BMRB Entry 30033

Name: Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
Published: 2016-06-24

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PDB ID: 5ipo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30033
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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 Hge36: Scorpine-like Peptide from Hadrurus Gertschi

Deposition date:

2016-03-09

Original release date:

2016-06-24

Authors:

Flores-Solis, D.; Rodriguez De La Vega, R.; del Rio-Portilla, F.

Citation:

Citation: Flores-Solis, D.; Toledano-Magana, Y.; Rodriguez-Lima, O.; Rodriguez De La Vega, R.; Cano-Sanchez, P.; del Rio-Portilla, F.. "Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi" FEBS Lett. 590, 2286-2296 (2016).
PubMed: 27314815

Assembly members:

Assembly members:
entity_1, polymer, 48 residues, 5310.272 Da.

Natural source:

Natural source: Common Name: Scorpion Taxonomy ID: 380989 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hadrurus gertschi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VHKMAKNQFGCFANVDVKGD CKRHCKAEDKEGICHGTKCK CGVPISYL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	139
15N chemical shifts	50
1H chemical shifts	331

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 48 residues - 5310.272 Da.

1

VAL

HIS

LYS

MET

ALA

LYS

ASN

GLN

PHE

GLY

2

CYS

PHE

ALA

ASN

VAL

ASP

VAL

LYS

GLY

ASP

3

CYS

LYS

ARG

HIS

CYS

LYS

ALA

GLU

ASP

LYS

4

GLU

GLY

ILE

CYS

HIS

GLY

THR

LYS

CYS

LYS

5

CYS

GLY

VAL

PRO

ILE

SER

TYR

LEU

Samples:

sample_1: Hge36 3.0 ± 0.1 mM

sample_2: Hge36, [U-13C; U-15N], 3.0 ± 0.1 mM

sample_conditions_1: ionic strength: 3 mM; pH: 3.0; pressure: 585 mmHg; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

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

NMR spectrometers:

Varian INOVA 500 MHz
Bruker AvanceIII 700 MHz

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