BMRB Entry 34385

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34385
MolProbity Validation Chart

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Title:
Solution Structure of ribosome-binding factor A (RbfA) under physiological conditions
Deposition date:
2019-04-01
Original release date:
2020-05-29
Authors:
Schedlbauer, A.; Ochoa Lizarralde, B.; Capuni, R.; Iturrioz, I.; Fucini, P.; Connell, S.
Citation:

Citation: Schedlbauer, Andreas; Iturrioz, Idoia; Ochoa-Lizarralde, Borja; Diercks, Tammo; Lopez-Alonso, Jorge Pedro; Lavin, Jose Luis; Kaminishi, Tatsuya; Capuni, Retina; Dhimole, Neha; de Astigarraga, Elisa; Gil-Carton, David; Fucini, Paola; Connell, Sean. "A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit"  Sci. Adv. 7, eabf7547-eabf7547 (2021).
PubMed: 34088665

Assembly members:

Assembly members:
entity_1, polymer, 140 residues, 15933.329 Da.

Natural source:

Natural source:   Common Name: Enterobacter sp. EC-NT1   Taxonomy ID: 2163603   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterobacter Enterobacter sp. EC-NT1

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SAKEFGRPQRVAQEMQKEIA LILQREIKDPRLGMMTTVSG VEMSRDLAYAKVYVTFLNDK DEDAVKAGIKALQEASGFIR SLLGKAMRLRIVPELTFFYD NSLVEGMRMSNLVTSVVKHD EERRVNPDDSKEDALEVLFQ

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts114
1H chemical shifts836

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 140 residues - 15933.329 Da.

1   SERALALYSGLUPHEGLYARGPROGLNARG
2   VALALAGLNGLUMETGLNLYSGLUILEALA
3   LEUILELEUGLNARGGLUILELYSASPPRO
4   ARGLEUGLYMETMETTHRTHRVALSERGLY
5   VALGLUMETSERARGASPLEUALATYRALA
6   LYSVALTYRVALTHRPHELEUASNASPLYS
7   ASPGLUASPALAVALLYSALAGLYILELYS
8   ALALEUGLNGLUALASERGLYPHEILEARG
9   SERLEULEUGLYLYSALAMETARGLEUARG
10   ILEVALPROGLULEUTHRPHEPHETYRASP
11   ASNSERLEUVALGLUGLYMETARGMETSER
12   ASNLEUVALTHRSERVALVALLYSHISASP
13   GLUGLUARGARGVALASNPROASPASPSER
14   LYSGLUASPALALEUGLUVALLEUPHEGLN

Samples:

sample_1: RbfA, [U-98% 13C; U-98% 15N], 400 uM; HEPES 10 mM; MgCl2 6 mM; NH4Cl 30 mM; TCEP 75 uM

sample_conditions_1: ionic strength: 40 mM; pH: 7.6; pressure: 1 atm; temperature: 293 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNH NOESYsample_1isotropicsample_conditions_1
3D CNH NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAHAsample_1isotropicsample_conditions_1
3D HCH NOESYsample_1isotropicsample_conditions_1

Software:

Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Sparky, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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