BMRB Entry 17989
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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/BMR17989
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Title: NMR resonance assignment of the UUP protein C-terminal domain PubMed: 22287065
Deposition date: 2011-10-11 Original release date: 2012-01-31
Authors: Carlier, Ludovic; Haase, Sander; Lequin, Olivier
Citation: Carlier, Ludovic; Haase, A. Sander; Burgos Zepeda, Monica; Dassa, Elie; Lequin, Olivier. "Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein." Biomol. NMR Assignments 6, 197-200 (2012).
Assembly members:
UUP, polymer, 112 residues, 12563 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):
UUP: GSHMGQQEQYVALKQPAVKK
TEEAAAAKAETVKRSSSKLS
YKLQRELEQLPQLLEDLEAK
LEALQTQVADASFFSQPHEQ
TQKVLADMAAAEQELEQAFE
RWEYLEALKNGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 478 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 771 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UUP protein C-terminal domain | 1 |
Entities:
Entity 1, UUP protein C-terminal domain 112 residues - 12563 Da.
Residues 1-4 represent a non-native affinity tag. Gly-5 corresponds to Gly-528 in the native UUP protein sequence.
| 1 | GLY | SER | HIS | MET | GLY | GLN | GLN | GLU | GLN | TYR | ||||
| 2 | VAL | ALA | LEU | LYS | GLN | PRO | ALA | VAL | LYS | LYS | ||||
| 3 | THR | GLU | GLU | ALA | ALA | ALA | ALA | LYS | ALA | GLU | ||||
| 4 | THR | VAL | LYS | ARG | SER | SER | SER | LYS | LEU | SER | ||||
| 5 | TYR | LYS | LEU | GLN | ARG | GLU | LEU | GLU | GLN | LEU | ||||
| 6 | PRO | GLN | LEU | LEU | GLU | ASP | LEU | GLU | ALA | LYS | ||||
| 7 | LEU | GLU | ALA | LEU | GLN | THR | GLN | VAL | ALA | ASP | ||||
| 8 | ALA | SER | PHE | PHE | SER | GLN | PRO | HIS | GLU | GLN | ||||
| 9 | THR | GLN | LYS | VAL | LEU | ALA | ASP | MET | ALA | ALA | ||||
| 10 | ALA | GLU | GLN | GLU | LEU | GLU | GLN | ALA | PHE | GLU | ||||
| 11 | ARG | TRP | GLU | TYR | LEU | GLU | ALA | LEU | LYS | ASN | ||||
| 12 | GLY | GLY |
Samples:
sample_1: UUP, [U-100% 15N], 0.7 mM; sodium chloride 170 mM; sodium phosphate 30 mM; DSS 0.111 mM; leupeptine 1 uM; pepstatine 1 uM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_2: UUP, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 170 mM; sodium phosphate 30 mM; DSS 0.111 mM; leupeptine 1 uM; pepstatine A 1 uM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_3: UUP, [U-100% 13C; U-100% 15N], 0.8 mM; sodium chloride 170 mM; sodium phosphate 30 mM; leupeptine 1 uM; pepstatine A 1 uM; sodium azide 0.02%; D2O 100%
sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, collection, peak picking
TOPSPIN v2.0, Bruker Biospin - geometry optimization
NMR spectrometers:
- Bruker Avance III 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA35707 BAB34456 BAG76534 BAI24392 BAI29842 |
| EMBL | CAA70589 CAP75412 CAQ31477 CAQ88615 CAQ97854 |
| GB | AAC74035 AAG55435 AAN42579 AAN79553 AAP16463 |
| REF | NP_309060 NP_415469 NP_706872 WP_000053029 WP_000053031 |
| SP | P43672 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts