BMRB Entry 15459

Title:
TolR
Deposition date:
2007-09-05
Original release date:
2008-06-25
Authors:
Parsons, Lisa; Bax, Ad
Citation:

Citation: Parsons, Lisa; Grishaev, Alexander; Bax, Ad. "The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data"  Biochemistry 47, 3131-3142 (2008).
PubMed: 18269247

Assembly members:

Assembly members:
TolR, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Haemophilus influenzae   Taxonomy ID: 727   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Haemophilus influenzae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts77
1H chemical shifts526

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21

Entities:

Entity 1, subunit 1 74 residues - Formula weight is not available

residues 19 & 20 are from the cloning tag. Residues 21-92 correspond to residues 59-130 in the full native protein.

1   GLYSERVALPROVALILELEUGLUVALALA
2   GLYILEGLYLYSTYRALAILESERILEGLY
3   GLYGLUARGGLNGLUGLYLEUTHRGLUGLU
4   METVALTHRGLNLEUSERARGGLNGLUPHE
5   ASPLYSASPASNASNTHRLEUPHELEUVAL
6   GLYGLYALALYSGLUVALPROTYRGLUGLU
7   VALILELYSALALEUASNLEULEUHISLEU
8   ALAGLYILELYS

Samples:

sample_1: TolR, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 50 mM; sodium chloride50 – 100 mM; EDTA 0.05 mM; D2O5 – 10%

sample_conditions_1: pH: 6.7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CBW28683 CBY81984 CBY86494 CKG87573
GB AAC22042 AAC44595 AAX87439 ABQ97704 ABQ99958
REF NP_438545 WP_005634116 WP_005649190 WP_005652225 WP_011961713
SP P43769
AlphaFold P43769

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