BMRB Entry 18431
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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/BMR18431
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Title: Solution structure of the mouse Rev1 C-terminal domain PubMed: 22700975
Deposition date: 2012-04-30 Original release date: 2012-06-18
Authors: Liu, Jiangxin; Wojtaszek, Jessica; Zhou, Pei
Citation: Wojtaszek, Jessica; Liu, Jiangxin; Wang, Sanjay; Xue, Su; Walker, Yaohua; Zhou, Graham. "Multifaceted recognition of vertebrate Rev1 by translesion polymerases and ." J. Biol. Chem. 287, 26400-26408 (2012).
Assembly members:
entity, polymer, 104 residues, 11166.953 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):
entity: GSGGFRPAAPNLAGAVEFSD
VKTLLKEWITTISDPMEEDI
LQVVRYCTDLIEEKDLEKLD
LVIKYMKRLMQQSVESVWNM
AFDFILDNVQVVLQQTYGST
LKVT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 363 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 764 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse Rev1 C-terminal domain | 1 |
Entities:
Entity 1, mouse Rev1 C-terminal domain 104 residues - 11166.953 Da.
| 1 | GLY | SER | GLY | GLY | PHE | ARG | PRO | ALA | ALA | PRO | ||||
| 2 | ASN | LEU | ALA | GLY | ALA | VAL | GLU | PHE | SER | ASP | ||||
| 3 | VAL | LYS | THR | LEU | LEU | LYS | GLU | TRP | ILE | THR | ||||
| 4 | THR | ILE | SER | ASP | PRO | MET | GLU | GLU | ASP | ILE | ||||
| 5 | LEU | GLN | VAL | VAL | ARG | TYR | CYS | THR | ASP | LEU | ||||
| 6 | ILE | GLU | GLU | LYS | ASP | LEU | GLU | LYS | LEU | ASP | ||||
| 7 | LEU | VAL | ILE | LYS | TYR | MET | LYS | ARG | LEU | MET | ||||
| 8 | GLN | GLN | SER | VAL | GLU | SER | VAL | TRP | ASN | MET | ||||
| 9 | ALA | PHE | ASP | PHE | ILE | LEU | ASP | ASN | VAL | GLN | ||||
| 10 | VAL | VAL | LEU | GLN | GLN | THR | TYR | GLY | SER | THR | ||||
| 11 | LEU | LYS | VAL | THR |
Samples:
sample_1: Rev1, [U-100% 15N], 0.9 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_2: Rev1, [U-100% 13C; U-100% 15N], 0.9 – 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_3: Rev1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; PMSF 1 mM; EDTA 1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.113 M; pH: 7; 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_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D (HCA)CO(CA)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO(CA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HA(CA)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HA(CACO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 4D HCCONH TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 4D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 4D 13C-HMQC-NOESY-HSQC | sample_3 | isotropic | sample_conditions_1 |
| 4D 13C-HMQC-NOESY-15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
XEASY, Bartels et al. - peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
| BMRB | 18433 |
| PDB | |
| DBJ | BAB64933 |
| GB | AAF23323 AAH58093 EDL14541 EGW11994 EHB10584 |
| REF | NP_062516 XP_001490149 XP_002709984 XP_003503378 XP_004669836 |
| SP | Q920Q2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts