BMRB Entry 19302
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19302
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution Structure of ERCC4 domain of human FAAP24 PubMed: 23999858
Deposition date: 2013-06-18 Original release date: 2013-09-16
Authors: Wu, Fangming; Han, Xiao; Shi, Chaowei; Gong, Weimin; Tian, Changlin
Citation: Wang, Yucai; Han, Xiao; Wu, Fangming; Leung, Justin; Lowery, Megan; Do, Huong; Chen, Junjie; Shi, Chaowei; Tian, Changlin; Li, Lei; Gong, Weimin. "Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response." Cell Res. 23, 1215-1228 (2013).
Assembly members:
FAAP24-ERCC4, polymer, 147 residues, 15680.295 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):
FAAP24-ERCC4: MEKNPPDDTGPVHVPLGHIV
ANEKWRGSQLAQEMQGKIKL
IFEDGLTPDFYLSNRCCILY
VTEADLVAGNGYRKRLVRVR
NSNNLKGIVVVEKTRMSEQY
FPALQKFTVLDLGMVLLPVA
SQMEASCLVIQLVQEQTKEL
EHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 867 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ERCC4 domain of human FAAP24 | 1 |
Entities:
Entity 1, ERCC4 domain of human FAAP24 147 residues - 15680.295 Da.
| 1 | MET | GLU | LYS | ASN | PRO | PRO | ASP | ASP | THR | GLY | ||||
| 2 | PRO | VAL | HIS | VAL | PRO | LEU | GLY | HIS | ILE | VAL | ||||
| 3 | ALA | ASN | GLU | LYS | TRP | ARG | GLY | SER | GLN | LEU | ||||
| 4 | ALA | GLN | GLU | MET | GLN | GLY | LYS | ILE | LYS | LEU | ||||
| 5 | ILE | PHE | GLU | ASP | GLY | LEU | THR | PRO | ASP | PHE | ||||
| 6 | TYR | LEU | SER | ASN | ARG | CYS | CYS | ILE | LEU | TYR | ||||
| 7 | VAL | THR | GLU | ALA | ASP | LEU | VAL | ALA | GLY | ASN | ||||
| 8 | GLY | TYR | ARG | LYS | ARG | LEU | VAL | ARG | VAL | ARG | ||||
| 9 | ASN | SER | ASN | ASN | LEU | LYS | GLY | ILE | VAL | VAL | ||||
| 10 | VAL | GLU | LYS | THR | ARG | MET | SER | GLU | GLN | TYR | ||||
| 11 | PHE | PRO | ALA | LEU | GLN | LYS | PHE | THR | VAL | LEU | ||||
| 12 | ASP | LEU | GLY | MET | VAL | LEU | LEU | PRO | VAL | ALA | ||||
| 13 | SER | GLN | MET | GLU | ALA | SER | CYS | LEU | VAL | ILE | ||||
| 14 | GLN | LEU | VAL | GLN | GLU | GLN | THR | LYS | GLU | LEU | ||||
| 15 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; H2O 90%; D2O 10%
sample_2: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; D2O 100%
sample_conditions_1: ionic strength: 0.35 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
SPARKY, Goddard - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 850 MHz
- Varian INOVA 700 MHz
Related Database Links:
| UNP | Q9BTP7 |
| PDB | |
| DBJ | BAG54708 |
| GB | AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732 |
| REF | NP_689479 XP_003780763 XP_003915337 XP_004093270 XP_005259450 |
| SP | Q9BTP7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts