BMRB Entry 11050

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11050
MolProbity Validation Chart

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Title:
Structure of the N-terminal BARpeptide in SDS micelles
Deposition date:
2008-06-26
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:
Data typeCount
15N chemical shifts38
1H chemical shifts250

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1BARpeptide (1-33)1

Entities:

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

1   METALAGLUMETGLYSERLYSGLYVALTHR
2   ALAGLYLYSILEALASERASNVALGLNLYS
3   LYSLEUTHRARGALAGLNGLULYSVALLEU
4   GLNLYSLEUTYR

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 11049
PDB
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

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