BMRB Entry 25775

Name: Structure of spider-venom peptide Hm1a
Published: 2016-08-25

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PDB ID: 2n6o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25775
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of spider-venom peptide Hm1a

Deposition date: 2015-08-27 Original release date: 2016-08-25

Authors: Undheim, Eivind; King, Glenn; Mobli, Mehdi

Citation: Undheim, Eivind; King, Glenn; Mobli, Mehdi; Petrou, Steven. "Structure of spider-venom peptide Hm1a" Not known ., .-..

Assembly members:
Hm1a, polymer, 35 residues, 4008.488 Da.

Natural source: Common Name: spiders Taxonomy ID: 268413 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Heteroscodra maculata

Experimental source: Production method: chemical synthesis Host organism: not applicable

Entity Sequences (FASTA):
Hm1a: ECRYLFGGCSSTSDCCKHLS CRSDWKYCAWDGTFS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	107
15N chemical shifts	38
1H chemical shifts	211

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spider-venom peptide Hm1a	1

Entities:

Entity 1, spider-venom peptide Hm1a 35 residues - 4008.488 Da.

1

GLU

CYS

ARG

TYR

LEU

PHE

GLY

CYS

SER

2

SER

THR

SER

ASP

CYS

LYS

HIS

LEU

SER

3

CYS

ARG

SER

ASP

TRP

LYS

TYR

CYS

ALA

TRP

4

ASP

GLY

THR

PHE

SER

Samples:

sample_1: Hm1a 1.0 mM; H2O 95%; D2O 5%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - dihedral angle estimation

NMR spectrometers:

Bruker Avance 900 MHz

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