BMRB Entry 25037
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25037
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Title: Solution structure of N terminal domain of the MuB AAA+ ATPase
Deposition date: 2014-06-23 Original release date: 2015-06-29
Authors: Lopez-Mendez, Blanca; Dramicanin, Marija; Campos-Olivas, Ramon; Ramon-Maiques, Santiago
Citation: Dramicanin, Marija; Lopez-Mendez, Blanca; Campos-Olivas, Ramon; Ramon-Maiques, Santiago. "Solution structure of N terminal domain of the MuB AAA+ ATPase" To be Published ., .-..
Assembly members:
MuB-NTD, polymer, 65 residues, 7353.184 Da.
Natural source: Common Name: Enterobacteria phage Mu Taxonomy ID: 10677 Superkingdom: Viruses Kingdom: not available Genus/species: bacteriophage Mu
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MuB-NTD: GPMNISDIRAGLRTLVENEE
TTFKQIALESGLSTGTISSF
INDKYNGDNERVSQTLQRWL
EKYHA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 183 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 454 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MuB-NTD | 1 |
Entities:
Entity 1, MuB-NTD 65 residues - 7353.184 Da.
| 1 | GLY | PRO | MET | ASN | ILE | SER | ASP | ILE | ARG | ALA | ||||
| 2 | GLY | LEU | ARG | THR | LEU | VAL | GLU | ASN | GLU | GLU | ||||
| 3 | THR | THR | PHE | LYS | GLN | ILE | ALA | LEU | GLU | SER | ||||
| 4 | GLY | LEU | SER | THR | GLY | THR | ILE | SER | SER | PHE | ||||
| 5 | ILE | ASN | ASP | LYS | TYR | ASN | GLY | ASP | ASN | GLU | ||||
| 6 | ARG | VAL | SER | GLN | THR | LEU | GLN | ARG | TRP | LEU | ||||
| 7 | GLU | LYS | TYR | HIS | ALA |
Samples:
sample_1: MuB-NTD 500 uM; sodium phosphate 20 mM; sodium chloride 100 mM
sample_2: MuB-NTD, [U-98% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.2.6, Guntert, Mumenthaler and Wuthrich - structure solution
OPAL v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPN v2.3.1, CCPN - chemical shift assignment, data analysis, peak picking
TOPSPIN v2.1, Bruker Biospin - collection, processing
TALOS+, Cornilescu, Delaglio and Bax - backbone torsion angle restraint generation
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| EMBL | CAA25599 CDP68213 CDU35404 CTU52180 CTV64249 |
| GB | AAA32370 AAA32382 AAF01100 AAW58941 ACV50263 |
| REF | NP_050608 WP_001026707 WP_001026708 WP_001026709 WP_001026710 |
| SP | P03763 P13771 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts