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 6226

Title: 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal domain of EW29   PubMed: 15756471

Authors: Hemmi, Hikaru

Citation: Hemmi, Hikaru; Kuno, Atsushi; Ito, Shigeyasu; Suzuki, Ryuichiro; Kaneko, Satoshi; Hasegawa, Tsunemi; Hirabayashi, Jun; Kasai, Ken-ichi. "Letter to the Editor: 1H, 13C and 15N chemical shift assignment of the C-terminal 15 kDa domain of novel galactose-binding protein from the earth worm Lumbricus terrestris"  J. Biomol. NMR 30, 377-378 (2004).

Assembly members:
C-terminal domain of EW29, polymer, 132 residues, Formula weight is not available

Natural source:   Common Name: common earthworm   Taxonomy ID: 6398   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lumbricus terrestris

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
C-terminal domain of EW29: MKPKFFYIKSELNGKVLDIE GQNPAPGSKIITWDQKKGPT AVNQLWYTDQQGVIRSKLND FAIDASHEQIETQPFDPNNP KRAWIVSGNTIAQLSDRDIV LDIIKSDKEAGAHICAWKQH GGPNQKFIIESE

Data sets:
Data typeCount
13C chemical shifts591
15N chemical shifts133
1H chemical shifts911

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EW29 monomer1

Entities:

Entity 1, EW29 monomer 132 residues - Formula weight is not available

1   METLYSPROLYSPHEPHETYRILELYSSER
2   GLULEUASNGLYLYSVALLEUASPILEGLU
3   GLYGLNASNPROALAPROGLYSERLYSILE
4   ILETHRTRPASPGLNLYSLYSGLYPROTHR
5   ALAVALASNGLNLEUTRPTYRTHRASPGLN
6   GLNGLYVALILEARGSERLYSLEUASNASP
7   PHEALAILEASPALASERHISGLUGLNILE
8   GLUTHRGLNPROPHEASPPROASNASNPRO
9   LYSARGALATRPILEVALSERGLYASNTHR
10   ILEALAGLNLEUSERASPARGASPILEVAL
11   LEUASPILEILELYSSERASPLYSGLUALA
12   GLYALAHISILECYSALATRPLYSGLNHIS
13   GLYGLYPROASNGLNLYSPHEILEILEGLU
14   SERGLU

Samples:

sample_1: C-terminal domain of EW29, [U-15N; U-13C], 0.9 mM

Ex-cond_1: pH: 6.1; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_1not availableEx-cond_1

Software:

xwinnmr v3.5 - acquisiton

FELIX v2000 - processing

SPARKY v3.100 - Peak assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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