BMRB Entry 34669

Name: Solution structure of the NRDI domain of Nab3
Published: 2022-01-07

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PDB ID: 7pre
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34669
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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:

Solution structure of the NRDI domain of Nab3

Deposition date:

2021-09-21

Original release date:

2022-01-07

Authors:

Chaves-Arquero, B.; Martinez-Lumbreras, S.; Perez-Canadillas, J.

Citation:

Citation: Chaves-Arquero, B.; Martinez-Lumbreras, S.; Camero, S.; Santiveri, C.; Mirassou, Y.; Campos-Olivas, R.; Jimenez, M.; Calvo, O.; Perez-Canadillas, J.. "Structural basis of Nrd1-Nab3 heterodimerization" Life Sci. Alliance 5, e202101252-e202101252 (2022).
PubMed: 35022249

Assembly members:

Assembly members:
entity_1, polymer, 53 residues, 6106.913 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSWGSMENVNYDLLQKQVKY IMDSNMLNLPQFQHLPQEEK MSAILAMLNSNSD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	217
15N chemical shifts	52
1H chemical shifts	342

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 53 residues - 6106.913 Da.

1

GLY

SER

TRP

GLY

SER

MET

GLU

ASN

VAL

ASN

2

TYR

ASP

LEU

GLN

LYS

GLN

VAL

LYS

TYR

3

ILE

MET

ASP

SER

ASN

MET

LEU

ASN

LEU

PRO

4

GLN

PHE

GLN

HIS

LEU

PRO

GLN

GLU

LYS

5

MET

SER

ALA

ILE

LEU

ALA

MET

LEU

ASN

SER

6

ASN

SER

ASP

Samples:

sample_1: potassium phosphate 25 mM; sodium chloride 25 mM; DTT 1 mM; Nab3, [U-100% 13C; U-100% 15N], 480 uM

sample_2: potassium phosphate 25 mM; sodium chloride 25 mM; DTT 1 mM; Nab3 480 uM

sample_3: potassium phosphate 25 mM; sodium chloride 25 mM; DTT 1 mM; Nab3 480 uM

sample_4: potassium phosphate 25 mM; sodium chloride 25 mM; DTT 1 mM; Nab3, [U-100% 13C; U-100% 15N], 480 uM

sample_conditions_1: ionic strength: 53.5 mM; pH: 6.6; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE 800 MHz

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