BMRB Entry 26591

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26591

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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:

NMR Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa

Deposition date:

2015-06-22

Original release date:

2015-12-18

Authors:

Kaur, Kawaljit; De Guzman, Roberto

Citation:

Citation: Chaudhury, Sukanya; Nordhues, Bryce; Kaur, Kawaljit; Zhang, Na; 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:
PcrG9-76, polymer, 76 residues, Formula weight is not available

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 208964 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PcrG9-76: EDTLRATVQAAELAIRDSEE RGRLLAEMWQGLGLAADAGE LLFQAPERELARAAEEELLA ELRRMRSSGSENLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	145
15N chemical shifts	75
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PcrG9-76	1

Entities:

Entity 1, PcrG9-76 76 residues - Formula weight is not available

Residues 77-84 corresponds to cloning artifact

1

GLU

ASP

THR

LEU

ARG

ALA

THR

VAL

GLN

ALA

2

ALA

GLU

LEU

ALA

ILE

ARG

ASP

SER

GLU

3

ARG

GLY

ARG

LEU

ALA

GLU

MET

TRP

GLN

4

GLY

LEU

GLY

LEU

ALA

ASP

ALA

GLY

GLU

5

LEU

PHE

GLN

ALA

PRO

GLU

ARG

GLU

LEU

6

ALA

ARG

ALA

GLU

LEU

ALA

7

GLU

LEU

ARG

MET

ARG

SER

GLY

SER

8

GLU

ASN

LEU

TYR

PHE

GLN

Samples:

sample_1: PcrG, [U-99% 13C; U-99% 15N], 0.7 mM; sodium chloride mM; sodium phosphate mM; D2O 10 mM; H2O 90 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7; pressure: 1 atm; 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

Software:

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