Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53522

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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 NTD-WGR domain of human PARP2
Published: 2026-03-24

Title:

Chemical shift assignments for the NTD-WGR domain 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, 212 residues, 24082.32 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 ESVKALLLKGKAPVDPECTA KVGKAHVYCEGNDVYDVMLN QTNLQFNNNKYYLIQLLEDD AQRNFSVWMRWGRVGKMGQH SLVACSGNLNKAKEIFQKKF LDKTKNNWEDREKFEKVPGK YDMLQMDYATNT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_4

Data type	Count
15N chemical shifts	163
1H chemical shifts	163

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP2 NTD-WGR	1

Entities:

Entity 1, PARP2 NTD-WGR 212 residues - 24082.32 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

GLY

10

LYS

ALA

PRO

VAL

ASP

PRO

GLU

CYS

THR

ALA

11

LYS

VAL

GLY

LYS

ALA

HIS

VAL

TYR

CYS

GLU

12

GLY

ASN

ASP

VAL

TYR

ASP

VAL

MET

LEU

ASN

13

GLN

THR

ASN

LEU

GLN

PHE

ASN

LYS

14

TYR

LEU

ILE

GLN

LEU

GLU

ASP

15

ALA

GLN

ARG

ASN

PHE

SER

VAL

TRP

MET

ARG

16

TRP

GLY

ARG

VAL

GLY

LYS

MET

GLY

GLN

HIS

17

SER

LEU

VAL

ALA

CYS

SER

GLY

ASN

LEU

ASN

18

LYS

ALA

LYS

GLU

ILE

PHE

GLN

LYS

PHE

19

LEU

ASP

LYS

THR

LYS

ASN

TRP

GLU

ASP

20

ARG

GLU

LYS

PHE

GLU

LYS

VAL

PRO

GLY

LYS

21

TYR

ASP

MET

LEU

GLN

MET

ASP

TYR

ALA

THR

22

ASN

THR

Samples:

sample_1: PARP2 NTD-WGR, [U-99% 15N], 727.6 uM; MES 25 mM; DTT 2 mM

sample_conditions_1: pH: 5.5; temperature: 288.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.2.0 - collection

NMRPipe v2024.061.14.29 - processing

CcpNMR v3.3.41 - 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 53522