BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16729

Title: NMR assignment of Salmonella typhimurium tip protein SipD   PubMed: 20397637

Deposition date: 2010-02-16 Original release date: 2010-05-03

Authors: Wang, Yu; Nordhues, Bryce; Zhong, Dalian; De Guzman, Roberto

Citation: Wang, Yu; Nordhues, Bryce; Zhong, Dalian; De Guzman, Roberto. "NMR characterization of the interaction of the Salmonella type III secretion system protein SipD and bile salts."  Biochemistry 49, 4220-4226 (2010).

Assembly members:
SipD, polymer, 343 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):
SipD: MLNIQNYSASPHPGIVAERP QTPSASEHVETAVVPSTTEH RGTDIISLSQAATKIHQAQQ TLQSTPPISEENNDERTLAR QQLTSSLNALAKSGVSLSAE QNENLRSAFSAPTSALFSAS PMAQPRTTISDAEIWDMVSQ NISAIGDSYLGVYENVVAVY TDFYQAFSDILSKMGGWLLP GKDGNTVKLDVTSLKNDLNS LVNKYNQINSNTVLFPAQSG SGVKVATEAEARQWLSELNL PNSCLKSYGSGYVVTVDLTP LQKMVQDIDGLGAPGKDSKL EMDNAKYQAWQSGFKAQEEN MKTTLQTLTQKYSNANSLYD NLVKVLSSTISSSLETAKSF LQG

Data sets:
Data typeCount
13C chemical shifts801
15N chemical shifts274
1H chemical shifts265

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SipDND381

Entities:

Entity 1, SipDND38 343 residues - Formula weight is not available

1   METLEUASNILEGLNASNTYRSERALASER
2   PROHISPROGLYILEVALALAGLUARGPRO
3   GLNTHRPROSERALASERGLUHISVALGLU
4   THRALAVALVALPROSERTHRTHRGLUHIS
5   ARGGLYTHRASPILEILESERLEUSERGLN
6   ALAALATHRLYSILEHISGLNALAGLNGLN
7   THRLEUGLNSERTHRPROPROILESERGLU
8   GLUASNASNASPGLUARGTHRLEUALAARG
9   GLNGLNLEUTHRSERSERLEUASNALALEU
10   ALALYSSERGLYVALSERLEUSERALAGLU
11   GLNASNGLUASNLEUARGSERALAPHESER
12   ALAPROTHRSERALALEUPHESERALASER
13   PROMETALAGLNPROARGTHRTHRILESER
14   ASPALAGLUILETRPASPMETVALSERGLN
15   ASNILESERALAILEGLYASPSERTYRLEU
16   GLYVALTYRGLUASNVALVALALAVALTYR
17   THRASPPHETYRGLNALAPHESERASPILE
18   LEUSERLYSMETGLYGLYTRPLEULEUPRO
19   GLYLYSASPGLYASNTHRVALLYSLEUASP
20   VALTHRSERLEULYSASNASPLEUASNSER
21   LEUVALASNLYSTYRASNGLNILEASNSER
22   ASNTHRVALLEUPHEPROALAGLNSERGLY
23   SERGLYVALLYSVALALATHRGLUALAGLU
24   ALAARGGLNTRPLEUSERGLULEUASNLEU
25   PROASNSERCYSLEULYSSERTYRGLYSER
26   GLYTYRVALVALTHRVALASPLEUTHRPRO
27   LEUGLNLYSMETVALGLNASPILEASPGLY
28   LEUGLYALAPROGLYLYSASPSERLYSLEU
29   GLUMETASPASNALALYSTYRGLNALATRP
30   GLNSERGLYPHELYSALAGLNGLUGLUASN
31   METLYSTHRTHRLEUGLNTHRLEUTHRGLN
32   LYSTYRSERASNALAASNSERLEUTYRASP
33   ASNLEUVALLYSVALLEUSERSERTHRILE
34   SERSERSERLEUGLUTHRALALYSSERPHE
35   LEUGLNGLY

Samples:

sample_1: SipD, [U-98% 15N], 0.6 ± 0.05 mM; SipD, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 ± 0.05 mM; H2O 90%; D2O 10%; sodium phosphate 10 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAJ37875 BAP08788
EMBL CAR34302 CAR38594 CBG25852 CBW18960 CBY97053
GB AAA86617 AAC43548 AAL21763 AAX66721 ABX68926
REF NP_461804 WP_000932241 WP_000932242 WP_000932245 WP_000932246
SP Q56026

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