BMRB Entry 50412

Name: Backbone and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor
Published: 2020-08-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50412

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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 and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor

Deposition date:

2020-07-27

Original release date:

2020-08-04

Authors:

Singh, Amrinder; Dyson, Jane; Wright, Peter

Citation:

Citation: Singh, Amrinder; Dyson, Jane. "Backbone and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor" Biomol. NMR Assign. 15, 29-33 (2021).
PubMed: 32936430

Assembly members:

Assembly members:
entity_1, polymer, 210 residues, Formula weight is not available
entity_2, 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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGPYLQILEQPKQRGFRFRY VCEGPSHGGLPGASSEKNKK SYPQVKICNYVGPAKVIVQL VTNGKNIHLHAHSLVGKHCE DGVCTVTAGPKDMVVGFANL GILHVTKKKVFETLEARMTE ACIRGYNPGLLVHSDLAYLQ AEGGGDRQLTDREKEIIRQA AVQQTKEMDLSVVRLMFTAF LPDSTGSFTRRLEPVVSDAI YDSKAPNASN
entity_2: MASNLKIVRMDRTAGCVTGG EEIYLLCDKVQKDDIQIRFY EEEENGGVWEGFGDFSPTDV HRQFAIVFKTPKYKDVNITK PASVFVQLRRKSDLETSEPK PFLYYPE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	1069
15N chemical shifts	283
1H chemical shifts	1708

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p50 DNA binding domain	1
2	p50 Dimerization Domain	2

Entities:

Entity 1, p50 DNA binding domain 210 residues - Formula weight is not available

1	MET	GLY	PRO	TYR	LEU	GLN	ILE	LEU	GLU	GLN
2	PRO	LYS	GLN	ARG	GLY	PHE	ARG	PHE	ARG	TYR
3	VAL	CYS	GLU	GLY	PRO	SER	HIS	GLY	GLY	LEU
4	PRO	GLY	ALA	SER	SER	GLU	LYS	ASN	LYS	LYS
5	SER	TYR	PRO	GLN	VAL	LYS	ILE	CYS	ASN	TYR
6	VAL	GLY	PRO	ALA	LYS	VAL	ILE	VAL	GLN	LEU
7	VAL	THR	ASN	GLY	LYS	ASN	ILE	HIS	LEU	HIS
8	ALA	HIS	SER	LEU	VAL	GLY	LYS	HIS	CYS	GLU
9	ASP	GLY	VAL	CYS	THR	VAL	THR	ALA	GLY	PRO
10	LYS	ASP	MET	VAL	VAL	GLY	PHE	ALA	ASN	LEU
11	GLY	ILE	LEU	HIS	VAL	THR	LYS	LYS	LYS	VAL
12	PHE	GLU	THR	LEU	GLU	ALA	ARG	MET	THR	GLU
13	ALA	CYS	ILE	ARG	GLY	TYR	ASN	PRO	GLY	LEU
14	LEU	VAL	HIS	SER	ASP	LEU	ALA	TYR	LEU	GLN
15	ALA	GLU	GLY	GLY	GLY	ASP	ARG	GLN	LEU	THR
16	ASP	ARG	GLU	LYS	GLU	ILE	ILE	ARG	GLN	ALA
17	ALA	VAL	GLN	GLN	THR	LYS	GLU	MET	ASP	LEU
18	SER	VAL	VAL	ARG	LEU	MET	PHE	THR	ALA	PHE
19	LEU	PRO	ASP	SER	THR	GLY	SER	PHE	THR	ARG
20	ARG	LEU	GLU	PRO	VAL	VAL	SER	ASP	ALA	ILE
21	TYR	ASP	SER	LYS	ALA	PRO	ASN	ALA	SER	ASN

Entity 2, 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

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 HNCOCA	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 HNCACO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_2
3D HCCH-COSY	sample_1	isotropic	sample_conditions_2
3D H(CCO)NH	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_3
3D HCCH-COSY	sample_3	isotropic	sample_conditions_3
3D H(CCO)NH	sample_3	isotropic	sample_conditions_3
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_3
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_3	isotropic	sample_conditions_3

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

BMRB Entry 50412

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	GLY	PRO	TYR	LEU	GLN	ILE	LEU	GLU	GLN
2	PRO	LYS	GLN	ARG	GLY	PHE	ARG	PHE	ARG	TYR
3	VAL	CYS	GLU	GLY	PRO	SER	HIS	GLY	GLY	LEU
4	PRO	GLY	ALA	SER	SER	GLU	LYS	ASN	LYS	LYS
5	SER	TYR	PRO	GLN	VAL	LYS	ILE	CYS	ASN	TYR
6	VAL	GLY	PRO	ALA	LYS	VAL	ILE	VAL	GLN	LEU
7	VAL	THR	ASN	GLY	LYS	ASN	ILE	HIS	LEU	HIS
8	ALA	HIS	SER	LEU	VAL	GLY	LYS	HIS	CYS	GLU
9	ASP	GLY	VAL	CYS	THR	VAL	THR	ALA	GLY	PRO
10	LYS	ASP	MET	VAL	VAL	GLY	PHE	ALA	ASN	LEU
11	GLY	ILE	LEU	HIS	VAL	THR	LYS	LYS	LYS	VAL
12	PHE	GLU	THR	LEU	GLU	ALA	ARG	MET	THR	GLU
13	ALA	CYS	ILE	ARG	GLY	TYR	ASN	PRO	GLY	LEU
14	LEU	VAL	HIS	SER	ASP	LEU	ALA	TYR	LEU	GLN
15	ALA	GLU	GLY	GLY	GLY	ASP	ARG	GLN	LEU	THR
16	ASP	ARG	GLU	LYS	GLU	ILE	ILE	ARG	GLN	ALA
17	ALA	VAL	GLN	GLN	THR	LYS	GLU	MET	ASP	LEU
18	SER	VAL	VAL	ARG	LEU	MET	PHE	THR	ALA	PHE
19	LEU	PRO	ASP	SER	THR	GLY	SER	PHE	THR	ARG
20	ARG	LEU	GLU	PRO	VAL	VAL	SER	ASP	ALA	ILE
21	TYR	ASP	SER	LYS	ALA	PRO	ASN	ALA	SER	ASN

