BMRB Entry 51303

Name: Backbone assignment for mature tardigrade HeLEA protein
Published: 2024-01-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51303

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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 assignment for mature tardigrade HeLEA protein

Deposition date:

2022-02-05

Original release date:

2024-01-09

Authors:

Li, Xiao-Han; Yu, Conny; Murthy, Andal; Malhotra, Ketan; Stancheva, Viktoriya; Johnson, Christopher; Blackledge, Martin; Santhanam, Balaji; Miller, Elizabeth; Freund, Stefan; Babu, M. Madan

Citation:

Citation: Li, Xiao-Han; Yu, Conny; Murthy, Andal; Malhotra, Ketan; Stancheva, Viktoriya; Johnson, Christopher; Blackledge, Martin; Santhanam, Balaji; Miller, Elizabeth; Freund, Stefan; Babu, M. Madan. "An intrinsically disordered protein protects mitochondria through membrane interaction" PNAS Nexus ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 200 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Hypsibius exemplaris Taxonomy ID: 2072580 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hypsibius exemplaris

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ASSSGSGRPADNWAESQKEK AKAGLKDAQAEVGKVAREVK DKAAGGIEQAKDAVKQGAND LKRSGSRTFENAKDDIQAKA QHAKSDLKGAKHQAEGVVEN VKEAAENAWEKTKDVAENLK DKVQSPGGLADKAANAWETV KDRAQDAASEVKHKAGDLKD KAQQVIHDATTQSGDNRKQD QQQRRDSQGSQSGQNSRSRN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	557
15N chemical shifts	187
1H chemical shifts	355

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HeLEA	1

Entities:

Entity 1, HeLEA 200 residues - Formula weight is not available

1	ALA	SER	SER	SER	GLY	SER	GLY	ARG	PRO	ALA
2	ASP	ASN	TRP	ALA	GLU	SER	GLN	LYS	GLU	LYS
3	ALA	LYS	ALA	GLY	LEU	LYS	ASP	ALA	GLN	ALA
4	GLU	VAL	GLY	LYS	VAL	ALA	ARG	GLU	VAL	LYS
5	ASP	LYS	ALA	ALA	GLY	GLY	ILE	GLU	GLN	ALA
6	LYS	ASP	ALA	VAL	LYS	GLN	GLY	ALA	ASN	ASP
7	LEU	LYS	ARG	SER	GLY	SER	ARG	THR	PHE	GLU
8	ASN	ALA	LYS	ASP	ASP	ILE	GLN	ALA	LYS	ALA
9	GLN	HIS	ALA	LYS	SER	ASP	LEU	LYS	GLY	ALA
10	LYS	HIS	GLN	ALA	GLU	GLY	VAL	VAL	GLU	ASN
11	VAL	LYS	GLU	ALA	ALA	GLU	ASN	ALA	TRP	GLU
12	LYS	THR	LYS	ASP	VAL	ALA	GLU	ASN	LEU	LYS
13	ASP	LYS	VAL	GLN	SER	PRO	GLY	GLY	LEU	ALA
14	ASP	LYS	ALA	ALA	ASN	ALA	TRP	GLU	THR	VAL
15	LYS	ASP	ARG	ALA	GLN	ASP	ALA	ALA	SER	GLU
16	VAL	LYS	HIS	LYS	ALA	GLY	ASP	LEU	LYS	ASP
17	LYS	ALA	GLN	GLN	VAL	ILE	HIS	ASP	ALA	THR
18	THR	GLN	SER	GLY	ASP	ASN	ARG	LYS	GLN	ASP
19	GLN	GLN	GLN	ARG	ARG	ASP	SER	GLN	GLY	SER
20	GLN	SER	GLY	GLN	ASN	SER	ARG	SER	ARG	ASN

Samples:

sample_1: HeLEA, [U-10% 13C; U-99% 15N], 50 uM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 278 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)NNH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.1 - collection, processing

NMRFAM-SPARKY v1.47 - chemical shift assignment, data analysis, peak picking

MddNMR - processing

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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

1	ALA	SER	SER	SER	GLY	SER	GLY	ARG	PRO	ALA
2	ASP	ASN	TRP	ALA	GLU	SER	GLN	LYS	GLU	LYS
3	ALA	LYS	ALA	GLY	LEU	LYS	ASP	ALA	GLN	ALA
4	GLU	VAL	GLY	LYS	VAL	ALA	ARG	GLU	VAL	LYS
5	ASP	LYS	ALA	ALA	GLY	GLY	ILE	GLU	GLN	ALA
6	LYS	ASP	ALA	VAL	LYS	GLN	GLY	ALA	ASN	ASP
7	LEU	LYS	ARG	SER	GLY	SER	ARG	THR	PHE	GLU
8	ASN	ALA	LYS	ASP	ASP	ILE	GLN	ALA	LYS	ALA
9	GLN	HIS	ALA	LYS	SER	ASP	LEU	LYS	GLY	ALA
10	LYS	HIS	GLN	ALA	GLU	GLY	VAL	VAL	GLU	ASN
11	VAL	LYS	GLU	ALA	ALA	GLU	ASN	ALA	TRP	GLU
12	LYS	THR	LYS	ASP	VAL	ALA	GLU	ASN	LEU	LYS
13	ASP	LYS	VAL	GLN	SER	PRO	GLY	GLY	LEU	ALA
14	ASP	LYS	ALA	ALA	ASN	ALA	TRP	GLU	THR	VAL
15	LYS	ASP	ARG	ALA	GLN	ASP	ALA	ALA	SER	GLU
16	VAL	LYS	HIS	LYS	ALA	GLY	ASP	LEU	LYS	ASP
17	LYS	ALA	GLN	GLN	VAL	ILE	HIS	ASP	ALA	THR
18	THR	GLN	SER	GLY	ASP	ASN	ARG	LYS	GLN	ASP
19	GLN	GLN	GLN	ARG	ARG	ASP	SER	GLN	GLY	SER
20	GLN	SER	GLY	GLN	ASN	SER	ARG	SER	ARG	ASN

