Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53616

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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 chemical shift assignments of SND1 SN3

Deposition date:

2026-03-11

Original release date:

2026-08-18

Authors:

Ajith, Shradha; Cubeddu, Liza; Gamsjaeger, Roland

Citation:

Citation: Ajith, Shradha; Cubeddu, Liza; Gamsjaeger, Roland. "Backbone resonance assignment of the third domain of the human staphylococcal nuclease domain-containing protein 1 (SND1) " Biomol. NMR Assignments 20, 18-18 (2026).
PubMed: 42142220

Assembly members:

Assembly members:
entity_1, polymer, 161 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: pGEX-6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PLGSDKQFVAKVMQVLNADA IVVKLNSGDYKTIHLSSIRP PRLEGENTQDKNKKLRPLYD IPYMFEAREFLRKKLIGKKV NVTVDYIRPASPATETVPAF SERTCATVTIGGINIAEALV SKGLATVIRYRQDDDQRSSH YDELLAAEARAIKNGKGLHS K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	411
15N chemical shifts	134
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	sn3	1

Entities:

Entity 1, sn3 161 residues - Formula weight is not available

1

PRO

LEU

GLY

SER

ASP

LYS

GLN

PHE

VAL

ALA

2

LYS

VAL

MET

GLN

VAL

LEU

ASN

ALA

ASP

ALA

3

ILE

VAL

LYS

LEU

ASN

SER

GLY

ASP

TYR

4

LYS

THR

ILE

HIS

LEU

SER

ILE

ARG

PRO

5

PRO

ARG

LEU

GLU

GLY

GLU

ASN

THR

GLN

ASP

6

LYS

ASN

LYS

LEU

ARG

PRO

LEU

TYR

ASP

7

ILE

PRO

TYR

MET

PHE

GLU

ALA

ARG

GLU

PHE

8

LEU

ARG

LYS

LEU

ILE

GLY

LYS

VAL

9

ASN

VAL

THR

VAL

ASP

TYR

ILE

ARG

PRO

ALA

10

SER

PRO

ALA

THR

GLU

THR

VAL

PRO

ALA

PHE

11

SER

GLU

ARG

THR

CYS

ALA

THR

VAL

THR

ILE

12

GLY

ILE

ASN

ILE

ALA

GLU

ALA

LEU

VAL

13

SER

LYS

GLY

LEU

ALA

THR

VAL

ILE

ARG

TYR

14

ARG

GLN

ASP

GLN

ARG

SER

HIS

15

TYR

ASP

GLU

LEU

ALA

GLU

ALA

ARG

16

ALA

ILE

LYS

ASN

GLY

LYS

GLY

LEU

HIS

SER

17

LYS

Samples:

sample_1: sn3, [U-13C; U-15N], 500 uM; sn3, [U-100% 15N], 500 uM; sodium phosphate 25 mM; NaCl 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRFAM-SPARKY - 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

BMRB Entry 53616