BMRB Entry 16214
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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/BMR16214
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Title: Zn finger protein YBIL from E.Coli; NESG target ET107; OCSP target EC0402
Deposition date: 2009-03-13 Original release date: 2009-04-14
Authors: Gutmanas, Aleksandras; Yee, Adelinda; Lemak, Alexander; Fares, Christophe; Guido, Valeria; Arrowsmith, Cheryl
Citation: Gutmanas, Aleksandras; Yee, Adelinda; Lemak, Alexander; Fares, Christophe; Arrowsmith, Cheryl. "Zn-finger protein YBIL from E. Coli" Not known ., .-..
Assembly members:
YBIL, polymer, 108 residues, 9768.879 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: E. coli Taxonomy ID: 62 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YBIL: MGSSHHHHHHSSGLVPRGSH
MASGWANDDAVNEQINSTIE
DAIARARGEIPRGESLDECE
ECGAPIPQARREAIPGVRLC
IHCQQEKDLQKPAYTGYNRR
GSKDSQLR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 349 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 573 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YBIL | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, YBIL 108 residues - 9768.879 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ALA | SER | GLY | TRP | ALA | ASN | ASP | ASP | ALA | ||||
| 4 | VAL | ASN | GLU | GLN | ILE | ASN | SER | THR | ILE | GLU | ||||
| 5 | ASP | ALA | ILE | ALA | ARG | ALA | ARG | GLY | GLU | ILE | ||||
| 6 | PRO | ARG | GLY | GLU | SER | LEU | ASP | GLU | CYS | GLU | ||||
| 7 | GLU | CYS | GLY | ALA | PRO | ILE | PRO | GLN | ALA | ARG | ||||
| 8 | ARG | GLU | ALA | ILE | PRO | GLY | VAL | ARG | LEU | CYS | ||||
| 9 | ILE | HIS | CYS | GLN | GLN | GLU | LYS | ASP | LEU | GLN | ||||
| 10 | LYS | PRO | ALA | TYR | THR | GLY | TYR | ASN | ARG | ARG | ||||
| 11 | GLY | SER | LYS | ASP | SER | GLN | LEU | ARG |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.7 – 1 mM; Zn sulfate 10 uM; DTT, [U-2H], 10 mM; TRIS, [U-2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM; Roche inhibitor 1 X; H20 90%; D20 10%
sample_conditions_1: ionic strength: 0.300 M; pH: 7.0; 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(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 C(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-NOESY-HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-NOESY-HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC long range | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
ABACUS, A. Lemak - chemical shift assignment, data analysis
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
Analysis v2.06, CCPN - data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDNMR, V. Orekhov, I. Ibraghimov - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA35469 BAB34304 BAG76383 BAI24246 BAI29690 |
| EMBL | CAP75272 CAQ31304 CAQ89806 CAQ97706 CAR02159 |
| GB | AAC73890 AAG55175 AAN79361 AAZ87530 ABB60978 |
| REF | NP_308908 NP_415324 WP_000135440 WP_000146315 WP_000146334 |
| SP | P41039 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts