Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53703

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Translation repressor RsmE dimer from Pseudomonas protegens with one of its two RNA binding sites occupied by SL2 of the noncoding RNA RsmZ.
Published: 2026-04-13

Title:

Translation repressor RsmE dimer from Pseudomonas protegens with one of its two RNA binding sites occupied by SL2 of the noncoding RNA RsmZ.

Deposition date:

2026-04-01

Original release date:

2026-04-13

Authors:

Finol, Esteban; Damberger, Fred; Allain, Frederic

Citation:

Citation: Finol, Esteban; Damberger, Fred; Krepl, Miroslav; Flugel, Timo; Dietrich, Priscilla; Michaels, Thomas; Vogeli, Beat; Sponer, Jiri; Allain, Frederic H-T. "Newton's cradle-like allosteric mechanism explains regulatory RsmE RNA binding." Res. Sq. ., .-. (2025).
PubMed: 40321760

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7937.068 Da.
entity_2, polymer, 22 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Pseudomonas protegens Taxonomy ID: 380021 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas protegens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b-64WRsmE

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLILTRKVGESINIGDDITI TILGVSGQQVRIGINAPKDV AVHREEIYQRIQAGLTAPDK RETWHHHHHH
entity_2: GGGCCAUCAAGGACGAUGGU CC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	520
15N chemical shifts	133
1H chemical shifts	873

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RsmE, chain 1	1
2	RsmE, chain 2	1
3	SL2	2

Entities:

Entity 1, RsmE, chain 1 70 residues - 7937.068 Da.

The C-terminal native P64 has been mutated to W64 to enhance absorbance for easier quantification of protein concentration, and it is followed by 6 Histidines (H65-H70) for protein purification.

1	MET	LEU	ILE	LEU	THR	ARG	LYS	VAL	GLY	GLU
2	SER	ILE	ASN	ILE	GLY	ASP	ASP	ILE	THR	ILE
3	THR	ILE	LEU	GLY	VAL	SER	GLY	GLN	GLN	VAL
4	ARG	ILE	GLY	ILE	ASN	ALA	PRO	LYS	ASP	VAL
5	ALA	VAL	HIS	ARG	GLU	GLU	ILE	TYR	GLN	ARG
6	ILE	GLN	ALA	GLY	LEU	THR	ALA	PRO	ASP	LYS
7	ARG	GLU	THR	TRP	HIS	HIS	HIS	HIS	HIS	HIS

Entity 2, SL2 22 residues - Formula weight is not available

Nucleotides G17 and C38 form the first base-pair of the stem region which extends up to and includes C24-G31. The loop consists of A25-C30.

1

G

C

A

U

C

A

2

G

A

C

G

A

U

G

U

3

C

Samples:

sample_1: RsmE, [U-99% 13C; U-99% 15N], 0.45 ± 0.05 mM; NaCl 30 ± 0.05 mM; Potassium phosphate, pH 7.2 50 ± 0.05 mM; SL2 0.22 ± 0.05 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.2; pressure: 1 atm; temperature: 313 K

sample_conditions_2: ionic strength: 0.1 M; pH: 7.2; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_2
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v3.133 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 500 MHz
Bruker AVANCE III 700 MHz

BMRB Entry 53703