Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53521

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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 WGR domain (90-212) of human PARP2
Published: 2026-03-24

Title:

Chemical shift assignments for the WGR domain (90-212) 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, 123 residues, 14305.23 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: GKAPVDPECTAKVGKAHVYC EGNDVYDVMLNQTNLQFNNN KYYLIQLLEDDAQRNFSVWM RWGRVGKMGQHSLVACSGNL NKAKEIFQKKFLDKTKNNWE DREKFEKVPGKYDMLQMDYA TNT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	353
15N chemical shifts	119
1H chemical shifts	425

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP2 WGR	1

Entities:

Entity 1, PARP2 WGR 123 residues - 14305.23 Da.

1

GLY

LYS

ALA

PRO

VAL

ASP

PRO

GLU

CYS

THR

2

ALA

LYS

VAL

GLY

LYS

ALA

HIS

VAL

TYR

CYS

3

GLU

GLY

ASN

ASP

VAL

TYR

ASP

VAL

MET

LEU

4

ASN

GLN

THR

ASN

LEU

GLN

PHE

ASN

5

LYS

TYR

LEU

ILE

GLN

LEU

GLU

ASP

6

ASP

ALA

GLN

ARG

ASN

PHE

SER

VAL

TRP

MET

7

ARG

TRP

GLY

ARG

VAL

GLY

LYS

MET

GLY

GLN

8

HIS

SER

LEU

VAL

ALA

CYS

SER

GLY

ASN

LEU

9

ASN

LYS

ALA

LYS

GLU

ILE

PHE

GLN

LYS

10

PHE

LEU

ASP

LYS

THR

LYS

ASN

TRP

GLU

11

ASP

ARG

GLU

LYS

PHE

GLU

LYS

VAL

PRO

GLY

12

LYS

TYR

ASP

MET

LEU

GLN

MET

ASP

TYR

ALA

13

THR

ASN

THR

Samples:

sample_2: PARP2 WGR, [U-99% 13C; U-99% 15N], 370 uM; MES 25 mM; DTT 2 mM

sample_conditions_1: pH: 5.5; temperature: 288.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D hahbcbcaconnh	sample_2	isotropic	sample_conditions_1
3D HNN	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	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 53521