Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53520

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Chemical shift assignments for the disordered N-terminal domain (NTD, 1-89) of human PARP2
Published: 2026-03-24

Title:

Chemical shift assignments for the disordered N-terminal domain (NTD, 1-89) of human PARP2

Deposition date:

2026-02-05

Original release date:

2026-03-24

Authors:

Virk, Rajbinder; Kim, Tae Hun

Citation:

Citation: Virk, Rajbinder; Kim, Tae Hun. "1H, 13C, and 15N resonance assignments of the N-terminal intrinsically disordered region and WGR domain of human PARP2" Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, 9795.10 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAARRRRSTGGGRARALNES KRVNNGNTAPEDSSPAKKTR RCQRQESKKMPVAGGKANKD RTEDKQDGMPGRSWASKRVS ESVKALLLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	259
15N chemical shifts	166
1H chemical shifts	166

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP2 NTD	1

Entities:

Entity 1, PARP2 NTD 89 residues - 9795.10 Da.

1

MET

ALA

ARG

SER

THR

GLY

2

GLY

ARG

ALA

ARG

ALA

LEU

ASN

GLU

SER

3

LYS

ARG

VAL

ASN

GLY

ASN

THR

ALA

PRO

4

GLU

ASP

SER

PRO

ALA

LYS

THR

ARG

5

ARG

CYS

GLN

ARG

GLN

GLU

SER

LYS

MET

6

PRO

VAL

ALA

GLY

LYS

ALA

ASN

LYS

ASP

7

ARG

THR

GLU

ASP

LYS

GLN

ASP

GLY

MET

PRO

8

GLY

ARG

SER

TRP

ALA

SER

LYS

ARG

VAL

SER

9

GLU

SER

VAL

LYS

ALA

LEU

LYS

Samples:

sample_1: PARP2 NTD, [U-99% 13C; U-99% 15N], 1 mM; MES 25 mM; DTT 2 mM

sample_conditions_1: pH: 5.5; temperature: 288.15 K

sample_conditions_2: pH: 5.5; temperature: 283.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_2
3D HN(CO)CA	sample_1	isotropic	sample_conditions_2
3D HNN	sample_1	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.2.0 - collection

NMRPipe v2024.061.14.29 - processing

CcpNMR v3.3.4.1 - data analysis

NMR spectrometers:

Bruker AVANCE NEO 700 MHz 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 53520