BMRB Entry 36426

Name: Solution structure of apo-WhiB4 from Mycobacterium tuberculosis
Published: 2022-03-19

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PDB ID: 7f7n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36426
MolProbity Validation Chart

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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:

Solution structure of apo-WhiB4 from Mycobacterium tuberculosis

Deposition date:

2021-06-30

Original release date:

2022-03-19

Authors:

Xia, B.; Duan, B.

Citation:

Citation: Duan, B.; Xia, B.. "DNA binding mechanism of WhiB4 from Mycobacterium tuberculosis" .

Assembly members:

Assembly members:
Transcriptional regulator WhiB4, polymer, 126 residues, 14305.289 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Transcriptional regulator WhiB4: MSGTRPAARRTNLTAAQNVV RSVDAEERIAWVSKALCRTT DPDELFVRGAAQRKAAVICR HCPVMQECAADALDNKVEFG VWGGMTERQRRALLKQHPEV VSWSDYLEKRKRRTGTAGLE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	484
15N chemical shifts	119
1H chemical shifts	781

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 126 residues - 14305.289 Da.

1

MET

SER

GLY

THR

ARG

PRO

ALA

ARG

2

THR

ASN

LEU

THR

ALA

GLN

ASN

VAL

3

ARG

SER

VAL

ASP

ALA

GLU

ARG

ILE

ALA

4

TRP

VAL

SER

LYS

ALA

LEU

CYS

ARG

THR

5

ASP

PRO

ASP

GLU

LEU

PHE

VAL

ARG

GLY

ALA

6

ALA

GLN

ARG

LYS

ALA

VAL

ILE

CYS

ARG

7

HIS

CYS

PRO

VAL

MET

GLN

GLU

CYS

ALA

8

ASP

ALA

LEU

ASP

ASN

LYS

VAL

GLU

PHE

GLY

9

VAL

TRP

GLY

MET

THR

GLU

ARG

GLN

ARG

10

ARG

ALA

LEU

LYS

GLN

HIS

PRO

GLU

VAL

11

VAL

SER

TRP

SER

ASP

TYR

LEU

GLU

LYS

ARG

12

LYS

ARG

THR

GLY

THR

ALA

GLY

LEU

GLU

13

HIS

Samples:

sample_1: WhiB4, [U-100% 13C; U-100% 15N], 0.4 mM; NaCl 50 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CCHCOSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

NMRView, Johnson, One Moon Scientific - peak picking

SANE, Duggan, Legge, Dyson & Wright - refinement

NMR spectrometers:

Bruker AVANCE III HD 700 MHz
Bruker AVANCE III HD 950 MHz

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