BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16866

Title: VAMP7(1-118):ISOLATED LONGIN DOMAIN   PubMed: 20378544

Deposition date: 2010-04-14 Original release date: 2010-04-29

Authors: Vivona, Sandro; Liu, Corey; Strop, Pavel; Rossi, Valeria; Filippini, Francesco; Brunger, Axel

Citation: Vivona, Sandro; Liu, Corey; Strop, Pavel; Rossi, Valeria; Filippini, Francesco; Brunger, Axel. "The longin SNARE VAMP7/TI-VAMP adopts a closed conformation."  J. Biol. Chem. 285, 17965-17973 (2010).

Assembly members:
VAMP7(1-118), polymer, 121 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET47b

Entity Sequences (FASTA):
VAMP7(1-118): GPGMAILFAVVARGTTILAK HAWCGGNFLEVTEQILAKIP SENNKLTYSHGNYLFHYICQ DRIVYLCITDDDFERSRAFN FLNEIKKRFQTTYGSRAQTA LPYAMNSEFSSVLAAQLKHH S

Data sets:
Data typeCount
15N chemical shifts108
1H chemical shifts108

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1VAMP7(1-118)1

Entities:

Entity 1, VAMP7(1-118) 121 residues - Formula weight is not available

1   GLYPROGLYMETALAILELEUPHEALAVAL
2   VALALAARGGLYTHRTHRILELEUALALYS
3   HISALATRPCYSGLYGLYASNPHELEUGLU
4   VALTHRGLUGLNILELEUALALYSILEPRO
5   SERGLUASNASNLYSLEUTHRTYRSERHIS
6   GLYASNTYRLEUPHEHISTYRILECYSGLN
7   ASPARGILEVALTYRLEUCYSILETHRASP
8   ASPASPPHEGLUARGSERARGALAPHEASN
9   PHELEUASNGLUILELYSLYSARGPHEGLN
10   THRTHRTYRGLYSERARGALAGLNTHRALA
11   LEUPROTYRALAMETASNSERGLUPHESER
12   SERVALLEUALAALAGLNLEULYSHISHIS
13   SER

Samples:

sample_1: VAMP7, [U-100% 15N], 18 uM; D2O 10%; potassium phosphate 20 mM; sodium chloride 100 mM; Dithiothreitol 1 mM; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16867
PDB
DBJ BAB22386 BAB27667 BAC40712 BAD96514 BAE38126
EMBL CAA63133 CAA65509 CAB94231 CAB96816 CAC16891
GB AAF88059 AAH03764 AAH56141 AAI18342 ABK42476
REF NP_001026292 NP_001069770 NP_001124684 NP_001159676 NP_001172112
SP P51809 P70280 Q17QI5 Q5RF94 Q5ZL74
TPG DAA13239
AlphaFold P70280 P51809 Q5RF94 Q5ZL74 Q17QI5

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