BMRB Entry 30721

Name: Solution structure of Pseudomonas aeruginosa IF3 C-terminal domain
Published: 2021-02-04

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PDB ID: 6vrj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30721
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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: Solution structure of Pseudomonas aeruginosa IF3 C-terminal domain

Deposition date: 2020-02-07 Original release date: 2021-02-04

Authors: Zhang, Y.; Li, L.

Citation: Zhang, Y.; Li, L.. "Solution structure of Pseudomonas aeruginosa IF3 C-terminal domain" .

Assembly members:
entity_1, polymer, 97 residues, 11287.258 Da.

Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

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

Entity Sequences (FASTA):
entity_1: VAKKNQKQAQVKEIKFRPGT EEGDYQVKLRNLVRFLSEGD KAKVSLRFRGREMAHQELGM ELLKRVEADLVEYGTVEQHP KLEGRQLMMVIAPKKKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	376
15N chemical shifts	90
1H chemical shifts	559

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 97 residues - 11287.258 Da.

1

VAL

ALA

LYS

ASN

GLN

LYS

GLN

ALA

GLN

2

VAL

LYS

GLU

ILE

LYS

PHE

ARG

PRO

GLY

THR

3

GLU

GLY

ASP

TYR

GLN

VAL

LYS

LEU

ARG

4

ASN

LEU

VAL

ARG

PHE

LEU

SER

GLU

GLY

ASP

5

LYS

ALA

LYS

VAL

SER

LEU

ARG

PHE

ARG

GLY

6

ARG

GLU

MET

ALA

HIS

GLN

GLU

LEU

GLY

MET

7

GLU

LEU

LYS

ARG

VAL

GLU

ALA

ASP

LEU

8

VAL

GLU

TYR

GLY

THR

VAL

GLU

GLN

HIS

PRO

9

LYS

LEU

GLU

GLY

ARG

GLN

LEU

MET

VAL

10

ILE

ALA

PRO

LYS

Samples:

sample_1: PaIF3C, [U-15N], 1.0 ± 0.2 mM; KPO4 25 mM

sample_2: PaIF3C, [U-13C; U-15N], 1.0 ± 0.2 mM; KPO4 25 mM

sample_3: PaIF3C, [U-99% 13C; U-99% 15N], 1.0 ± 0.2 mM; KPO4 25 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1

Software:

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

Sparky, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE 700 MHz

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