BMRB Entry 50355

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50355

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Title:
1H, 13C, 15N backbone and ILMVA methyl group assignment of the N-terminal RecA domain of the DEAD-box RNA helicase DbpA from E.coli
Deposition date:
2020-06-25
Original release date:
2021-07-27
Authors:
Wurm, Jan Philip
Citation:

Citation: Wurm, Jan Philip. "Assignment of the Ile, Leu, Val, Met and Ala methyl group resonances of the DEAD-box RNA helicase DbpA from E. coli"  Biomol. NMR Assign. 15, 121-128 (2021).
PubMed: 33277687

Assembly members:

Assembly members:
entity_1, polymer, 214 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTAFSTLNVLPPAQLTNLNE LGYLTMTPVQAAALPAILAG KDVRVQAKTGSGKTAAFGLG LLQQIDASLFQTQALVLCPT RELADQVAGELRRLARFLPN TKILTLCGGQPFGMQRDSLQ HAPHIIVATPGRLLDHLQKG TVSLDALNTLVMDEADRMLD MGFSDAIDDVIRFAPASRQT LLFSATWPEAIAAISGRVQR DPLAIEIDSTDALP

Data sets:
Data typeCount
13C chemical shifts671
15N chemical shifts189
1H chemical shifts994

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal RecA domain1

Entities:

Entity 1, N-terminal RecA domain 214 residues - Formula weight is not available

Residues 1-214 N-terminal RecA domain of E.coli DbpA

1   METTHRALAPHESERTHRLEUASNVALLEU
2   PROPROALAGLNLEUTHRASNLEUASNGLU
3   LEUGLYTYRLEUTHRMETTHRPROVALGLN
4   ALAALAALALEUPROALAILELEUALAGLY
5   LYSASPVALARGVALGLNALALYSTHRGLY
6   SERGLYLYSTHRALAALAPHEGLYLEUGLY
7   LEULEUGLNGLNILEASPALASERLEUPHE
8   GLNTHRGLNALALEUVALLEUCYSPROTHR
9   ARGGLULEUALAASPGLNVALALAGLYGLU
10   LEUARGARGLEUALAARGPHELEUPROASN
11   THRLYSILELEUTHRLEUCYSGLYGLYGLN
12   PROPHEGLYMETGLNARGASPSERLEUGLN
13   HISALAPROHISILEILEVALALATHRPRO
14   GLYARGLEULEUASPHISLEUGLNLYSGLY
15   THRVALSERLEUASPALALEUASNTHRLEU
16   VALMETASPGLUALAASPARGMETLEUASP
17   METGLYPHESERASPALAILEASPASPVAL
18   ILEARGPHEALAPROALASERARGGLNTHR
19   LEULEUPHESERALATHRTRPPROGLUALA
20   ILEALAALAILESERGLYARGVALGLNARG
21   ASPPROLEUALAILEGLUILEASPSERTHR
22   ASPALALEUPRO

Samples:

sample_1: N-terminal RecA domain, [U-13C; U-15N], 400 uM; sodium chloride 125 mM; HEPES 25 mM; DTT 1 mM

sample_2: N-terminal RecA domain, [U-15N; U-2H; 95% 1H13CD-Ile,Leu; 95% 1H13CG-Val, 1H13CB-Ala, 1H13CE-Met], 300 uM; sodium chloride 125 mM; HEPES 25 mM; DTT 1 mM

sample_conditions_1: ionic strength: 140 mM; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C-1H NOESY methyl groupssample_2isotropicsample_conditions_1
3D 13C-13C-1H NOESY methyl groupssample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.2 - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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