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 19693

Title: Solution structure of oxidized dimeric form of human defensin 5   PubMed: 25181039

Deposition date: 2013-12-19 Original release date: 2014-09-08

Authors: Ziarek, Joshua; Wommack, Andrew; Robson, Scott; Wagner, Gerhard; Nolan, Elizabeth

Citation: Ziarek, Joshua; Wommack, Andrew; Robson, Scott; Wagner, Gerhard; Nolan, Elizabeth. "Discovery and Characterization of a Disulfide-Locked C2-Symmetric Defensin Peptide"  J. Am. Chem. Soc. ., .-. (2014).

Assembly members:
entity, polymer, 32 residues, 3594.227 Da.

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

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

Entity Sequences (FASTA):
entity: ATCYCRTGRCATRESLSGVC EISGRLYRLCCR

Data sets:
Data typeCount
1H chemical shifts394
13C chemical shifts236
15N chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human_defensin_5 11
2human_defensin_5 21

Entities:

Entity 1, human_defensin_5 1 32 residues - 3594.227 Da.

1   ALATHRCYSTYRCYSARGTHRGLYARGCYS
2   ALATHRARGGLUSERLEUSERGLYVALCYS
3   GLUILESERGLYARGLEUTYRARGLEUCYS
4   CYSARG

Samples:

sample_1: HD5, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_2: HD5, [U-99% 13C; U-99% 15N], 0.3 mM; HD5 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

WhatIF, Vriend - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian Avance 500 MHz

Related Database Links:

BMRB 18705
PDB
EMBL CCD28566
GB AAA35754 AAH69690 AAI07080 AAT68886 ADQ32910
REF NP_066290
SP Q01523

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