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 17615

Title: Solution Structure of RfaH carboxyterminal domain   PubMed: 22817892

Deposition date: 2011-05-02 Original release date: 2012-07-30

Authors: Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul

Citation: Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul; Knauer, Stefan; Mooney, Rachel; Sevostyanova, Anastasia; Landick, Robert; Artsimovitch, Irina. "An alpha-helix to beta-barrel domain switch transforms the transcription factor RfaH into a translation factor"  Cell 150, 291-303 (2012).

Assembly members:
entity, polymer, 66 residues, 7269.401 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):
entity: GAMGPKDIVDPATPYPGDKV IITEGAFEGFQAIFTEPDGE ARSMLLLNLINKEIKHSVKN TEFRKL

Data sets:
Data typeCount
13C chemical shifts211
15N chemical shifts62
1H chemical shifts473

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RfaH1

Entities:

Entity 1, RfaH 66 residues - 7269.401 Da.

1   GLYALAMETGLYPROLYSASPILEVALASP
2   PROALATHRPROTYRPROGLYASPLYSVAL
3   ILEILETHRGLUGLYALAPHEGLUGLYPHE
4   GLNALAILEPHETHRGLUPROASPGLYGLU
5   ALAARGSERMETLEULEULEUASNLEUILE
6   ASNLYSGLUILELYSHISSERVALLYSASN
7   THRGLUPHEARGLYSLEU

Samples:

sample_1: RfaH-CTD, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 0.025 mM; NaCl 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 75 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB38193 BAE77461 BAG79652 BAI27905 BAI33028
EMBL CAA46147 CAP78305 CAQ34199 CAR00816 CAR05481
GB AAA67638 AAA91060 AAC76845 AAG10071 AAG59036
REF NP_312797 NP_418284 NP_709646 WP_001161073 WP_001192387
SP P0AFW0 P0AFW1 Q0TAL4 Q8FBI4

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