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

Samples:

sample_1: VirB9Ct, [U-99% 15N], 500 ± 50 uM; NaOAc 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

sample_conditions_2: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 280 K

sample_conditions_3: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

sample_conditions_4: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 283 K

sample_conditions_5: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 286 K

sample_conditions_6: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 289 K

sample_conditions_7: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 292 K

sample_conditions_8: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 295 K

sample_conditions_9: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_10: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 301 K

sample_conditions_11: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 304 K

sample_conditions_12: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

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

Software:

CcpNMR v2.0 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz