BMRB Entry 10035

Title:
Solution structure of Lectin C-type domain derived from a hypothetical protein from C. elegans
Deposition date:
2006-11-01
Original release date:
2008-08-13
Authors:
Kobayashi, N.; Koshiba, S.; Inoue, M.; Tochio, N.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Kobayashi, N.; Koshiba, S.; Inoue, M.; Tochio, N.; Kigawa, T.; Yokoyama, S.. "Solution structure of Lectin C-type domain derived from a hypothetical protein from C. elegans"  .

Assembly members:

Assembly members:
Lectin C-type homologue domain, polymer, 150 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: nematode   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P030929-39

Data sets:
Data typeCount
13C chemical shifts633
15N chemical shifts165
1H chemical shifts962

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hypothetical protein yk1067a121

Entities:

Entity 1, Hypothetical protein yk1067a12 150 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALLYSPHE
2   LEUTHRVALASNASPASPILELEUSERMET
3   PROGLNALAARGASNPHECYSALASERALA
4   GLYGLYTYRLEUALAASPASPLEUGLYASP
5   ASPLYSASNASNPHETYRSERSERILEALA
6   ALAASNTHRGLNPHETRPILEGLYLEUPHE
7   LYSASNSERASPGLYGLNPHETYRTRPASP
8   ARGGLYGLNGLYILEASNPROASPLEULEU
9   ASNGLNPROILETHRTYRTRPALAASNGLY
10   GLUPROSERASNASPPROTHRARGGLNCYS
11   VALTYRPHEASPGLYARGSERGLYASPLYS
12   SERLYSVALTRPTHRTHRASPTHRCYSALA
13   THRPROARGPROPHEILECYSGLNLYSHIS
14   ARGTYRASPSERASPHISLYSPROASNTHR
15   ILEGLYASPALASERGLYPROSERSERGLY

Samples:

sample_1: Lectin C-type domain, [U-13C; U-15N], 0.89 mM; Phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.901, Kobayashi, N. - data analysis

CYANA v2.0.17, Guentert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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