BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15045

Title: NMR SOLUTION STRUCTURE OF A MINIMAL TRANSMEMBRANE BETA-BARREL PLATFORM PROTEIN   PubMed: 17260943

Authors: Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin

Citation: Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin. "A Minimal Transmembrane Beta-Barrel Platform Protein Studied by NMR"  Biochemistry 46, 1128-1140 (2007).

Assembly members:
BBP+EF, polymer, 156 residues, 17206.318 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
BBP+EF: MPKDNTWYTGAKLGWSQYSR ENQLGAGAFGGYQVNPYVGF EMGYDWLGRMPRKAQGVQLT AKLGYPKLGTDDLDIYTRLG GMVWRADTSDKDGNGYISAA EASVSPVFAGGVEYVIRRRI TPEIATRLEYQWTNNASDNG MLSLGVSYRFGQGEAA

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts110
1H chemical shifts110

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BBP+EF in DHPC micelles1

Entities:

Entity 1, BBP+EF in DHPC micelles 156 residues - 17206.318 Da.

1   METPROLYSASPASNTHRTRPTYRTHRGLY
2   ALALYSLEUGLYTRPSERGLNTYRSERARG
3   GLUASNGLNLEUGLYALAGLYALAPHEGLY
4   GLYTYRGLNVALASNPROTYRVALGLYPHE
5   GLUMETGLYTYRASPTRPLEUGLYARGMET
6   PROARGLYSALAGLNGLYVALGLNLEUTHR
7   ALALYSLEUGLYTYRPROLYSLEUGLYTHR
8   ASPASPLEUASPILETYRTHRARGLEUGLY
9   GLYMETVALTRPARGALAASPTHRSERASP
10   LYSASPGLYASNGLYTYRILESERALAALA
11   GLUALASERVALSERPROVALPHEALAGLY
12   GLYVALGLUTYRVALILEARGARGARGILE
13   THRPROGLUILEALATHRARGLEUGLUTYR
14   GLNTRPTHRASNASNALASERASPASNGLY
15   METLEUSERLEUGLYVALSERTYRARGPHE
16   GLYGLNGLYGLUALAALA

Samples:

sample_1: BBP+EF, [U-100% 13C; U-100% 15N; 80% 2H], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

GROMACS, Lindahl, Hess and van der Spoel - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB 2JMM