-Trx

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KEDKPRKSLFNDAGNKKNSI KMWFSPRSKKVRYVVSKASV QTQPAIKKDASAQQDSYEFV SPSPPADVSERAKKASARSG KKQKKKTLAEINQKWNLEAE KEDGEFDSKEESKQKLVSFC SQPSVISSPQINGEIDLLAS GSLTESE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	134
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BARD1 124-270	1

Entities:

Entity 1, BARD1 124-270 147 residues - Formula weight is not available

1

LYS

GLU

ASP

LYS

PRO

ARG

LYS

SER

LEU

PHE

2

ASN

ASP

ALA

GLY

ASN

LYS

ASN

SER

ILE

3

LYS

MET

TRP

PHE

SER

PRO

ARG

SER

LYS

4

VAL

ARG

TYR

VAL

SER

LYS

ALA

SER

VAL

5

GLN

THR

GLN

PRO

ALA

ILE

LYS

ASP

ALA

6

SER

ALA

GLN

ASP

SER

TYR

GLU

PHE

VAL

7

SER

PRO

SER

PRO

ALA

ASP

VAL

SER

GLU

8

ARG

ALA

LYS

ALA

SER

ALA

ARG

SER

GLY

9

LYS

GLN

LYS

THR

LEU

ALA

GLU

10

ILE

ASN

GLN

LYS

TRP

ASN

LEU

GLU

ALA

GLU

11

LYS

GLU

ASP

GLY

GLU

PHE

ASP

SER

LYS

GLU

12

GLU

SER

LYS

GLN

LYS

LEU

VAL

SER

PHE

CYS

13

SER

GLN

PRO

SER

VAL

ILE

SER

PRO

GLN

14

ILE

ASN

GLY

GLU

ILE

ASP

LEU

ALA

SER

15

GLY

SER

LEU

THR

GLU

SER

GLU

Samples:

sample_1: BARD1 124-270, [U-100% 13C; U-100% 15N], 90 uM; KCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR - chemical shift assignment

NMRPipe - processing

NMRDraw - processing

TOPSPIN - collection

NMR spectrometers:

Bruker Avance 700 MHz

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

BMRB Entry 53586