BMRB Entry 5034

Name: Solution structure of novispirin-2
Published: 2002-09-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5034

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of novispirin-2 PubMed: 11932493

Deposition date: 2001-03-14 Original release date: 2002-09-23

Authors: Sawai, M.; Waring, A.; Kearney, W.; McCray, P.; Forsyth, W.; Lehrer, R.; Tack, B.

Citation: Sawai, M.; Waring, A.; Kearney, W.; McCray, P.; Forsyth, W.; Lehrer, R.; Tack, B.. "Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides" Protein Eng. 15, 225-232 (2002).

Assembly members:
NOVISPIRIN-2, polymer, 18 residues, Formula weight is not available

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: .

Entity Sequences (FASTA):
NOVISPIRIN-2: KNLRRITRKIIHIIKKYG

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- J-values_set_1

Data type	Count
1H chemical shifts	148
coupling constants	7

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NOVISPIRIN-2	1

Entities:

Entity 1, NOVISPIRIN-2 18 residues - Formula weight is not available

1

LYS

ASN

LEU

ARG

ILE

THR

ARG

LYS

ILE

2

ILE

HIS

ILE

LYS

TYR

GLY

Samples:

sample_1: NOVISPIRIN-2 1.89 mM; sodium phosphate buffer 50 mM; TFE, [U-2H], 40%; H2O 50%; D2O 10%

sample_cond_1: ionic strength: 0.05 M; pH: 6.38; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	not available	sample_cond_1
2D DQF-COSY	sample_1	not available	sample_cond_1
2D TOCSY	sample_1	not available	sample_cond_1

Software:

DYANA v1.5 - refinement, structure solution

NMR spectrometers:

Varian INOVA 500 MHz

Biological Magnetic Resonance Data Bank