BMRB Entry 51694

Name: Backbone resonance assignments of DNA binding domain of HigA antitoxin (HigA_DBD) from E. coli K12
Published: 2025-06-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51694

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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 resonance assignments of DNA binding domain of HigA antitoxin (HigA_DBD) from E. coli K12

Deposition date:

2022-11-14

Original release date:

2025-06-04

Authors:

Jadhav, Pankaj; Singh, Mahavir

Citation:

Citation: Jadhav, Pankaj; Singh, Mahavir. "Backbone resonance assignments of DNA binding domain of HigA antitoxin (HigA_DBD) from E. coli K12" .

Assembly members:

Assembly members:
entity_1, polymer, 75 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHHMHMPGGIAV IRTLMDQYGLTLSDLPEIGS KSMVSRVLSGKRKLTLEHAK KLATRFGISPALFID

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	167
15N chemical shifts	54
1H chemical shifts	54

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DNA binding domain	1

Entities:

Entity 1, DNA binding domain 75 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

HIS

MET

HIS

MET

PRO

GLY

ILE

ALA

VAL

3

ILE

ARG

THR

LEU

MET

ASP

GLN

TYR

GLY

LEU

4

THR

LEU

SER

ASP

LEU

PRO

GLU

ILE

GLY

SER

5

LYS

SER

MET

VAL

SER

ARG

VAL

LEU

SER

GLY

6

LYS

ARG

LYS

LEU

THR

LEU

GLU

HIS

ALA

LYS

7

LYS

LEU

ALA

THR

ARG

PHE

GLY

ILE

SER

PRO

8

ALA

LEU

PHE

ILE

ASP

Samples:

sample_1: HigA_DBD, [U-99% 13C; U-99% 15N], 0.7 mM; Tris 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR v3.0.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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