BMRB Entry 52392

Name: NFkappaB p52 DD (225-328) Homodimer
Published: 2024-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52392

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NFkappaB p52 DD (225-328) Homodimer

Deposition date:

2024-04-09

Original release date:

2024-07-22

Authors:

Sahoo, Sunirmala; Dhaka, Nitin; Mukherjee, Sulakshana

Citation:

Citation: Sahoo, Sunirmala; Dhaka, Nitin; Mukherjee, Sulakshana. "Backbone triple resonance assignments of the dimerization domain of NF-kappaB p52 subunit" Biomol. NMR Assign. ., .-. (2024).
PubMed: 38856960

Assembly members:

Assembly members:
entity_1, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ASNLKISRMDKTAGSVRGGD EVYLLCDKVQKDDIEVRFYE DDENGWQAFGDFSPTDVHKQ YAIVFRTPPYHKMKIERPVT VFLQLKRKRGGDVSDSKQFT YYPL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	292
15N chemical shifts	97
1H chemical shifts	202

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p52, chain 1	1
2	p52, chain 2	1

Entities:

Entity 1, p52, chain 1 104 residues - Formula weight is not available

1

ALA

SER

ASN

LEU

LYS

ILE

SER

ARG

MET

ASP

2

LYS

THR

ALA

GLY

SER

VAL

ARG

GLY

ASP

3

GLU

VAL

TYR

LEU

CYS

ASP

LYS

VAL

GLN

4

LYS

ASP

ILE

GLU

VAL

ARG

PHE

TYR

GLU

5

ASP

GLU

ASN

GLY

TRP

GLN

ALA

PHE

GLY

6

ASP

PHE

SER

PRO

THR

ASP

VAL

HIS

LYS

GLN

7

TYR

ALA

ILE

VAL

PHE

ARG

THR

PRO

TYR

8

HIS

LYS

MET

LYS

ILE

GLU

ARG

PRO

VAL

THR

9

VAL

PHE

LEU

GLN

LEU

LYS

ARG

LYS

ARG

GLY

10

GLY

ASP

VAL

SER

ASP

SER

LYS

GLN

PHE

THR

11

TYR

PRO

LEU

Samples:

sample_1: p52 Dimerization Domain, [U-100% 13C; U-100% 15N], 0.700 mM; p52 Dimerization Domain, [U-100% 15N], 0.400 mM; Bis-Tris 20 mM; NaCl 50 mM; beta-Me 20 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HANH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

TOPSPIN - collection

NMRPipe - processing

TALOS-N - structure solution

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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