BMRB Entry 19149

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19149
MolProbity Validation Chart

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Title:
The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase
Deposition date:
2013-04-06
Original release date:
2013-05-06
Authors:
Liu, Bing; Parsy, Marie Laurie; O'Dwyer, Kathleen; Paget, Mark; Matthews, Stephen
Citation:

Citation: Tabib-Salazar, Aline; Liu, Bing; Doughty, Philip; Lewis, Richard; Ghosh, Somadri; Parsy, Marie Laurie; O'Dwyer, Kathleen; Simpson, Pete; Matthews, Stephen; Paget, Mark. "The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase"  Nucleic Acids Res. 41, 5679-5691 (2013).
PubMed: 23605043

Assembly members:

Assembly members:
RbpA, polymer, 46 residues, 5213.725 Da.

Natural source:

Natural source:   Common Name: Enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet-20b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RbpA: PRQIARYRTDNGEEFEVPFA DDAEIPGTWLCRNGMEGTLI EGDLPE

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts45
1H chemical shifts290

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RbpA1

Entities:

Entity 1, RbpA 46 residues - 5213.725 Da.

1   PROARGGLNILEALAARGTYRARGTHRASP
2   ASNGLYGLUGLUPHEGLUVALPROPHEALA
3   ASPASPALAGLUILEPROGLYTHRTRPLEU
4   CYSARGASNGLYMETGLUGLYTHRLEUILE
5   GLUGLYASPLEUPROGLU

Samples:

sample_1: beta-mercaptoethanol 3 mM; sodium chloride 500 mM; TRIS 20 mM; H2O 90%; D2O 10%; RbpA mM

sample_conditions_1: ionic strength: 0.5 M; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19023
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