BMRB Entry 34153

Name: M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1
Published: 2017-12-26

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PDB ID: 5oay
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34153
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: M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1

Deposition date: 2017-06-25 Original release date: 2017-12-26

Authors: Williamson, M.; Green, J.; Hounslow, A.

Citation: Kudhair, B.; Hounslow, A.; Rolfe, M.; Crack, J.; Hunt, D.; Buxton, R.; Smith, L.; Le Brun, N.; Williamson, M.; Green, J.. "M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1" in preparation ., .-..

Assembly members:
Transcriptional regulator WhiB1, polymer, 94 residues, 10383.681 Da.
IRON/SULFUR CLUSTER, non-polymer, 351.640 Da.

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

Experimental source: Production method: recombinant technology Host organism: Mycobacterium smegmatis

Entity Sequences (FASTA):
Transcriptional regulator WhiB1: AGENLYFQGAMDWRHKAVCR DEDPELFFPVGNSGPALAQI ADAKLVCNRCPVTTECLSWA LNTGQDSGVWGGMSEDERRA LKRRNARTKARTGV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	86
1H chemical shifts	449

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 94 residues - 10383.681 Da.

1

ALA

GLY

GLU

ASN

LEU

TYR

PHE

GLN

GLY

ALA

2

MET

ASP

TRP

ARG

HIS

LYS

ALA

VAL

CYS

ARG

3

ASP

GLU

ASP

PRO

GLU

LEU

PHE

PRO

VAL

4

GLY

ASN

SER

GLY

PRO

ALA

LEU

ALA

GLN

ILE

5

ALA

ASP

ALA

LYS

LEU

VAL

CYS

ASN

ARG

CYS

6

PRO

VAL

THR

GLU

CYS

LEU

SER

TRP

ALA

7

LEU

ASN

THR

GLY

GLN

ASP

SER

GLY

VAL

TRP

8

GLY

MET

SER

GLU

ASP

GLU

ARG

ALA

9

LEU

LYS

ARG

ASN

ALA

ARG

THR

LYS

ALA

10

ARG

THR

GLY

VAL

Entity 2, entity_2 - Fe4 S4 - 351.640 Da.

1

SF4

Samples:

sample_1: WhiB1 protein 0.3 mM; sodium chloride 250 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
HNCA(N)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
HBCB(CGCD)HD	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts