BMRB Entry 27964

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27964

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Title:
Delta subunit of RNA polymerase from Bacillus subtilis with mutated lisine strecht to glutamic acid
Deposition date:
2019-06-30
Original release date:
2019-09-30
Authors:
Zidek, Lukas; Kuban, Vojtech; Srb, Pavel; Stegnerova, Hana; Padrta, Petr; Zachrdla, Milan; Jasenakova, Zuzana; Sanderova, Hana; Krasny, Libor
Citation:

Citation: Kuban, Vojtech; Srb, Pavel; Stegnerova, Hana; Padrta, Petr; Zachrdla, Milan; Jasenakova, Zuzana; Sanderova, Hana; Vitovska, Dragana; Krasny, Libor; Koval, Tomas; Dohnalek, Jan; Ziemska-Legi Cka, Joanna; Grynberg, Marcin; Jarnot, Patryk; Gruca, Aleksandra; Jensen, Malene Ringkjobing; Blackledge, Martin; Zidek, Lukas. "Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase"  J. Am. Chem. Soc. 141, 16817-16828 (2019).
PubMed: 31550880

Assembly members:

Assembly members:
Mutant_of_Delta_Subunit, polymer, 173 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mutant_of_Delta_Subunit: MGIKQYSQEELKEMALVEIA HELFEEHKKPVPFQELLNEI ASLLGVKKEELGDRIAQFYT DLNIDGRFLALSDQTWGLRS WYPYDQLDEETQPTVEAEEE EAEEAVEEDLDLDEFEEIDE DDLDLDEVEEELDLEADDFD EEDLDEDDDDLEIEEDIIDE DDEDYDDEEEEIK

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts87
1H chemical shifts167
residual dipolar couplings663

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Delta-KE1

Entities:

Entity 1, Delta-KE 173 residues - Formula weight is not available

1   METGLYILELYSGLNTYRSERGLNGLUGLU
2   LEULYSGLUMETALALEUVALGLUILEALA
3   HISGLULEUPHEGLUGLUHISLYSLYSPRO
4   VALPROPHEGLNGLULEULEUASNGLUILE
5   ALASERLEULEUGLYVALLYSLYSGLUGLU
6   LEUGLYASPARGILEALAGLNPHETYRTHR
7   ASPLEUASNILEASPGLYARGPHELEUALA
8   LEUSERASPGLNTHRTRPGLYLEUARGSER
9   TRPTYRPROTYRASPGLNLEUASPGLUGLU
10   THRGLNPROTHRVALGLUALAGLUGLUGLU
11   GLUALAGLUGLUALAVALGLUGLUASPLEU
12   ASPLEUASPGLUPHEGLUGLUILEASPGLU
13   ASPASPLEUASPLEUASPGLUVALGLUGLU
14   GLULEUASPLEUGLUALAASPASPPHEASP
15   GLUGLUASPLEUASPGLUASPASPASPASP
16   LEUGLUILEGLUGLUASPILEILEASPGLU
17   ASPASPGLUASPTYRASPASPGLUGLUGLU
18   GLUILELYS

Samples:

sample_1: Mutant of Delta Subunit of Bacterial RNA Polymerase, [U-100% 13C; U-100% 15N], 0.6 mM; sodium chloride 10 mM; sodium phosphate 20 mM; sodium azide 0.05%

sample_gel: Mutant of Delta Subunit of Bacterial RNA Polymerase, [U-100% 13C; U-100% 15N], 0.25 mM; sodium chloride 10 mM; sodium azide 0.05%; sodium phosphate 20 mM; polyacrylamide gel 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
13C-detected 5D CACONCACOsample_1isotropicsample_conditions_1
13C-detected 5D HC(CC-TOCSY)CACONsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D IPAP HNCOsample_gelanisotropicsample_conditions_1
3D a/b-HNCOsample_gelanisotropicsample_conditions_1
4D IPAP (HA)CACONHsample_gelanisotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • 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