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 17842

Title: Solution structure of outer membrane protein H (OprH) from P. aeruginosa in DHPC micelles.   PubMed: 21865172

Deposition date: 2011-08-08 Original release date: 2011-08-25

Authors: Edrington, Thomas; Tamm, Lukas

Citation: Edrington, Thomas; Kintz, Erica; Goldberg, Joanna; Tamm, Lukas. "Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa."  J. Biol. Chem. 286, 39211-39223 (2011).

Assembly members:
entity, polymer, 179 residues, 19620.729 Da.

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas Aeruginosa

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a+

Entity Sequences (FASTA):
entity: ADNFVGLTWGETSNNIQKSK SLNRNLNSPNLDKVIDNTGT WGIRAGQQFEQGRYYATYEN ISDTSSGNKLRQQNLLGSYD AFLPIGDNNTKLFGGATLGL VKLEQDGKGFKRDSDVGYAA GLQAGILQELSKNASIEGGY RYLRTNASTEMTPHGGNKLG SLDLHSSSQFYLGANYKFL

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts156
1H chemical shifts156

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OprH1

Entities:

Entity 1, OprH 179 residues - 19620.729 Da.

1   ALAASPASNPHEVALGLYLEUTHRTRPGLY
2   GLUTHRSERASNASNILEGLNLYSSERLYS
3   SERLEUASNARGASNLEUASNSERPROASN
4   LEUASPLYSVALILEASPASNTHRGLYTHR
5   TRPGLYILEARGALAGLYGLNGLNPHEGLU
6   GLNGLYARGTYRTYRALATHRTYRGLUASN
7   ILESERASPTHRSERSERGLYASNLYSLEU
8   ARGGLNGLNASNLEULEUGLYSERTYRASP
9   ALAPHELEUPROILEGLYASPASNASNTHR
10   LYSLEUPHEGLYGLYALATHRLEUGLYLEU
11   VALLYSLEUGLUGLNASPGLYLYSGLYPHE
12   LYSARGASPSERASPVALGLYTYRALAALA
13   GLYLEUGLNALAGLYILELEUGLNGLULEU
14   SERLYSASNALASERILEGLUGLYGLYTYR
15   ARGTYRLEUARGTHRASNALASERTHRGLU
16   METTHRPROHISGLYGLYASNLYSLEUGLY
17   SERLEUASPLEUHISSERSERSERGLNPHE
18   TYRLEUGLYALAASNTYRLYSPHELEU

Samples:

sample_1: OprH, [U-13C; U-15N; U-2H], 1.0 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%

sample_conditions_1: pH: 6.1; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC-TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-TROSY-NOESYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

PDB
DBJ BAK88910 BAP20537 BAP52118 BAQ41215 BAR69069
EMBL CAW28898 CCQ86522 CDH72267 CDH78538 CDI89324
GB AAA25911 AAG04567 AAT50763 ABJ10346 ABR84660
REF NP_249869 WP_003082431 WP_012076667 WP_024915192 WP_031670686

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