BMRB Entry 51467

Name: Backbone 1H, 13C and 15N chemical shift assignments of the distal domain of a K6-linked ubiquitin dimer (K6-linked diUb) comprising an artificial triazole linkage
Published: 2023-07-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51467

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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:

Backbone 1H, 13C and 15N chemical shift assignments of the distal domain of a K6-linked ubiquitin dimer (K6-linked diUb) comprising an artificial triazole linkage

Deposition date:

2022-05-21

Original release date:

2023-07-27

Authors:

Schneider, Tobias; Sawade, Kevin; Berner, Frederic; Peter, Christine; Kovermann, Michael

Citation:

Citation: Schneider, Tobias; Sawade, Kevin; Berner, Frederic; Peter, Christine; Kovermann, Michael. "Specifying conformational heterogeneity of multi-domain proteins at atomic resolution" Structure 31, 1259-1274 (2023).
PubMed: 37557171

Assembly members:

Assembly members:
entity_1, polymer, 80 residues, Formula weight is not available

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: pGEX2TK UbG75M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RASVGSQIFVKTLTGKTITL EVEPSDTIENVKAKIQDKEG IPPDQQRLIFAGKQLEDGRT LSDYNIQKESTLHLVLRLRX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	78
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	K6-linked diUb (distal)	1

Entities:

Entity 1, K6-linked diUb (distal) 80 residues - Formula weight is not available

residues 1-5 result from an N-terminal thrombin cleavage site

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY HSQC	sample_1	isotropic	sample_conditions_1
3D TROSY HNCA	sample_1	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 51467

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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