BMRB Entry 30110

Name: NMR structure of human antimicrobial peptide KAMP-19
Published: 2016-11-17

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PDB ID: 5ki0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30110
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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 structure of human antimicrobial peptide KAMP-19

Deposition date:

2016-06-16

Original release date:

2016-11-17

Authors:

Wang, G.

Citation:

Citation: Lee, Judy; Wang, Guangshun; Tam, Yu Tong; Tam, Connie. "Membrane-Active Epithelial Keratin 6A Fragments (KAMPs) Are Unique Human Antimicrobial Peptides with a Non-AlphaBeta Structure" Front Microbiol 7, 1799-1799 (2016).
PubMed: 27891122

Assembly members:

Assembly members:
Antimicrobial peptide KAMP-19, polymer, 19 residues, 1768.971 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo Sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Antimicrobial peptide KAMP-19: RAIGGGLSSVGGGSSTIKY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	44
15N chemical shifts	18
1H chemical shifts	109

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 19 residues - 1768.971 Da.

1

ARG

ALA

ILE

GLY

LEU

SER

VAL

2

GLY

SER

THR

ILE

LYS

TYR

Samples:

sample_1: KAMP-19 3.4 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

PIPP, Garrett - chemical shift assignment, peak picking

XPLOR-NIH v1, G. Marius Clore (NIH) - structure calculation

NMR spectrometers:

Varian INOVA 600 MHz

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