BMRB Entry 25405
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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/BMR25405
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Title: Solution structure of the C-terminal domain of MvaT PubMed: 26068099
Deposition date: 2014-12-25 Original release date: 2015-06-29
Authors: Ding, Pengfei; Xia, Bin
Citation: Ding, Pengfei; McFarland, Kirsty; Jin, Shujuan; Tong, Grace; Duan, Bo; Yang, Ally; Hughes, Timothy; Liu, Jun; Dove, Simon; Navarre, William; Xia, Bin. "A Novel AT-Rich DNA Recognition Mechanism for Bacterial Xenogeneic Silencer MvaT" Plos Pathog. 11, e1004967-e1004967 (2015).
Assembly members:
MvaT, polymer, 55 residues, 5352.173 Da.
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MvaT: MKRARKVKQYKNPHTGEVIE
TKGGNHKTLKEWKAKWGPEA
VESWATLLGHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 207 |
15N chemical shifts | 50 |
1H chemical shifts | 331 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | C-terminal domain of MvaT | 1 |
Entities:
Entity 1, C-terminal domain of MvaT 55 residues - 5352.173 Da.
1 | MET | LYS | ARG | ALA | ARG | LYS | VAL | LYS | GLN | TYR | ||||
2 | LYS | ASN | PRO | HIS | THR | GLY | GLU | VAL | ILE | GLU | ||||
3 | THR | LYS | GLY | GLY | ASN | HIS | LYS | THR | LEU | LYS | ||||
4 | GLU | TRP | LYS | ALA | LYS | TRP | GLY | PRO | GLU | ALA | ||||
5 | VAL | GLU | SER | TRP | ALA | THR | LEU | LEU | GLY | HIS | ||||
6 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: MvaT, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K
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 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | 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:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
BMRB | 25407 |
PDB | |
DBJ | BAK88160 BAP21250 BAP52811 BAQ41953 BAR69621 |
EMBL | CAW29447 CCQ87551 CDH72901 CDH79198 CDI92830 |
GB | AAG07703 AAP33788 ABJ13585 ABR84836 AEO76886 |
REF | NP_253005 WP_003093888 WP_003125172 WP_012077126 WP_015478773 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts