BMRB Entry 25232
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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/BMR25232
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Title: Solution structure of the F231L mutant ERCC1-XPF dimerization region PubMed: 26085086
Deposition date: 2014-09-17 Original release date: 2015-06-22
Authors: Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Kaptein, Robert; Hoeijmakers, Jan; Boelens, Rolf
Citation: Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Boelens, Rolf. "The Cerebro-Oculo-Facio-Skeletal (COFS) Syndrome point mutation F231L in the ERCC1 DNA repair protein causes dissociation of the ERCC1-XPF complex" J. Biol. Chem. ., .-. (2015).
Assembly members:
entity_1, polymer, 96 residues, 10985.764 Da.
entity_2, polymer, 84 residues, 9230.592 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: RIRRRYNMADLLMEKLEQDL
VSRVTECLTTVKSVNKTDSQ
TLLTTFGSLEQLIAASREDL
ALCPGLGPQKARRLFDVLHE
PFLKVPGGLEHHHHHH
entity_2: MDSETLPESEKYNPGPQDFL
LKMPGVNAKNCRSLMHHVKN
IAELAALSQDELTSILGNAA
NAKQLYDFIHTSFAEVVSKG
KGKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 695 |
| 15N chemical shifts | 172 |
| 1H chemical shifts | 1173 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 96 residues - 10985.764 Da.
| 1 | ARG | ILE | ARG | ARG | ARG | TYR | ASN | MET | ALA | ASP | ||||
| 2 | LEU | LEU | MET | GLU | LYS | LEU | GLU | GLN | ASP | LEU | ||||
| 3 | VAL | SER | ARG | VAL | THR | GLU | CYS | LEU | THR | THR | ||||
| 4 | VAL | LYS | SER | VAL | ASN | LYS | THR | ASP | SER | GLN | ||||
| 5 | THR | LEU | LEU | THR | THR | PHE | GLY | SER | LEU | GLU | ||||
| 6 | GLN | LEU | ILE | ALA | ALA | SER | ARG | GLU | ASP | LEU | ||||
| 7 | ALA | LEU | CYS | PRO | GLY | LEU | GLY | PRO | GLN | LYS | ||||
| 8 | ALA | ARG | ARG | LEU | PHE | ASP | VAL | LEU | HIS | GLU | ||||
| 9 | PRO | PHE | LEU | LYS | VAL | PRO | GLY | GLY | LEU | GLU | ||||
| 10 | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, entity_2 84 residues - 9230.592 Da.
| 1 | MET | ASP | SER | GLU | THR | LEU | PRO | GLU | SER | GLU | ||||
| 2 | LYS | TYR | ASN | PRO | GLY | PRO | GLN | ASP | PHE | LEU | ||||
| 3 | LEU | LYS | MET | PRO | GLY | VAL | ASN | ALA | LYS | ASN | ||||
| 4 | CYS | ARG | SER | LEU | MET | HIS | HIS | VAL | LYS | ASN | ||||
| 5 | ILE | ALA | GLU | LEU | ALA | ALA | LEU | SER | GLN | ASP | ||||
| 6 | GLU | LEU | THR | SER | ILE | LEU | GLY | ASN | ALA | ALA | ||||
| 7 | ASN | ALA | LYS | GLN | LEU | TYR | ASP | PHE | ILE | HIS | ||||
| 8 | THR | SER | PHE | ALA | GLU | VAL | VAL | SER | LYS | GLY | ||||
| 9 | LYS | GLY | LYS | LYS |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.4 mM; entity_2, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 8%; H2O 92%; sodium phosphate 50 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 290 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D HSQC | sample_1 | isotropic | sample_conditions_1 |
| triple resonance | sample_1 | isotropic | sample_conditions_1 |
| NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CING, Doreleijers et al - validation
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAG37398 BAG52472 |
| GB | AAA35810 AAA52394 AAC16253 AAH08930 AAM34796 |
| PRF | 1403276A |
| REF | NP_001181860 NP_001974 XP_003817569 XP_003915760 XP_003915761 |
| SP | P07992 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts