BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27857

Title: Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments of RbfA

Deposition date: 2019-03-29 Original release date: 2019-04-01

Authors: Schedlbauer, Andreas; Kaminishi, Tatsuya; Lopez-Alonso, Jorge; Iturrioz, Idoia; Ochoa Lizarralde, Borja; Gil-Carton, David; Fucini, Paola; Connell, Sean

Citation: Schedlbauer, Andreas; Kaminishi, Tatsuya; Lopez-Alonso, Jorge; Iturrioz, Idoia; Ochoa Lizarralde, Borja; Gil-Carton, David; Fucini, Paola; Connell, Sean. "Structural of Ribosomal States associated with late stage assembly factors"  Not known ., .-..

Assembly members:
RbfA, polymer, 140 residues, 15911.32 Da.

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

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

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

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts114
1H chemical shifts835

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RbfA1

Entities:

Entity 1, RbfA 140 residues - 15911.32 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: pH: 7.6; pressure: 1 atm; temperature: 298 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 HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CNH NOESYsample_1isotropicsample_conditions_1
3D HNH NOESYsample_1isotropicsample_conditions_1
3D HCH NOESYsample_1isotropicsample_conditions_1
3D HNCAHAsample_1isotropicsample_conditions_1
3D HN(CO)CAHAsample_1isotropicsample_conditions_1

Software:

NMRPipe v9.8, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P0A7G2

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts