BMRB Entry 52444

Title:
NMR Assignment of Backbone (1H, 15N, and 13C) resonances of RfaH protein
Deposition date:
2024-05-06
Original release date:
2024-08-03
Authors:
Cai, Mengli; Agarwal, Nipanshu; Clore, Marius
Citation:

Citation: Cai, Mengli; Agarwal, Nipanshu; Garrett, Daniel; Baber, James; Clore, G Marius. "A Transient, Excited Species of the Autoinhibited a-State of the Bacterial Transcription Factor RfaH May Represent an Early Intermediate on the Fold-Switching Pathway"  Biochemistry 63, 2030-2039 (2024).
PubMed: 39088556

Assembly members:

Assembly members:
entity_1, polymer, 162 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: pET 11a

Data sets:
Data typeCount
13C chemical shifts760
15N chemical shifts292
1H chemical shifts292

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RfaH1

Entities:

Entity 1, RfaH 162 residues - Formula weight is not available

1   METGLNSERTRPTYRLEULEUTYRCYSLYS
2   ARGGLYGLNLEUGLNARGALAGLNGLUHIS
3   LEUGLUARGGLNALAVALASNCYSLEUALA
4   PROMETILETHRLEUGLULYSILEVALARG
5   GLYLYSARGTHRALAVALSERGLUPROLEU
6   PHEPROASNTYRLEUPHEVALGLUPHEASP
7   PROGLUVALILEHISTHRTHRTHRILEASN
8   ALATHRARGGLYVALSERHISPHEVALARG
9   PHEGLYALASERPROALAILEVALPROSER
10   ALAVALILEHISGLNLEUSERVALTYRLYS
11   PROLYSASPILEVALASPPROALATHRPRO
12   TYRPROGLYASPLYSVALILEILETHRGLU
13   GLYALAPHEGLUGLYPHEGLNALAILEPHE
14   THRGLUPROASPGLYGLUALAARGSERMET
15   LEULEULEUASNLEUILEASNLYSGLUILE
16   LYSHISSERVALLYSASNTHRGLUPHEARG
17   LYSLEU

Samples:

sample_1: RfaH, [U-100% 13C; U-100% 15N; U-80% 2H], 0.35 mM; Sodium Phosphate 50 mM; Deuterated Glycerol 5%; TCEP 1 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 289 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 2468 atm; temperature: 289 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_2
3D CBCACONHsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2

Software:

TOPSPIN - collection

NMRPipe - processing

Xipp - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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