BMRB Entry 36072

Name: C-terminal zinc finger of RING finger protein 141
Published: 2018-04-30

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PDB ID: 5xek
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36072
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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:

C-terminal zinc finger of RING finger protein 141

Deposition date:

2017-04-05

Original release date:

2018-04-30

Authors:

Miyamoto, K.

Citation:

Citation: Miyamoto, Kazuhide; Uechi, Airi; Saito, Kazuki. "The zinc finger domain of RING finger protein 141 reveals a unique RING fold." Protein Sci. 26, 1681-1686 (2017).
PubMed: 28547869

Assembly members:

Assembly members:
RING finger protein 141, polymer, 42 residues, 4920.788 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RING finger protein 141: EEECCICMDGRADLILPCAH SFCQKCIDKWSDRHRNCPIC RL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	41

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 42 residues - 4920.788 Da.

1

GLU

CYS

ILE

CYS

MET

ASP

GLY

2

ARG

ALA

ASP

LEU

ILE

LEU

PRO

CYS

ALA

HIS

3

SER

PHE

CYS

GLN

LYS

CYS

ILE

ASP

LYS

TRP

4

SER

ASP

ARG

HIS

ARG

ASN

CYS

PRO

ILE

CYS

5

ARG

LEU

Entity 2, entity_ZN_1 - Zn 2 - 65.409 Da.

1

ZN

Samples:

sample_1: RING finger protein 141, [U-13C; U-15N], 1.0 mM; Tris-HCl 20 mM; NaCl 50 mM; dithiothreitol 1 mM; ZnCl2 50 uM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.9; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, refinement

Discovery Studio v2.1, Accelrys Software Inc. - structure calculation

NMR spectrometers:

Bruker Avance 800 MHz