BMRB Entry 30039

Name: NMR structure of antibacterial factor-2
Published: 2017-03-27

Click here to enlarge.

PDB ID: 5ix5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30039
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:

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:

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:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	197
15N chemical shifts	59
1H chemical shifts	404

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 68 residues - 7140.460 Da.

1

MET

ASP

ILE

ASP

PHE

SER

THR

CYS

ALA

ARG

2

MET

ASP

VAL

PRO

ILE

LEU

LYS

ALA

3

GLN

GLY

LEU

CYS

ILE

THR

SER

CYS

SER

MET

4

GLN

ASN

CYS

GLY

THR

GLY

SER

CYS

LYS

5

ARG

SER

GLY

ARG

PRO

THR

CYS

VAL

CYS

TYR

6

ARG

CYS

ALA

ASN

GLY

ASP

ILE

PRO

7

LEU

GLY

ALA

LEU

ILE

LYS

ARG

GLY

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks