BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26052

Title: Solution structure of MapZ extracellular domain first subdomain   PubMed: 27346279

Deposition date: 2016-05-11 Original release date: 2016-06-27

Authors: Jean, Nicolas; Manuse, Sylvie; Guinot, Megane; Bougault, Catherine; Grangeasse, Christophe; Simorre, Jean-Pierre

Citation: Manuse, Sylvie; Jean, Nicolas; Guinot, Megane; Lavergne, Jean-Pierre; Laguri, Cedric; Bougault, Catherine; Van Nieuwenhze, Michael; Grangeasse, Christophe; Simorre, Jean-Pierre. "Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ"  Nat. commun. 7, 12071-12071 (2016).

Assembly members:
MapZ_QG, polymer, 135 residues, 14847.4638 Da.

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

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

Entity Sequences (FASTA):
MapZ_QG: GHMQVARSTKEIETSQSTTA NQSDVDDFNTLYDAFYTNSN KTALKNSQFDKLSQLKTLLD KLEGSREHTLAKSKYDSLAT QIKAIQDVNAQFEKPAIVDG VLDTNAKAKSDAKFTDIKTG NTELDKVLDKAISLG

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts137
1H chemical shifts841

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MapZ QG1

Entities:

Entity 1, MapZ QG 135 residues - 14847.4638 Da.

Residues 1 to 3 correspond to the remnant of the Histidine-tag after cleavage.

1   GLYHISMETGLNVALALAARGSERTHRLYS
2   GLUILEGLUTHRSERGLNSERTHRTHRALA
3   ASNGLNSERASPVALASPASPPHEASNTHR
4   LEUTYRASPALAPHETYRTHRASNSERASN
5   LYSTHRALALEULYSASNSERGLNPHEASP
6   LYSLEUSERGLNLEULYSTHRLEULEUASP
7   LYSLEUGLUGLYSERARGGLUHISTHRLEU
8   ALALYSSERLYSTYRASPSERLEUALATHR
9   GLNILELYSALAILEGLNASPVALASNALA
10   GLNPHEGLULYSPROALAILEVALASPGLY
11   VALLEUASPTHRASNALALYSALALYSSER
12   ASPALALYSPHETHRASPILELYSTHRGLY
13   ASNTHRGLULEUASPLYSVALLEUASPLYS
14   ALAILESERLEUGLY

Samples:

sample_1: MapZ_extra1, [U-100% 13C; U-100% 15N], 2.0 mM; Tris 50 mM; NaCl 100 mM; H2O 95%; D2O 5%

CondSet1: ionic strength: 0.1 M; pH: 7.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCsample_1isotropicCondSet1
3D HN(CA)COsample_1isotropicCondSet1
3D HNCOsample_1isotropicCondSet1
3D HNCACBsample_1isotropicCondSet1
3D HN(CO)CACBsample_1isotropicCondSet1
3D C(CO)NHsample_1isotropicCondSet1
3D 1H-15N NOESYsample_1isotropicCondSet1
3D H(CCO)NHsample_1isotropicCondSet1
2D 1H-13C HSQC/HMQCsample_1isotropicCondSet1
2D 1H-13C HSQC/HMQCsample_1isotropicCondSet1
3D 1H-13C NOESYsample_1isotropicCondSet1

Software:

Aria v2.3.1, W. Rieping, M. Habeck, B. Bardiaux, A. Bernard, T.E. Malliavin and M. Nilges - Structure calculation

CNS v1.1, A. Brunger, P. Adams, G. Clore, P. Gros, M. Nilges and R. Read - Refinement

CcpNmr_Analysis v2.4, CCPN - Data analysis

Talos+ v1, Y. Shen, F. Delaglio, G. Cornilescu and A. Bax - Data analysis

Unio10' v2.0.2, T. Herrmann - Peakpicking

nmrPipe vany, F. Delaglio, S. Grzesiek,G.W. Vuister, G. Zhu, J. Pfeifer and A. Bax - Spectrum processing

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 850 MHz

Related Database Links:

UNP Q8DR55

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts