BMRB Entry 15201

Title:
Sequence-specific resonance assignments for OmpX in 8 M urea aqueous solution
Deposition date:
2007-04-03
Original release date:
2007-04-26
Authors:
Tafer, Hakim; Hiller, Sebastian; Hilty, Christian; Fernandez, Caesar; Wuthrich, Kurt
Citation:

Citation: Tafer, Hakim; Hiller, Sebastian; Hilty, Christian; Fernandez, Cesar; Wuthrich, Kurt. "Nonrandom Structure in the Urea-Unfolded Escherichia coli Outer Membrane Protein X (OmpX)"  Biochemistry 43, 860-869 (2004).
PubMed: 14744128

Assembly members:

Assembly members:
Outer_membrane_protein_X, polymer, 148 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts146
1H chemical shifts869

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OmpX1

Entities:

Entity 1, OmpX 148 residues - Formula weight is not available

1   ALATHRSERTHRVALTHRGLYGLYTYRALA
2   GLNSERASPALAGLNGLYGLNMETASNLYS
3   METGLYGLYPHEASNLEULYSTYRARGTYR
4   GLUGLUASPASNSERPROLEUGLYVALILE
5   GLYSERPHETHRTYRTHRGLULYSSERARG
6   THRALASERSERGLYASPTYRASNLYSASN
7   GLNTYRTYRGLYILETHRALAGLYPROALA
8   TYRARGILEASNASPTRPALASERILETYR
9   GLYVALVALGLYVALGLYTYRGLYLYSPHE
10   GLNTHRTHRGLUTYRPROTHRTYRLYSHIS
11   ASPTHRSERASPTYRGLYPHESERTYRGLY
12   ALAGLYLEUGLNPHEASNPROMETGLUASN
13   VALALALEUASPPHESERTYRGLUGLNSER
14   ARGILEARGSERVALASPVALGLYTHRTRP
15   ILEALAGLYVALGLYTYRARGPHE

Samples:

sample_1: Outer membrane protein X, [U-100% 13C; U-100% 15N], 3 mM; urea 8 M; D2O, [U-100% 2H], 5%; sodium phosphate 20 mM; sodium azide 0.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 750 MHz

Related Database Links:

BMRB 18796 18797 19892
PDB
DBJ BAA35486 BAB34315 BAG76394 BAI24257 BAI29701
EMBL CAP75284 CAQ31315 CAQ97717 CAR02170 CAR06985
GB AAA21856 AAA66329 AAC73901 AAG55186 AAN42399
REF NP_308919 NP_415335 NP_706692 WP_001295296 WP_001340109
SP P0A917 P0A918 P0A919 P0A920
AlphaFold P0A917 P0A918 P0A919 P0A920

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