BMRB Entry 27036

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27036

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Title:
PR-R7 from staphylocoagulase of S. aureus Newman D2 Tager 104 strain
Deposition date:
2017-02-17
Original release date:
2017-09-15
Authors:
Voehler, Markus; Bock, Paul; Maddur Appajaiah, Ashoka
Citation:

Citation: Voehler, Markus; Ashoka, Maddur Appajaiah; Meiler, Jens; Bock, Paul. "Carbon and amide detect backbone assignment methods of a novel repeat protein from the staphylocoagulase in S. aureus"  Biomol. NMR Assign. 11, 243-249 (2017).
PubMed: 28819722

Assembly members:

Assembly members:
PR-R7, polymer, 75 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PR-R7: SETTEASHYPARPQFNKTPK YVKYRDAGTGIREYNDGTFG YEARPTYKKPSETNAYNVTT HADGTATYGSRVTKC

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts74
1H chemical shifts392

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1prr7 dissordered protein1

Entities:

Entity 1, prr7 dissordered protein 75 residues - Formula weight is not available

1   SERGLUTHRTHRGLUALASERHISTYRPRO
2   ALAARGPROGLNPHEASNLYSTHRPROLYS
3   TYRVALLYSTYRARGASPALAGLYTHRGLY
4   ILEARGGLUTYRASNASPGLYTHRPHEGLY
5   TYRGLUALAARGPROTHRTYRLYSLYSPRO
6   SERGLUTHRASNALATYRASNVALTHRTHR
7   HISALAASPGLYTHRALATHRTYRGLYSER
8   ARGVALTHRLYSCYS

Samples:

sample_1: PR-R7, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 150 mM; sodium phosphate 20 mM; FPR-CK 100 uM; FFR-CK 100 uM; DSS 500 uM

sample_2: PRR7, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 150 mM; sodium phosphate 20 mM; FPR-CK 100 uM; FFR-CK 100 uM; DSS 500 uM

sample_conditions_2: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_2
3D (H)CCONHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
2D CONsample_2isotropicsample_conditions_2
3D hnCOcaNCOsample_1isotropicsample_conditions_1
3D hNcocaNCOsample_1isotropicsample_conditions_1
3D hacacoNcaNCOsample_2isotropicsample_conditions_2
3D hacaCOncaNCOsample_2isotropicsample_conditions_2
1D protonsample_2isotropicsample_conditions_2

Software:

TOPSPIN v3.2 pl6, Bruker Biospin - collection, processing

NMRView v9.1b35, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

TALOS v3.80F1 Rev 2012.080.14.41, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

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