BMRB Entry 34678

Name: Solution structure of the C terminal domain of MgtC (PA4635) from Pseudomonas aeruginosa
Published: 2022-04-27

Click here to enlarge.

PDB ID: 7qa5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34678
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the C terminal domain of MgtC (PA4635) from Pseudomonas aeruginosa

Deposition date:

2021-11-16

Original release date:

2022-04-27

Authors:

Barthe, P.; Cohen-Gonsaud, M.

Citation:

Citation: Barthe, P.; Cohen-Gonsaud, M.. "Solution structure of the C terminal domain of MgtC (PA4635) from Pseudomonas aeruginosa" .

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, 10836.162 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMASEAEQRYEVQIVCRA EDEIQVRSLMLHSLGSSDLR LQSLHSEDLDNPAKLEVRAE LLGTPEAPAQLERLVSRVSL EKGVSSVRWQVFELAAD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	222
15N chemical shifts	97
1H chemical shifts	647

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 97 residues - 10836.162 Da.

1

GLY

PRO

HIS

MET

ALA

SER

GLU

ALA

GLU

GLN

2

ARG

TYR

GLU

VAL

GLN

ILE

VAL

CYS

ARG

ALA

3

GLU

ASP

GLU

ILE

GLN

VAL

ARG

SER

LEU

MET

4

LEU

HIS

SER

LEU

GLY

SER

ASP

LEU

ARG

5

LEU

GLN

SER

LEU

HIS

SER

GLU

ASP

LEU

ASP

6

ASN

PRO

ALA

LYS

LEU

GLU

VAL

ARG

ALA

GLU

7

LEU

GLY

THR

PRO

GLU

ALA

PRO

ALA

GLN

8

LEU

GLU

ARG

LEU

VAL

SER

ARG

VAL

SER

LEU

9

GLU

LYS

GLY

VAL

SER

VAL

ARG

TRP

GLN

10

VAL

PHE

GLU

LEU

ALA

ASP

Samples:

sample_1: PA4635, [U-15N], 0.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_2: PA4635, [U-13C; U-15N], 0.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_3: PA4635, [U-13C; U-15N], 0.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_4: PA4635, [U-13C; U-15N], 0.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D DQF-COSY	sample_3	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_4	isotropic	sample_conditions_1

Software:

TopSpin v3.6.2, Bruker Biospin - processing

CINDY v2.1, PAdilla, A., Padilla, A. - chemical shift assignment, peak picking

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 700 MHz

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