BMRB Entry 11177
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11177
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Title: Backbone chemical shift assignments for Thermus thermophilus RecO PubMed: 21169364
Deposition date: 2010-07-08 Original release date: 2011-06-03
Authors: Inoue, Jin; Nagae, Takayuki; Mishima, Masaki; Ito, Yutaka; Shibata, Takehiko; Mikawa, Tsutomu
Citation: Inoue, Jin; Nagae, Takayuki; Mishima, Masaki; Ito, Yutaka; Shibata, Takehiko; Mikawa, Tsutomu. "A mechanism for single-stranded DNA-binding protein (SSB) displacement from single-stranded DNA upon SSB-RecO interaction." J. Biol. Chem. 286, 6720-6732 (2011).
Assembly members:
RecO, polymer, 229 residues, Formula weight is not available
Natural source: Common Name: Thermus thermophilus HB8 Taxonomy ID: 300852 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RecO: MAPAYTGKVERYRLEEGIVV
GRKPLPQGDLLLRLVTPRGS
LEAVVRKGQRPTGRTGRLSL
FHHVRFQLYAKGEGLPTLTQ
AELLGRLHGLEAPRRFLLAA
FLAELAYRLASPEAAPRIYP
LLVSGLRGIAKHEDPLLPLV
WAGWRVAKAGGIGPNLEGEG
LRLKRGRLGEEGVYLGREGV
EALKATLRLPGAQALPHLEG
APLNRLFLALKAHAEEALGP
LRSAEAIGV
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 189 |
1H chemical shifts | 189 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RecO | 1 |
Entities:
Entity 1, RecO 229 residues - Formula weight is not available
1 | MET | ALA | PRO | ALA | TYR | THR | GLY | LYS | VAL | GLU | ||||
2 | ARG | TYR | ARG | LEU | GLU | GLU | GLY | ILE | VAL | VAL | ||||
3 | GLY | ARG | LYS | PRO | LEU | PRO | GLN | GLY | ASP | LEU | ||||
4 | LEU | LEU | ARG | LEU | VAL | THR | PRO | ARG | GLY | SER | ||||
5 | LEU | GLU | ALA | VAL | VAL | ARG | LYS | GLY | GLN | ARG | ||||
6 | PRO | THR | GLY | ARG | THR | GLY | ARG | LEU | SER | LEU | ||||
7 | PHE | HIS | HIS | VAL | ARG | PHE | GLN | LEU | TYR | ALA | ||||
8 | LYS | GLY | GLU | GLY | LEU | PRO | THR | LEU | THR | GLN | ||||
9 | ALA | GLU | LEU | LEU | GLY | ARG | LEU | HIS | GLY | LEU | ||||
10 | GLU | ALA | PRO | ARG | ARG | PHE | LEU | LEU | ALA | ALA | ||||
11 | PHE | LEU | ALA | GLU | LEU | ALA | TYR | ARG | LEU | ALA | ||||
12 | SER | PRO | GLU | ALA | ALA | PRO | ARG | ILE | TYR | PRO | ||||
13 | LEU | LEU | VAL | SER | GLY | LEU | ARG | GLY | ILE | ALA | ||||
14 | LYS | HIS | GLU | ASP | PRO | LEU | LEU | PRO | LEU | VAL | ||||
15 | TRP | ALA | GLY | TRP | ARG | VAL | ALA | LYS | ALA | GLY | ||||
16 | GLY | ILE | GLY | PRO | ASN | LEU | GLU | GLY | GLU | GLY | ||||
17 | LEU | ARG | LEU | LYS | ARG | GLY | ARG | LEU | GLY | GLU | ||||
18 | GLU | GLY | VAL | TYR | LEU | GLY | ARG | GLU | GLY | VAL | ||||
19 | GLU | ALA | LEU | LYS | ALA | THR | LEU | ARG | LEU | PRO | ||||
20 | GLY | ALA | GLN | ALA | LEU | PRO | HIS | LEU | GLU | GLY | ||||
21 | ALA | PRO | LEU | ASN | ARG | LEU | PHE | LEU | ALA | LEU | ||||
22 | LYS | ALA | HIS | ALA | GLU | GLU | ALA | LEU | GLY | PRO | ||||
23 | LEU | ARG | SER | ALA | GLU | ALA | ILE | GLY | VAL |
Samples:
sample_1: RecO, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 20 mM; DTT 2 mM; EDTA 2 mM; Magnesium chloride 10 mM; D2O 10%; H2O 90%
sample_conditions_1: pH: 7.5; temperature: 313 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
ANSIG, Kraulis - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
BMRB | 11047 |
DBJ | BAD70446 |
GB | AAS80606 AEG33049 AFH39328 EIA39541 |
REF | WP_008632002 WP_011228077 WP_014510042 WP_014629934 WP_024119227 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts