BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 11054

Title: Solution structure of a novel insect chemokine isolated from integument   PubMed: 19375321

Deposition date: 2008-07-27 Original release date: 2009-10-14

Authors: Kamiya, Masakatsu; Nakatogawa, Shin-ichi; Oda, Yasunori; Kamijima, Tatsuro; Aizawa, Tomoyasu; Demura, Makoto; Hayakawa, Yoichi; Kawano, Keiichi

Citation: Nakatogawa, Shin-ichi; Oda, Yasunori; Kamiya, Masakatsu; Kamijima, Tatsuro; Aizawa, Tomoyasu; Clark, Kevin; Demura, Makoto; Kawano, Keiichi; Strand, Michael; Hayakawa, Yoichi. "A novel peptide mediates aggregation and migration of hemocytes from an insect"  Curr. Biol. 19, 779-785 (2009).

Assembly members:
insect chemokine, polymer, 32 residues, 3545.022 Da.

Natural source:   Common Name: northern armyworm   Taxonomy ID: 271217   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mythimna separata

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32b+

Entity Sequences (FASTA):
insect chemokine: SVQILRCPDGMQMLRSGQCV ATTEPPFDPDSY

Data sets:
Data typeCount
15N chemical shifts32
1H chemical shifts158

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1insect chemokine1

Entities:

Entity 1, insect chemokine 32 residues - 3545.022 Da.

1   SERVALGLNILELEUARGCYSPROASPGLY
2   METGLNMETLEUARGSERGLYGLNCYSVAL
3   ALATHRTHRGLUPROPROPHEASPPROASP
4   SERTYR

Samples:

sample_1: insect chemokine1 – 3 mM; DSS 10 uM

sample_2: entity, [U-15N], 1 – 3 mM; DSS 10 uM

sample_conditions_1: ionic strength: 0 M; pH: 5.1; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • JEOL ECA 600 MHz

Related Database Links:

PDB
DBJ BAH03491

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