BMRB Entry 18433
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18433
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Title: Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa PubMed: 22700975
Deposition date: 2012-05-01 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_1, polymer, 119 residues, 11166.953 Da.
entity_2, polymer, 25 residues, 1747.002 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_1: GSGGGAQDLSSLLPGQSSCF
RPAAPNLAGAVEFSDVKTLL
KEWITTISDPMEEDILQVVR
YCTDLIEEKDLEKLDLVIKY
MKRLMQQSVESVWNMAFDFI
LDNVQVVLQQTYGSTLKVT
entity_2: SHMSHKKSFFDKKRSERISN
CQDTS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 460 |
15N chemical shifts | 132 |
1H chemical shifts | 960 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | mouse Rev1 CTD | 1 |
2 | RIR of Pol Kappa | 2 |
Entities:
Entity 1, mouse Rev1 CTD 119 residues - 11166.953 Da.
1 | GLY | SER | GLY | GLY | GLY | ALA | GLN | ASP | LEU | SER | ||||
2 | SER | LEU | LEU | PRO | GLY | GLN | SER | SER | CYS | PHE | ||||
3 | ARG | PRO | ALA | ALA | PRO | ASN | LEU | ALA | GLY | ALA | ||||
4 | VAL | GLU | PHE | SER | ASP | VAL | LYS | THR | LEU | LEU | ||||
5 | LYS | GLU | TRP | ILE | THR | THR | ILE | SER | ASP | PRO | ||||
6 | MET | GLU | GLU | ASP | ILE | LEU | GLN | VAL | VAL | ARG | ||||
7 | TYR | CYS | THR | ASP | LEU | ILE | GLU | GLU | LYS | ASP | ||||
8 | LEU | GLU | LYS | LEU | ASP | LEU | VAL | ILE | LYS | TYR | ||||
9 | MET | LYS | ARG | LEU | MET | GLN | GLN | SER | VAL | GLU | ||||
10 | SER | VAL | TRP | ASN | MET | ALA | PHE | ASP | PHE | ILE | ||||
11 | LEU | ASP | ASN | VAL | GLN | VAL | VAL | LEU | GLN | GLN | ||||
12 | THR | TYR | GLY | SER | THR | LEU | LYS | VAL | THR |
Entity 2, RIR of Pol Kappa 25 residues - 1747.002 Da.
1 | SER | HIS | MET | SER | HIS | LYS | LYS | SER | PHE | PHE | ||||
2 | ASP | LYS | LYS | ARG | SER | GLU | ARG | ILE | SER | ASN | ||||
3 | CYS | GLN | ASP | THR | SER |
Samples:
sample_1: Rev1_CTD, [U-100% 15N], 0.7 1 mM; RIR, [U-100% 15N], 0.7 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_2: Rev1_CTD, [U-100% 13C; U-100% 15N], 0.7 1 mM; RIR, [U-100% 13C; U-100% 15N], 0.7 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_3: Rev1_CTD, [U-100% 13C; U-100% 15N], 0.7 1 mM; RIR, [U-100% 13C; U-100% 15N], 0.7 1 mM; sodium phosphate 25 mM; potassium chloride 100 mM; DTT 10 mM; EDTA 1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 310 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 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 HN(COCA)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 HNCO | sample_2 | isotropic | sample_conditions_1 |
3D (HCA)CO(CA)NH | sample_2 | isotropic | sample_conditions_1 |
4D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
4D HCCONH-TOCSY | sample_3 | 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 13C-HMQC-NOESY-15N-HSQC | sample_2 | isotropic | sample_conditions_1 |
4D 13C-HMQC-NOESY-13C-HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
TALOS, Cornilescu, Delaglio and Bax - data analysis
SPARKY, Goddard - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
BMRB | 18431 |
PDB | |
DBJ | BAB64933 |
GB | AAF23323 AAH58093 EDL14541 |
REF | NP_062516 XP_006496216 XP_006496217 XP_006496218 XP_006496219 |
SP | Q920Q2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts