BMRB Entry 34110

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: 5nb9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34110
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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

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:

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).
PubMed: 28193673

Assembly members:

Assembly members:
entity_1, polymer, 133 residues, 15107.911 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 585035 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: ProQ-NTD-pET-DUET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSQDPMENQPK LNSSKEVIAFLAERFPHCFS AEGEARPLKIGIFQDLVDRV AGEMNLSKTQLRSALRLYTS SWRYLYGVKPGATRVDLDGN PCGELDEQHVEHARKQLEEA KARVQAQRAEQQA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	493
15N chemical shifts	126
1H chemical shifts	722

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_1 133 residues - 15107.911 Da.

1

MET

GLY

SER

HIS

2

SER

GLN

ASP

PRO

MET

GLU

ASN

GLN

PRO

LYS

3

LEU

ASN

SER

LYS

GLU

VAL

ILE

ALA

PHE

4

LEU

ALA

GLU

ARG

PHE

PRO

HIS

CYS

PHE

SER

5

ALA

GLU

GLY

GLU

ALA

ARG

PRO

LEU

LYS

ILE

6

GLY

ILE

PHE

GLN

ASP

LEU

VAL

ASP

ARG

VAL

7

ALA

GLY

GLU

MET

ASN

LEU

SER

LYS

THR

GLN

8

LEU

ARG

SER

ALA

LEU

ARG

LEU

TYR

THR

SER

9

SER

TRP

ARG

TYR

LEU

TYR

GLY

VAL

LYS

PRO

10

GLY

ALA

THR

ARG

VAL

ASP

LEU

ASP

GLY

ASN

11

PRO

CYS

GLY

GLU

LEU

ASP

GLU

GLN

HIS

VAL

12

GLU

HIS

ALA

ARG

LYS

GLN

LEU

GLU

ALA

13

LYS

ALA

ARG

VAL

GLN

ALA

GLN

ARG

ALA

GLU

14

GLN

ALA

Samples:

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

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

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 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 HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2

Software:

Analysis v2.4, CCPN - data analysis

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

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker DRX 500 MHz
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