BMRB Entry 51836

Name: Backbone (1HN, 15N, 13C) resonance assignments for the VirB9 C-terminal domain in the unbound state
Published: 2024-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51836

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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:

Backbone (1HN, 15N, 13C) resonance assignments for the VirB9 C-terminal domain in the unbound state

Deposition date:

2023-02-16

Original release date:

2024-09-28

Authors:

Favaro, Denize; Davalos, Angy; Salinas, Roberto

Citation:

Citation: Davalos Macias, Angy; Rivera, Jose; Favaro, Denize; Oliveira, Ronaldo; Carretero, Gustavo; Lacerda, Caroline; Cuccovia, Iolanda; Cardoso, Marcus; Farah, Chuck; Kopke Salinas, Roberto. "Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins" ACS Chem. Biol. 19, 669-686 (2024).
PubMed: 38486495

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, 14332.1 Da.

Natural source:

Natural source: Common Name: Xanthomonas citri Taxonomy ID: 346 Superkingdom: Bacteria Kingdom: not available Genus/species: Xanthomonas citri

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMNAKILKDRRYYYDYDY ATRTKKSWLIPSRVYDDGKF TYINMDLTRFPTGNFPAVFA REKEHAEDFLVNTTVEGNTL IVHGTYPFLVVRHGDNVVGL RRNKQK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	223
15N chemical shifts	70
1H chemical shifts	70

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VirB9	1

Entities:

Entity 1, VirB9 106 residues - 14332.1 Da.

VirB9 residues 154 - 255 corresponding to the C-terminal domain. The first four amino acids (GSHM) are derived from the plasmid.

1

GLY

SER

HIS

MET

ASN

ALA

LYS

ILE

LEU

LYS

2

ASP

ARG

TYR

ASP

TYR

ASP

TYR

3

ALA

THR

ARG

THR

LYS

SER

TRP

LEU

ILE

4

PRO

SER

ARG

VAL

TYR

ASP

GLY

LYS

PHE

5

THR

TYR

ILE

ASN

MET

ASP

LEU

THR

ARG

PHE

6

PRO

THR

GLY

ASN

PHE

PRO

ALA

VAL

PHE

ALA

7

ARG

GLU

LYS

GLU

HIS

ALA

GLU

ASP

PHE

LEU

8

VAL

ASN

THR

VAL

GLU

GLY

ASN

THR

LEU

9

ILE

VAL

HIS

GLY

THR

TYR

PRO

PHE

LEU

VAL

10

VAL

ARG

HIS

GLY

ASP

ASN

VAL

GLY

LEU

11

ARG

ASN

LYS

GLN

LYS

Samples:

sample_1: VirB9, [U-99% 13C; U-99% 15N], 0.5 ± 0.1 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 5.0; pressure: 1 atm; temperature: 280 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS v2.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz