BMRB Entry 20078

Name: Solution Structure of Antimicrobial Peptide Hedistin
Published: 2010-03-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20078

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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:

Solution Structure of Antimicrobial Peptide Hedistin

Deposition date:

2009-03-05

Original release date:

2010-03-01

Authors:

Xu, Guohua; Cui, Yanfang

Citation:

Citation: Xu, Guohua; Wu, Min; Wang, Lin; Zhang, Xu; Cao, Shufen; Liu, Maili; Cui, Yanfang. "Conformational and dynamics simulation study of antimicrobial peptide hedistin-heterogeneity of its helix-turn-helix motif." Biochim. Biophys. Acta, Biomembr. 1788, 2497-2508 (2009).
PubMed: 19819221

Assembly members:

Assembly members:
HEDISTIN, polymer, 22 residues, 2366 Da.

Natural source:

Natural source: Common Name: segmented worms Taxonomy ID: 6352 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Neanthes diversicolor

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HEDISTIN: LGAWLAGKVAGTVATYAWNR YV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	156
conformer coordinate sets	1

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HEDISTIN	1

Entities:

Entity 1, HEDISTIN 22 residues - 2366 Da.

1

LEU

GLY

ALA

TRP

LEU

ALA

GLY

LYS

VAL

ALA

2

GLY

THR

VAL

ALA

THR

TYR

ALA

TRP

ASN

ARG

3

TYR

VAL

Samples:

sample_1: HEDISTIN 2 mM; DPC, [U-100% 2H], 140 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.2; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH vv2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

SPARKY, Goddard - chemical shift assignment

ProcheckNMR, Laskowski and MacArthur - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Varian INOVA 600 MHz