BMRB Entry 50769

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50769

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

Title:
1H and 15N chemical-shift assignments of the backbone amide groups of the RecA_N domain of Bombyx Mori Vasa
Deposition date:
2021-02-17
Original release date:
2024-10-15
Authors:
Codutti, Luca; Nesme, Leo; Kirkpatrick, John; Carlomagno, Teresa
Citation:

Citation: Codutti, Luca; Kirkpatrick, John; zur Lage, Suzanne; Carlomagno, Teresa. "Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa"  Biophys. J. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 274 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: domestic silkworm   Taxonomy ID: 7091   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bombyx mori

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMDPAEFVTYVPPEPTNDE TEIFSSTISSGINFDKFDHI AVKVSGENPPRPIESFETAN LRKYVLDNVLKAGYRKPTPI QKNAIPIIMSGRDLMGCAQT GSGKTAAFLVPIINMLLQDP KDLISENGCAQPQVIIVSPT RELTLQIFNEARKFSYGSVL KVAVAYGGTAVRHQGDNIAR GCHILVATPGRLHDFVERNR VSFGSVRFVVLDEADRMLDM GFMPSIEKMMLHPTMVETTK RQTLMFSATFPEDIQHLAGR FLNNYLFVAVGIVG

Data sets:
Data typeCount
15N chemical shifts164
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RecA_N1

Entities:

Entity 1, RecA_N 274 residues - Formula weight is not available

The first residue of the native Vasa sequence is residue 9 in the sequence above, which corresponds to residue 135 in the native Vasa sequence; hence residue 1 of the sequence above should be numbered as residue 127 (i.e. the first 8 residues are cloning artifacts).

1   GLYALAMETASPPROALAGLUPHEVALTHR
2   TYRVALPROPROGLUPROTHRASNASPGLU
3   THRGLUILEPHESERSERTHRILESERSER
4   GLYILEASNPHEASPLYSPHEASPHISILE
5   ALAVALLYSVALSERGLYGLUASNPROPRO
6   ARGPROILEGLUSERPHEGLUTHRALAASN
7   LEUARGLYSTYRVALLEUASPASNVALLEU
8   LYSALAGLYTYRARGLYSPROTHRPROILE
9   GLNLYSASNALAILEPROILEILEMETSER
10   GLYARGASPLEUMETGLYCYSALAGLNTHR
11   GLYSERGLYLYSTHRALAALAPHELEUVAL
12   PROILEILEASNMETLEULEUGLNASPPRO
13   LYSASPLEUILESERGLUASNGLYCYSALA
14   GLNPROGLNVALILEILEVALSERPROTHR
15   ARGGLULEUTHRLEUGLNILEPHEASNGLU
16   ALAARGLYSPHESERTYRGLYSERVALLEU
17   LYSVALALAVALALATYRGLYGLYTHRALA
18   VALARGHISGLNGLYASPASNILEALAARG
19   GLYCYSHISILELEUVALALATHRPROGLY
20   ARGLEUHISASPPHEVALGLUARGASNARG
21   VALSERPHEGLYSERVALARGPHEVALVAL
22   LEUASPGLUALAASPARGMETLEUASPMET
23   GLYPHEMETPROSERILEGLULYSMETMET
24   LEUHISPROTHRMETVALGLUTHRTHRLYS
25   ARGGLNTHRLEUMETPHESERALATHRPHE
26   PROGLUASPILEGLNHISLEUALAGLYARG
27   PHELEUASNASNTYRLEUPHEVALALAVAL
28   GLYILEVALGLY

Samples:

sample_1: RecA_N, [U-15N; U-2H], 60 ± 20 uM; TRIS 50 mM; sodium chloride 350 mM; arginine 100 mM; glutamic acid 100 mM; magnesium chloride 1 mM; TCEP 1 mM; sodium azide 0.01%

sample_conditions_1: pH: 8.0; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection, processing

NMRPipe v10.1 - processing

CcpNMR v2.4 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 850 MHz

Related Database Links:

NCBI NP_001037347.1

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