BMRB Entry 52495
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52495
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Simonsen, Signe; Prestel, Andreas; Kragelund, Birthe. "Responses to ligand binding in the bacterial DNA sliding clamp, b-clamp manifest in dynamic allosteric effects" .
Assembly members:
entity_1, polymer, 374 residues, Formula weight is not available
entity_2, polymer, 9 residues, Formula weight is not available
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 Vector: pET16b
Entity Sequences (FASTA):
entity_1: MGHHHHHHMKFTVEREHLLK
PLQQVSGPLGGRPTLPILGN
LLLQVADGTLSLTGTDLEME
MVARVALVQPHEPGATTVPA
RKFFDICRGLPEGAEIAVQL
EGERMLVRSGRSRFSLSTLP
AADFPNLDDWQSEVEFTLPQ
ATMKRLIEATQFSMAHQDVR
YYLNGMLFETEGEELRTVAT
DGHRLAVCSMPIGQSLPSHS
VIVPRKGVIELMRMLDGGDN
PLRVQIGSNNIRAHVGDFIF
TSKLVDGRFPDYRRVLPKNP
DKHLEAGCDLLKQAFARAAI
LSNEKFRGVRLYVSENQLKI
TANNPEQEEAEEILDVTYSG
AEMEIGFNVSYVLDVLNALK
CENVRMMLTDSVSSVQIEDA
ASQSAAYVVMPMRL
entity_2: XEQVELEFD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 810 |
| 15N chemical shifts | 305 |
| 1H chemical shifts | 305 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | b-clamp, chain 1 | 1 |
| 2 | b-clamp, chain 2 | 1 |
| 3 | pol III peptide, chain 1 | 2 |
| 4 | pol III peptide, chain 2 | 2 |
Entities:
Entity 1, b-clamp, chain 1 374 residues - Formula weight is not available
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | MET | LYS | ||||
| 2 | PHE | THR | VAL | GLU | ARG | GLU | HIS | LEU | LEU | LYS | ||||
| 3 | PRO | LEU | GLN | GLN | VAL | SER | GLY | PRO | LEU | GLY | ||||
| 4 | GLY | ARG | PRO | THR | LEU | PRO | ILE | LEU | GLY | ASN | ||||
| 5 | LEU | LEU | LEU | GLN | VAL | ALA | ASP | GLY | THR | LEU | ||||
| 6 | SER | LEU | THR | GLY | THR | ASP | LEU | GLU | MET | GLU | ||||
| 7 | MET | VAL | ALA | ARG | VAL | ALA | LEU | VAL | GLN | PRO | ||||
| 8 | HIS | GLU | PRO | GLY | ALA | THR | THR | VAL | PRO | ALA | ||||
| 9 | ARG | LYS | PHE | PHE | ASP | ILE | CYS | ARG | GLY | LEU | ||||
| 10 | PRO | GLU | GLY | ALA | GLU | ILE | ALA | VAL | GLN | LEU | ||||
| 11 | GLU | GLY | GLU | ARG | MET | LEU | VAL | ARG | SER | GLY | ||||
| 12 | ARG | SER | ARG | PHE | SER | LEU | SER | THR | LEU | PRO | ||||
| 13 | ALA | ALA | ASP | PHE | PRO | ASN | LEU | ASP | ASP | TRP | ||||
| 14 | GLN | SER | GLU | VAL | GLU | PHE | THR | LEU | PRO | GLN | ||||
| 15 | ALA | THR | MET | LYS | ARG | LEU | ILE | GLU | ALA | THR | ||||
| 16 | GLN | PHE | SER | MET | ALA | HIS | GLN | ASP | VAL | ARG | ||||
| 17 | TYR | TYR | LEU | ASN | GLY | MET | LEU | PHE | GLU | THR | ||||
| 18 | GLU | GLY | GLU | GLU | LEU | ARG | THR | VAL | ALA | THR | ||||
| 19 | ASP | GLY | HIS | ARG | LEU | ALA | VAL | CYS | SER | MET | ||||
| 20 | PRO | ILE | GLY | GLN | SER | LEU | PRO | SER | HIS | SER | ||||
| 21 | VAL | ILE | VAL | PRO | ARG | LYS | GLY | VAL | ILE | GLU | ||||
| 22 | LEU | MET | ARG | MET | LEU | ASP | GLY | GLY | ASP | ASN | ||||
| 23 | PRO | LEU | ARG | VAL | GLN | ILE | GLY | SER | ASN | ASN | ||||
| 24 | ILE | ARG | ALA | HIS | VAL | GLY | ASP | PHE | ILE | PHE | ||||
| 25 | THR | SER | LYS | LEU | VAL | ASP | GLY | ARG | PHE | PRO | ||||
| 26 | ASP | TYR | ARG | ARG | VAL | LEU | PRO | LYS | ASN | PRO | ||||
| 27 | ASP | LYS | HIS | LEU | GLU | ALA | GLY | CYS | ASP | LEU | ||||
| 28 | LEU | LYS | GLN | ALA | PHE | ALA | ARG | ALA | ALA | ILE | ||||
| 29 | LEU | SER | ASN | GLU | LYS | PHE | ARG | GLY | VAL | ARG | ||||
| 30 | LEU | TYR | VAL | SER | GLU | ASN | GLN | LEU | LYS | ILE | ||||
| 31 | THR | ALA | ASN | ASN | PRO | GLU | GLN | GLU | GLU | ALA | ||||
| 32 | GLU | GLU | ILE | LEU | ASP | VAL | THR | TYR | SER | GLY | ||||
| 33 | ALA | GLU | MET | GLU | ILE | GLY | PHE | ASN | VAL | SER | ||||
| 34 | TYR | VAL | LEU | ASP | VAL | LEU | ASN | ALA | LEU | LYS | ||||
| 35 | CYS | GLU | ASN | VAL | ARG | MET | MET | LEU | THR | ASP | ||||
| 36 | SER | VAL | SER | SER | VAL | GLN | ILE | GLU | ASP | ALA | ||||
| 37 | ALA | SER | GLN | SER | ALA | ALA | TYR | VAL | VAL | MET | ||||
| 38 | PRO | MET | ARG | LEU |
Entity 2, pol III peptide, chain 1 9 residues - Formula weight is not available
| 1 | ACE | GLU | GLN | VAL | GLU | LEU | GLU | PHE | ASP |
Samples:
sample_1: b-clamp homodimer, [U-99% 13C; U-99% 15N; U-97% 2H], 610 uM; D2O, [U-99.9% 2H], 5 % v/v; DSS 125 uM; DTT 5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; pol III peptide (Ac-EQVELEFD) 1300 ± 100 uM
sample_conditions_1: pH: 7.4; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TROSY-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpN Analysis v2.5 - chemical shift assignment
TOPSPIN v4.1 - processing
qMDD v3 - processing
NMR spectrometers:
- Bruker AVANCE III 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks