BMRB Entry 31093

Name: Solution NMR structure of synthetic peptide AMPCry10Aa_5 rational designed from Cry10Aa bacterial protein
Published: 2024-06-20

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PDB ID: 8t3n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31093
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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 NMR structure of synthetic peptide AMPCry10Aa_5 rational designed from Cry10Aa bacterial protein

Deposition date:

2023-06-07

Original release date:

2024-06-20

Authors:

Barra, J.; Freitas, C.; Rios, T.; Maximiano, M.; Fernandes, F.; Amorim, G.; Porto, W.; Grossi-de-Sa, M.; Franco, O.; Liao, L.

Citation:

Citation: Barra, J.; Freitas, C.; Rios, T.; Maximiano, M.; Fernandes, F.; Amorim, G.; Porto, W.; Grossi-de-Sa, M.; Franco, O.; Liao, L.. "Solution NMR structure of synthetic peptide AMPCry10Aa_5 rational designed from Cry10Aa bacterial protein" .

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, 2255.763 Da.

Natural source:

Natural source: Common Name: Bacillus thuringiensis Taxonomy ID: 1428 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus thuringiensis

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IINVKTSLKTIIKNALDKIQ X

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	72
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 21 residues - 2255.763 Da.

1

ILE

ASN

VAL

LYS

THR

SER

LEU

LYS

THR

2

ILE

LYS

ASN

ALA

LEU

ASP

LYS

ILE

GLN

3

NH2

Samples:

sample_1: AMPCry10Aa_5 - Peptide 1.5 mM; SDS-d25, [U-99% 2H], 75 mM; DSS-d6, [U-99% 2H], 0.05%; H2O 90 % v/v; D2O, [U-99% 2H], 10 % v/v

sample_conditions_1: ionic strength: acid Not defined; pH: 4.7; 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-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CcpNmr Analysis, CCPN - data analysis

CcpNmr Analysis Assign, CCPN - chemical shift assignment

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE III 500 MHz