BMRB Entry 26335

Name: 1H, 13C, and 15N chemical shift assignments of a minimal trimeric Rec114-Mei4 complex
Published: 2023-08-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26335

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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:

1H, 13C, and 15N chemical shift assignments of a minimal trimeric Rec114-Mei4 complex

Deposition date:

2022-09-16

Original release date:

2023-08-04

Authors:

Volkov, Oleksandr; Daccache, Dima; Claeys Bouuaert, Corentin

Citation:

Citation: Daccache, Dima; Volkov, Oleksandr; Claeys Bouuaert, Corentin. "Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes." Genes. Dev. 37, 535-553 (2023).
PubMed: 37442581

Assembly members:

Assembly members:
Rec114, polymer, 55 residues, Formula weight is not available
Mei4, polymer, 43 residues, Formula weight is not available

Natural source:

Natural source: Common Name: budding yeasts Taxonomy ID: 580239 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDD009

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rec114: MEASPSEGLTIRVKNVNRNA SRKISKRLIKEKLKDEEFIK WVNKVETVLNKMFEK
Mei4: MSRGKLEDMEQKETSEVDWI ICFALIQSRNPTLWKRALSR KKG

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	444
15N chemical shifts	122
1H chemical shifts	621

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rec114_A	1
2	Rec114_B	1
3	Mei4	2

Entities:

Entity 1, Rec114_A 55 residues - Formula weight is not available

1

MET

GLU

ALA

SER

PRO

SER

GLU

GLY

LEU

THR

2

ILE

ARG

VAL

LYS

ASN

VAL

ASN

ARG

ASN

ALA

3

SER

ARG

LYS

ILE

SER

LYS

ARG

LEU

ILE

LYS

4

GLU

LYS

LEU

LYS

ASP

GLU

PHE

ILE

LYS

5

TRP

VAL

ASN

LYS

VAL

GLU

THR

VAL

LEU

ASN

6

LYS

MET

PHE

GLU

LYS

Entity 2, Mei4 43 residues - Formula weight is not available

1

MET

SER

ARG

GLY

LYS

LEU

GLU

ASP

MET

GLU

2

GLN

LYS

GLU

THR

SER

GLU

VAL

ASP

TRP

ILE

3

ILE

CYS

PHE

ALA

LEU

ILE

GLN

SER

ARG

ASN

4

PRO

THR

LEU

TRP

LYS

ARG

ALA

LEU

SER

ARG

5

LYS

GLY

Samples:

sample_1: Rec114_A, [U-100% 13C; U-100% 15N], 1.4 mM; Rec114_B, [U-100% 13C; U-100% 15N], 1.4 mM; Mei4, [U-100% 13C; U-100% 15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 30 mM; DTT 5 mM; sodium azide 0.02%; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 47 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(C)CH TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CCH TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6 - collection, processing

NMRPipe - processing

CcpNmr Analysis - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 800 MHz

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