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 18917

Title: Solution NMR structure of the N-terminal domain of STM1478 from Salmonella typhimurium LT2: Target STR147A of the Northeast Structural Genomics consortium (NESG), and APC101565 of the Midwest Center for Structural Genomics (MCSG).

Deposition date: 2012-12-21 Original release date: 2013-02-15

Authors: Houliston, Scott; Yee, Adelinda; Lemak, Alexander; Garcia, Maite; Wu, Bin; Savchenko, Alexei; Arrowsmith, Cheryl

Citation: Houliston, Scott; Yee, Adelinda; Lemak, Alexander; Garcia, Maite; Wu, Bin; Savchenko, Alexei; Arrowsmith, Cheryl. "NMR solution structure of the N-terminal STM1478, from Salmonella typhimurium LT2"  Not known ., .-..

Assembly members:
entity, polymer, 92 residues, 7611.469 Da.

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

Entity Sequences (FASTA):
entity: MGSSHHHHHHSSGRENLYFQ GHAATELTPEQAAALKPYDR IVITGRFNAIGDAVSAVSRR ADEEGAASFYVVDTSEFGNS GNWRVVADVYKA

Data typeCount
13C chemical shifts262
15N chemical shifts67
1H chemical shifts422

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tstm13951

Entities:

Entity 1, tstm1395 92 residues - 7611.469 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISALAALATHRGLULEUTHRPROGLU
4   GLNALAALAALALEULYSPROTYRASPARG
5   ILEVALILETHRGLYARGPHEASNALAILE
6   GLYASPALAVALSERALAVALSERARGARG
7   ALAASPGLUGLUGLYALAALASERPHETYR
8   VALVALASPTHRSERGLUPHEGLYASNSER
9   GLYASNTRPARGVALVALALAASPVALTYR
10   LYSALA

Samples:

sample_1: entity, [U-13C; U-15N], 0.5 mM; BIS-TRIS 10 mM; sodium chloride 200 mM; ZnSO4 10 uM; DTT 10 mM; benzamidine 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AHS60141

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