BMRB Entry 52005

Name: Unbound VirB9Ct assignments and 15N-CEST experiments at 35 degrees
Published: 2024-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52005

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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:

Unbound VirB9Ct assignments and 15N-CEST experiments at 35 degrees

Deposition date:

2023-06-19

Original release date:

2024-09-28

Authors:

Davalos Macias, Angy; Kopke Salinas, Roberto; Rivera, Jose David

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: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

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
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VirB9Ct	1

Entities:

Entity 1, VirB9Ct 106 residues - 14332.1 Da.

The VirB9 first amino acid is N154

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
ZZ-exchange	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_4
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_5
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_6
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_7
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_8
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_9
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_10
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_11
15N-CEST	sample_1	isotropic	sample_conditions_1
15N-CEST	sample_1	isotropic	sample_conditions_12

BMRB Entry 52005

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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