BMRB Entry 52029

Name: Backbone and side chain assignment of BCL11A zinc finger 456
Published: 2025-03-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52029

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:

Backbone and side chain assignment of BCL11A zinc finger 456

Deposition date:

2023-07-12

Original release date:

2025-03-14

Authors:

Viennet, Thibault; Yin, Maolu; Orkin, Stuart; Arthanari, Haribabu

Citation:

Citation: Viennet, Thibault; Yin, Maolu; Jayaraj, Abhilash; Kim, Woojin; Sun, Zhen-Yu; Fujiwara, Yuko; Zhang, Kevin; Seruggia, Davide; Seo, Hyuk-Soo; Dhe-Paganon, Sirano; Orkin, Stuart; Arthanari, Haribabu. "Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6" Structure 32, 2276-2286 (2024).
PubMed: 39423807

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEGRRSDTCEYCGKVFKNCS NLTVHRRSHTGERPYKCELC NYACAQSSKLTRHMKTHGQV GKDVYKCEICKMPFSVYSTL EKHMKKWHSDRVLNNDIKTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	97
1H chemical shifts	551

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ZnF456	1
2	Zn ion, 1	2
3	Zn ion, 2	2
4	Zn ion, 3	2

Entities:

Entity 1, ZnF456 100 residues - Formula weight is not available

1	SER	GLU	GLY	ARG	ARG	SER	ASP	THR	CYS	GLU
2	TYR	CYS	GLY	LYS	VAL	PHE	LYS	ASN	CYS	SER
3	ASN	LEU	THR	VAL	HIS	ARG	ARG	SER	HIS	THR
4	GLY	GLU	ARG	PRO	TYR	LYS	CYS	GLU	LEU	CYS
5	ASN	TYR	ALA	CYS	ALA	GLN	SER	SER	LYS	LEU
6	THR	ARG	HIS	MET	LYS	THR	HIS	GLY	GLN	VAL
7	GLY	LYS	ASP	VAL	TYR	LYS	CYS	GLU	ILE	CYS
8	LYS	MET	PRO	PHE	SER	VAL	TYR	SER	THR	LEU
9	GLU	LYS	HIS	MET	LYS	LYS	TRP	HIS	SER	ASP
10	ARG	VAL	LEU	ASN	ASN	ASP	ILE	LYS	THR	GLU

Entity 2, Zn ion, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: BCL11A ZnF456, [U-100% 13C; U-100% 15N], 200 uM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_conditions_1: ionic strength: 0.163 M; pH: 6.0; pressure: 1 atm; temperature: 308 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCOCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CG)CD	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)CE	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D (H)C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMRPipe - processing

TOPSPIN - collection

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

1	SER	GLU	GLY	ARG	ARG	SER	ASP	THR	CYS	GLU
2	TYR	CYS	GLY	LYS	VAL	PHE	LYS	ASN	CYS	SER
3	ASN	LEU	THR	VAL	HIS	ARG	ARG	SER	HIS	THR
4	GLY	GLU	ARG	PRO	TYR	LYS	CYS	GLU	LEU	CYS
5	ASN	TYR	ALA	CYS	ALA	GLN	SER	SER	LYS	LEU
6	THR	ARG	HIS	MET	LYS	THR	HIS	GLY	GLN	VAL
7	GLY	LYS	ASP	VAL	TYR	LYS	CYS	GLU	ILE	CYS
8	LYS	MET	PRO	PHE	SER	VAL	TYR	SER	THR	LEU
9	GLU	LYS	HIS	MET	LYS	LYS	TRP	HIS	SER	ASP
10	ARG	VAL	LEU	ASN	ASN	ASP	ILE	LYS	THR	GLU

1	SER	GLU	GLY	ARG	ARG	SER	ASP	THR	CYS	GLU
2	TYR	CYS	GLY	LYS	VAL	PHE	LYS	ASN	CYS	SER
3	ASN	LEU	THR	VAL	HIS	ARG	ARG	SER	HIS	THR
4	GLY	GLU	ARG	PRO	TYR	LYS	CYS	GLU	LEU	CYS
5	ASN	TYR	ALA	CYS	ALA	GLN	SER	SER	LYS	LEU
6	THR	ARG	HIS	MET	LYS	THR	HIS	GLY	GLN	VAL
7	GLY	LYS	ASP	VAL	TYR	LYS	CYS	GLU	ILE	CYS
8	LYS	MET	PRO	PHE	SER	VAL	TYR	SER	THR	LEU
9	GLU	LYS	HIS	MET	LYS	LYS	TRP	HIS	SER	ASP
10	ARG	VAL	LEU	ASN	ASN	ASP	ILE	LYS	THR	GLU

1	SER	GLU	GLY	ARG	ARG	SER	ASP	THR	CYS	GLU
2	TYR	CYS	GLY	LYS	VAL	PHE	LYS	ASN	CYS	SER
3	ASN	LEU	THR	VAL	HIS	ARG	ARG	SER	HIS	THR
4	GLY	GLU	ARG	PRO	TYR	LYS	CYS	GLU	LEU	CYS
5	ASN	TYR	ALA	CYS	ALA	GLN	SER	SER	LYS	LEU
6	THR	ARG	HIS	MET	LYS	THR	HIS	GLY	GLN	VAL
7	GLY	LYS	ASP	VAL	TYR	LYS	CYS	GLU	ILE	CYS
8	LYS	MET	PRO	PHE	SER	VAL	TYR	SER	THR	LEU
9	GLU	LYS	HIS	MET	LYS	LYS	TRP	HIS	SER	ASP
10	ARG	VAL	LEU	ASN	ASN	ASP	ILE	LYS	THR	GLU