BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 50357

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50357

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: 1H, 15N backbone and ILMVA methyl group assignment of the DEAD-box RNA helicase DbpA from E.coli   PubMed: 33277687

Deposition date: 2020-06-25 Original release date: 2021-07-27

Authors: Wurm, Jan Philip

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).

Assembly members:
entity_1, polymer, 457 residues, Formula weight is not available

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   Vector: pETM11

Entity Sequences (FASTA):
entity_1: MTAFSTLNVLPPAQLTNLNE LGYLTMTPVQAAALPAILAG KDVRVQAKTGSGKTAAFGLG LLQQIDASLFQTQALVLCPT RELADQVAGELRRLARFLPN TKILTLCGGQPFGMQRDSLQ HAPHIIVATPGRLLDHLQKG TVSLDALNTLVMDEADRMLD MGFSDAIDDVIRFAPASRQT LLFSATWPEAIAAISGRVQR DPLAIEIDSTDALPPIEQQF YETSSKGKIPLLQRLLSLHQ PSSCVVFCNTKKDCQAVCDA LNEVGQSALSLHGDLEQRDR DQTLVRFANGSARVLVATDV AARGLDIKSLELVVNFELAW DPEVHVHRIGRTARAGNSGL AISFCAPEEAQRANIISDML QIKLNWQTPPANSSIATLEA EMATLCIDGGKKAKMRPGDV LGALTGDIGLDGADIGKIAV HPAHVYVAVRQAVAHKAWKQ LQGGKIKGKTCRVRLLK

Data sets:
Data typeCount
13C chemical shifts246
15N chemical shifts415
1H chemical shifts1150

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1full length DbpA1

Entities:

Entity 1, full length DbpA 457 residues - Formula weight is not available

Residues 1-457 (full length) 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   ASPALALEUPROPROILEGLUGLNGLNPHE
23   TYRGLUTHRSERSERLYSGLYLYSILEPRO
24   LEULEUGLNARGLEULEUSERLEUHISGLN
25   PROSERSERCYSVALVALPHECYSASNTHR
26   LYSLYSASPCYSGLNALAVALCYSASPALA
27   LEUASNGLUVALGLYGLNSERALALEUSER
28   LEUHISGLYASPLEUGLUGLNARGASPARG
29   ASPGLNTHRLEUVALARGPHEALAASNGLY
30   SERALAARGVALLEUVALALATHRASPVAL
31   ALAALAARGGLYLEUASPILELYSSERLEU
32   GLULEUVALVALASNPHEGLULEUALATRP
33   ASPPROGLUVALHISVALHISARGILEGLY
34   ARGTHRALAARGALAGLYASNSERGLYLEU
35   ALAILESERPHECYSALAPROGLUGLUALA
36   GLNARGALAASNILEILESERASPMETLEU
37   GLNILELYSLEUASNTRPGLNTHRPROPRO
38   ALAASNSERSERILEALATHRLEUGLUALA
39   GLUMETALATHRLEUCYSILEASPGLYGLY
40   LYSLYSALALYSMETARGPROGLYASPVAL
41   LEUGLYALALEUTHRGLYASPILEGLYLEU
42   ASPGLYALAASPILEGLYLYSILEALAVAL
43   HISPROALAHISVALTYRVALALAVALARG
44   GLNALAVALALAHISLYSALATRPLYSGLN
45   LEUGLNGLYGLYLYSILELYSGLYLYSTHR
46   CYSARGVALARGLEULEULYS

Samples:

sample_1: sodium chloride 125 mM; HEPES 25 mM; DTT 1 mM; DbpA full length, [U-15N; U-2H; 95% 1H13CD-Ile,Leu; 95% 1H13CG-Val, 1H13CB-Ala, 1H13CE-Met], 250 uM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C-1H NOESYsample_1isotropicsample_conditions_1
3D 13C-13C-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.2 - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

Uniprot P21693
AlphaFold P21693

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