BMRB Entry 25913

Name: Solution structure of RNF126 N-terminal zinc finger domain
Published: 2016-05-23

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PDB ID: 2n9o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25913
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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 RNF126 N-terminal zinc finger domain

Deposition date:

2015-12-01

Original release date:

2016-05-23

Authors:

Martinez-Lumbreras, Santiago; Krysztofinska, Ewelina; Thapaliya, Arjun; Isaacson, Rivka

Citation:

Citation: Krysztofinska, Ewelina; Martinez-Lumbreras, Santiago; Thapaliya, Arjun; Evans, Nicola; High, Stephen; Isaacson, Rivka. "Structural and functional insights into the E3 ligase, RNF126" Sci. Rep. 6, 26433-26433 (2016).
PubMed: 27193484

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4705.417 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 Vector: PET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMAEASPHPGRYFCHCCSV EIVPRLPDYICPRCESGFIE EL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	183
15N chemical shifts	38
1H chemical shifts	261

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	ZINC ION	2

Entities:

Entity 1, entity_1 42 residues - 4705.417 Da.

'GS' correspond to TEV cleavage tag

1

GLY

SER

MET

ALA

GLU

ALA

SER

PRO

HIS

PRO

2

GLY

ARG

TYR

PHE

CYS

HIS

CYS

SER

VAL

3

GLU

ILE

VAL

PRO

ARG

LEU

PRO

ASP

TYR

ILE

4

CYS

PRO

ARG

CYS

GLU

SER

GLY

PHE

ILE

GLU

5

GLU

LEU

Entity 2, ZINC ION - 65.409 Da.

1

ZN

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 350-750 uM; ZINC ION 350-750 uM; potassium phosphate 10 mM; sodium chloride 100 mM; TCEP 250 uM; DSS 10 uM; H2O 90%; D2O 10%

sample_2: entity_1, [U-99% 13C; U-99% 15N], 350-750 uM; ZINC ION 350-750 uM; potassium phosphate 10 mM; sodium chloride 100 mM; TCEP 250 uM; DSS 10 uM; D2O 90%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.0; 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_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

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

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

CcpNMR_Analysis v2.3, CCPN - chemical shift assignment, peak picking, structure solution

ARIA v2.1, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 500 MHz

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