BMRB Entry 52345

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52345

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Title:
Backbone assignments of E. coli RfaH
Deposition date:
2024-03-06
Original release date:
2024-03-20
Authors:
Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul
Citation:

Citation: Burmann, Bjorn; Knauer, Stefan; Sevostyanova, Anastasia; Schweimer, Kristian; Mooney, Rachel; Landick, Robert; Artsimovitch, Irina; Rosch, Paul. "An a helix to b barrel domain switch transforms the transcription factor RfaH into a translation factor."  Cell 150, 291-303 (2012).
PubMed: 22817892

Assembly members:

Assembly members:
entity_1, polymer, 165 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   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: BL21-DE3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMQSWYLLYCKRGQLQRA QEHLERQAVNCLAPMITLEK IVRGKRTAVSEPLFPNYLFV EFDPEVIHTTTINATRGVSH FVRFGASPAIVPSAVIHQLS VYKPKDIVDPATPYPGDKVI ITEGAFEGFQAIFTEPDGEA RSMLLLNLINKEIKHSVKNT EFRKL

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts135
1H chemical shifts135

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RfaH1

Entities:

Entity 1, RfaH 165 residues - Formula weight is not available

1   GLYSERHISMETGLNSERTRPTYRLEULEU
2   TYRCYSLYSARGGLYGLNLEUGLNARGALA
3   GLNGLUHISLEUGLUARGGLNALAVALASN
4   CYSLEUALAPROMETILETHRLEUGLULYS
5   ILEVALARGGLYLYSARGTHRALAVALSER
6   GLUPROLEUPHEPROASNTYRLEUPHEVAL
7   GLUPHEASPPROGLUVALILEHISTHRTHR
8   THRILEASNALATHRARGGLYVALSERHIS
9   PHEVALARGPHEGLYALASERPROALAILE
10   VALPROSERALAVALILEHISGLNLEUSER
11   VALTYRLYSPROLYSASPILEVALASPPRO
12   ALATHRPROTYRPROGLYASPLYSVALILE
13   ILETHRGLUGLYALAPHEGLUGLYPHEGLN
14   ALAILEPHETHRGLUPROASPGLYGLUALA
15   ARGSERMETLEULEULEUASNLEUILEASN
16   LYSGLUILELYSHISSERVALLYSASNTHR
17   GLUPHEARGLYSLEU

Samples:

sample_1: RfaH, [U-90%-2H; U-99% 13C; U-99% 15N], 0.5 mM; HEPES 25 mM; NaCl 50 mM; H2O 90%; D2O 10%; glycerol 5%; DTT 1 mM

sample_conditions_1: ionic strength: 75 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

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