BMRB Entry 51229

Name: The N-terminal domain of RNAse Y is organized as a coiled-coil domain, which displays two different conformations, one of them binding enolase.
Published: 2024-08-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51229

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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:

The N-terminal domain of RNAse Y is organized as a coiled-coil domain, which displays two different conformations, one of them binding enolase.

Deposition date:

2021-12-14

Original release date:

2024-08-09

Authors:

Hardouin, Pierre; Morellet, Nelly; Assrir, Nadine; Bou Nader, Charles; van Heijenoort, Carine; Golinelli-Pimpaneau, Beatrice

Citation:

Citation: Morellet, Nelly; Hardouin, Pierre; Assrir, Nadine; van Heijenoort, Carine; Golinelli-Pimpaneau, Beatrice. "Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold" Biomolecules 12, 1798-1798 (2022).
PubMed: 36551226

Assembly members:

Assembly members:
entity_1, polymer, 176 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21(DE3) star

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVRKTIAEAKIAGARGAAEQ ILEDAKRDAEALKKEALLEA KDEIHKLRIDAEQEVRERRN ELQKQENRLLQKEENLDRKH EGIDKREAMLEKKDHSLNER QQHIEEMESKVDEMIRMQQS ELERISSLTRDEAKQIILER VENELSHDIAIMTKETENRA KEEADKKAKNHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	460
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nter-BsRNaseY, chain A	1
2	Nter-BsRNaseY, chain B	1

Entities:

Entity 1, Nter-BsRNaseY, chain A 176 residues - Formula weight is not available

1

MET

VAL

ARG

LYS

THR

ILE

ALA

GLU

ALA

LYS

2

ILE

ALA

GLY

ALA

ARG

GLY

ALA

GLU

GLN

3

ILE

LEU

GLU

ASP

ALA

LYS

ARG

ASP

ALA

GLU

4

ALA

LEU

LYS

GLU

ALA

LEU

GLU

ALA

5

LYS

ASP

GLU

ILE

HIS

LYS

LEU

ARG

ILE

ASP

6

ALA

GLU

GLN

GLU

VAL

ARG

GLU

ARG

ASN

7

GLU

LEU

GLN

LYS

GLN

GLU

ASN

ARG

LEU

8

GLN

LYS

GLU

ASN

LEU

ASP

ARG

LYS

HIS

9

GLU

GLY

ILE

ASP

LYS

ARG

GLU

ALA

MET

LEU

10

GLU

LYS

ASP

HIS

SER

LEU

ASN

GLU

ARG

11

GLN

HIS

ILE

GLU

MET

GLU

SER

LYS

12

VAL

ASP

GLU

MET

ILE

ARG

MET

GLN

SER

13

GLU

LEU

GLU

ARG

ILE

SER

LEU

THR

ARG

14

ASP

GLU

ALA

LYS

GLN

ILE

LEU

GLU

ARG

15

VAL

GLU

ASN

GLU

LEU

SER

HIS

ASP

ILE

ALA

16

ILE

MET

THR

LYS

GLU

THR

GLU

ASN

ARG

ALA

17

LYS

GLU

ALA

ASP

LYS

ALA

LYS

ASN

18

HIS

Samples:

sample_1: Nter-BsRNaseY dimer, [U-100% 13C; U-100% 15N; U-80% 2H], 970 uM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz