BMRB Entry 18856

Title:
HADDOCK structure of GtYybT PAS Homodimer
Deposition date:
2012-11-25
Original release date:
2013-03-25
Authors:
Liang, Zhao-xun; Pervushin, Konstantin; Tan, Edward; Rao, Feng; Pasunooti, Swathi; Soehano, Ishin; Lescar, Julien
Citation:

Citation: Tan, Edward; Rao, Feng; Pasunooti, Swathi; Pham, Thi Huong; Soehano, Ishin; Turner, Mark; Liew, Chong Wai; Lescar, Julien; Pervushin, Konstantin; Liang, Zhao-Xun. "Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site."  J. Biol. Chem. 288, 11949-11959 (2013).
PubMed: 23504327

Assembly members:

Assembly members:
PAS_domain_of_DHH_subfamily_1_protein, polymer, 113 residues, 13209.449 Da.

Natural source:

Natural source:   Common Name: Geobacillus thermodenitrificans   Taxonomy ID: 33940   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacillus thermodenitrificans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts122
1H chemical shifts865

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAS domain of DHH subfamily 1 protein_11
2PAS domain of DHH subfamily 1 protein_21

Entities:

Entity 1, PAS domain of DHH subfamily 1 protein_1 113 residues - 13209.449 Da.

1   ARGGLYSERHISMETARGSERLEUHISLYS
2   GLULEUGLNGLNTYRILESERASNLEUSER
3   TYRARGVALLYSLYSVALSERGLUGLUALA
4   LEUMETGLNMETPROILEGLYILELEULEU
5   LEUASPGLUGLUASPLYSILEGLUTRPSER
6   ASNARGPHELEUALAALACYSPHELYSGLU
7   GLNTHRLEUILEGLYARGSERLEUALAGLU
8   LEUSERGLUPROLEUALAALAPHEVALLYS
9   LYSGLYLYSTHRASPGLUGLUILEILEGLU
10   LEUASNGLYLYSGLNLEULYSVALILEVAL
11   HISARGHISGLUARGLEULEUTYRPHEPHE
12   ASPVALTHR

Samples:

sample: PAS domain of DHH subfamily 1 protein, [U-99% 13C; U-99% 15N], 0.7 mM; phosphate buffer 50 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D_15N_TROSY-HSQCsampleisotropicsample_conditions_1
2D_13C_HMQCsampleisotropicsample_conditions_1
3D_HNCAsampleisotropicsample_conditions_1
3D_HN(CO)CAsampleisotropicsample_conditions_1
3D_HNCOsampleisotropicsample_conditions_1
3D_HN(CA)COsampleisotropicsample_conditions_1
3D_CBCA(CO)NHsampleisotropicsample_conditions_1
3D_HN(CA)CBsampleisotropicsample_conditions_1
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESYsampleisotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker AVANCE II 600, 700 MHz

Related Database Links:

PDB
GB ABO68756 EDY05509 KQB91469
REF WP_008880810 WP_011888454 WP_029761080

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