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 16254

Title: NMR Structure of human alpha defensin HNP-1   PubMed: 19963419

Authors: Zhang, Yuan; Li, Shenhui; Doherty, Timothy; Lubkowski, Jacek; Lu, Wuyuan; Li, Jing; Barinka, Cyril; Hong, Mei

Citation: Li, Shenhui; Zhang, Yuan; Hong, Mei. "3D (13)C-(13)C-(13)C correlation NMR for de novo distance determination of solid proteins and application to a human alpha-defensin."  J. Magn. Reson. 202, 203-210 (2010).

Assembly members:
HNP-1, polymer, 30 residues, 3452.115 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):
HNP-1: ACYCRIPACIAGERRYGTCI YQGRLWAFCC

Data sets:
Data typeCount
13C chemical shifts115
15N chemical shifts30

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HNP-11

Entities:

Entity 1, HNP-1 30 residues - 3452.115 Da.

1   ALACYSTYRCYSARGILEPROALACYSILE
2   ALAGLYGLUARGARGTYRGLYTHRCYSILE
3   TYRGLNGLYARGLEUTRPALAPHECYSCYS

Samples:

sample_1: HNP-1; PEG400 60% w/v; Cacodylate 30 mM; Lithium Sulfate 60 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 268 K

sample_conditions_2: pH: 6.5; pressure: 1 atm; temperature: 253 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARR 40 ms, 100 ms & 200 mssample_1solidsample_conditions_1
2D 15N-15N PDSD 3 ssample_1solidsample_conditions_1
2D CM5RR 0.8 ms & 1.5 mssample_1solidsample_conditions_2
2D CHHC 200 us & 300 ussample_1solidsample_conditions_2
3D 15N-13C-13C NCACXsample_1solidsample_conditions_1
3D 15N-13C-13C NCOCXsample_1solidsample_conditions_1
2D 15N-13C NCXsample_1solidsample_conditions_2

Software:

X-PLOR NIH v2.21, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY v3.113, Goddard - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - processing

Chimera v1.3, Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., and Ferrin, T.E - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAJ20578
EMBL CAA31952 CAA36280
GB AAA35753 AAA36382 AAA52302 AAA52303 AAA52304
PIR B40499
PRF 1811319A 1912193A 2115200A
REF NP_001035965 NP_001289194 NP_004075 NP_005208 XP_004046640
SP P59665 P59666