BMRB Entry 26744

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26744

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the m1A22 tRNA methyltransferase TrmK from Bacillus subtilis
Deposition date:
2016-02-11
Original release date:
2016-07-14
Authors:
Degut, Clement; Barraud, Pierre; Larue, Valery; Tisne, Carine
Citation:

Citation: Degut, Clement; Barraud, Pierre; Larue, Valery; Tisne, Carine. "Backbone resonance assignments of the m1A22 tRNA methyltransferase TrmK from Bacillus subtilis"  Biomol. NMR Assign. 10, 253-257 (2016).
PubMed: 27098549

Assembly members:

Assembly members:
TrmK, polymer, 241 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TrmK: GSHMNELKLSKRLQTVAEYI PNGAVMADIGSDHAYLPSYA VLNHKASGAIAGEITDGPFL SAKRQVEKSGLNSHISVRQG DGLEVIKKGEADAITIAGMG GALIAHILEAGKDKLTGKER LILQPNIHAVHIREWLYKER YALIDEVILEEDGKSYEVLV AEAGDRDAAYDGISLSAGML VGPFLAKEKNAVFLKKWTQE LQHTQSIYEQISQAADTEQN KQKLKELADRMELLKEVIDH G

Data sets:
Data typeCount
13C chemical shifts660
15N chemical shifts222
1H chemical shifts222

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TrmK1

Entities:

Entity 1, TrmK 241 residues - Formula weight is not available

1   GLYSERHISMETASNGLULEULYSLEUSER
2   LYSARGLEUGLNTHRVALALAGLUTYRILE
3   PROASNGLYALAVALMETALAASPILEGLY
4   SERASPHISALATYRLEUPROSERTYRALA
5   VALLEUASNHISLYSALASERGLYALAILE
6   ALAGLYGLUILETHRASPGLYPROPHELEU
7   SERALALYSARGGLNVALGLULYSSERGLY
8   LEUASNSERHISILESERVALARGGLNGLY
9   ASPGLYLEUGLUVALILELYSLYSGLYGLU
10   ALAASPALAILETHRILEALAGLYMETGLY
11   GLYALALEUILEALAHISILELEUGLUALA
12   GLYLYSASPLYSLEUTHRGLYLYSGLUARG
13   LEUILELEUGLNPROASNILEHISALAVAL
14   HISILEARGGLUTRPLEUTYRLYSGLUARG
15   TYRALALEUILEASPGLUVALILELEUGLU
16   GLUASPGLYLYSSERTYRGLUVALLEUVAL
17   ALAGLUALAGLYASPARGASPALAALATYR
18   ASPGLYILESERLEUSERALAGLYMETLEU
19   VALGLYPROPHELEUALALYSGLULYSASN
20   ALAVALPHELEULYSLYSTRPTHRGLNGLU
21   LEUGLNHISTHRGLNSERILETYRGLUGLN
22   ILESERGLNALAALAASPTHRGLUGLNASN
23   LYSGLNLYSLEULYSGLULEUALAASPARG
24   METGLULEULEULYSGLUVALILEASPHIS
25   GLY

Samples:

TrmK-2H: TrmK, [U-13C; U-15N; U-2H], 800 uM

TrmK-DSS: TrmK, [U-99% 13C; U-99% 15N], 200 uM; DSS 1 mM

TrmK-15N: TrmK, [U-100% 15N], 800 uM

sample_conditions_1: pH: 8.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTrmK-2Hisotropicsample_conditions_1
2D 1H-15N HSQCTrmK-2Hisotropicsample_conditions_1
2D 1H-15N HSQCTrmK-2Hisotropicsample_conditions_1
2D 1H-15N HSQCTrmK-DSSisotropicsample_conditions_1
3D HNCATrmK-2Hisotropicsample_conditions_1
3D HNCACBTrmK-2Hisotropicsample_conditions_1
3D HN(CO)CACBTrmK-2Hisotropicsample_conditions_1
3D HNCOTrmK-2Hisotropicsample_conditions_1
3D 1H-15N NOESYTrmK-15Nisotropicsample_conditions_1
3D HN(CACO)NHTrmK-2Hisotropicsample_conditions_1
2D 1H-15N HSQCTrmK-15Nisotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz
  • 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