BMRB Entry 25877

Title:
Solution structure of cecropin P1 with LPS
Deposition date:
2015-11-04
Original release date:
2016-06-15
Authors:
Baek, Mihwa; Kamiya, Masakatsu; Kushibiki, Takahiro; Nakazumi, Taichi; Tomisawa, Satoshi; Abe, Chiharu; Kumaki, Yasuhiro; Kushibiki, Takahiro; Kikukawa, Takashi; Demura, Makoto; Kawano, Keiichi; Aizawa, Tomoyasu
Citation:

Citation: Baek, Mihwa; Kamiya, Masakatsu; Kushibiki, Takahiro; Nakazumi, Taichi; Tomisawa, Satoshi; Abe, Chiharu; Kumaki, Yasuhiro; Kushibiki, Takahiro; Kikukawa, Takashi; Demura, Makoto; Kawano, Keiichi; Aizawa, Tomoyasu. "Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy"  J. Pep. Sci. 22, 214-221 (2016).
PubMed: 26939541

Assembly members:

Assembly members:
cp1, polymer, 31 residues, 3345.946 Da.

Natural source:

Natural source:   Common Name: pig   Taxonomy ID: 9823   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Sus scrofa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cp1: SWLSKTAKKLENSAKKRISE GIAIAIQGGPR

Data sets:
Data typeCount
13C chemical shifts100
15N chemical shifts29
1H chemical shifts217

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cp11

Entities:

Entity 1, cp1 31 residues - 3345.946 Da.

1   SERTRPLEUSERLYSTHRALALYSLYSLEU
2   GLUASNSERALALYSLYSARGILESERGLU
3   GLYILEALAILEALAILEGLNGLYGLYPRO
4   ARG

Samples:

natural_CP1: cp1 1 mM; H2O 90%; D2O 10%

13C15N-CP1: cp1, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

15N-CP1: cp1, [U-15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-CP1isotropicsample_conditions_1
2D 1H-13C HSQC13C15N-CP1isotropicsample_conditions_1
2D 1H-1H TOCSYnatural_CP1isotropicsample_conditions_1
2D 1H-1H COSYnatural_CP1isotropicsample_conditions_1
3D CBCA(CO)NH13C15N-CP1isotropicsample_conditions_1
3D C(CO)NH13C15N-CP1isotropicsample_conditions_1
3D HNCA13C15N-CP1isotropicsample_conditions_1
3D HNCACB13C15N-CP1isotropicsample_conditions_1
3D HNCACB13C15N-CP1isotropicsample_conditions_1
3D 1H-15N NOESY15N-CP1isotropicsample_conditions_1
3D 1H-15N TOCSY15N-CP1isotropicsample_conditions_1
3D 1H-13C NOESY13C15N-CP1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

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