BMRB Entry 15289
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15289
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Title: 1H, 15N chemical shift assignment of the THAP domain 1-81 from human THAP1 protein PubMed: 18073205
Deposition date: 2007-06-06 Original release date: 2008-02-21
Authors: BESSIERE, Damien; CAMPAGNE, Sebastien; MILON, Alain; GERVAIS, Virginie
Citation: Bessiere, Damien; Lacroix, Chrystelle; Campagne, Sebastien; Ecochard, Vincent; Guillet, Valerie; Mourey, Lionel; Lopez, Frederic; Czaplicki, J.; Demange, Pascal; Milon, Alain; Cirard, Jean-Philippe; Gervais, Virginie. "Structure-Function Analysis of the THAP Zinc Finger of THAP1, a Large C2CH DNA-binding Module Linked to Rb/E2F Pathways." J. Biol. Chem. 283, 4352-4363 (2008).
Assembly members:
THAP_domain, polymer, 87 residues, Formula weight is not available
ZN, 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):
THAP_domain: MVQSCSAYGCKNRYDKDKPV
SFHKFPLTRPSLCKEWEAAV
RRKNFKPTKYSSICSEHFTP
DCFKRECNNKLLKENAVPTI
FLELVPR
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 76 |
1H chemical shifts | 565 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | THAP domain polypeptide | 1 |
2 | ZINC ION | 2 |
Entities:
Entity 1, THAP domain polypeptide 87 residues - Formula weight is not available
1 | MET | VAL | GLN | SER | CYS | SER | ALA | TYR | GLY | CYS | ||||
2 | LYS | ASN | ARG | TYR | ASP | LYS | ASP | LYS | PRO | VAL | ||||
3 | SER | PHE | HIS | LYS | PHE | PRO | LEU | THR | ARG | PRO | ||||
4 | SER | LEU | CYS | LYS | GLU | TRP | GLU | ALA | ALA | VAL | ||||
5 | ARG | ARG | LYS | ASN | PHE | LYS | PRO | THR | LYS | TYR | ||||
6 | SER | SER | ILE | CYS | SER | GLU | HIS | PHE | THR | PRO | ||||
7 | ASP | CYS | PHE | LYS | ARG | GLU | CYS | ASN | ASN | LYS | ||||
8 | LEU | LEU | LYS | GLU | ASN | ALA | VAL | PRO | THR | ILE | ||||
9 | PHE | LEU | GLU | LEU | VAL | PRO | ARG |
Entity 2, ZINC ION - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_U: THAP domain 1 mM; NaCl 10 mM; Tris 50 mM; DTT 1 mM
sample_U-15N: THAP domain, [U-15N], 1 mM; NaCl 10 mM; Tris 50 mM; DTT 1 mM
sample_conditions: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H NOESY | sample_U | isotropic | sample_conditions |
2D 1H-1H TOCSY | sample_U | isotropic | sample_conditions |
2D 1H-1H COSY | sample_U | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_U-15N | isotropic | sample_conditions |
3D 1H-15N NOESY | sample_U-15N | isotropic | sample_conditions |
3D 1H-15N TOCSY | sample_U-15N | isotropic | sample_conditions |
Software:
XEASY, Bartels et al. - chemical shift assignment
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 16485 |
PDB | |
DBJ | BAA91635 BAD96951 BAE02260 BAI45652 |
EMBL | CAG33537 CAH90563 |
GB | AAH21721 AAI02410 ADZ15806 AIC51723 AKI69887 |
REF | NP_001029820 NP_001125299 NP_001244808 NP_001271632 NP_060575 |
SP | Q3T0G1 Q4R3Q6 Q5RCE4 Q9NVV9 |
TPG | DAA14452 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts