BMRB Entry 53286

Name: Assignment of 1H, 13C, 15N backbone chemical shifts of RAD52 217-418
Published: 2025-08-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53286

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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 RAD52 217-418

Deposition date:

2025-07-18

Original release date:

2025-08-01

Authors:

Dinh, Hoang; DiDomenico, Sarah; Baudin, Antoine; Mazin, Alexander; Libich, David

Citation:

Citation: DiDomenico, Sarah; Dinh, Hoang; Rossi, Matthew; Baudin, Antoine; Chazin, Walter; Libich, David; Mazin, Alexander. "RAD52 and RPA act in a concert promoting inverse RNA strand exchange" .

Assembly members:

Assembly members:
entity_1, polymer, 202 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: pGEX-6P-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PQLQQVTSPSRPSHAVIPAD QDCSSRSLSSSAVESEATHQ RKLRQKQLQQQFRERMEKQQ VRVSTPSAEKSEAAPPAPPV THSTPVTVSEPLLEKDFLAG VTQELIKTLEDNSEKWAVTP DAGDGVVKPSSRADPAQTSD TLALNNQMVTQNRTPHSVCH QKPQAKSGSWDLQTYSADQR TTGNWESHRKSQDMKKRKYD PS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	500
15N chemical shifts	145
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RAD52-CTD	1

Entities:

Entity 1, RAD52-CTD 202 residues - Formula weight is not available

1

PRO

GLN

LEU

GLN

VAL

THR

SER

PRO

SER

2

ARG

PRO

SER

HIS

ALA

VAL

ILE

PRO

ALA

ASP

3

GLN

ASP

CYS

SER

ARG

SER

LEU

SER

4

SER

ALA

VAL

GLU

SER

GLU

ALA

THR

HIS

GLN

5

ARG

LYS

LEU

ARG

GLN

LYS

GLN

LEU

GLN

6

GLN

PHE

ARG

GLU

ARG

MET

GLU

LYS

GLN

7

VAL

ARG

VAL

SER

THR

PRO

SER

ALA

GLU

LYS

8

SER

GLU

ALA

PRO

ALA

PRO

VAL

9

THR

HIS

SER

THR

PRO

VAL

THR

VAL

SER

GLU

10

PRO

LEU

GLU

LYS

ASP

PHE

LEU

ALA

GLY

11

VAL

THR

GLN

GLU

LEU

ILE

LYS

THR

LEU

GLU

12

ASP

ASN

SER

GLU

LYS

TRP

ALA

VAL

THR

PRO

13

ASP

ALA

GLY

ASP

GLY

VAL

LYS

PRO

SER

14

SER

ARG

ALA

ASP

PRO

ALA

GLN

THR

SER

ASP

15

THR

LEU

ALA

LEU

ASN

GLN

MET

VAL

THR

16

GLN

ASN

ARG

THR

PRO

HIS

SER

VAL

CYS

HIS

17

GLN

LYS

PRO

GLN

ALA

LYS

SER

GLY

SER

TRP

18

ASP

LEU

GLN

THR

TYR

SER

ALA

ASP

GLN

ARG

19

THR

GLY

ASN

TRP

GLU

SER

HIS

ARG

LYS

20

SER

GLN

ASP

MET

LYS

ARG

LYS

TYR

ASP

21

PRO

SER

Samples:

sample_1: RAD52-CTD, [U-100% 13C; U-100% 15N], 130 uM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

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