BMRB Entry 18635

Name: Backbone resonance assignments of human beta-defensin 1
Published: 2019-08-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18635

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

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Title:

Backbone resonance assignments of human beta-defensin 1

Deposition date:

2012-08-02

Original release date:

2019-08-30

Authors:

de Paula, Viviane; Gomes, Natalia; Lima, Luize; Miyamoto, Catarina; Monteiro, Robson; Almeida, Fabio; Valente, Ana Paula

Citation:

Citation: De Paula, Viviane; Pomin, Vitor; Valente, Ana Paula. "Unique properties of human beta-defensin 6 (hBD6) and glycosaminoglycan complex: sandwich-like dimerization and competition with the chemokine receptor 2 (CCR2) binding site" J. Biol. Chem. 289, 22969-22979 (2014).
PubMed: 24970887

Assembly members:

Assembly members:
HbD1, polymer, 36 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HbD1: DHYNCVSSGGQCLYSACPIF TKIQGTCYRGKAKCCK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	61
15N chemical shifts	33
1H chemical shifts	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HbD1	1

Entities:

Entity 1, HbD1 36 residues - Formula weight is not available

1

ASP

HIS

TYR

ASN

CYS

VAL

SER

GLY

2

GLN

CYS

LEU

TYR

SER

ALA

CYS

PRO

ILE

PHE

3

THR

LYS

ILE

GLN

GLY

THR

CYS

TYR

ARG

GLY

4

LYS

ALA

LYS

CYS

LYS

Samples:

sample_1: HbD1 0.5 mM; sodium phosphate0.2 – 0.6 mM; H2O 90%; D2O 10%; phosphate buffer 30 mM; sodium chloride 50 mM; potassium chloride 0.9 mM

sample_conditions_1: ionic strength: 20 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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