BMRB Entry 51892

Name: 1H, 15N and 13C backbone assignments for human PARP-1 BRCT domain
Published: 2023-06-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51892

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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:

1H, 15N and 13C backbone assignments for human PARP-1 BRCT domain

Deposition date:

2023-03-31

Original release date:

2023-06-19

Authors:

Yang, Ji-Chun; Wu, Wing-Fung; Neuhaus, David

Citation:

Citation: Suskiewicz, Marcin; Munnur, Deeksha; Stromland, Oyvind; Yang, Ji-Chun; Easton, Laura; Chatrin, Chatrin; Zhu, Kang; Baretic, Domagoj; Goffinont, Stephane; Schuller, Marion; Wu, Wing-Fung; Elkins, Jonathan; Ahel, Dragana; Sanyal, Sumana; Neuhaus, David; Ahel, Ivan. "Updated protein domain annotation of the PARP protein family sheds new light on biological function" Nucleic Acids Res. 51, 8217-8236 (2023).
PubMed: 37326024

Assembly members:

Assembly members:
entity_1, polymer, 146 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: pET28a-lip

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNSSASADKPLSNMKILTLG KLSRNKDEVKAMIEKLGGKL TGTANKASLCISTKKEVEKM NKKMEEVKEANIRVVSEDFL QDVSASTKSLQELFLAHILS PWGAEVKAEPVEVVAPRGKS GAALSKKSKGQVKEEGINKS EKRMKL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	138
1H chemical shifts	244

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PARP1 BRCT domain	1

Entities:

Entity 1, PARP1 BRCT domain 146 residues - Formula weight is not available

The first three residues Gly-Asn-Ser as shown above are a cloning artefact. The native sequence of PARP-1 BRCT starts at Ser 383 and runs to Leu 525.

1

GLY

ASN

SER

ALA

SER

ALA

ASP

LYS

PRO

2

LEU

SER

ASN

MET

LYS

ILE

LEU

THR

LEU

GLY

3

LYS

LEU

SER

ARG

ASN

LYS

ASP

GLU

VAL

LYS

4

ALA

MET

ILE

GLU

LYS

LEU

GLY

LYS

LEU

5

THR

GLY

THR

ALA

ASN

LYS

ALA

SER

LEU

CYS

6

ILE

SER

THR

LYS

GLU

VAL

GLU

LYS

MET

7

ASN

LYS

MET

GLU

VAL

LYS

GLU

ALA

8

ASN

ILE

ARG

VAL

SER

GLU

ASP

PHE

LEU

9

GLN

ASP

VAL

SER

ALA

SER

THR

LYS

SER

LEU

10

GLN

GLU

LEU

PHE

LEU

ALA

HIS

ILE

LEU

SER

11

PRO

TRP

GLY

ALA

GLU

VAL

LYS

ALA

GLU

PRO

12

VAL

GLU

VAL

ALA

PRO

ARG

GLY

LYS

SER

13

GLY

ALA

LEU

SER

LYS

SER

LYS

GLY

14

GLN

VAL

LYS

GLU

GLY

ILE

ASN

LYS

SER

15

GLU

LYS

ARG

MET

LYS

LEU

Samples:

sample_1: PARP1 BRCT domain, [U-13C; U-15N], 0.5 mM; TRIS, [U-2H], 50 mM; sodium chloride 200 mM; zinc sulfate 0.1 mM; DTT, [U-2H], 4 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.2004 M; 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 constant-time	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3 - collection, processing

CcpNMR v2.1 - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz

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