BMRB Entry 18434
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18434
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Title: C-terminal domain of human REV1 in complex with DNA-polymerase H (eta) PubMed: 22691049
Deposition date: 2012-05-01 Original release date: 2012-06-18
Authors: Pozhidaeva, Alexandra; Pustovalova, Yulia; Pustovalova, Irina; Korzhnev, Dmitry
Citation: Pozhidaeva, Alexandra; Pustovalova, Yulia; Bezsonova, Sanjay; Walker, Irina; Korzhnev, Graham. "NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase ." Biochemistry 51, 5506-5520 (2012).
Assembly members:
entity_1, polymer, 95 residues, 11011.758 Da.
entity_2, polymer, 16 residues, 1826.117 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GNLAGAVEFNDVKTLLREWI
TTISDPMEEDILQVVKYCTD
LIEEKDLEKLDLVIKYMKRL
MQQSVESVWNMAFDFILDNV
QVVLQQTYGSTLKVT
entity_2: QSTGTEPFFKQKSLLL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 382 |
15N chemical shifts | 97 |
1H chemical shifts | 639 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | C-terminal domain of human REV1 | 1 |
2 | DNA-polymerase H (eta) | 2 |
Entities:
Entity 1, C-terminal domain of human REV1 95 residues - 11011.758 Da.
1 | GLY | ASN | LEU | ALA | GLY | ALA | VAL | GLU | PHE | ASN | ||||
2 | ASP | VAL | LYS | THR | LEU | LEU | ARG | GLU | TRP | ILE | ||||
3 | THR | THR | ILE | SER | ASP | PRO | MET | GLU | GLU | ASP | ||||
4 | ILE | LEU | GLN | VAL | VAL | LYS | TYR | CYS | THR | ASP | ||||
5 | LEU | ILE | GLU | GLU | LYS | ASP | LEU | GLU | LYS | LEU | ||||
6 | ASP | LEU | VAL | ILE | LYS | TYR | MET | LYS | ARG | LEU | ||||
7 | MET | GLN | GLN | SER | VAL | GLU | SER | VAL | TRP | ASN | ||||
8 | MET | ALA | PHE | ASP | PHE | ILE | LEU | ASP | ASN | VAL | ||||
9 | GLN | VAL | VAL | LEU | GLN | GLN | THR | TYR | GLY | SER | ||||
10 | THR | LEU | LYS | VAL | THR |
Entity 2, DNA-polymerase H (eta) 16 residues - 1826.117 Da.
1 | GLN | SER | THR | GLY | THR | GLU | PRO | PHE | PHE | LYS | ||||
2 | GLN | LYS | SER | LEU | LEU | LEU |
Samples:
sample_1: REV1, [U-99% 13C; U-99% 15N], 0.9 mM; DNA-polymerase 0.9 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 0.25 mM; DTT 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS, Cornilescu, Delaglio and Bax - data analysis
CARA, Kurt W thrich - data analysis
NMR spectrometers:
- Varian Avance 800 MHz
- Varian Avance 500 MHz
Related Database Links:
BMRB | 18432 18455 |
PDB | |
DBJ | BAB21441 BAA81666 BAB18601 BAG51237 BAG53738 BAG57675 |
EMBL | CAB38231 CAH93279 |
GB | AAF06731 AAF18986 AAI30412 AAK43708 AAY24314 AAD43810 AAQ81300 ACQ91143 EAX04210 EAX04211 |
REF | NP_001032961 NP_001126930 NP_057400 XP_001160264 XP_001363717 NP_001278898 NP_006493 XP_003833292 XP_004048392 XP_005249243 |
SP | Q5R4N7 Q9UBZ9 Q9Y253 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts