BMRB Entry 18184

Name: ShB peptide structure bound to negatively charged lipid-bilayer after Molecular Dynamics refinement
Published: 2012-08-06

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PDB ID: 2lny
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18184
MolProbity Validation Chart

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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:

ShB peptide structure bound to negatively charged lipid-bilayer after Molecular Dynamics refinement

Deposition date:

2012-01-06

Original release date:

2012-08-06

Authors:

Weingarth, Markus

Citation:

Citation: Weingarth, Markus; Ader, Christian; Melquiond, Adrien; Nand, Deepak; Pongs, Olaf; Becker, Stefan; Bonvin, Alexandre M J J; Baldus, Marc. "Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations." Biophys. J. 103, 29-37 (2012).
PubMed: 22828329

Assembly members:

Assembly members:
entity, polymer, 20 residues, 2233.591 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: obtained from a collaborator Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAAVAGLYGLGEDRQHRKKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	43
15N chemical shifts	11

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ShB peptide	1

Entities:

Entity 1, ShB peptide 20 residues - 2233.591 Da.

1		MET	ALA	ALA	VAL	ALA	GLY	LEU	TYR	GLY	LEU
2		GLY	GLU	ASP	ARG	GLN	HIS	ARG	LYS	LYS	GLN

Samples:

sample_1: DOPC 7 mM; Cardiolipin 3 mM; H2O 100%; sodium citrate 100 mM; Calbiochem 4 mM; Entity 0.055 mg/uL

sample_conditions_1: ionic strength: 0.3 M; pH: 4.0; temperature: 280 K

Experiments:

Name	Sample	Sample state	Sample conditions
13C-13C PARISxy	sample_1	solid	sample_conditions_1
13c-13C PDSD	sample_1	solid	sample_conditions_1
SPECIFIC-NCA	sample_1	solid	sample_conditions_1
SPECIFIC-NCO	sample_1	solid	sample_conditions_1
CHHC	sample_1	solid	sample_conditions_1
NHHC	sample_1	solid	sample_conditions_1
HHC	sample_1	solid	sample_conditions_1

Software:

GROMOS v53a6, van Gunsteren and Berendsen - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 700 MHz

PDB	2LNY
EMBL	CAA29917 CAA30143 CAA30146
GB	AAA28417 AAF48785 AAF48786 AAS65396 AGB95507
PRF	1402312A
REF	NP_001259665 NP_001303569 NP_523393 NP_728123 NP_996497
SP	P08510
AlphaFold	P08510

1		MET	ALA	ALA	VAL	ALA	GLY	LEU	TYR	GLY	LEU
2		GLY	GLU	ASP	ARG	GLN	HIS	ARG	LYS	LYS	GLN

1		MET	ALA	ALA	VAL	ALA	GLY	LEU	TYR	GLY	LEU
2		GLY	GLU	ASP	ARG	GLN	HIS	ARG	LYS	LYS	GLN