BMRB Entry 26739

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26739

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Title:
NMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions
Deposition date:
2016-01-28
Original release date:
2016-07-14
Authors:
McShan, Andrew; Kaur, Kawaljit; Chatterjee, Srirupa; Knight, Kevin; De Guzman, Roberto
Citation:

Citation: McShan, Andrew; Kaur, Kawaljit; Chatterjee, Srirupa; Knight, Kevin; De Guzman, Roberto. "NMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions"  Proteins 84, 1097-1107 (2016).
PubMed: 27093649

Assembly members:

Assembly members:
SipD, polymer, 308 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Salmonella enterica   Taxonomy ID: 28901   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SipD: GHMEHRGTDIISLSQAATKI HQAQQTLQSTPPISEENNDE RTLARQQLTSSLNALAKSGV SLSAEQNENLRSAFSAPTSA LFSASPMAQPRTTISDAEIW DMVSQNISAIGDSYLGVYEN VVAVYTDFYQAFSDILSKMG GWLLPGKDGNTVKLDVTSLK NDLNSLVNKYNQINSNTVLF PAQSGSGVKVATEAEARQWL SELNLPNSSLKSYGSGYVVT VDLTPLQKMVQDIDGLGAPG KDSKLEMDNAKYQAWQSGFK AQEENMKTTLQTLTQKYSNA NSLYDNLVKVLSSTISSSLE TAKSFLQG

Data sets:
Data typeCount
13C chemical shifts114
1H chemical shifts342

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SipD1

Entities:

Entity 1, SipD 308 residues - Formula weight is not available

1   GLYHISMETGLUHISARGGLYTHRASPILE
2   ILESERLEUSERGLNALAALATHRLYSILE
3   HISGLNALAGLNGLNTHRLEUGLNSERTHR
4   PROPROILESERGLUGLUASNASNASPGLU
5   ARGTHRLEUALAARGGLNGLNLEUTHRSER
6   SERLEUASNALALEUALALYSSERGLYVAL
7   SERLEUSERALAGLUGLNASNGLUASNLEU
8   ARGSERALAPHESERALAPROTHRSERALA
9   LEUPHESERALASERPROMETALAGLNPRO
10   ARGTHRTHRILESERASPALAGLUILETRP
11   ASPMETVALSERGLNASNILESERALAILE
12   GLYASPSERTYRLEUGLYVALTYRGLUASN
13   VALVALALAVALTYRTHRASPPHETYRGLN
14   ALAPHESERASPILELEUSERLYSMETGLY
15   GLYTRPLEULEUPROGLYLYSASPGLYASN
16   THRVALLYSLEUASPVALTHRSERLEULYS
17   ASNASPLEUASNSERLEUVALASNLYSTYR
18   ASNGLNILEASNSERASNTHRVALLEUPHE
19   PROALAGLNSERGLYSERGLYVALLYSVAL
20   ALATHRGLUALAGLUALAARGGLNTRPLEU
21   SERGLULEUASNLEUPROASNSERSERLEU
22   LYSSERTYRGLYSERGLYTYRVALVALTHR
23   VALASPLEUTHRPROLEUGLNLYSMETVAL
24   GLNASPILEASPGLYLEUGLYALAPROGLY
25   LYSASPSERLYSLEUGLUMETASPASNALA
26   LYSTYRGLNALATRPGLNSERGLYPHELYS
27   ALAGLNGLUGLUASNMETLYSTHRTHRLEU
28   GLNTHRLEUTHRGLNLYSTYRSERASNALA
29   ASNSERLEUTYRASPASNLEUVALLYSVAL
30   LEUSERSERTHRILESERSERSERLEUGLU
31   THRALALYSSERPHELEUGLNGLY

Samples:

sample_1: SipD, [U-2H; U-99% 13C methyl of ILV; U-99% 15N], 0.9%; D2O 99%

sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz