BMRB Entry 36143

Name: zinc finger domain of METTL3-METTL14 N6-methyladenosine methyltransferase
Published: 2018-05-25

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PDB ID: 5yz9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36143
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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:

zinc finger domain of METTL3-METTL14 N6-methyladenosine methyltransferase

Deposition date:

2017-12-13

Original release date:

2018-05-25

Authors:

Dong, X.; Tang, C.; Gong, Z.; Yin, P.; Huang, J.

Citation:

Citation: Huang, J.; Dong, X.; Gong, Z.; Qin, L.; Yang, S.; Zhu, Y.; Wang, X.; Zhang, D.; Zou, T.; Yin, P.; Tang, C.. "Solution structure of the RNA recognition domain of METTL3-METTL14 N6-methyladenosine methyltransferase" Protein Cell 10, 272-284 (2019).
PubMed: 29542011

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, 11753.191 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AHMSIVEKFRSRGRAQVQEF CDYGTKEECMKASDADRPCR KLHFRRIINKHTDESLGDCS FLNTCFHMDTCKYVHYEIDA SMDSEAPGSKDHTPSQELAL TQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	365
15N chemical shifts	95
1H chemical shifts	501

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_ZN_1	2
3	entity_ZN_2	2

Entities:

Entity 1, entity_1 102 residues - 11753.191 Da.

1

ALA

HIS

MET

SER

ILE

VAL

GLU

LYS

PHE

ARG

2

SER

ARG

GLY

ARG

ALA

GLN

VAL

GLN

GLU

PHE

3

CYS

ASP

TYR

GLY

THR

LYS

GLU

CYS

MET

4

LYS

ALA

SER

ASP

ALA

ASP

ARG

PRO

CYS

ARG

5

LYS

LEU

HIS

PHE

ARG

ILE

ASN

LYS

6

HIS

THR

ASP

GLU

SER

LEU

GLY

ASP

CYS

SER

7

PHE

LEU

ASN

THR

CYS

PHE

HIS

MET

ASP

THR

8

CYS

LYS

TYR

VAL

HIS

TYR

GLU

ILE

ASP

ALA

9

SER

MET

ASP

SER

GLU

ALA

PRO

GLY

SER

LYS

10

ASP

HIS

THR

PRO

SER

GLN

GLU

LEU

ALA

LEU

11

THR

GLN

Entity 2, entity_ZN_1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: ZFD, [U-13C; U-15N], 0.8 mM; PBS 20 mM; sodium chloride 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker AvanceIII 850 MHz

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