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 30039

Title: NMR structure of antibacterial factor-2

Deposition date: 2016-03-23 Original release date: 2017-03-27

Authors: Masakatsu, K.; Umetsu, Y.; Rumi, F.; Kikukawa, T.; Ohki, S.; Mizuguchi, M.; Demura, M.; Aizawa, T.

Citation: Rumi, F.; Kamiya, M.; Umetsu, Y.; Kikukawa, T.; Demura, M.; Aizawa, T.. "NMR structure of ABF-2 (antibacterial factor-2) from C. elegans and the interaction with membrane mimetic systems"  . ., .-..

Assembly members:
Antibacterial factor-related peptide 2, polymer, 68 residues, 7140.460 Da.

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

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

Entity Sequences (FASTA):
Antibacterial factor-related peptide 2: MDIDFSTCARMDVPILKKAA QGLCITSCSMQNCGTGSCKK RSGRPTCVCYRCANGGGDIP LGALIKRG

Data sets:
Data typeCount
13C chemical shifts197
15N chemical shifts59
1H chemical shifts404

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 68 residues - 7140.460 Da.

1   METASPILEASPPHESERTHRCYSALAARG
2   METASPVALPROILELEULYSLYSALAALA
3   GLNGLYLEUCYSILETHRSERCYSSERMET
4   GLNASNCYSGLYTHRGLYSERCYSLYSLYS
5   ARGSERGLYARGPROTHRCYSVALCYSTYR
6   ARGCYSALAASNGLYGLYGLYASPILEPRO
7   LEUGLYALALEUILELYSARGGLY

Samples:

sample_1: Antibacterial factor-2, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: Antibacterial factor-2, [U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

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

SPARKY v3.115, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker DRX 800 MHz

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