BMRB Entry 19007
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19007
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of Bacillus subtilis MinC N-terminal domain PubMed: 24366721
Deposition date: 2013-02-05 Original release date: 2014-03-03
Authors: Castellen, Patricia; Sforca, Mauricio; Zeri, Ana; Gueiros-Filho, Frederico
Citation: Castellen, Patricia; Sforca, Mauricio; Gueiros-Filho, Frederico; de Mattos Zeri, Ana Carolina. "Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis." Biomol. NMR Assignments ., .-. (2013).
Assembly members:
N_MinC, polymer, 105 residues, 12028.750 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
N_MinC: GSHMKTKKQQYVTIKGTKNG
LTLHLDDACSFDELLDGLQN
MLSIEQYTDGKGQKISVHVK
LGNRFLYKEQEEQLTELIAS
KKDLFVHSIDSEVITKKEAQ
QIREE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 396 |
| 15N chemical shifts | 105 |
| 1H chemical shifts | 570 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MinC N-terminal monomer | 1 |
Entities:
Entity 1, MinC N-terminal monomer 105 residues - 12028.750 Da.
| 1 | GLY | SER | HIS | MET | LYS | THR | LYS | LYS | GLN | GLN | ||||
| 2 | TYR | VAL | THR | ILE | LYS | GLY | THR | LYS | ASN | GLY | ||||
| 3 | LEU | THR | LEU | HIS | LEU | ASP | ASP | ALA | CYS | SER | ||||
| 4 | PHE | ASP | GLU | LEU | LEU | ASP | GLY | LEU | GLN | ASN | ||||
| 5 | MET | LEU | SER | ILE | GLU | GLN | TYR | THR | ASP | GLY | ||||
| 6 | LYS | GLY | GLN | LYS | ILE | SER | VAL | HIS | VAL | LYS | ||||
| 7 | LEU | GLY | ASN | ARG | PHE | LEU | TYR | LYS | GLU | GLN | ||||
| 8 | GLU | GLU | GLN | LEU | THR | GLU | LEU | ILE | ALA | SER | ||||
| 9 | LYS | LYS | ASP | LEU | PHE | VAL | HIS | SER | ILE | ASP | ||||
| 10 | SER | GLU | VAL | ILE | THR | LYS | LYS | GLU | ALA | GLN | ||||
| 11 | GLN | ILE | ARG | GLU | GLU |
Samples:
sample_1: N_MinC, [U-99% 13C; U-99% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%
sample_2: protein, [U-100% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%
sample_3: protein, [U-99% 13C; U-99% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| T1 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| T2 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| NOE 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
NMRView, Johnson, One Moon Scientific - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, refinement
VNMRJ, Varian - collection, processing
Smart_Notebook, (Smart Notebook) Slupsky et al., 2003. - processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAI86288 BAM53235 BAM58877 GAK80357 |
| EMBL | CAA78817 CAB14760 CCU59291 CEI58029 CEJ78451 |
| GB | AAA22400 AAA22608 ADV93591 AEP87646 AEP91794 |
| REF | NP_390678 WP_003222613 WP_003237567 WP_004398901 WP_014477549 |
| SP | Q01463 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts