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 18553

Title: ZirS C-terminal Domain   PubMed: 22810234

Deposition date: 2012-06-28 Original release date: 2012-08-21

Authors: Prehna, Gerd; Li, Yuling; Stoynov, Nikolay; Okon, Mark; Vukovic, Marija; McIntosh, Lawrence; Foster, Leonard; Finlay, B. Brett; Strynadka, Natalie

Citation: Prehna, Gerd; Li, Yuling; Stoynov, Nikolay; Okon, Mark; Vuckovic, Marija; McIntosh, Lawrence; Foster, Leonard; Finlay, B. Brett; Strynadka, Natalie. "The zinc regulated antivirulence pathway of Salmonella is a multiprotein immunoglobulin adhesion system."  J. Biol. Chem. 287, 32324-32337 (2012).

Assembly members:
ZirS, polymer, 146 residues, 16105.249 Da.

Natural source:   Common Name: Enterobacteria   Taxonomy ID: 90371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

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

Entity Sequences (FASTA):
ZirS: GPLGSGSKIKLEIYNETDMA SASGYTPVPSVSEFQYIETE TISNTPSPDLTVMSIDKSVL SPGESATITTIVKDIDGNPV NEVHINKTVARENLKGLWDY GPLKKENVPGKYTQVITYRG HSNERIDISFKYAMSFTKEI SIRGRL

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts125
1H chemical shifts917

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ZirS C-terminal Domain1

Entities:

Entity 1, ZirS C-terminal Domain 146 residues - 16105.249 Da.

1   GLYPROLEUGLYSERGLYSERLYSILELYS
2   LEUGLUILETYRASNGLUTHRASPMETALA
3   SERALASERGLYTYRTHRPROVALPROSER
4   VALSERGLUPHEGLNTYRILEGLUTHRGLU
5   THRILESERASNTHRPROSERPROASPLEU
6   THRVALMETSERILEASPLYSSERVALLEU
7   SERPROGLYGLUSERALATHRILETHRTHR
8   ILEVALLYSASPILEASPGLYASNPROVAL
9   ASNGLUVALHISILEASNLYSTHRVALALA
10   ARGGLUASNLEULYSGLYLEUTRPASPTYR
11   GLYPROLEULYSLYSGLUASNVALPROGLY
12   LYSTYRTHRGLNVALILETHRTYRARGGLY
13   HISSERASNGLUARGILEASPILESERPHE
14   LYSTYRALAMETSERPHETHRLYSGLUILE
15   SERILEARGGLYARGLEU

Samples:

sample_1: ZirS, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 50 mM; sodium chloride 50 mM; TCEP 0.1 mM; PMSF 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.1; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
CCC-TOCSY-NNHsample_1isotropicsample_conditions_1
CT-HSQCsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HD_aromaticsample_1isotropicsample_conditions_1
HBCBGCCC-TOCSYsample_1isotropicsample_conditions_1
HCC-TOCSY-NNHsample_1isotropicsample_conditions_1

Software:

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

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

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian Unity 500 MHz
  • Varian Unity 600 MHz

Related Database Links:

PDB
DBJ BAJ36633 BAP07530
EMBL CBG24675 CBW17693 CCF89381 CCR01301 CCR05077
GB AAL20585 AAX65569 ACH49127 ACN46197 ACY88485
REF NP_460626 WP_000033763 WP_000033764 WP_001242915 WP_001517944

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