BMRB Entry 51598

Name: SNAP25a (Rattus norvegicus)
Published: 2022-08-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51598

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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:

SNAP25a (Rattus norvegicus)

Deposition date:

2022-08-24

Original release date:

2022-08-31

Authors:

Stief, Tobias; Lakomek, Nils-Alexander

Citation:

Citation: Stief, Tobias; Gremer, Lothar; Pribicevic, Sonja; Espinueva, Delane; Vormann, Katharina; Biehl, Ralf; Jahn, Reinhard; Perez-Lara, Angel; Lakomek, Nils-Alexander. "Intrinsic Disorder of the Neuronal SNARE Protein SNAP25a in its Pre-fusion Conformation" J. Mol. Biol. 435, 168069-168069 (2023).
PubMed: 37003471

Assembly members:

Assembly members:
entity_1, polymer, 206 residues, 23272 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAEDADMRNELEEMQRRADQ LADESLESTRRMLQLVEESK DAGIRTLVMLDEQGEQLDRV EEGMNHINQDMKEAEKNLKD LGKSSGLFISPSNKLKSSDA YKKAWGNNQDGVVASQPARV VDEREQMAISGGFIRRVTND ARENEMDENLEQVSGIIGNL RHMALDMGNEIDTQNRQIDR IMEKADSNKTRIDEANQRAT KMLGSG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	595
15N chemical shifts	204
1H chemical shifts	204

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SNAP25a	1

Entities:

Entity 1, SNAP25a 206 residues - 23272 Da.

1

MET

ALA

GLU

ASP

ALA

ASP

MET

ARG

ASN

GLU

2

LEU

GLU

MET

GLN

ARG

ALA

ASP

GLN

3

LEU

ALA

ASP

GLU

SER

LEU

GLU

SER

THR

ARG

4

ARG

MET

LEU

GLN

LEU

VAL

GLU

SER

LYS

5

ASP

ALA

GLY

ILE

ARG

THR

LEU

VAL

MET

LEU

6

ASP

GLU

GLN

GLY

GLU

GLN

LEU

ASP

ARG

VAL

7

GLU

GLY

MET

ASN

HIS

ILE

ASN

GLN

ASP

8

MET

LYS

GLU

ALA

GLU

LYS

ASN

LEU

LYS

ASP

9

LEU

GLY

LYS

SER

GLY

LEU

PHE

ILE

SER

10

PRO

SER

ASN

LYS

LEU

LYS

SER

ASP

ALA

11

TYR

LYS

ALA

TRP

GLY

ASN

GLN

ASP

12

GLY

VAL

ALA

SER

GLN

PRO

ALA

ARG

VAL

13

VAL

ASP

GLU

ARG

GLU

GLN

MET

ALA

ILE

SER

14

GLY

PHE

ILE

ARG

VAL

THR

ASN

ASP

15

ALA

ARG

GLU

ASN

GLU

MET

ASP

GLU

ASN

LEU

16

GLU

GLN

VAL

SER

GLY

ILE

GLY

ASN

LEU

17

ARG

HIS

MET

ALA

LEU

ASP

MET

GLY

ASN

GLU

18

ILE

ASP

THR

GLN

ASN

ARG

GLN

ILE

ASP

ARG

19

ILE

MET

GLU

LYS

ALA

ASP

SER

ASN

LYS

THR

20

ARG

ILE

ASP

GLU

ALA

ASN

GLN

ARG

ALA

THR

21

LYS

MET

LEU

GLY

SER

GLY

Samples:

sample_1: SNAP25a, [U-99% 13C; U-99% 15N], 150 uM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 288.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 - processing

CcpNMR v3 - peak picking

NMR spectrometers:

Bruker AVANCE III 750 MHz

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