BMRB Entry 34334

Name: NMR solution structure of the HVO_2922 protein from Haloferax volcanii
Published: 2019-06-07

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34334

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of the HVO_2922 protein from Haloferax volcanii

Deposition date: 2018-12-03 Original release date: 2019-06-07

Authors: Kubatova, N.; Jonker, H.; Saxena, K.; Richter, C.; Marchfelder, A.; Schwalbe, H.

Citation: Kubatova, N.; Jonker, H.; Saxena, K.; Richter, C.; Marchfelder, A.; Schwalbe, H.. "Solution structure and dynamics of HVO_2922 protein from Haloferax volcanii" to be published ., .-..

Assembly members:
entity_1, polymer, 60 residues, 6686.416 Da.

Natural source: Common Name: Halobacterium volcanii Taxonomy ID: 309800 Superkingdom: Archaea Kingdom: not available Genus/species: Halobacterium volcanii

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

Entity Sequences (FASTA):
entity_1: MNKAHFEVFVDAADKYRWRL VHDNGNILADSGEGYASKQK AKQGIESVKRNAPDADVIEA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	235
15N chemical shifts	63
1H chemical shifts	399

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HETNOE	sample_1	isotropic	sample_conditions_1
2D 1H-15N T1	sample_1	isotropic	sample_conditions_1
2D 1H-15N T2	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C TOCSY aromatic	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_2	isotropic	sample_conditions_1

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts

1	MET	ASN	LYS	ALA	HIS	PHE	GLU	VAL	PHE	VAL
2	ASP	ALA	ALA	ASP	LYS	TYR	ARG	TRP	ARG	LEU
3	VAL	HIS	ASP	ASN	GLY	ASN	ILE	LEU	ALA	ASP
4	SER	GLY	GLU	GLY	TYR	ALA	SER	LYS	GLN	LYS
5	ALA	LYS	GLN	GLY	ILE	GLU	SER	VAL	LYS	ARG
6	ASN	ALA	PRO	ASP	ALA	ASP	VAL	ILE	GLU	ALA

Biological Magnetic Resonance Data Bank

BMRB Entry 34334

Title: NMR solution structure of the HVO_2922 protein from Haloferax volcanii

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	ASN	LYS	ALA	HIS	PHE	GLU	VAL	PHE	VAL
2	ASP	ALA	ALA	ASP	LYS	TYR	ARG	TRP	ARG	LEU
3	VAL	HIS	ASP	ASN	GLY	ASN	ILE	LEU	ALA	ASP
4	SER	GLY	GLU	GLY	TYR	ALA	SER	LYS	GLN	LYS
5	ALA	LYS	GLN	GLY	ILE	GLU	SER	VAL	LYS	ARG
6	ASN	ALA	PRO	ASP	ALA	ASP	VAL	ILE	GLU	ALA

1	MET	ASN	LYS	ALA	HIS	PHE	GLU	VAL	PHE	VAL
2	ASP	ALA	ALA	ASP	LYS	TYR	ARG	TRP	ARG	LEU
3	VAL	HIS	ASP	ASN	GLY	ASN	ILE	LEU	ALA	ASP
4	SER	GLY	GLU	GLY	TYR	ALA	SER	LYS	GLN	LYS
5	ALA	LYS	GLN	GLY	ILE	GLU	SER	VAL	LYS	ARG
6	ASN	ALA	PRO	ASP	ALA	ASP	VAL	ILE	GLU	ALA

1	MET	ASN	LYS	ALA	HIS	PHE	GLU	VAL	PHE	VAL
2	ASP	ALA	ALA	ASP	LYS	TYR	ARG	TRP	ARG	LEU
3	VAL	HIS	ASP	ASN	GLY	ASN	ILE	LEU	ALA	ASP
4	SER	GLY	GLU	GLY	TYR	ALA	SER	LYS	GLN	LYS
5	ALA	LYS	GLN	GLY	ILE	GLU	SER	VAL	LYS	ARG
6	ASN	ALA	PRO	ASP	ALA	ASP	VAL	ILE	GLU	ALA