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 4945

Title: VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE   PubMed: 11224573

Authors: Dulubova, I.; Yamaguchi, T.; Wang, Y.; Sudhof, T.; Rizo, J.

Citation: Dulubova, I.; Yamaguchi, T.; Wang, Y.; Sudhof, T.; Rizo, J.. "Vam3p Structure Reveals Conserved and Divergent Properties of Syntaxins"  Nat. Struct. Biol. 8, 258-264 (2001).

Assembly members:
single chain biopolimer, polymer, 123 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
single chain biopolimer: GSSQQEPQFSTNQKTKELSN LIETFAEQSRVLEKECTKIG SKRDSKELRYKIETELIPNC TSVRDKIESNILIHQNGKLS ADFKNLKTKYQSLQQSYNQR KSLFPLKTPISPGTSKERKD IHP

Data sets:
Data typeCount
1H chemical shifts869
13C chemical shifts502
15N chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Vam3p N-terminal domain1

Entities:

Entity 1, Vam3p N-terminal domain 123 residues - Formula weight is not available

1   GLYSERSERGLNGLNGLUPROGLNPHESER
2   THRASNGLNLYSTHRLYSGLULEUSERASN
3   LEUILEGLUTHRPHEALAGLUGLNSERARG
4   VALLEUGLULYSGLUCYSTHRLYSILEGLY
5   SERLYSARGASPSERLYSGLULEUARGTYR
6   LYSILEGLUTHRGLULEUILEPROASNCYS
7   THRSERVALARGASPLYSILEGLUSERASN
8   ILELEUILEHISGLNASNGLYLYSLEUSER
9   ALAASPPHELYSASNLEULYSTHRLYSTYR
10   GLNSERLEUGLNGLNSERTYRASNGLNARG
11   LYSSERLEUPHEPROLEULYSTHRPROILE
12   SERPROGLYTHRSERLYSGLUARGLYSASP
13   ILEHISPRO

Samples:

sample_1: single chain biopolimer, [U-99% 15N], 0.9 mM; phosphate buffer 20 mM

sample_2: single chain biopolimer, [U-99% 13C; U-99% 15N], 0.85 mM; phosphate buffer 20 mM

sample_cond_1: pH: 6.0; temperature: 303 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available

Software:

VNMR v6.1B - collection

NMRPipe v1.7 - processing

NMRView v4.1 - data analysis

CNS v0.9 - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ GAA26424
EMBL CAA64026 CAA99304 CAY86392
GB AAC49737 AHY77403 EDN63969 EDV10703 EEU07936
REF NP_014749
SP Q12241
TPG DAA10881