1	ALA	SER	SER	SER	GLY	SER	GLY	ARG	PRO	ALA
2	ASP	ASN	TRP	ALA	GLU	SER	GLN	LYS	GLU	LYS
3	ALA	LYS	ALA	GLY	LEU	LYS	ASP	ALA	GLN	ALA
4	GLU	VAL	GLY	LYS	VAL	ALA	ARG	GLU	VAL	LYS
5	ASP	LYS	ALA	ALA	GLY	GLY	ILE	GLU	GLN	ALA
6	LYS	ASP	ALA	VAL	LYS	GLN	GLY	ALA	ASN	ASP
7	LEU	LYS	ARG	SER	GLY	SER	ARG	THR	PHE	GLU
8	ASN	ALA	LYS	ASP	ASP	ILE	GLN	ALA	LYS	ALA
9	GLN	HIS	ALA	LYS	SER	ASP	LEU	LYS	GLY	ALA
10	LYS	HIS	GLN	ALA	GLU	GLY	VAL	VAL	GLU	ASN
11	VAL	LYS	GLU	ALA	ALA	GLU	ASN	ALA	TRP	GLU
12	LYS	THR	LYS	ASP	VAL	ALA	GLU	ASN	LEU	LYS
13	ASP	LYS	VAL	GLN	SER	PRO	GLY	GLY	LEU	ALA
14	ASP	LYS	ALA	ALA	ASN	ALA	TRP	GLU	THR	VAL
15	LYS	ASP	ARG	ALA	GLN	ASP	ALA	ALA	SER	GLU
16	VAL	LYS	HIS	LYS	ALA	GLY	ASP	LEU	LYS	ASP
17	LYS	ALA	GLN	GLN	VAL	ILE	HIS	ASP	ALA	THR
18	THR	GLN	SER	GLY	ASP	ASN	ARG	LYS	GLN	ASP
19	GLN	GLN	GLN	ARG	ARG	ASP	SER	GLN	GLY	SER
20	GLN	SER	GLY	GLN	ASN	SER	ARG	SER	ARG	ASN

1	ALA	SER	SER	SER	GLY	SER	GLY	ARG	PRO	ALA
2	ASP	ASN	TRP	ALA	GLU	SER	GLN	LYS	GLU	LYS
3	ALA	LYS	ALA	GLY	LEU	LYS	ASP	ALA	GLN	ALA
4	GLU	VAL	GLY	LYS	VAL	ALA	ARG	GLU	VAL	LYS
5	ASP	LYS	ALA	ALA	GLY	GLY	ILE	GLU	GLN	ALA
6	LYS	ASP	ALA	VAL	LYS	GLN	GLY	ALA	ASN	ASP
7	LEU	LYS	ARG	SER	GLY	SER	ARG	THR	PHE	GLU
8	ASN	ALA	LYS	ASP	ASP	ILE	GLN	ALA	LYS	ALA
9	GLN	HIS	ALA	LYS	SER	ASP	LEU	LYS	GLY	ALA
10	LYS	HIS	GLN	ALA	GLU	GLY	VAL	VAL	GLU	ASN
11	VAL	LYS	GLU	ALA	ALA	GLU	ASN	ALA	TRP	GLU
12	LYS	THR	LYS	ASP	VAL	ALA	GLU	ASN	LEU	LYS
13	ASP	LYS	VAL	GLN	SER	PRO	GLY	GLY	LEU	ALA
14	ASP	LYS	ALA	ALA	ASN	ALA	TRP	GLU	THR	VAL
15	LYS	ASP	ARG	ALA	GLN	ASP	ALA	ALA	SER	GLU
16	VAL	LYS	HIS	LYS	ALA	GLY	ASP	LEU	LYS	ASP
17	LYS	ALA	GLN	GLN	VAL	ILE	HIS	ASP	ALA	THR
18	THR	GLN	SER	GLY	ASP	ASN	ARG	LYS	GLN	ASP
19	GLN	GLN	GLN	ARG	ARG	ASP	SER	GLN	GLY	SER
20	GLN	SER	GLY	GLN	ASN	SER	ARG	SER	ARG	ASN