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 34082

Title: Solution structure of the B. subtilis anti-sigma-F factor, FIN   PubMed: 28598017

Deposition date: 2017-01-05 Original release date: 2017-06-15

Authors: Martinez-Lumbreras, S.; Alfano, C.; Isaacson, R.

Citation: Wang Erickson, A.; Deighan, P.; Chen, S.; Barrasso, K.; Garcia, C.; Martinez-Lumbreras, S.; Alfano, C.; Krysztofinska, E.; Thapaliya, A.; Camp, A.; Isaacson, R.; Hochschild, A.; Losick, R.. "A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site."  Mol. Microbiol. 105, 652-662 (2017).

Assembly members:
entity_1, polymer, 75 residues, 8686.572 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21

Entity Sequences (FASTA):
entity_1: QSMALHYYCRHCGVKVGSLE SSMVSTDSLGFQHLTNEERN DMISYKENGDVHVLTICEDC QEALDRNPHYHEYHT

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts79
1H chemical shifts443

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 75 residues - 8686.572 Da.

1   GLNSERMETALALEUHISTYRTYRCYSARG
2   HISCYSGLYVALLYSVALGLYSERLEUGLU
3   SERSERMETVALSERTHRASPSERLEUGLY
4   PHEGLNHISLEUTHRASNGLUGLUARGASN
5   ASPMETILESERTYRLYSGLUASNGLYASP
6   VALHISVALLEUTHRILECYSGLUASPCYS
7   GLNGLUALALEUASPARGASNPROHISTYR
8   HISGLUTYRHISTHR

Entity 2, entity_2 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: FIN 400 uM; TCEP 250 uM; potassium phosphate 10 mM; sodium chloride 150 mM

sample_2: FIN, [U-100% 13C; U-100% 15N], 450 uM; TCEP 250 uM; potassium phosphate 10 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 166 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

Analysis, CCPN - chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 700 MHz

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