BMRB Entry 18496
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18496
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Title: Solution NMR Structure of YdbC:dT19G1 complex. Northeast Structural Genomics Consortium (NESG) Target KR150
Deposition date: 2012-05-31 Original release date: 2012-07-02
Authors: Rossi, Paolo; Barbieri, Christopher; Aramini, James; Bini, Elisabetta; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Rossi, Paolo; Barbieri, Christopher; Aramini, James; Bini, Elisabetta; Acton, Thomas; Xiao, Rong; Montelione, Gaetano. "Solution NMR Structure of YdbC:dT19G1 complex. Northeast Structural Genomics Consortium (NESG) Target KR150" To be published ., .-..
Assembly members:
entity_1, polymer, 74 residues, 8659.957 Da.
DNA_(5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')_, polymer, 14 residues, 4213.782 Da.
Natural source: Common Name: Lactococcus Lactis Taxonomy ID: 1358 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactococcus Lactis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MADKLKFEIIEELIVLSENA
KGWRKELNRVSWNDAEPKYD
IRTWSPDHEKMGKGITLSEE
EFGVLLKELGNKLE
DNA_(5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')_: TTTTTTTTTTTTTT
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 330 |
15N chemical shifts | 70 |
1H chemical shifts | 655 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | KR150_1 | 1 |
2 | KR150_2 | 1 |
3 | DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') | 2 |
Entities:
Entity 1, KR150_1 74 residues - 8659.957 Da.
1 | MET | ALA | ASP | LYS | LEU | LYS | PHE | GLU | ILE | ILE | ||||
2 | GLU | GLU | LEU | ILE | VAL | LEU | SER | GLU | ASN | ALA | ||||
3 | LYS | GLY | TRP | ARG | LYS | GLU | LEU | ASN | ARG | VAL | ||||
4 | SER | TRP | ASN | ASP | ALA | GLU | PRO | LYS | TYR | ASP | ||||
5 | ILE | ARG | THR | TRP | SER | PRO | ASP | HIS | GLU | LYS | ||||
6 | MET | GLY | LYS | GLY | ILE | THR | LEU | SER | GLU | GLU | ||||
7 | GLU | PHE | GLY | VAL | LEU | LEU | LYS | GLU | LEU | GLY | ||||
8 | ASN | LYS | LEU | GLU |
Entity 2, DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') 14 residues - 4213.782 Da.
1 | DT | DT | DT | DT | DT | DT | DT | DT | DT | DT | ||||
2 | DT | DT | DT | DT |
Samples:
sample_1: KR150.020, [U-100% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; NaCL 100 mM; D2O 10%; DSS 50 uM; TRIS-HCl 10 mM; DNA chain 0.3 mM; H2O 90%
sample_conditions_1: pH: 7.5; 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D-13C,15N X-filt-13C,15N-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
1H-15N Hetnoe | sample_1 | isotropic | sample_conditions_1 |
1D T1 | sample_1 | isotropic | sample_conditions_1 |
1D T2(cpmg) | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
HADDOCK, Bonvin A. M. J. J. - refinemen,structure solution,geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts