BMRB Entry 16512

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16512

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Title:
NMR chemical shift of synaptobrevin fragment 60-116
Deposition date:
2009-09-23
Original release date:
2009-10-05
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:
syb60-116, polymer, 57 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):
syb60-116: LSELDDRADALQAGASQFET SAAKLKRKYWWKNLKMMIIL GVICAIILIIIIVYFST

Data sets:
Data typeCount
13C chemical shifts151
15N chemical shifts55
1H chemical shifts200

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1syb60-1161

Entities:

Entity 1, syb60-116 57 residues - Formula weight is not available

1   LEUSERGLULEUASPASPARGALAASPALA
2   LEUGLNALAGLYALASERGLNPHEGLUTHR
3   SERALAALALYSLEULYSARGLYSTYRTRP
4   TRPLYSASNLEULYSMETMETILEILELEU
5   GLYVALILECYSALAILEILELEUILEILE
6   ILEILEVALTYRPHESERTHR

Samples:

sample_1: syb60-116, [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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16508 16514 4272
PDB
DBJ BAC34586 BAC34723 BAC41125 BAE38479 BAE40328
EMBL CAA12385 CAA53792 CAJ81663
GB AAA42321 AAA60604 AAB03463 AAB03490 AAB27554
PRF 1918358A
REF NP_001016972 NP_001027992 NP_001034578 NP_001039380 NP_001088233
SP P63024 P63025 P63026 P63027 P63044
TPG DAA18807 DAA21271
AlphaFold P63024 P63025 P63026 P63027 P63044

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