BMRB Entry 11525
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11525
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain PubMed: 23868391
Deposition date: 2013-04-24 Original release date: 2013-08-05
Authors: Aramaki, Takahiko; Abe, Yoshito; Katayama, Tsutomu; Ueda, Tadashi
Citation: Aramaki, Takahiko; Abe, Yoshito; Katayama, Tsutomu; Ueda, Tadashi. "Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli" Protein Sci. ., .-..
Assembly members:
PriC_N-terminal_domain, polymer, 98 residues, 11007.640 Da.
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
Entity Sequences (FASTA):
PriC_N-terminal_domain: MKTALLLEKLEGQLATLRQR
CAPVSQFATLSARFDRHLFQ
TRATTLQACLDEAGDNLAAL
RHAVEQQQLPQVAWLAEHLA
AQLEAIAREASAWSLREW
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 423 |
15N chemical shifts | 112 |
1H chemical shifts | 696 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PriC_N-terminal_domain | 1 |
Entities:
Entity 1, PriC_N-terminal_domain 98 residues - 11007.640 Da.
1 | MET | LYS | THR | ALA | LEU | LEU | LEU | GLU | LYS | LEU | ||||
2 | GLU | GLY | GLN | LEU | ALA | THR | LEU | ARG | GLN | ARG | ||||
3 | CYS | ALA | PRO | VAL | SER | GLN | PHE | ALA | THR | LEU | ||||
4 | SER | ALA | ARG | PHE | ASP | ARG | HIS | LEU | PHE | GLN | ||||
5 | THR | ARG | ALA | THR | THR | LEU | GLN | ALA | CYS | LEU | ||||
6 | ASP | GLU | ALA | GLY | ASP | ASN | LEU | ALA | ALA | LEU | ||||
7 | ARG | HIS | ALA | VAL | GLU | GLN | GLN | GLN | LEU | PRO | ||||
8 | GLN | VAL | ALA | TRP | LEU | ALA | GLU | HIS | LEU | ALA | ||||
9 | ALA | GLN | LEU | GLU | ALA | ILE | ALA | ARG | GLU | ALA | ||||
10 | SER | ALA | TRP | SER | LEU | ARG | GLU | TRP |
Samples:
sample_1: PriC N-terminal domain, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_2: PriC N-terminal domain, [U-98% 15N], 0.2 mM; sodium chloride 150 mM; D2O 100%
sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
Olivia v1.16.6, Olivia Developer Team - chemical shift assignment, data analysis
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
PDB | |
DBJ | BAA03055 BAB33943 BAE76246 BAG76016 BAI23841 |
EMBL | CAP75000 CAQ30940 CAQ97342 CAR01811 CAR06700 |
GB | AAB40221 AAC73569 AAN42067 AAN79064 AAP15944 |
REF | NP_308547 NP_415000 NP_706360 WP_000626986 WP_000844845 |
SP | P23862 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts