BMRB Entry 19124

Name: NMR spatial structure of the antimicrobial peptide Tk-Amp-X2
Published: 2014-03-31

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PDB ID: 2m6a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19124
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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:

NMR spatial structure of the antimicrobial peptide Tk-Amp-X2

Deposition date:

2013-03-28

Original release date:

2014-03-31

Authors:

Usmanova, Dinara; Mineev, Konstantin; Arseniev, Alexander

Citation:

Citation: Usmanova, Dinara; Mineev, Konstantin; Arseniev, Alexander. "NMR spatial structure of the antimicrobial peptide Tk-Amp-X2" To be Published ., .-..

Assembly members:

Assembly members:
antimicrobial_peptide, polymer, 28 residues, 3533.107 Da.

Natural source:

Natural source: Common Name: Triticum kiharae Taxonomy ID: 376535 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum kiharae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
antimicrobial_peptide: ADDRCERMCQRYHDRREKKQ CMKGCRYG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	76
15N chemical shifts	31
1H chemical shifts	177

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	antimicrobial peptide Tk-Amp-X2	1

Entities:

Entity 1, antimicrobial peptide Tk-Amp-X2 28 residues - 3533.107 Da.

1

ALA

ASP

ARG

CYS

GLU

ARG

MET

CYS

GLN

2

ARG

TYR

HIS

ASP

ARG

GLU

LYS

GLN

3

CYS

MET

LYS

GLY

CYS

ARG

TYR

GLY

Samples:

sample_1: antimicrobial peptide, [U-13C; U-15N], mM

sample_2: antimicrobial peptide, [U-13C; U-15N], mM

sample_conditions_1: pH: 5.6; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1

Software:

CYANA v3.0 - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

PDB	2M6A
EMBL	CCP19158 CCP19160 CCP19162 CCP19169 CCP19171
GB	EMS59180