BMRB Entry 30192

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30192
MolProbity Validation Chart

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Title:
Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus subtilis
Deposition date:
2016-10-13
Original release date:
2017-10-19
Authors:
Draughn, G.; Bobay, B.; Stowe, S.; Thompson, R.; Cavanagh, J.
Citation:

Citation: Milton, Morgan; Draughn, G Logan; Bobay, Benjamin; Stowe, Sean; Olson, Andrew; Feldmann, Erik; Thompson, Richele; Myers, Katherine; Santoro, Michael; Kearns, Daniel; Cavanagh, John. "The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis"  J. Mol. Biol. 432, 343-357 (2020).
PubMed: 31493408

Assembly members:

Assembly members:
Protein SinI, polymer, 63 residues, 7184.149 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 224308   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein SinI: GSHMASMKNAKQEHFELDQE WVELMVEAKEANISPEEIRK YLLLNKKSAHPGPAARSHTV NPF

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts51
1H chemical shifts389

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21

Entities:

Entity 1, entity_1, chain 1 63 residues - 7184.149 Da.

1   GLYSERHISMETALASERMETLYSASNALA
2   LYSGLNGLUHISPHEGLULEUASPGLNGLU
3   TRPVALGLULEUMETVALGLUALALYSGLU
4   ALAASNILESERPROGLUGLUILEARGLYS
5   TYRLEULEULEUASNLYSLYSSERALAHIS
6   PROGLYPROALAALAARGSERHISTHRVAL
7   ASNPROPHE

Samples:

sample_1: MES 20 mM; NaCl 200 mM; SinI, [U-15N], 1 mM; H2O 90%; D2O 10%

sample_2: MES 20 mM; NaCl 200 mM; SinI, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

sample_3: MES 20 mM; NaCl 200 mM; SinI, [U-13C; U-15N], 1 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCOCAsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

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