BMRB Entry 19182
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19182
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of human Aprataxin PubMed: 23943084
Deposition date: 2013-04-19 Original release date: 2013-05-17
Authors: Bellstedt, Peter; Seiboth, Thomas; Goerlach, Matthias
Citation: Bellstedt, Peter; Seiboth, Thomas; Haefner, Sabine; Kutscha, Henriette; Ramachandran, Ramadurai; Goerlach, Matthias. "Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets" J. Biomol. NMR 57, 65-72 (2013).
Assembly members:
Aprataxin, polymer, 202 residues, 23387 Da.
ZINC ION, non-polymer, 65.409 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):
Aprataxin: GSHMLECSVPLKKGKDAPIK
KESLGHWSQGLKISMQDPKM
QVYKDEQVVVIKDKYPKARY
HWLVLPWTSISSLKAVAREH
LELLKHMHTVGEKVIVDFAG
SSKLRFRLGYHAIPSMSHVH
LHVISQDFDSPCLKNKKHWN
SFNTEYFLESQAVIEMVQEA
GRVTVRDGMPELLKLPLRCH
ECQQLLPSIPQLKEHLRKHW
TQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 334 |
15N chemical shifts | 150 |
1H chemical shifts | 150 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Aprataxin, chain 1 | 1 |
2 | Aprataxin, chain 2 | 1 |
3 | zinc ion | 2 |
Entities:
Entity 1, Aprataxin, chain 1 202 residues - 23387 Da.
Residues 1-6 are vector coded residues
1 | GLY | SER | HIS | MET | LEU | GLU | CYS | SER | VAL | PRO | ||||
2 | LEU | LYS | LYS | GLY | LYS | ASP | ALA | PRO | ILE | LYS | ||||
3 | LYS | GLU | SER | LEU | GLY | HIS | TRP | SER | GLN | GLY | ||||
4 | LEU | LYS | ILE | SER | MET | GLN | ASP | PRO | LYS | MET | ||||
5 | GLN | VAL | TYR | LYS | ASP | GLU | GLN | VAL | VAL | VAL | ||||
6 | ILE | LYS | ASP | LYS | TYR | PRO | LYS | ALA | ARG | TYR | ||||
7 | HIS | TRP | LEU | VAL | LEU | PRO | TRP | THR | SER | ILE | ||||
8 | SER | SER | LEU | LYS | ALA | VAL | ALA | ARG | GLU | HIS | ||||
9 | LEU | GLU | LEU | LEU | LYS | HIS | MET | HIS | THR | VAL | ||||
10 | GLY | GLU | LYS | VAL | ILE | VAL | ASP | PHE | ALA | GLY | ||||
11 | SER | SER | LYS | LEU | ARG | PHE | ARG | LEU | GLY | TYR | ||||
12 | HIS | ALA | ILE | PRO | SER | MET | SER | HIS | VAL | HIS | ||||
13 | LEU | HIS | VAL | ILE | SER | GLN | ASP | PHE | ASP | SER | ||||
14 | PRO | CYS | LEU | LYS | ASN | LYS | LYS | HIS | TRP | ASN | ||||
15 | SER | PHE | ASN | THR | GLU | TYR | PHE | LEU | GLU | SER | ||||
16 | GLN | ALA | VAL | ILE | GLU | MET | VAL | GLN | GLU | ALA | ||||
17 | GLY | ARG | VAL | THR | VAL | ARG | ASP | GLY | MET | PRO | ||||
18 | GLU | LEU | LEU | LYS | LEU | PRO | LEU | ARG | CYS | HIS | ||||
19 | GLU | CYS | GLN | GLN | LEU | LEU | PRO | SER | ILE | PRO | ||||
20 | GLN | LEU | LYS | GLU | HIS | LEU | ARG | LYS | HIS | TRP | ||||
21 | THR | GLN |
Entity 2, zinc ion - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: Aprataxin, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-2H], 10 mM; sodium chloride 150 mM; sodium azide 0.05 w/v; H2O 90%; D2O 10%
sample_2: Aprataxin, [U-13C; U-15N]; [U-14N; U12C]-specific amino acid, 0.38 mM; TRIS, [U-2H], 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
standard_condition: ionic strength: 160 mM; pH: 7.5; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | standard_condition |
3D HNCO | sample_1 | isotropic | standard_condition |
3D HN(CA)CO | sample_1 | isotropic | standard_condition |
3D HNCA | sample_1 | isotropic | standard_condition |
3D HN(CO)CA | sample_1 | isotropic | standard_condition |
2D 1H-15N HSQC | sample_2 | isotropic | standard_condition |
2D HN(CO) | sample_1 | isotropic | standard_condition |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CcpNMR v2.2.2, CCPN - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 750 MHz
Related Database Links:
UniProtKB | Q7Z2E3-1 |
PDB | |
DBJ | BAA90985 BAD51939 BAG51552 BAI47119 BAK31015 |
EMBL | CAD98041 |
GB | AAH01628 AAH32650 AAI04882 AAK91768 AAP86319 |
REF | NP_001182177 NP_001182178 NP_001182179 NP_001182180 NP_001182183 |
SP | Q7Z2E3 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts