BMRB Entry 50495

Name: RelAdd_mutant
Published: 2021-04-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50495

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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:

RelAdd_mutant

Deposition date:

2020-10-01

Original release date:

2021-04-13

Authors:

Kumar, Manish; Dhaka, Nitin; Raza, Tahseen; 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

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 GPGWEARGSFSQADVHRQFA IVFRTPPYADPSLQAPVRVS MQLRRPSDRELSEPMEFQYL PD

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	70
T2 relaxation values	70
heteronuclear NOE values	70

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RelA(V248F), chain 1	1
2	RelA(V248F), chain 2	1

Entities:

Entity 1, RelA(V248F), chain 1 102 residues - Formula weight is not available

Starts at 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

PHE

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

Samples:

sample_1: RelA(V248F) dd, [U-99% 15N], 0.44 mM; 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