BMRB Entry 28056

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28056

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Title:
Backbone resonance assignments of the apo form of the solute binding protein PiuA from Streptococcus pneumoniae
Deposition date:
2019-12-22
Original release date:
2020-06-12
Authors:
Edmonds, Katherine; Zhang, Yifan; Giedroc, David
Citation:

Citation: Edmonds, Katherine; Zhang, Yifan; Raines, Daniel; Duhme-Klair, Anne-K; Giedroc, David. "1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the solute binding protein PiuA from Streptococcus pneumoniae"  Biomol. NMR Assign. 14, 233-238 (2020).
PubMed: 32495035

Assembly members:

Assembly members:
PiuA, polymer, 288 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus pneumoniae   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PiuA: SHMSAPTEITIKSSLDEVKL SKVPEKIVTFDLGAADTIRA LGFEKNIVGMPTKTVPTYLK DLVGTVKNVGSMKEPDLEAI AALEPDLIIASPRTQKFVDK FKEIAPTVLFQASKDDYWTS TKANIESLASAFGETSTQKA KEELAKLDKSIQEVATKNES SDKKALAILLNEGKMAAFGA KSRFSFLYQTLKFKPTDTKF EDSRHGQEVSFESVKEINPD ILFVINRTLAIGGDNSSNDG VLENALIAETPAAKNGKIIQ LTPDLWYLSGGGLESTKLMI EDIQKALK

Data sets:
Data typeCount
13C chemical shifts837
15N chemical shifts271
1H chemical shifts271

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PiuA1

Entities:

Entity 1, PiuA 288 residues - Formula weight is not available

The first 3 residues of this construct are a cloning artifact. Remaining residues are the soluble, extracellular domain, residues 37-321.

1   SERHISMETSERALAPROTHRGLUILETHR
2   ILELYSSERSERLEUASPGLUVALLYSLEU
3   SERLYSVALPROGLULYSILEVALTHRPHE
4   ASPLEUGLYALAALAASPTHRILEARGALA
5   LEUGLYPHEGLULYSASNILEVALGLYMET
6   PROTHRLYSTHRVALPROTHRTYRLEULYS
7   ASPLEUVALGLYTHRVALLYSASNVALGLY
8   SERMETLYSGLUPROASPLEUGLUALAILE
9   ALAALALEUGLUPROASPLEUILEILEALA
10   SERPROARGTHRGLNLYSPHEVALASPLYS
11   PHELYSGLUILEALAPROTHRVALLEUPHE
12   GLNALASERLYSASPASPTYRTRPTHRSER
13   THRLYSALAASNILEGLUSERLEUALASER
14   ALAPHEGLYGLUTHRSERTHRGLNLYSALA
15   LYSGLUGLULEUALALYSLEUASPLYSSER
16   ILEGLNGLUVALALATHRLYSASNGLUSER
17   SERASPLYSLYSALALEUALAILELEULEU
18   ASNGLUGLYLYSMETALAALAPHEGLYALA
19   LYSSERARGPHESERPHELEUTYRGLNTHR
20   LEULYSPHELYSPROTHRASPTHRLYSPHE
21   GLUASPSERARGHISGLYGLNGLUVALSER
22   PHEGLUSERVALLYSGLUILEASNPROASP
23   ILELEUPHEVALILEASNARGTHRLEUALA
24   ILEGLYGLYASPASNSERSERASNASPGLY
25   VALLEUGLUASNALALEUILEALAGLUTHR
26   PROALAALALYSASNGLYLYSILEILEGLN
27   LEUTHRPROASPLEUTRPTYRLEUSERGLY
28   GLYGLYLEUGLUSERTHRLYSLEUMETILE
29   GLUASPILEGLNLYSALALEULYS

Samples:

DCN_apo_PiuA: PiuA, [U-13C; U-15N; U-2H], 0.9 mM; D2O, [U-2H], 10%; DSS 0.3 mM; sodium chloride 150 mM; MES 25 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCDCN_apo_PiuAisotropicsample_conditions_1
3D HNCODCN_apo_PiuAisotropicsample_conditions_1
3D HN(CO)CADCN_apo_PiuAisotropicsample_conditions_1
3D HN(CO)CACBDCN_apo_PiuAisotropicsample_conditions_1
3D HNCADCN_apo_PiuAisotropicsample_conditions_1
3D HNCACBDCN_apo_PiuAisotropicsample_conditions_1
3D HN(CA)CODCN_apo_PiuAisotropicsample_conditions_1

Software:

TOPSPIN v4.0.7, Bruker Biospin - collection

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

Sparky, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance Neo 600 MHz

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