BMRB Entry 11527
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11527
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriB PubMed: 24200676
Deposition date: 2013-06-08 Original release date: 2017-03-13
Authors: Abe, Yoshito; Takenawa, Taichi; Shioi, Seijiro; Fujiyama, Saki; Aramaki, Takahiko; Katayama, Tsutomu; Ueda, Tadashi
Citation: Fujiyama, Saki; Abe, Yoshito; Takenawa, Taichi; Aramaki, Takahiko; Shioi, Seijiro; Katayama, Tsutomu; Ueda, Tadashi. "Involvement of histidine in complex formation of PriB and single-stranded DNA" Biochim. Biophys. Acta 1844, 299-307 (2014).
Assembly members:
PriB, polymer, 104 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Entity Sequences (FASTA):
PriB: MTNRLVLSGTVCRAPLRKVS
PSGIPHCQFVLEHRSVQEEA
GFHRQAWCQMPVIVSGHENQ
AITHSITVGSRITVQGFISC
HKAKNGLSKMVLHAEQIELI
DSGD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 282 |
15N chemical shifts | 93 |
1H chemical shifts | 93 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PriB homodimer, subunit 1 | 1 |
2 | PriB homodimer, subunit 2 | 1 |
Entities:
Entity 1, PriB homodimer, subunit 1 104 residues - Formula weight is not available
1 | MET | THR | ASN | ARG | LEU | VAL | LEU | SER | GLY | THR | ||||
2 | VAL | CYS | ARG | ALA | PRO | LEU | ARG | LYS | VAL | SER | ||||
3 | PRO | SER | GLY | ILE | PRO | HIS | CYS | GLN | PHE | VAL | ||||
4 | LEU | GLU | HIS | ARG | SER | VAL | GLN | GLU | GLU | ALA | ||||
5 | GLY | PHE | HIS | ARG | GLN | ALA | TRP | CYS | GLN | MET | ||||
6 | PRO | VAL | ILE | VAL | SER | GLY | HIS | GLU | ASN | GLN | ||||
7 | ALA | ILE | THR | HIS | SER | ILE | THR | VAL | GLY | SER | ||||
8 | ARG | ILE | THR | VAL | GLN | GLY | PHE | ILE | SER | CYS | ||||
9 | HIS | LYS | ALA | LYS | ASN | GLY | LEU | SER | LYS | MET | ||||
10 | VAL | LEU | HIS | ALA | GLU | GLN | ILE | GLU | LEU | ILE | ||||
11 | ASP | SER | GLY | ASP |
Samples:
sample_1: PriB, [U-98% 13C; U-98% 15N], 0.5 0.8 mM; HEPES 20 mM; ammonium sulfate 200 mM; D2O 10%; H2O 90%; DTT 5 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Olivia, hokkaido university - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts