BMRB Entry 34630

Name: The NMR structure of the Zf-GRF domains from the mouse Endonuclease VIII-LIKE 3 (mNEIL3)
Published: 2022-05-26

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PDB ID: 7omk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34630
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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:

The NMR structure of the Zf-GRF domains from the mouse Endonuclease VIII-LIKE 3 (mNEIL3)

Deposition date:

2021-05-24

Original release date:

2022-05-26

Authors:

Dinesh, D.; Huskova, A.; Srb, P.; Veverka, V.; Silhan, J.

Citation:

Citation: Dinesh, D.; Huskova, A.; Srb, P.; Veverka, V.; Silhan, J.. "The NMR structure of the Zf-GRF domains from the mouse Endonuclease VIII-LIKE 3 (mNEIL3)" .

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 10818.668 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21 Vector: pSUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SPLCKMHHRRCVLRVVRKDG ENKGRQFYACSLPRGAQCGF FEWADLSFPFCKHGKRSIMK TVLKIGPNNGKNFFVCPLEK EKQCNFFQWAENG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	99
1H chemical shifts	659

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 93 residues - 10818.668 Da.

1

SER

PRO

LEU

CYS

LYS

MET

HIS

ARG

2

CYS

VAL

LEU

ARG

VAL

ARG

LYS

ASP

GLY

3

GLU

ASN

LYS

GLY

ARG

GLN

PHE

TYR

ALA

CYS

4

SER

LEU

PRO

ARG

GLY

ALA

GLN

CYS

GLY

PHE

5

PHE

GLU

TRP

ALA

ASP

LEU

SER

PHE

PRO

PHE

6

CYS

LYS

HIS

GLY

LYS

ARG

SER

ILE

MET

LYS

7

THR

VAL

LEU

LYS

ILE

GLY

PRO

ASN

GLY

8

LYS

ASN

PHE

VAL

CYS

PRO

LEU

GLU

LYS

9

GLU

LYS

GLN

CYS

ASN

PHE

GLN

TRP

ALA

10

GLU

ASN

GLY

Samples:

sample_1: NEIL3-GRF, [U-13C; U-15N], 250 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - data analysis

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, YASARA - structure calculation

NMR spectrometers:

Bruker AVANCE 850 MHz

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