BMRB Entry 25914

Name: Solution structure of RNF126 N-terminal zinc finger domain in complex with BAG6 Ubiquitin-like domain
Published: 2016-05-23

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PDB ID: 2n9p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25914
MolProbity Validation Chart

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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 in complex with BAG6 Ubiquitin-like 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.
entity_2, polymer, 100 residues, 11276.897 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
entity_2: MAHHHHHHVDDDDKMLEVLV KTLDSQTRTFIVGAQMNVKE FKEHIAASVSIPSEKQRLIY QGRVLQDDKKLQEYNVGGKV IHLVERAPPQTHLPSGASSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	548
15N chemical shifts	136
1H chemical shifts	862

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_2	2
3	ZINC ION	3

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, entity_2 100 residues - 11276.897 Da.

'MAHHHHHHDDDDKM' correspond to His-tag

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	VAL	ASP
2	ASP	ASP	ASP	LYS	MET	LEU	GLU	VAL	LEU	VAL
3	LYS	THR	LEU	ASP	SER	GLN	THR	ARG	THR	PHE
4	ILE	VAL	GLY	ALA	GLN	MET	ASN	VAL	LYS	GLU
5	PHE	LYS	GLU	HIS	ILE	ALA	ALA	SER	VAL	SER
6	ILE	PRO	SER	GLU	LYS	GLN	ARG	LEU	ILE	TYR
7	GLN	GLY	ARG	VAL	LEU	GLN	ASP	ASP	LYS	LYS
8	LEU	GLN	GLU	TYR	ASN	VAL	GLY	GLY	LYS	VAL
9	ILE	HIS	LEU	VAL	GLU	ARG	ALA	PRO	PRO	GLN
10	THR	HIS	LEU	PRO	SER	GLY	ALA	SER	SER	GLY

Entity 3, ZINC ION - 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_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 12C14N filtered 13C edited NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
3D 12C14N filtered 13C edited NOESY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	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 25914

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	VAL	ASP
2	ASP	ASP	ASP	LYS	MET	LEU	GLU	VAL	LEU	VAL
3	LYS	THR	LEU	ASP	SER	GLN	THR	ARG	THR	PHE
4	ILE	VAL	GLY	ALA	GLN	MET	ASN	VAL	LYS	GLU
5	PHE	LYS	GLU	HIS	ILE	ALA	ALA	SER	VAL	SER
6	ILE	PRO	SER	GLU	LYS	GLN	ARG	LEU	ILE	TYR
7	GLN	GLY	ARG	VAL	LEU	GLN	ASP	ASP	LYS	LYS
8	LEU	GLN	GLU	TYR	ASN	VAL	GLY	GLY	LYS	VAL
9	ILE	HIS	LEU	VAL	GLU	ARG	ALA	PRO	PRO	GLN
10	THR	HIS	LEU	PRO	SER	GLY	ALA	SER	SER	GLY

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	VAL	ASP
2	ASP	ASP	ASP	LYS	MET	LEU	GLU	VAL	LEU	VAL
3	LYS	THR	LEU	ASP	SER	GLN	THR	ARG	THR	PHE
4	ILE	VAL	GLY	ALA	GLN	MET	ASN	VAL	LYS	GLU
5	PHE	LYS	GLU	HIS	ILE	ALA	ALA	SER	VAL	SER
6	ILE	PRO	SER	GLU	LYS	GLN	ARG	LEU	ILE	TYR
7	GLN	GLY	ARG	VAL	LEU	GLN	ASP	ASP	LYS	LYS
8	LEU	GLN	GLU	TYR	ASN	VAL	GLY	GLY	LYS	VAL
9	ILE	HIS	LEU	VAL	GLU	ARG	ALA	PRO	PRO	GLN
10	THR	HIS	LEU	PRO	SER	GLY	ALA	SER	SER	GLY

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	VAL	ASP
2	ASP	ASP	ASP	LYS	MET	LEU	GLU	VAL	LEU	VAL
3	LYS	THR	LEU	ASP	SER	GLN	THR	ARG	THR	PHE
4	ILE	VAL	GLY	ALA	GLN	MET	ASN	VAL	LYS	GLU
5	PHE	LYS	GLU	HIS	ILE	ALA	ALA	SER	VAL	SER
6	ILE	PRO	SER	GLU	LYS	GLN	ARG	LEU	ILE	TYR
7	GLN	GLY	ARG	VAL	LEU	GLN	ASP	ASP	LYS	LYS
8	LEU	GLN	GLU	TYR	ASN	VAL	GLY	GLY	LYS	VAL
9	ILE	HIS	LEU	VAL	GLU	ARG	ALA	PRO	PRO	GLN
10	THR	HIS	LEU	PRO	SER	GLY	ALA	SER	SER	GLY