BMRB Entry 15910
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15910
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: NMR solution structure of the Bacillus subtilis ClpC N-domain PubMed: 19361434
Deposition date: 2008-08-04 Original release date: 2009-05-19
Authors: Kojetin, Douglas; McLaughlin, Patrick; Thompson, Richele; Rance, Mark; Cavanagh, John
Citation: Kojetin, Douglas; McLaughlin, Patrick; Thompson, Richele; Dubnau, David; Prepiak, Peter; Rance, Mark; Cavanagh, John. "Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions" J. Mol. Biol. 387, 639-652 (2009).
Assembly members:
N-ClpCR, polymer, 146 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
N-ClpCR: HMMFGRFTERAQKVLALAQE
EALRLGHNNIGTEHILLGLV
REGEGIAAKALQALGLGSEK
IQKEVESLIGRGQEMSQTIH
YTPRAKKVIELSMDEARKLG
HSYVGTEHILLGLIREGEGV
AARVLNNLGVSLNKARQQVL
QLLGSN
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
- RDCs
| Data type | Count |
| heteronuclear NOE values | 236 |
| residual dipolar couplings | 78 |
| T1 relaxation values | 236 |
| T2 relaxation values | 236 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-ClpCR | 1 |
Entities:
Entity 1, N-ClpCR 146 residues - Formula weight is not available
One additional, unobservable residue (His) was added to the N-terminus of the protein as a consequence of the removal of the His tag.
| 1 | HIS | MET | MET | PHE | GLY | ARG | PHE | THR | GLU | ARG | ||||
| 2 | ALA | GLN | LYS | VAL | LEU | ALA | LEU | ALA | GLN | GLU | ||||
| 3 | GLU | ALA | LEU | ARG | LEU | GLY | HIS | ASN | ASN | ILE | ||||
| 4 | GLY | THR | GLU | HIS | ILE | LEU | LEU | GLY | LEU | VAL | ||||
| 5 | ARG | GLU | GLY | GLU | GLY | ILE | ALA | ALA | LYS | ALA | ||||
| 6 | LEU | GLN | ALA | LEU | GLY | LEU | GLY | SER | GLU | LYS | ||||
| 7 | ILE | GLN | LYS | GLU | VAL | GLU | SER | LEU | ILE | GLY | ||||
| 8 | ARG | GLY | GLN | GLU | MET | SER | GLN | THR | ILE | HIS | ||||
| 9 | TYR | THR | PRO | ARG | ALA | LYS | LYS | VAL | ILE | GLU | ||||
| 10 | LEU | SER | MET | ASP | GLU | ALA | ARG | LYS | LEU | GLY | ||||
| 11 | HIS | SER | TYR | VAL | GLY | THR | GLU | HIS | ILE | LEU | ||||
| 12 | LEU | GLY | LEU | ILE | ARG | GLU | GLY | GLU | GLY | VAL | ||||
| 13 | ALA | ALA | ARG | VAL | LEU | ASN | ASN | LEU | GLY | VAL | ||||
| 14 | SER | LEU | ASN | LYS | ALA | ARG | GLN | GLN | VAL | LEU | ||||
| 15 | GLN | LEU | LEU | GLY | SER | ASN |
Samples:
sample_1: N-ClpCR, [U-13C; U-15N], 0.5-1.0 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_2: N-ClpCR, [U-15N], 0.5 – 1.0 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 305.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D [1H,1H]-NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D [1H,15N,1H]-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H,13C,1H]-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D [1H,13C]-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D [1H,13C]-HMQC-NOESY-[1H,13C]-HMQC | sample_1 | isotropic | sample_conditions_1 |
| 4D [1H,13C]-HMQC-NOESY-[1H,15N]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O, . - chemical shift assignment, structure solution
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
Relax v1.2, d, . - model-free analysis of relaxation data
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz