BMRB Entry 28006

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28006

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Title:
Backbone and Aliphatic Side-chain 1H, 13C, and 15N Chemical Shift Assignments for cytoplasmic domain of MapZ protein
Deposition date:
2019-08-22
Original release date:
2020-04-03
Authors:
Hosek, Tomas; Bougault, Catherine; Simorre, Jean-Pierre
Citation:

Citation: Hosek, Tomas; Bougault, Catherine; Lavergne, Jean-Pierre; Martinez, Denis; Ayala, Isabel; Fenel, Daphna; Restelli, Marine; Morlot, Cecile; Habenstein, Birgit; Grangeasse, Christophe; Simorre, Jean-Pierre. "Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae"  Sci. Rep. 10, 4051-4051 (2020).
PubMed: 32132631

Assembly members:

Assembly members:
MapZcyto-WT, polymer, 168 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: pEtPhos

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MapZcyto-WT: MSKKRRNRHKKEAQEPQFDF DEAKELTVGQAIRKNEEVEA GVLPEDSILDKYVKQHRDEI EADKFATRQYKKEEFVETQS LDDLIQEMREAVEKSEASSE EVPSSEDILLPLPLDDEEQG LDPLLLDDENPTEMTEEVEE EQNLSRLDQEDSEKKSKKGL QGENLYFQ

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts153
1H chemical shifts987

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cytoplasmic domain1

Entities:

Entity 1, cytoplasmic domain 168 residues - Formula weight is not available

Residues 159-168 represent the rest of a non-native tag used for purification. This is the cytoplasmic domain of a transmembrane protein

1   METSERLYSLYSARGARGASNARGHISLYS
2   LYSGLUALAGLNGLUPROGLNPHEASPPHE
3   ASPGLUALALYSGLULEUTHRVALGLYGLN
4   ALAILEARGLYSASNGLUGLUVALGLUALA
5   GLYVALLEUPROGLUASPSERILELEUASP
6   LYSTYRVALLYSGLNHISARGASPGLUILE
7   GLUALAASPLYSPHEALATHRARGGLNTYR
8   LYSLYSGLUGLUPHEVALGLUTHRGLNSER
9   LEUASPASPLEUILEGLNGLUMETARGGLU
10   ALAVALGLULYSSERGLUALASERSERGLU
11   GLUVALPROSERSERGLUASPILELEULEU
12   PROLEUPROLEUASPASPGLUGLUGLNGLY
13   LEUASPPROLEULEULEUASPASPGLUASN
14   PROTHRGLUMETTHRGLUGLUVALGLUGLU
15   GLUGLNASNLEUSERARGLEUASPGLNGLU
16   ASPSERGLULYSLYSSERLYSLYSGLYLEU
17   GLNGLYGLUASNLEUTYRPHEGLN

Samples:

sample_1: MapZcyto-WT, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 30 mM; potassium chloride 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST-TROSYsample_1isotropicsample_conditions_1
3D BEST-TROSY iHNCACBsample_1isotropicsample_conditions_1
3D BEST-TROSY HN(CO)CACBsample_1isotropicsample_conditions_1
3D BEST-TROSY HNCOsample_1isotropicsample_conditions_1
3D BEST-TROSY HN(CA)COsample_1isotropicsample_conditions_1
3D BEST-TROSY H(NCACO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz

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