BMRB Entry 52940

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52940

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Title:
Backbone chemical shift assignments of ParA
Deposition date:
2025-02-26
Original release date:
2025-03-13
Authors:
Hennig, Janosch; Perez-Borrajero, Cecilia
Citation:

Citation: Schnabel, Lucas; Osorio-Valeriano, Manuel; Perez-Borrajero, Cecilia; Steinchen, Wieland; Mais, Christopher-Nils; Simon, Bernd; Thamm, Maria; Hennig, Janosch; Bange, Gert; Thanbichler, Martin. "Molecular and structural insights into ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation"  .

Assembly members:

Assembly members:
entity_1, polymer, 265 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Myxococcus xanthus   Taxonomy ID: 34   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Myxococcus xanthus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMO105

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AHHHHHHVGTGVGRIICISN QKGGVGKTTTAINLAASLAS AERRTLLVDMDPQGNAGSGL GIKQDNITGTIYEALLNDRP IQELLHPTELRYLQVVPATP DLTGAEVELVNQDNREFRLR DALRPLAAEYDYIIIDCPPS LGLLTLNALAAADSVLIPLQ CEYYALEGLSQLTHTIDLVK QGLNPDLKMEGILLTMFDSR ANIAHQVVEEVRGYFKKQVF EVIVPRNVRLSECPSFGKPI ILYDIKSKGCESYLALGREL MKRDT

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts79
1H chemical shifts79

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ParA, chain 11
2ParA, chain 21

Entities:

Entity 1, ParA, chain 1 265 residues - Formula weight is not available

1   ALAHISHISHISHISHISHISVALGLYTHR
2   GLYVALGLYARGILEILECYSILESERASN
3   GLNLYSGLYGLYVALGLYLYSTHRTHRTHR
4   ALAILEASNLEUALAALASERLEUALASER
5   ALAGLUARGARGTHRLEULEUVALASPMET
6   ASPPROGLNGLYASNALAGLYSERGLYLEU
7   GLYILELYSGLNASPASNILETHRGLYTHR
8   ILETYRGLUALALEULEUASNASPARGPRO
9   ILEGLNGLULEULEUHISPROTHRGLULEU
10   ARGTYRLEUGLNVALVALPROALATHRPRO
11   ASPLEUTHRGLYALAGLUVALGLULEUVAL
12   ASNGLNASPASNARGGLUPHEARGLEUARG
13   ASPALALEUARGPROLEUALAALAGLUTYR
14   ASPTYRILEILEILEASPCYSPROPROSER
15   LEUGLYLEULEUTHRLEUASNALALEUALA
16   ALAALAASPSERVALLEUILEPROLEUGLN
17   CYSGLUTYRTYRALALEUGLUGLYLEUSER
18   GLNLEUTHRHISTHRILEASPLEUVALLYS
19   GLNGLYLEUASNPROASPLEULYSMETGLU
20   GLYILELEULEUTHRMETPHEASPSERARG
21   ALAASNILEALAHISGLNVALVALGLUGLU
22   VALARGGLYTYRPHELYSLYSGLNVALPHE
23   GLUVALILEVALPROARGASNVALARGLEU
24   SERGLUCYSPROSERPHEGLYLYSPROILE
25   ILELEUTYRASPILELYSSERLYSGLYCYS
26   GLUSERTYRLEUALALEUGLYARGGLULEU
27   METLYSARGASPTHR

Samples:

sample_1: ParA, [U-13C; U-15N; U-2H], 300 uM; D2O, [U-100% 2H], 10%; HEPES 50 mM; potassium chloride 150 mM; Magnesium sulfate 5 mM; DTT 1 mM; ATP 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CARA - chemical shift assignment

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

ParA Q1CVJ3

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