BMRB Entry 27424

Name: Chemical shifts of PrgK (19-92)
Published: 2018-08-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27424

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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:

Chemical shifts of PrgK (19-92)

Deposition date:

2018-03-12

Original release date:

2018-08-15

Authors:

Bergeron, Julien; McIntosh, Lawrence; Brockerman, Jacob

Citation:

Citation: Bergeron, Julien; Brockerman, Jacob; Vuckovic, Marija; Deng, Wanyin; Okon, Mark; McIntosh, Lawrence; Finlay, Brett; Strynadka, Natalie. "Characterization of the two conformations adopted by the T3SS inner-membrane protein PrgK" Protein Sci. 27, 1680-1691 (2018).
PubMed: 30095200

Assembly members:

Assembly members:
PrgK, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PrgK: KDKDLLKGLDQEQANEVIAV LQMHNIEANKIDSGKLGYSI TVAEPDFTAAVYWIKTYQLP PRPRVEIAQMFPAD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	454
15N chemical shifts	137
1H chemical shifts	183

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PrgK, conformer a	1
2	PrgK, conformer b	1

Entities:

Entity 1, PrgK, conformer a 74 residues - Formula weight is not available

1

LYS

ASP

LYS

ASP

LEU

LYS

GLY

LEU

ASP

2

GLN

GLU

GLN

ALA

ASN

GLU

VAL

ILE

ALA

VAL

3

LEU

GLN

MET

HIS

ASN

ILE

GLU

ALA

ASN

LYS

4

ILE

ASP

SER

GLY

LYS

LEU

GLY

TYR

SER

ILE

5

THR

VAL

ALA

GLU

PRO

ASP

PHE

THR

ALA

6

VAL

TYR

TRP

ILE

LYS

THR

TYR

GLN

LEU

PRO

7

PRO

ARG

PRO

ARG

VAL

GLU

ILE

ALA

GLN

MET

8

PHE

PRO

ALA

ASP

Samples:

PrgK19-92: PrgK, [U-100% 13C; U-100% 15N], 1 mM; HEPES 50 mM; NaCl 50 mM

sample_conditions_PrgK19-92: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	PrgK19-92	isotropic	sample_conditions_PrgK19-92
3D HNCACB	PrgK19-92	isotropic	sample_conditions_PrgK19-92
3D CBCA(CO)NH	PrgK19-92	isotropic	sample_conditions_PrgK19-92
3D HNCO	PrgK19-92	isotropic	sample_conditions_PrgK19-92
3D HCACO	PrgK19-92	isotropic	sample_conditions_PrgK19-92
3D HCCH-TOCSY	PrgK19-92	isotropic	sample_conditions_PrgK19-92

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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