BMRB Entry 50494

Name: RelA-p50 heterodimer
Published: 2021-04-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50494

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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:

RelA-p50 heterodimer

Deposition date:

2020-09-30

Original release date:

2021-04-13

Authors:

Kumar, Manish; Dhaka, Nitin; Raza, Tahseen; Dadhwal, Prikshat; Atreya, Hanudatta; Mukherjee, Sulakshana

Citation:

Citation: Kumar, Manish; Dhaka, Nitin; Raza, Tahseen; Dadhwal, Prikshat; Atreya, Hanudatta; Mukherjee, Sulakshana. "Domain stability regulated through the dimer interface controls the formation kinetics of a specific NF-kappaB dimer" Biochemistry 60, 513-523 (2021).
PubMed: 33555182

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, Formula weight is not available
entity_2, polymer, 106 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: NTAELKICRVNRNSGSCLGG DEIFLLCDKVQKEDIEVYFT GPGWEARGSFSQADVHRQVA IVFRTPPYADPSLQAPVRVS MQLRRPSDRELSEPMEFQYL PD
entity_2: ASNLKIVRMDRTAGCVTGGE EIYLLCDKVQKDDIQIRFYE EEENGGVWEGFGDFSPTDVH RQFAIVFKTPKYKDVNITKP ASVFVQLRRKSDLETSEPKP FLYYPE

Data sets:

heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
T1 relaxation values	73
T2 relaxation values	73
heteronuclear NOE values	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RelA	1
2	p50	2

Entities:

Entity 1, RelA 102 residues - Formula weight is not available

Starts from 190

1

ASN

THR

ALA

GLU

LEU

LYS

ILE

CYS

ARG

VAL

2

ASN

ARG

ASN

SER

GLY

SER

CYS

LEU

GLY

3

ASP

GLU

ILE

PHE

LEU

CYS

ASP

LYS

VAL

4

GLN

LYS

GLU

ASP

ILE

GLU

VAL

TYR

PHE

THR

5

GLY

PRO

GLY

TRP

GLU

ALA

ARG

GLY

SER

PHE

6

SER

GLN

ALA

ASP

VAL

HIS

ARG

GLN

VAL

ALA

7

ILE

VAL

PHE

ARG

THR

PRO

TYR

ALA

ASP

8

PRO

SER

LEU

GLN

ALA

PRO

VAL

ARG

VAL

SER

9

MET

GLN

LEU

ARG

PRO

SER

ASP

ARG

GLU

10

LEU

SER

GLU

PRO

MET

GLU

PHE

GLN

TYR

LEU

11

PRO

ASP

Entity 2, p50 106 residues - Formula weight is not available

Starts from 245

1

ALA

SER

ASN

LEU

LYS

ILE

VAL

ARG

MET

ASP

2

ARG

THR

ALA

GLY

CYS

VAL

THR

GLY

GLU

3

GLU

ILE

TYR

LEU

CYS

ASP

LYS

VAL

GLN

4

LYS

ASP

ILE

GLN

ILE

ARG

PHE

TYR

GLU

5

GLU

ASN

GLY

VAL

TRP

GLU

GLY

6

PHE

GLY

ASP

PHE

SER

PRO

THR

ASP

VAL

HIS

7

ARG

GLN

PHE

ALA

ILE

VAL

PHE

LYS

THR

PRO

8

LYS

TYR

LYS

ASP

VAL

ASN

ILE

THR

LYS

PRO

9

ALA

SER

VAL

PHE

VAL

GLN

LEU

ARG

LYS

10

SER

ASP

LEU

GLU

THR

SER

GLU

PRO

LYS

PRO

11

PHE

LEU

TYR

PRO

GLU

Samples:

sample_1: RelA dimerization domain, [U-99% 15N], 360 uM; p50 dimerization domain 396 uM; TRIS 20 mM; sodium chloride 50 mM; beta-mercaptoethanol 20 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
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

CARA - data analysis

Relax - data analysis

NMR spectrometers:

Bruker Ascend 800 MHz