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 25030

Title: Solution structure of Escherichia coli Outer membrane protein A C-terminal domain   PubMed: 25135663

Authors: Ishida, Hiroaki; Vogel, Hans

Citation: Ishida, Hiroaki; Garcia-Herrero, Alicia; Vogel, Hans. "The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition"  Biochim. Biophys. Acta ., .-. (2014).

Assembly members:
entity, polymer, 146 residues, 15712.804 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):
entity: APAPAPAPEVQTKHFTLKSD VLFNFNKATLKPEGQAALDQ LYSQLSNLDPKDGSVVVLGY TDRIGSDAYNQGLSERRAQS VVDYLISKGIPADKISARGM GESNPVTGNTCDNVKQRAAL IDCLAPDRRVEIEVKGIKDV VTQPQA

Data sets:
Data typeCount
1H chemical shifts127
15N chemical shifts127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OMPA C-terminal domain1

Entities:

Entity 1, OMPA C-terminal domain 146 residues - 15712.804 Da.

1   ALAPROALAPROALAPROALAPROGLUVAL
2   GLNTHRLYSHISPHETHRLEULYSSERASP
3   VALLEUPHEASNPHEASNLYSALATHRLEU
4   LYSPROGLUGLYGLNALAALALEUASPGLN
5   LEUTYRSERGLNLEUSERASNLEUASPPRO
6   LYSASPGLYSERVALVALVALLEUGLYTYR
7   THRASPARGILEGLYSERASPALATYRASN
8   GLNGLYLEUSERGLUARGARGALAGLNSER
9   VALVALASPTYRLEUILESERLYSGLYILE
10   PROALAASPLYSILESERALAARGGLYMET
11   GLYGLUSERASNPROVALTHRGLYASNTHR
12   CYSASPASNVALLYSGLNARGALAALALEU
13   ILEASPCYSLEUALAPROASPARGARGVAL
14   GLUILEGLUVALLYSGLYILELYSASPVAL
15   VALTHRGLNPROGLNALA

Samples:

sample_1: entity, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.03%; DSS 0.5 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.03%; DSS 0.5 mM

sample_3: entity, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.03%; DSS 0.5 mM

sample_conditions_1: temperature: 298 K; pH: 6; pressure: 1 atm; ionic strength: 0 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

X-PLOR_NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution, refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAA35715 BAB34464 BAG76542 BAI24400 BAI29850
EMBL CAA23588 CAA24638 CAP75420 CAQ31485 CAQ88623
GB AAA24232 AAA24236 AAA24240 AAC74043 AAF37887
REF NP_309068 NP_415477 NP_706879 WP_000315441 WP_000315442
SP B7LNW7 P02935 P0A910 P0A911 P0C8Z2