BMRB Entry 26053
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26053
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Title: Solution structure of MapZ extracellular domain second 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_SY, polymer, 113 residues, 12299.3762 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_SY: GHMSRSEVNMGLSSAGVAVQ
RSASRVAYNQSAIDDSNNSA
WDFADGVLEQILATSRSRGY
ITGDQYILERVNIVNGNGYY
NLYKPDGTYLFTLNCKTGYF
VGNGAGHADDLDY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 426 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 677 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MapZ SY | 1 |
Entities:
Entity 1, MapZ SY 113 residues - 12299.3762 Da.
Residues 1 to 3 correspond to the remnant of the Histidine-tag after cleavage.
| 1 | GLY | HIS | MET | SER | ARG | SER | GLU | VAL | ASN | MET | ||||
| 2 | GLY | LEU | SER | SER | ALA | GLY | VAL | ALA | VAL | GLN | ||||
| 3 | ARG | SER | ALA | SER | ARG | VAL | ALA | TYR | ASN | GLN | ||||
| 4 | SER | ALA | ILE | ASP | ASP | SER | ASN | ASN | SER | ALA | ||||
| 5 | TRP | ASP | PHE | ALA | ASP | GLY | VAL | LEU | GLU | GLN | ||||
| 6 | ILE | LEU | ALA | THR | SER | ARG | SER | ARG | GLY | TYR | ||||
| 7 | ILE | THR | GLY | ASP | GLN | TYR | ILE | LEU | GLU | ARG | ||||
| 8 | VAL | ASN | ILE | VAL | ASN | GLY | ASN | GLY | TYR | TYR | ||||
| 9 | ASN | LEU | TYR | LYS | PRO | ASP | GLY | THR | TYR | LEU | ||||
| 10 | PHE | THR | LEU | ASN | CYS | LYS | THR | GLY | TYR | PHE | ||||
| 11 | VAL | GLY | ASN | GLY | ALA | GLY | HIS | ALA | ASP | ASP | ||||
| 12 | LEU | ASP | TYR |
Samples:
sample_1: MapZ_extra2, [U-100% 13C; U-100% 15N], 2.5 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 3D HN(CA)CO | sample_1 | isotropic | CondSet1 |
| 3D HNCO | sample_1 | isotropic | CondSet1 |
| 3D HNCACB | sample_1 | isotropic | CondSet1 |
| 3D HN(CO)CACB | sample_1 | isotropic | CondSet1 |
| 3D C(CO)NH | sample_1 | isotropic | CondSet1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | CondSet1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | CondSet1 |
| 3D H(CCO)NH | sample_1 | isotropic | CondSet1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | CondSet1 |
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 - Processing
NMR spectrometers:
- Bruker Avance 850 MHz
- Bruker Avance 950 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts