BMRB Entry 26608

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26608

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the active domains of the type II topoisomerases from Pseudomonas aeruginosa
Deposition date:
2015-07-13
Original release date:
2015-12-18
Authors:
Li, Yan; Ng, Hui Qi; Lee, Michelle Yueqi; Huang, Qiwei; Wong, Ying Lei; Kang, CongBao
Citation:

Citation: Kang, CongBao; Li, Yan; Cherian, Joseph; Liu, Boping; Ng, Hui Qi; Lee, Michelle Yueqi; Poh, Zhi Ying; Wong, Yun Xuan; Huang, Qiwei; Wong, Ying Lei; Hung, Alvin; Hill, Jeffrey; Keller, Thomas H. "Biophysical Studies of Bacterial Topoisomerases Substantiate Their Binding Modes to an Inhibitor"  Biophys. J. 109, 1969-1977 (2015).
PubMed: 26536273

Assembly members:

Assembly members:
Pseudomonas_aeruginosa_active_domains_of_the_type_II_topoisomerases, polymer, 225 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Pseudomonas_aeruginosa_active_domains_of_the_type_II_topoisomerases: MATYNADAIEVLSGLDPVRK RPGMYTDTTRPNHLAQEVID NSVDEALAGHAKSVQVILHQ DNSLEVIDDGRGMPVDIHPE EGVPGVELILTKLHAGGKFS NKNYQFSGGLHGVGISVVNA LSTRVEVRVKRDANEYRMTF ADGFKDSDLEVIGTVGKRNT GTSVHFWPDPKYFDSAKFSV SRLKHVLKAKAVLCPGLSVV FEDKNTGERVEWHFEDGLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts607
15N chemical shifts204
1H chemical shifts204

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1active domains of the type II topoisomerases1

Entities:

Entity 1, active domains of the type II topoisomerases 225 residues - Formula weight is not available

1   METALATHRTYRASNALAASPALAILEGLU
2   VALLEUSERGLYLEUASPPROVALARGLYS
3   ARGPROGLYMETTYRTHRASPTHRTHRARG
4   PROASNHISLEUALAGLNGLUVALILEASP
5   ASNSERVALASPGLUALALEUALAGLYHIS
6   ALALYSSERVALGLNVALILELEUHISGLN
7   ASPASNSERLEUGLUVALILEASPASPGLY
8   ARGGLYMETPROVALASPILEHISPROGLU
9   GLUGLYVALPROGLYVALGLULEUILELEU
10   THRLYSLEUHISALAGLYGLYLYSPHESER
11   ASNLYSASNTYRGLNPHESERGLYGLYLEU
12   HISGLYVALGLYILESERVALVALASNALA
13   LEUSERTHRARGVALGLUVALARGVALLYS
14   ARGASPALAASNGLUTYRARGMETTHRPHE
15   ALAASPGLYPHELYSASPSERASPLEUGLU
16   VALILEGLYTHRVALGLYLYSARGASNTHR
17   GLYTHRSERVALHISPHETRPPROASPPRO
18   LYSTYRPHEASPSERALALYSPHESERVAL
19   SERARGLEULYSHISVALLEULYSALALYS
20   ALAVALLEUCYSPROGLYLEUSERVALVAL
21   PHEGLUASPLYSASNTHRGLYGLUARGVAL
22   GLUTRPHISPHEGLUASPGLYLEUGLUHIS
23   HISHISHISHISHIS

Samples:

sample_1: Pseudomonas aeruginosa active domains of the type II topoisomerases, [U-13C; U-15N; U-2H], 0.8 mM; sodium phosphate 20 mM; potassium chloride 180 mM; DTT 2 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 180 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing

NMR spectrometers:

  • Bruker Avance 700 MHz

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