BMRB Entry 16508

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16508

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Title:
NMR chemical shift assignments of lipid-bound synaptobrevin
Deposition date:
2009-09-22
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:
synaptobrevin, polymer, 116 residues, 12703.840 Da.

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):
synaptobrevin: MSATAATVPPAAPAGEGGPP APPPNLTSNRRLQQTQAQVD EVVDIMRVNVDKVLERDQKL SELDDRADALQAGASQFETS AAKLKRKYWWKNLKMMIILG VICAIILIIIIVYFST

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts106
1H chemical shifts713

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1synaptobrevin1

Entities:

Entity 1, synaptobrevin 116 residues - 12703.840 Da.

1   METSERALATHRALAALATHRVALPROPRO
2   ALAALAPROALAGLYGLUGLYGLYPROPRO
3   ALAPROPROPROASNLEUTHRSERASNARG
4   ARGLEUGLNGLNTHRGLNALAGLNVALASP
5   GLUVALVALASPILEMETARGVALASNVAL
6   ASPLYSVALLEUGLUARGASPGLNLYSLEU
7   SERGLULEUASPASPARGALAASPALALEU
8   GLNALAGLYALASERGLNPHEGLUTHRSER
9   ALAALALYSLEULYSARGLYSTYRTRPTRP
10   LYSASNLEULYSMETMETILEILELEUGLY
11   VALILECYSALAILEILELEUILEILEILE
12   ILEVALTYRPHESERTHR

Samples:

sample_1: synaptobrevin, [U-99% 13C; U-99% 15N], 1 mM; DPC 200 mM; MES 20 mM; NaCl 150 mM; DTT 5 mM; EDTA 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16514 4272
PDB
DBJ BAC41125 BAE90084 BAF82244 BAG73857
EMBL CAA12385 CAA53792 CAB43509
GB AAA42321 AAA60604 AAB03463 AAB62931 AAF15551
REF NP_001027992 NP_001034578 NP_001088233 NP_001272142 NP_033523
SP P63026 P63027 P63044 P63045 Q9N0Y0
TPG DAA18807
AlphaFold P63026 P63027 P63044 P63045 Q9N0Y0

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