BMRB Entry 26592

Name: The LcrG tip chaperone protein of the Yersinia pestis type III secretion system is partially folded
Published: 2015-12-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26592

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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:

The LcrG tip chaperone protein of the Yersinia pestis type III secretion system is partially folded

Deposition date:

2015-06-22

Original release date:

2015-12-18

Authors:

De Guzman, Roberto; Chaudhury, Sukanya

Citation:

Citation: Chaudhury, Sukanya; Souza, Clarice; Plano, Gregory; De Guzman, Roberto. "The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded" J. Mol. Biol. 427, 3096-3109 (2015).
PubMed: 26259880

Assembly members:

Assembly members:
LcrG, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 632 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pestis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LcrG: DEYDKTLKQAELAIADSDHR AKLLQEMSADIGLTPEAVMK IFAGRSAEEIKPAERELLDE IKRQRER

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	163
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LcrG 7-73	1

Entities:

Entity 1, LcrG 7-73 67 residues - Formula weight is not available

The sequence corresponds to LcrG residues 7-73

1

ASP

GLU

TYR

ASP

LYS

THR

LEU

LYS

GLN

ALA

2

GLU

LEU

ALA

ILE

ALA

ASP

SER

ASP

HIS

ARG

3

ALA

LYS

LEU

GLN

GLU

MET

SER

ALA

ASP

4

ILE

GLY

LEU

THR

PRO

GLU

ALA

VAL

MET

LYS

5

ILE

PHE

ALA

GLY

ARG

SER

ALA

GLU

ILE

6

LYS

PRO

ALA

GLU

ARG

GLU

LEU

ASP

GLU

7

ILE

LYS

ARG

GLN

ARG

GLU

ARG

Samples:

sample_1: LcrG, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%

sample_2: LcrG in complex with LcrV, U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

sample_conditions_2: ionic strength: 10 mM; pH: 7.0; temperature: 273 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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