BMRB Entry 50356

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50356

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Title:
1H, 13C, 15N backbone and ILMVAT methyl group assignment of the C-terminal RecA and RBD domains of the DEAD-box RNA helicase DbpA from E.coli
Deposition date:
2020-06-25
Original release date:
2021-07-12
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, 251 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: GGSTDALPPIEQQFYETSSK GKIPLLQRLLSLHQPSSCVV FCNTKKDCQAVCDALNEVGQ SALSLHGDLEQRDRDQTLVR FANGSARVLVATDVAARGLD IKSLELVVNFELAWDPEVHV HRIGRTARAGNSGLAISFCA PEEAQRANIISDMLQIKLNW QTPPANSSIATLEAEMATLC IDGGKKAKMRPGDVLGALTG DIGLDGADIGKIAVHPAHVY VAVRQAVAHKAWKQLQGGKI KGKTCRVRLLK

Data sets:
Data typeCount
13C chemical shifts804
15N chemical shifts251
1H chemical shifts738

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal RecA domain + RNA binding domain1

Entities:

Entity 1, C-terminal RecA domain + RNA binding domain 251 residues - Formula weight is not available

Residues 209-457 C-terminal RecA domain + RNA binding domain of E.coli DbpA

1   GLYGLYSERTHRASPALALEUPROPROILE
2   GLUGLNGLNPHETYRGLUTHRSERSERLYS
3   GLYLYSILEPROLEULEUGLNARGLEULEU
4   SERLEUHISGLNPROSERSERCYSVALVAL
5   PHECYSASNTHRLYSLYSASPCYSGLNALA
6   VALCYSASPALALEUASNGLUVALGLYGLN
7   SERALALEUSERLEUHISGLYASPLEUGLU
8   GLNARGASPARGASPGLNTHRLEUVALARG
9   PHEALAASNGLYSERALAARGVALLEUVAL
10   ALATHRASPVALALAALAARGGLYLEUASP
11   ILELYSSERLEUGLULEUVALVALASNPHE
12   GLULEUALATRPASPPROGLUVALHISVAL
13   HISARGILEGLYARGTHRALAARGALAGLY
14   ASNSERGLYLEUALAILESERPHECYSALA
15   PROGLUGLUALAGLNARGALAASNILEILE
16   SERASPMETLEUGLNILELYSLEUASNTRP
17   GLNTHRPROPROALAASNSERSERILEALA
18   THRLEUGLUALAGLUMETALATHRLEUCYS
19   ILEASPGLYGLYLYSLYSALALYSMETARG
20   PROGLYASPVALLEUGLYALALEUTHRGLY
21   ASPILEGLYLEUASPGLYALAASPILEGLY
22   LYSILEALAVALHISPROALAHISVALTYR
23   VALALAVALARGGLNALAVALALAHISLYS
24   ALATRPLYSGLNLEUGLNGLYGLYLYSILE
25   LYSGLYLYSTHRCYSARGVALARGLEULEU
26   LYS

Samples:

sample_1: sodium chloride 250 mM; HEPES 25 mM; DTT 1 mM; C-terminal RecA domain + RNA binding domain, [U-13C; U-15N; U-2H; 95% 1HD-Ile,Leu; 95% 1HG-Val,95% 1H,13CE-Met], 750 uM; Arginine 25 mM; Glutamate 25 mM

sample_2: sodium chloride 250 mM; HEPES 25 mM; DTT 1 mM; C-terminal RecA domain + RNA binding domain, [U-15N; U-2H; 95% 1H13CD-Ile,Leu; 95% 1H13CG-Val, 1H13CB-Ala, 1H13CE-Met, 1H13CG-Thr,U-1H-Tyr], 800 uM; Arginine 25 mM; Glutamate 25 mM

sample_3: sodium chloride 250 mM; HEPES 25 mM; DTT 1 mM; C-terminal RecA domain + RNA binding domain, [U-15N; U-2H; 95% 1H13CD-Ile,Leu; 95% 1H13CG-Val, 1H13CB-Ala, 1H13CE-Met], 800 uM; Arginine 25 mM; Glutamate 25 mM

sample_conditions_1: ionic strength: 265 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 HN(CO)CACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(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 1H-15N-1H NOESYsample_2isotropicsample_conditions_1
3D 13C-15N-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N-1H NOESYsample_3isotropicsample_conditions_1
3D 13C-15N-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_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