Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53344

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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:

1H, 13C and 15N backbone resonance assignments of the exonuclease protein SNase.

Deposition date:

2025-09-11

Original release date:

2026-08-03

Authors:

Koduru, Tejaswi

Citation:

Citation: Koduru, Tejaswi; Barthe, Philippe; Hantman, Noam; De Guillen, Karine; McCallum, Scott; Morgan, Joel; Yee, Estella; Leonardi, Pierce; Foland, Jack; Roumestand, Christian; Royer, Catherine. "Adaptation of Folding and Function of a Nuclease from the Cold Deep Sea " J. Mol. Biol. 438, 169602-169602 (2026).
PubMed: 41443464

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HEQHLRKSEAQAKKEKLNIW SEDNADSGQR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	373
15N chemical shifts	120
1H chemical shifts	239

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SNASE	1

Entities:

Entity 1, SNASE 150 residues - Formula weight is not available

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

Samples:

sample_1: SNASE, [U-100% 13C; U-100% 15N], 0.5 M; TRIS 10 mM

sample_2: SNASE, [U-100% 15N], 0.5 M; TRIS 10 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	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 HNCACO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5.6 - collection

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	THR	SER	THR	LYS	LYS	LEU	HIS	LYS	GLU
2	PRO	ALA	THR	LEU	ILE	LYS	ALA	ILE	ASP	GLY
3	ASP	THR	VAL	LYS	LEU	MET	TYR	LYS	GLY	GLN
4	PRO	MET	THR	PHE	ARG	LEU	LEU	LEU	VAL	ASP
5	THR	PRO	GLU	THR	LYS	HIS	PRO	LYS	LYS	GLY
6	VAL	GLU	LYS	TYR	GLY	PRO	GLU	ALA	SER	ALA
7	PHE	THR	LYS	LYS	MET	VAL	GLU	ASN	ALA	LYS
8	LYS	ILE	GLU	VAL	GLU	PHE	ASP	LYS	GLY	GLN
9	ARG	THR	ASP	LYS	TYR	GLY	ARG	GLY	LEU	ALA
10	TYR	ILE	TYR	ALA	ASP	GLY	LYS	MET	VAL	ASN
11	GLU	ALA	LEU	VAL	ARG	GLN	GLY	LEU	ALA	LYS
12	VAL	ALA	TYR	VAL	TYR	LYS	PRO	ASN	ASN	THR
13	HIS	GLU	GLN	HIS	LEU	ARG	LYS	SER	GLU	ALA
14	GLN	ALA	LYS	LYS	GLU	LYS	LEU	ASN	ILE	TRP
15	SER	GLU	ASP	ASN	ALA	ASP	SER	GLY	GLN	ARG

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

BMRB Entry 53344