BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 50332

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50332

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Title: Backbone relaxation rates for apo form of the solute binding protein PiuA   PubMed: 32795535

Deposition date: 2020-06-19 Original release date: 2020-08-25

Authors: Edmonds, Katherine; Zhang, Yifan; Wu, Hongwei; Giedroc, David

Citation: Zhang, Yifan; Edmonds, Katherine; Raines, Daniel; Murphy, Brennan; Wu, Hongwei; Guo, Chuchu; Nolan, Elizabeth; VanNieuwenhze, Michael; Duhme-Klair, Anne; Giedroc, David. "The pneumococcal iron uptake protein A (PiuA) specifically recognizes tetradentate FeIII bis- and mono-catechol complexes"  J. Mol. Biol. 432, 5390-5410 (2020).

Assembly members:
entity_1, polymer, 288 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity_1: SHMSAPTEITIKSSLDEVKL SKVPEKIVTFDLGAADTIRA LGFEKNIVGMPTKTVPTYLK DLVGTVKNVGSMKEPDLEAI AALEPDLIIASPRTQKFVDK FKEIAPTVLFQASKDDYWTS TKANIESLASAFGETSTQKA KEELAKLDKSIQEVATKNES SDKKALAILLNEGKMAAFGA KSRFSFLYQTLKFKPTDTKF EDSRHGQEVSFESVKEINPD ILFVINRTLAIGGDNSSNDG VLENALIAETPAAKNGKIIQ LTPDLWYLSGGGLESTKLMI EDIQKALK

Data sets:
Data typeCount
T1 relaxation values234
T2 relaxation values236
heteronuclear NOE values234

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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:

sample_1: PiuA, [U-15N], 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
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
backbone relaxation dispersionsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.7 - collection

NMRPipe - processing

SPARKY - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz