BMRB Entry 17952
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17952
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for E.coli Ribonuclease P protein PubMed: 22423363
Deposition date: 2011-09-21 Original release date: 2011-12-09
Authors: Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyongseok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok
Citation: Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyoung-Seok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok. "Structural analysis of Escherichia coli C5 protein." Proteins 80, 963-967 (2012).
Assembly members:
E.coli_Ribonuclease_P_protein, polymer, 119 residues, 13818.382 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):
E.coli_Ribonuclease_P_protein: MVKLAFPRELRLLTPSQFTF
VFQQPQRAGTPQITILGRLN
SLGHPRIGLTVAKKNVRRAH
ERNRIKRLTRESFRLRQHEL
PAMDFVVVAKKGVADLDNRA
LSEALEKLWRRHCRLARGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 312 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 560 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C5 protein monomer | 1 |
Entities:
Entity 1, C5 protein monomer 119 residues - 13818.382 Da.
| 1 | MET | VAL | LYS | LEU | ALA | PHE | PRO | ARG | GLU | LEU | ||||
| 2 | ARG | LEU | LEU | THR | PRO | SER | GLN | PHE | THR | PHE | ||||
| 3 | VAL | PHE | GLN | GLN | PRO | GLN | ARG | ALA | GLY | THR | ||||
| 4 | PRO | GLN | ILE | THR | ILE | LEU | GLY | ARG | LEU | ASN | ||||
| 5 | SER | LEU | GLY | HIS | PRO | ARG | ILE | GLY | LEU | THR | ||||
| 6 | VAL | ALA | LYS | LYS | ASN | VAL | ARG | ARG | ALA | HIS | ||||
| 7 | GLU | ARG | ASN | ARG | ILE | LYS | ARG | LEU | THR | ARG | ||||
| 8 | GLU | SER | PHE | ARG | LEU | ARG | GLN | HIS | GLU | LEU | ||||
| 9 | PRO | ALA | MET | ASP | PHE | VAL | VAL | VAL | ALA | LYS | ||||
| 10 | LYS | GLY | VAL | ALA | ASP | LEU | ASP | ASN | ARG | ALA | ||||
| 11 | LEU | SER | GLU | ALA | LEU | GLU | LYS | LEU | TRP | ARG | ||||
| 12 | ARG | HIS | CYS | ARG | LEU | ALA | ARG | GLY | SER |
Samples:
E.coli_Ribonuclease_P_protein_sample: E.coli Ribonuclease P protein, [U-95% 13C; U-95% 15N], 0.8 ± 0.2 mM; H2O 90%; D2O 10%; Sodium Phosphate 25 mM; Sodium Chloride 200 mM
E.coli_Ribonuclease_P_protein_conditions: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 2D 1H-13C HSQC | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D CBCA(CO)NH | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D C(CO)NH | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D HNCO | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D HNCACB | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D HBHA(CO)NH | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D HCCH-TOCSY | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D HCCH-COSY | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D 1H-13C NOESY aliphatic | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
| 3D 1H-15N NOESY | E.coli_Ribonuclease_P_protein_sample | isotropic | E.coli_Ribonuclease_P_protein_conditions |
Software:
SPARKY, Goddard - data analysis
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB38062 BAE77590 BAG79514 BAI28036 BAI33155 |
| EMBL | CAA25983 CAD03155 CAP78163 CAQ34048 CAQ91434 |
| GB | AAA24567 AAA62055 AAC76727 AAG58901 AAL22699 |
| PIR | AG0957 |
| PRF | 1112173A |
| REF | NP_312666 NP_418159 NP_458102 NP_462740 NP_709496 |
| SP | A1AHN8 A7ZTR0 A8A6G5 A8ACL6 A9MJT8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts