BMRB Entry 52494

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52494

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Title:
Backbone resonance assignment of the bacterial DNA sliding clamp, b-clamp
Deposition date:
2024-06-05
Original release date:
2025-07-24
Authors:
Simonsen, Signe; Prestel, Andreas; Kragelund, Birthe
Citation:

Citation: Simonsen, Signe; Prestel, Andreas; Kragelund, Birthe. "Responses to ligand binding in the bacterial DNA sliding clamp, b-clamp manifest in dynamic allosteric effects"  .

Assembly members:

Assembly members:
entity_1, polymer, 374 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHMKFTVEREHLLK PLQQVSGPLGGRPTLPILGN LLLQVADGTLSLTGTDLEME MVARVALVQPHEPGATTVPA RKFFDICRGLPEGAEIAVQL EGERMLVRSGRSRFSLSTLP AADFPNLDDWQSEVEFTLPQ ATMKRLIEATQFSMAHQDVR YYLNGMLFETEGEELRTVAT DGHRLAVCSMPIGQSLPSHS VIVPRKGVIELMRMLDGGDN PLRVQIGSNNIRAHVGDFIF TSKLVDGRFPDYRRVLPKNP DKHLEAGCDLLKQAFARAAI LSNEKFRGVRLYVSENQLKI TANNPEQEEAEEILDVTYSG AEMEIGFNVSYVLDVLNALK CENVRMMLTDSVSSVQIEDA ASQSAAYVVMPMRL

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts294
1H chemical shifts294

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1b-clamp, chain 11
2b-clamp, chain 21

Entities:

Entity 1, b-clamp, chain 1 374 residues - Formula weight is not available

1   METGLYHISHISHISHISHISHISMETLYS
2   PHETHRVALGLUARGGLUHISLEULEULYS
3   PROLEUGLNGLNVALSERGLYPROLEUGLY
4   GLYARGPROTHRLEUPROILELEUGLYASN
5   LEULEULEUGLNVALALAASPGLYTHRLEU
6   SERLEUTHRGLYTHRASPLEUGLUMETGLU
7   METVALALAARGVALALALEUVALGLNPRO
8   HISGLUPROGLYALATHRTHRVALPROALA
9   ARGLYSPHEPHEASPILECYSARGGLYLEU
10   PROGLUGLYALAGLUILEALAVALGLNLEU
11   GLUGLYGLUARGMETLEUVALARGSERGLY
12   ARGSERARGPHESERLEUSERTHRLEUPRO
13   ALAALAASPPHEPROASNLEUASPASPTRP
14   GLNSERGLUVALGLUPHETHRLEUPROGLN
15   ALATHRMETLYSARGLEUILEGLUALATHR
16   GLNPHESERMETALAHISGLNASPVALARG
17   TYRTYRLEUASNGLYMETLEUPHEGLUTHR
18   GLUGLYGLUGLULEUARGTHRVALALATHR
19   ASPGLYHISARGLEUALAVALCYSSERMET
20   PROILEGLYGLNSERLEUPROSERHISSER
21   VALILEVALPROARGLYSGLYVALILEGLU
22   LEUMETARGMETLEUASPGLYGLYASPASN
23   PROLEUARGVALGLNILEGLYSERASNASN
24   ILEARGALAHISVALGLYASPPHEILEPHE
25   THRSERLYSLEUVALASPGLYARGPHEPRO
26   ASPTYRARGARGVALLEUPROLYSASNPRO
27   ASPLYSHISLEUGLUALAGLYCYSASPLEU
28   LEULYSGLNALAPHEALAARGALAALAILE
29   LEUSERASNGLULYSPHEARGGLYVALARG
30   LEUTYRVALSERGLUASNGLNLEULYSILE
31   THRALAASNASNPROGLUGLNGLUGLUALA
32   GLUGLUILELEUASPVALTHRTYRSERGLY
33   ALAGLUMETGLUILEGLYPHEASNVALSER
34   TYRVALLEUASPVALLEUASNALALEULYS
35   CYSGLUASNVALARGMETMETLEUTHRASP
36   SERVALSERSERVALGLNILEGLUASPALA
37   ALASERGLNSERALAALATYRVALVALMET
38   PROMETARGLEU

Samples:

sample_1: b-clamp homodimer, [U-99% 13C; U-99% 15N; U-97% 2H], 1083 uM; D2O, [U-99.9% 2H], 5 % v/v; DSS 125 uM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: pH: 7.4; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TROSY-NOESYsample_1isotropicsample_conditions_1

Software:

CcpN Analysis v2.5 - chemical shift assignment

TOPSPIN v4.1 - processing

qMDD v3 - processing

NMR spectrometers:

  • Bruker AVANCE III 750 MHz

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