BMRB Entry 34102

Name: Solution structure of B. subtilis Sigma G inhibitor CsfB
Published: 2018-02-23

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PDB ID: 5n7y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34102
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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 B. subtilis Sigma G inhibitor CsfB

Deposition date:

2017-02-21

Original release date:

2018-02-23

Authors:

Martinez-Lumbreras, S.; Alfano, C.; Atkinson, A.; Isaacson, R.

Citation:

Citation: Martinez-Lumbreras, Santiago; Alfano, Caterina; Evans, Nicola; Collins, Katherine; Flanagan, Kelly; Atkinson, R Andrew; Krysztofinska, Ewelina; Vydyanath, Anupama; Jackter, Jacquelin; Fixon-Owoo, Sarah; Camp, Amy; Isaacson, Rivka. "Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB." Structure 26, 640-648 (2018).
PubMed: 29526435

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5630.390 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMDETVKLNHTCVICDQEKN RGIHLYTKFICLDCERKVIS TSTSDPDYA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	166
15N chemical shifts	47
1H chemical shifts	321

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1
3	entity_2, 1	2
4	entity_2, 2	2

Entities:

Entity 1, entity_1, 1 49 residues - 5630.390 Da.

1

SER

MET

ASP

GLU

THR

VAL

LYS

LEU

ASN

HIS

2

THR

CYS

VAL

ILE

CYS

ASP

GLN

GLU

LYS

ASN

3

ARG

GLY

ILE

HIS

LEU

TYR

THR

LYS

PHE

ILE

4

CYS

LEU

ASP

CYS

GLU

ARG

LYS

VAL

ILE

SER

5

THR

SER

THR

SER

ASP

PRO

ASP

TYR

ALA

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: CsfB-labelled, [U-100% 13C; U-100% 15N], 1 mM

sample_2: CsfB-labelled, [U-100% 13C; U-100% 15N], 0.5 mM; CsfB 0.5 mM

sample_conditions_1: ionic strength: 250 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D filtered/edited 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis v2.4, CCPN - chemical shift assignment

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement, structure calculation

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 950 MHz

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