BMRB Entry 27895

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for dimerization domain of NF-kappaB p50 subunit
Published: 2019-11-25

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27895

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for dimerization domain of NF-kappaB p50 subunit

Deposition date:

2019-05-09

Original release date:

2019-11-25

Authors:

Mukherjee, Sulakshana; Kumar, Manish; Dadhwal, Prikshat; Atreya, Hanudatta

Citation:

Citation: Kumar, Manish; Dadhwal, Prikshat; Atreya, Hanudatta; Mukherjee, Sulakshana. "Backbone resonance assignments of the dimeric domain of the p50 NF-kappaB subunit" Biomol. NMR Assignments 14, 9-11 (2019).
PubMed: 31446566

Assembly members:

Assembly members:
p50-DD, polymer, 107 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p50-DD: MASNLKIVRMDRTAGCVTGG EEIYLLCDKVQKDDIQIRFY EEEENGGVWEGFGDFSPTDV HRQFAIVFKTPKYKDVNITK PASVFVQLRRKSDLETSEPK PFLYYPE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	297
15N chemical shifts	98
1H chemical shifts	201

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p50 dimerization domain	1

Entities:

Entity 1, p50 dimerization domain 107 residues - Formula weight is not available

1

MET

ALA

SER

ASN

LEU

LYS

ILE

VAL

ARG

MET

2

ASP

ARG

THR

ALA

GLY

CYS

VAL

THR

GLY

3

GLU

ILE

TYR

LEU

CYS

ASP

LYS

VAL

4

GLN

LYS

ASP

ILE

GLN

ILE

ARG

PHE

TYR

5

GLU

ASN

GLY

VAL

TRP

GLU

6

GLY

PHE

GLY

ASP

PHE

SER

PRO

THR

ASP

VAL

7

HIS

ARG

GLN

PHE

ALA

ILE

VAL

PHE

LYS

THR

8

PRO

LYS

TYR

LYS

ASP

VAL

ASN

ILE

THR

LYS

9

PRO

ALA

SER

VAL

PHE

VAL

GLN

LEU

ARG

10

LYS

SER

ASP

LEU

GLU

THR

SER

GLU

PRO

LYS

11

PRO

PHE

LEU

TYR

PRO

GLU

Samples:

sample_1: p50-DD, [U-98% 13C; U-98% 15N], 1.2 mM; NaCl 50 mM

sample_2: p50-DD, [U-15N], 2 mM; NaCl 50 mM

sample_3: p50-DD, [U-99% 13C; U-99% 15N], 1.2 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

CARA, Keller - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Ascend 800 MHz

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