BMRB Entry 19023

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19023
MolProbity Validation Chart

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Title:
Solution structure and sigma factor interactions of Mycobacterium tuberculosis RNA polymerase binding protein A
Deposition date:
2013-02-11
Original release date:
2013-04-11
Authors:
Bortoluzzi, Alessio; Muskett, Frederick; Waters, Lorna; Adiss, Philip; Rieck, Barbara; Munder, Thomas; Schleier, Susanne; Forti, Francesca; Ghisotti, Daniela; Carr, Mark; O'Hare, Helen
Citation:

Citation: Bortoluzzi, Alessio; Muskett, Frederick; Waters, Lorna; Adiss, Philip; Rieck, Barbara; Munder, Thomas; Schleier, Susanne; Forti, Francesca; Ghisotti, Daniela; Carr, Mark; O'Hare, Helen. "Structural characterization of Mycobacterium tuberculosis RNA polymerase binding protein A (RbpA) and its interactions with sigma factors"  J. Biol. Chem. 288, 14438-14450 (2013).
PubMed: 23548911

Assembly members:

Assembly members:
entity, polymer, 80 residues, 9026.145 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-43.1a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SMADRVLRGSRLGAVSYETD RNHDLAPRQIARYRTDNGEE FEVPFADDAEIPGTWLCRNG MEGTLIEGDLPEPKKVKPPR

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts76
1H chemical shifts485

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA polymerase binding protein A (RbpA)1

Entities:

Entity 1, RNA polymerase binding protein A (RbpA) 80 residues - 9026.145 Da.

1   SERMETALAASPARGVALLEUARGGLYSER
2   ARGLEUGLYALAVALSERTYRGLUTHRASP
3   ARGASNHISASPLEUALAPROARGGLNILE
4   ALAARGTYRARGTHRASPASNGLYGLUGLU
5   PHEGLUVALPROPHEALAASPASPALAGLU
6   ILEPROGLYTHRTRPLEUCYSARGASNGLY
7   METGLUGLYTHRLEUILEGLUGLYASPLEU
8   PROGLUPROLYSLYSVALLYSPROPROARG

Samples:

sample_1: RbpA, [U-15N], 0.30 – 0.35 mM; potassium chloride 100 mM; potassium phosphate 25 mM; DTT 0.5 mM; EDTA 0.5 mM; sodium azide 0.02 % w/v; TCEP 0.5 mM; AEBSF protease inhibitor 0.2 mM

sample_2: RbpA, [U-13C; U-15N]-His-Phe-Tyr-Trp, 0.30 – 0.35 mM; potassium chloride 100 mM; potassium phosphate 25 mM; DTT 0.5 mM; EDTA 0.5 mM; sodium azide 0.02 % w/v; TCEP 0.5 mM; AEBSF protease inhibitor 0.2 mM

sample_3: RbpA, [U-15N], 0.30 – 0.35 mM; potassium chloride 100 mM; potassium phosphate 25 mM; DTT 0.5 mM; EDTA 0.5 mM; sodium azide 0.02 % w/v; TCEP 0.5 mM; AEBSF protease inhibitor 0.2 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance II 800 MHz

Related Database Links:

BMRB 19149
PDB
DBJ BAH26349 BAL66056 BAN31760 BAQ06108 GAA45755
EMBL CAB11301 CAC30389 CAL72057 CAR71533 CCC27135
GB AAK46389 AAS04115 ABK68564 ABQ73825 ABR06418
REF NP_216566 NP_302017 NP_855726 WP_003410601 WP_003872122
SP P9WHJ4 P9WHJ5
AlphaFold P9WHJ4 P9WHJ5

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