BMRB Entry 19148

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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/BMR19148
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; Tabib-Salazar1, Aline; Doughty, Philip; Lewis, Richard; Ghosh, Somadri; Parsy, Marie Laure; Simpson, Peter; O'Dwyer, Kathleen; Matthews, Steve; Paget, Mark
Citation:

Citation: Tabib-Salazar1, Aline; Liu, Bing; Doughty, Philip; Lewis, Richard; Ghosh, Somadri; Parsy, Marie Laure; Simpson, Peter; O'Dwyer, Kathleen; Matthews, Steve; 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:
entity, polymer, 48 residues, 5358.058 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: pSET152

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QAVEYACEKGHRFEMPFSVE AEIPPEWECKVCGAQALLVD GDGPEEKK

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts44
1H chemical shifts279

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RbpA1

Entities:

Entity 1, RbpA 48 residues - 5358.058 Da.

1   GLNALAVALGLUTYRALACYSGLULYSGLY
2   HISARGPHEGLUMETPROPHESERVALGLU
3   ALAGLUILEPROPROGLUTRPGLUCYSLYS
4   VALCYSGLYALAGLNALALEULEUVALASP
5   GLYASPGLYPROGLUGLULYSLYS

Samples:

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

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

Software:

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC74636 GAP46830
EMBL CAB61670 CAJ90366 CBG74560 CCA54299 CCK31546
GB AEY88130 AGF62286 AGS68293 AIJ17023 AIR97165
REF NP_625703 WP_003977404 WP_003988897 WP_009187548 WP_010046329
SP Q9RKY0
AlphaFold Q9RKY0

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