BMRB Entry 25877

Name: Solution structure of cecropin P1 with LPS
Published: 2016-06-15

Click here to enlarge.

PDB ID: 2n92
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25877
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	100
15N chemical shifts	29
1H chemical shifts	217

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cp1	1

Entities:

Entity 1, cp1 31 residues - 3345.946 Da.

1

SER

TRP

LEU

SER

LYS

THR

ALA

LYS

LEU

2

GLU

ASN

SER

ALA

LYS

ARG

ILE

SER

GLU

3

GLY

ILE

ALA

ILE

ALA

ILE

GLN

GLY

PRO

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-CP1	isotropic	sample_conditions_1
2D 1H-13C HSQC	13C15N-CP1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	natural_CP1	isotropic	sample_conditions_1
2D 1H-1H COSY	natural_CP1	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C15N-CP1	isotropic	sample_conditions_1
3D C(CO)NH	13C15N-CP1	isotropic	sample_conditions_1
3D HNCA	13C15N-CP1	isotropic	sample_conditions_1
3D HNCACB	13C15N-CP1	isotropic	sample_conditions_1
3D HNCACB	13C15N-CP1	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-CP1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N-CP1	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C15N-CP1	isotropic	sample_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