BMRB Entry 30754

Name: NMR solution structure of Asterix/Gtsf1 from mouse (CHHC zinc finger domains)
Published: 2021-02-20

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PDB ID: 6x46
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30754
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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:

NMR solution structure of Asterix/Gtsf1 from mouse (CHHC zinc finger domains)

Deposition date:

2020-05-22

Original release date:

2021-02-20

Authors:

Ipsaro, J.; O'Brien, P.; Bhattacharya, S.; Palmer III, A.; Joshua-Tor, L.

Citation:

Citation: Ipsaro, J.; O'Brien, P.; Bhattacharya, S.; Palmer III, A.; Joshua-Tor, L.. "Asterix/Gtsf1 links tRNAs and piRNA silencing of retrotransposons" Cell Rep. 34, 108914-108914 (2021).
PubMed: 33789107

Assembly members:

Assembly members:
entity_1, polymer, 121 residues, 14217.607 Da.
entity_ZN, non-polymer, 65.409 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: Spodoptera frugiperda Vector: pFL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEDTYIDSLDPEKLLQCPYD KNHQIRASRFPYHLIKCRKN HPDVANKLATCPFNARHQVP RAEISHHISSCDDKSSIEQD VVNQTRNLGQETLAESTWQS PPSDEDWDKDLWEQTENLYF Q

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	80
1H chemical shifts	485

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2
3	unit_3	2

Entities:

Entity 1, unit_1 121 residues - 14217.607 Da.

1

MET

GLU

ASP

THR

TYR

ILE

ASP

SER

LEU

ASP

2

PRO

GLU

LYS

LEU

GLN

CYS

PRO

TYR

ASP

3

LYS

ASN

HIS

GLN

ILE

ARG

ALA

SER

ARG

PHE

4

PRO

TYR

HIS

LEU

ILE

LYS

CYS

ARG

LYS

ASN

5

HIS

PRO

ASP

VAL

ALA

ASN

LYS

LEU

ALA

THR

6

CYS

PRO

PHE

ASN

ALA

ARG

HIS

GLN

VAL

PRO

7

ARG

ALA

GLU

ILE

SER

HIS

ILE

SER

8

CYS

ASP

LYS

SER

ILE

GLU

GLN

ASP

9

VAL

ASN

GLN

THR

ARG

ASN

LEU

GLY

GLN

10

GLU

THR

LEU

ALA

GLU

SER

THR

TRP

GLN

SER

11

PRO

SER

ASP

GLU

ASP

TRP

ASP

LYS

ASP

12

LEU

TRP

GLU

GLN

THR

GLU

ASN

LEU

TYR

PHE

13

GLN

Entity 2, unit_2 - Zn - 65.409 Da.

1

ZN

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D (H)C(CCO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 30754

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: