BMRB Entry 19809

Title:
Solution structure of YSCUCN in a micellar complex with SDS
Deposition date:
2014-02-20
Original release date:
2014-11-24
Authors:
Weise, Christoph; Wolf-Watz, Magnus
Citation:

Citation: Weise, Christoph; Login, Frederic; Ho, Oanh; Grobner, Gerhard; Wolf-Watz, Hans; Wolf-Watz, Magnus. "Negatively Charged Lipid Membranes Promote a Disorder-Order Transition in the Yersinia YscU Protein"  Biophys. J. 107, 1950-1961 (2014).

Assembly members:

Assembly members:
entity, polymer, 58 residues, 6832.921 Da.

Natural source:

Natural source:   Common Name: Yersinia pseudotuberculosis   Taxonomy ID: 633   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pseudotuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGex-6p3

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts95
13C chemical shifts55
15N chemical shifts55

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 58 residues - 6832.921 Da.

1   GLYPROLEUGLYSERILELYSGLULEULYS
2   METSERLYSASPGLUILELYSARGGLUTYR
3   LYSGLUMETGLUGLYSERPROGLUILELYS
4   SERLYSARGARGGLNPHEHISGLNGLUILE
5   GLNSERARGASNMETARGGLUASNVALLYS
6   ARGSERSERVALVALVALALAASN

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 100 uM; sodium phosphate 30 mM; sodium chloride 50 mM; SDS 26 mM

sample_conditions_1: temperature: 310 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.12 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANSIG, Kraulis - chemical shift assignment

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ProcheckNMR, Laskowski and MacArthur - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAB54924 CAF25417 CAL10055 CBW54704 CBY78168
GB AAA27681 AAC62556 AAC69784 AAD16831 AAK69230
REF NP_052408 NP_395181 NP_783682 NP_857735 NP_857930
SP P69986 P69987
AlphaFold P69986 P69987

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