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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17019
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Escobar-Cabrera, Eric; Lau, Desmond; Giovinazzi, Serena; Alexander, Ishov; McIntosh, Lawrence. "Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C" Structure 18, 1642-1653 (2010).
PubMed: 21134643
Assembly members:
DAXX, polymer, 94 residues, 10950.916 Da.
Rassf1C, polymer, 18 residues, 2149.186 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 Vector: pET28a
Entity Sequences (FASTA):
DAXX: GSHMGKKCYKLENEKLFEEF
LELCKMQTADHPEVVPFLYN
RQQRAHSLFLASAEFCNILS
RVLSRARSRPAKLYVYINEL
CTVLKAHSAKKKLN
Rassf1C: GSQEDSDSELEQYFTARW
Data type | Count |
13C chemical shifts | 387 |
15N chemical shifts | 115 |
1H chemical shifts | 790 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DAXX | 1 |
2 | Rassf1C | 2 |
Entity 1, DAXX 94 residues - 10950.916 Da.
residues 51-54 are residual from removing the His-tag with thrombin from a pET28a construct
1 | GLY | SER | HIS | MET | GLY | LYS | LYS | CYS | TYR | LYS | ||||
2 | LEU | GLU | ASN | GLU | LYS | LEU | PHE | GLU | GLU | PHE | ||||
3 | LEU | GLU | LEU | CYS | LYS | MET | GLN | THR | ALA | ASP | ||||
4 | HIS | PRO | GLU | VAL | VAL | PRO | PHE | LEU | TYR | ASN | ||||
5 | ARG | GLN | GLN | ARG | ALA | HIS | SER | LEU | PHE | LEU | ||||
6 | ALA | SER | ALA | GLU | PHE | CYS | ASN | ILE | LEU | SER | ||||
7 | ARG | VAL | LEU | SER | ARG | ALA | ARG | SER | ARG | PRO | ||||
8 | ALA | LYS | LEU | TYR | VAL | TYR | ILE | ASN | GLU | LEU | ||||
9 | CYS | THR | VAL | LEU | LYS | ALA | HIS | SER | ALA | LYS | ||||
10 | LYS | LYS | LEU | ASN |
Entity 2, Rassf1C 18 residues - 2149.186 Da.
residue 22 is residual from removing the GST with thrombin from a PGEX construct Residue 39 is non-native, introduced to quantify the peptide.
1 | GLY | SER | GLN | GLU | ASP | SER | ASP | SER | GLU | LEU | ||||
2 | GLU | GLN | TYR | PHE | THR | ALA | ARG | TRP |
Dr: DAXX, [U-100% 13C; U-100% 15N], 1.1 mM; Rassf1C 1.65 mM; H2O 95%; D2O 5%
Rd: DAXX 1.8 mM; Rassf1C, [U-100% 13C; U-100% 15N], 1.2 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | Dr | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | Rd | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | Rd | isotropic | sample_conditions_1 |
3D HNCACB | Rd | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | Dr | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | Dr | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | