BMRB Entry 34111

Name: Structure of the N-terminal domain of the Escherichia Coli ProQ RNA binding protein
Published: 2017-05-04

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PDB ID: 5nbb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34111
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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: Structure of the N-terminal domain of the Escherichia Coli ProQ RNA binding protein PubMed: 28193673

Deposition date: 2017-03-01 Original release date: 2017-05-04

Authors: Gonzales, G.; Hardwick, S.; Maslen, S.; Skehel, M.; Holmqvist, E.; Vogel, J.; Bateman, A.; Luisi, B.; Broadhurst, R.

Citation: Gonzalez, G.; Hardwick, S.; Maslen, S.; Skehel, J.; Holmqvist, E.; Vogel, J.; Bateman, A.; Luisi, B.; Broadhurst, R.. "Structure of the Escherichia coli ProQ RNA-binding protein." RNA 23, 696-711 (2017).

Assembly members:
entity_1, polymer, 53 residues, 5601.499 Da.

Natural source: Common Name: E. coli Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: ProQ-pET-DUET

Entity Sequences (FASTA):
entity_1: VSDISALTVGQALKVKAGQN AMDATVLEITKDGVRVQLNS GMSLIVRAEHLVF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	156
15N chemical shifts	54
1H chemical shifts	349

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 53 residues - 5601.499 Da.

1

VAL

SER

ASP

ILE

SER

ALA

LEU

THR

VAL

GLY

2

GLN

ALA

LEU

LYS

VAL

LYS

ALA

GLY

GLN

ASN

3

ALA

MET

ASP

ALA

THR

VAL

LEU

GLU

ILE

THR

4

LYS

ASP

GLY

VAL

ARG

VAL

GLN

LEU

ASN

SER

5

GLY

MET

SER

LEU

ILE

VAL

ARG

ALA

GLU

HIS

6

LEU

VAL

PHE

Samples:

sample_1: entity_1 mM; 3,3,3-trimethylsilylpropionate 0.0025 ± 0.0005 %; TCEP 1 ± 0.1 mM; sodium chloride 100 ± 5 mM; sodium phosphate 20 ± 1 mM

sample_2: entity_1 mM; 3,3,3-trimethylsilylpropionate 0.0025 ± 0.0005 %; TCEP 1 ± 0.1 mM; sodium chloride 20 ± 1 mM; sodium phosphate 100 ± 5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.4, CCPN - data analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz

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