BMRB Entry 16514

Name: NMR chemical shifts of soluble synaptobrevin (1-96) in buffer and in DPC micelle
Published: 2009-11-20

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16514

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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:

NMR chemical shifts of soluble synaptobrevin (1-96) in buffer and in DPC micelle

Deposition date:

2009-09-23

Original release date:

2009-11-20

Authors:

Ellena, Jeffrey; Liang, Binyong; Wiktor, Maciej; Stein, Alexander; Cafiso, David; Jahn, Reinhard; Tamm, Lukas

Citation:

Citation: Ellena, Jeffrey; Liang, Binyong; Wiktor, Maciej; Stein, Alexander; Cafiso, David; Jahn, Reinhard; Tamm, Lukas. "Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation." Proc. Natl. Acad. Sci. U.S.A. 106, 20306-20311 (2009).
PubMed: 19918058

Assembly members:

Assembly members:
syb96, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Norway 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
syb96: MSATAATVPPAAPAGEGGPP APPPNLTSNRRLQQTQAQVD EVVDIMRVNVDKVLERDQKL SELDDRADALQAGASQFETS AAKLKRKYWWKNLKMM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	543
15N chemical shifts	174
1H chemical shifts	174

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	syb96	1

Entities:

Entity 1, syb96 96 residues - Formula weight is not available

1

MET

SER

ALA

THR

ALA

THR

VAL

PRO

2

ALA

PRO

ALA

GLY

GLU

GLY

PRO

3

ALA

PRO

ASN

LEU

THR

SER

ASN

ARG

4

ARG

LEU

GLN

THR

GLN

ALA

GLN

VAL

ASP

5

GLU

VAL

ASP

ILE

MET

ARG

VAL

ASN

VAL

6

ASP

LYS

VAL

LEU

GLU

ARG

ASP

GLN

LYS

LEU

7

SER

GLU

LEU

ASP

ARG

ALA

ASP

ALA

LEU

8

GLN

ALA

GLY

ALA

SER

GLN

PHE

GLU

THR

SER

9

ALA

LYS

LEU

LYS

ARG

LYS

TYR

TRP

10

LYS

ASN

LEU

LYS

MET

Samples:

sample_1: syb96, [U-99% 13C; U-99% 15N], 0.2 mM; potassium phosphate 60 mM; NaCl 300 mM; DTT 5 mM; EDTA 1 mM; H2O 95%; D2O 5%

sample_2: syb96, [U-99% 13C; U-99% 15N], 0.5 mM; DPC 300 mM; potassium phosphate 60 mM; NaCl 300 mM; DTT 5 mM; EDTA 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 300 mM; pH: 6.1; pressure: 1 atm; temperature: 291 K

sample_conditions_2: ionic strength: 300 mM; pH: 6.1; pressure: 1 atm; temperature: 318 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2

Software:

SPARKY, Goddard - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	16508 4272
PDB	1KIL 1N7S 1SFC 2KOG 2N1T 3HD7 3IPD 3J96 3J97 3J98 3J99 5CCG 5CCH 5CCI
DBJ	BAC41125 BAE90084 BAF82244 BAG73857
EMBL	CAA12385 CAA53792 CAB43509 CDQ77958
GB	AAA42321 AAA60604 AAB03463 AAB62931 AAB88138
REF	NP_001027992 NP_001034578 NP_001080944 NP_001088233 NP_001272142
SP	P47193 P63026 P63027 P63044 P63045
TPG	DAA18807
AlphaFold	P47193 P63026 P63027 P63044 P63045