BMRB Entry 11049

Name: Structure of the N-terminal BARpeptide in DPC micelles
Published: 2009-03-03

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PDB ID: 2rnd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11049
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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:

Structure of the N-terminal BARpeptide in DPC micelles

Deposition date:

2008-06-09

Original release date:

2009-03-03

Authors:

Loew, Christian; Weininger, Ulrich; Balbach, Jochen

Citation:

Citation: Loew, Christian; Weininger, Ulrich; Lee, Hwankyu; Schweimer, Kristian; Neundorf, Ines; Beck-Sickinger, Annette; Pastor, Richard; Balbach, Jochen. "Structure and Dynamics of Helix-0 of the N-BAR Domain in Lipid Micelles and Bilayers" Biophys. J. 95, 4315-4323 (2008).
PubMed: 18658220

Assembly members:

Assembly members:
BARpeptide (1-33), polymer, 34 residues, 3714.452 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: recombinant technology Host organism: Escherichia coli Vector: petSUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BARpeptide (1-33): MAEMGSKGVTAGKIASNVQK KLTRAQEKVLQKLY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	38
1H chemical shifts	238

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BARpeptide (1-33)	1

Entities:

Entity 1, BARpeptide (1-33) 34 residues - 3714.452 Da.

1

MET

ALA

GLU

MET

GLY

SER

LYS

GLY

VAL

THR

2

ALA

GLY

LYS

ILE

ALA

SER

ASN

VAL

GLN

LYS

3

LYS

LEU

THR

ARG

ALA

GLN

GLU

LYS

VAL

LEU

4

GLN

LYS

LEU

TYR

Samples:

sample_1: BARpeptide (1-33), [U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 298 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-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v2.1, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

BMRB	11050
PDB	2FIC 2RMY 2RND
DBJ	BAE87346 BAH12028 BAJ17746
EMBL	CAA73807 CAD28496 CAG31301 CAL37828
GB	AAB61363 AAB63263 AAC17461 AAC23440 AAC23441
REF	NP_001006524 NP_001040006 NP_001076803 NP_001090909 NP_004296
SP	O00499 O08539 O08839
TPG	DAA32871
AlphaFold	O00499 O08539 O08839