BMRB Entry 50770

Name: 1H and 15N chemical-shift assignments of the backbone amide groups of the RecA_C domain of Bombyx Mori Vasa
Published: 2024-10-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50770

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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 and 15N chemical-shift assignments of the backbone amide groups of the RecA_C domain of Bombyx Mori Vasa

Deposition date:

2021-02-17

Original release date:

2024-10-15

Authors:

Codutti, Luca; Nesme, Leo; Kirkpatrick, John; Carlomagno, Teresa

Citation:

Citation: Codutti, Luca; Kirkpatrick, John; zur Lage, Suzanne; Carlomagno, Teresa. "Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa" Biophys. J. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 166 residues, Formula weight is not available

Natural source:

Natural source: Common Name: domestic silkworm Taxonomy ID: 7091 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bombyx mori

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMASTDVEQIFIEVTKYEK RNSLKQLIEENDGKRILVFV ETKRNADFIAAMLSEQQLLT SSIHGDRMQREREEALQNFK SGKHCILVATAVAARGLDIK NVDIVVNYDLPKSIDEYVHR IGRTGRVGNRGKAVSFYDSD QDLALVADLSKILRQADQSV PDFLKG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RecA_C	1

Entities:

Entity 1, RecA_C 166 residues - Formula weight is not available

The first residue of the native Vasa sequence is residue 5 in the sequence above, which corresponds to residue 403 in the native Vasa sequence; hence residue 1 of the sequence above should be numbered as residue 399 (i.e. the first 3 residues are cloning artifacts).

1

GLY

ALA

MET

ALA

SER

THR

ASP

VAL

GLU

GLN

2

ILE

PHE

ILE

GLU

VAL

THR

LYS

TYR

GLU

LYS

3

ARG

ASN

SER

LEU

LYS

GLN

LEU

ILE

GLU

4

ASN

ASP

GLY

LYS

ARG

ILE

LEU

VAL

PHE

VAL

5

GLU

THR

LYS

ARG

ASN

ALA

ASP

PHE

ILE

ALA

6

ALA

MET

LEU

SER

GLU

GLN

LEU

THR

7

SER

ILE

HIS

GLY

ASP

ARG

MET

GLN

ARG

8

GLU

ARG

GLU

ALA

LEU

GLN

ASN

PHE

LYS

9

SER

GLY

LYS

HIS

CYS

ILE

LEU

VAL

ALA

THR

10

ALA

VAL

ALA

ARG

GLY

LEU

ASP

ILE

LYS

11

ASN

VAL

ASP

ILE

VAL

ASN

TYR

ASP

LEU

12

PRO

LYS

SER

ILE

ASP

GLU

TYR

VAL

HIS

ARG

13

ILE

GLY

ARG

THR

GLY

ARG

VAL

GLY

ASN

ARG

14

GLY

LYS

ALA

VAL

SER

PHE

TYR

ASP

SER

ASP

15

GLN

ASP

LEU

ALA

LEU

VAL

ALA

ASP

LEU

SER

16

LYS

ILE

LEU

ARG

GLN

ALA

ASP

GLN

SER

VAL

17

PRO

ASP

PHE

LEU

LYS

GLY

Samples:

sample_1: RecA_C, [U-13C; U-15N], 0.3 ± 0.05 mM; sodium chloride 150 mM; sodium phosphate 50 mM

sample_conditions_1: pH: 6.5; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection, processing

CcpNMR v2.4 - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz