BMRB Entry 30417

Name: NMR Structure of Salmonella Type III Secretion system protein OrgC
Published: 2018-07-24

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PDB ID: 6cjd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30417
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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 Structure of Salmonella Type III Secretion system protein OrgC

Deposition date:

2018-02-26

Original release date:

2018-07-24

Authors:

Dey, S.; De Guzman, R.

Citation:

Citation: Kato, Junya; Dey, Supratim; Soto, Jose; Butan, Carmen; Wilkinson, Mason; De Guzman, Roberto; Galan, Jorge. "A protein secreted by the Salmonella type III secretion system controls needle filament assembly" Elife 7, e35886-e35886 (2018).
PubMed: 30015613

Assembly members:

Assembly members:
entity_1, polymer, 131 residues, 14293.888 Da.

Natural source:

Natural source: Common Name: Salmonella enterica Taxonomy ID: 59201 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMVSLSARAAMLNNMDSAP LSNGGDVDLYDAFYQRLLAL PESASSETLKDSIYQEMNAF KDPNSGDSAFVSFEQQTAML QNMLAKVEPGTHLYEALNGV LVGSMNAQSQMTSWMQEIIL SGGENKEAIDW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	238
15N chemical shifts	123
1H chemical shifts	245

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 131 residues - 14293.888 Da.

1

GLY

HIS

MET

VAL

SER

LEU

SER

ALA

ARG

ALA

2

ALA

MET

LEU

ASN

MET

ASP

SER

ALA

PRO

3

LEU

SER

ASN

GLY

ASP

VAL

ASP

LEU

TYR

4

ASP

ALA

PHE

TYR

GLN

ARG

LEU

ALA

LEU

5

PRO

GLU

SER

ALA

SER

GLU

THR

LEU

LYS

6

ASP

SER

ILE

TYR

GLN

GLU

MET

ASN

ALA

PHE

7

LYS

ASP

PRO

ASN

SER

GLY

ASP

SER

ALA

PHE

8

VAL

SER

PHE

GLU

GLN

THR

ALA

MET

LEU

9

GLN

ASN

MET

LEU

ALA

LYS

VAL

GLU

PRO

GLY

10

THR

HIS

LEU

TYR

GLU

ALA

LEU

ASN

GLY

VAL

11

LEU

VAL

GLY

SER

MET

ASN

ALA

GLN

SER

GLN

12

MET

THR

SER

TRP

MET

GLN

GLU

ILE

LEU

13

SER

GLY

GLU

ASN

LYS

GLU

ALA

ILE

ASP

14

TRP

Samples:

sample_1: OrgC, [U-99% 15N], 1.2 mM; OrgC, [U-13C; U-15N], 1.2 mM; OrgC, [U-13C], 1.2 mM; MES 2 mM; NaCl 75 mM

sample_conditions_1: ionic strength: 75 mM; pH: 6.5 pH*; pressure: 1 mbar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
HMQC NOESY	sample_1	isotropic	sample_conditions_1
HSQC NOESY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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