1	MET	GLY	PRO	TYR	LEU	GLN	ILE	LEU	GLU	GLN
2	PRO	LYS	GLN	ARG	GLY	PHE	ARG	PHE	ARG	TYR
3	VAL	CYS	GLU	GLY	PRO	SER	HIS	GLY	GLY	LEU
4	PRO	GLY	ALA	SER	SER	GLU	LYS	ASN	LYS	LYS
5	SER	TYR	PRO	GLN	VAL	LYS	ILE	CYS	ASN	TYR
6	VAL	GLY	PRO	ALA	LYS	VAL	ILE	VAL	GLN	LEU
7	VAL	THR	ASN	GLY	LYS	ASN	ILE	HIS	LEU	HIS
8	ALA	HIS	SER	LEU	VAL	GLY	LYS	HIS	CYS	GLU
9	ASP	GLY	VAL	CYS	THR	VAL	THR	ALA	GLY	PRO
10	LYS	ASP	MET	VAL	VAL	GLY	PHE	ALA	ASN	LEU
11	GLY	ILE	LEU	HIS	VAL	THR	LYS	LYS	LYS	VAL
12	PHE	GLU	THR	LEU	GLU	ALA	ARG	MET	THR	GLU
13	ALA	CYS	ILE	ARG	GLY	TYR	ASN	PRO	GLY	LEU
14	LEU	VAL	HIS	SER	ASP	LEU	ALA	TYR	LEU	GLN
15	ALA	GLU	GLY	GLY	GLY	ASP	ARG	GLN	LEU	THR
16	ASP	ARG	GLU	LYS	GLU	ILE	ILE	ARG	GLN	ALA
17	ALA	VAL	GLN	GLN	THR	LYS	GLU	MET	ASP	LEU
18	SER	VAL	VAL	ARG	LEU	MET	PHE	THR	ALA	PHE
19	LEU	PRO	ASP	SER	THR	GLY	SER	PHE	THR	ARG
20	ARG	LEU	GLU	PRO	VAL	VAL	SER	ASP	ALA	ILE
21	TYR	ASP	SER	LYS	ALA	PRO	ASN	ALA	SER	ASN

1	MET	GLY	PRO	TYR	LEU	GLN	ILE	LEU	GLU	GLN
2	PRO	LYS	GLN	ARG	GLY	PHE	ARG	PHE	ARG	TYR
3	VAL	CYS	GLU	GLY	PRO	SER	HIS	GLY	GLY	LEU
4	PRO	GLY	ALA	SER	SER	GLU	LYS	ASN	LYS	LYS
5	SER	TYR	PRO	GLN	VAL	LYS	ILE	CYS	ASN	TYR
6	VAL	GLY	PRO	ALA	LYS	VAL	ILE	VAL	GLN	LEU
7	VAL	THR	ASN	GLY	LYS	ASN	ILE	HIS	LEU	HIS
8	ALA	HIS	SER	LEU	VAL	GLY	LYS	HIS	CYS	GLU
9	ASP	GLY	VAL	CYS	THR	VAL	THR	ALA	GLY	PRO
10	LYS	ASP	MET	VAL	VAL	GLY	PHE	ALA	ASN	LEU
11	GLY	ILE	LEU	HIS	VAL	THR	LYS	LYS	LYS	VAL
12	PHE	GLU	THR	LEU	GLU	ALA	ARG	MET	THR	GLU
13	ALA	CYS	ILE	ARG	GLY	TYR	ASN	PRO	GLY	LEU
14	LEU	VAL	HIS	SER	ASP	LEU	ALA	TYR	LEU	GLN
15	ALA	GLU	GLY	GLY	GLY	ASP	ARG	GLN	LEU	THR
16	ASP	ARG	GLU	LYS	GLU	ILE	ILE	ARG	GLN	ALA
17	ALA	VAL	GLN	GLN	THR	LYS	GLU	MET	ASP	LEU
18	SER	VAL	VAL	ARG	LEU	MET	PHE	THR	ALA	PHE
19	LEU	PRO	ASP	SER	THR	GLY	SER	PHE	THR	ARG
20	ARG	LEU	GLU	PRO	VAL	VAL	SER	ASP	ALA	ILE
21	TYR	ASP	SER	LYS	ALA	PRO	ASN	ALA	SER	ASN