BMRB Entry 25086
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25086
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: truncated EcMazE PubMed: 25564525
Deposition date: 2014-07-12 Original release date: 2015-02-02
Authors: Zorzini, Valentina; Buts, Lieven; Loris, Remy; van Nuland, Nico
Citation: Zorzini, Valentina; Buts, Lieven; Schrank, Evelyne; Sterckx, Yann; Respondek, Michal; Engelberg-Kulka, Hanna; Loris, Remy; Zangger, Klaus; van Nuland, Nico. "Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding" Nucleic Acids Res. 43, 1241-1256 (2015).
Assembly members:
truncEcMazE, polymer, 67 residues, 7675.774 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
truncEcMazE: NHKVHHHHHHMSDDDDKGIH
SSVKRWGNSPAVRIPATLMQ
ALNLNIDDEVKIDLVDGKLI
IEPVRKE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 442 |
| 13C chemical shifts | 269 |
| 15N chemical shifts | 65 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | truncated EcMazE_1 | 1 |
| 2 | truncated EcMazE_2 | 1 |
Entities:
Entity 1, truncated EcMazE_1 67 residues - 7675.774 Da.
| 1 | ASN | HIS | LYS | VAL | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | MET | SER | ASP | ASP | ASP | ASP | LYS | GLY | ILE | HIS | ||||
| 3 | SER | SER | VAL | LYS | ARG | TRP | GLY | ASN | SER | PRO | ||||
| 4 | ALA | VAL | ARG | ILE | PRO | ALA | THR | LEU | MET | GLN | ||||
| 5 | ALA | LEU | ASN | LEU | ASN | ILE | ASP | ASP | GLU | VAL | ||||
| 6 | LYS | ILE | ASP | LEU | VAL | ASP | GLY | LYS | LEU | ILE | ||||
| 7 | ILE | GLU | PRO | VAL | ARG | LYS | GLU |
Samples:
sample_1: truncEcMazE, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 50 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian VNMRS 600 MHz
- Varian VNMRS 800 MHz
Related Database Links:
| BMRB | 25092 25093 25094 |
| PDB | |
| DBJ | BAA41177 BAB37066 BAE76857 BAG78565 BAI27044 |
| EMBL | CAP77216 CAQ33107 CAQ87849 CAQ99711 CAR04293 |
| GB | AAA03238 AAA69293 AAC75825 AAG57896 AAZ89539 |
| REF | NP_311670 NP_417263 WP_000581935 WP_000581936 WP_000581937 |
| SP | P0AE72 P0AE73 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts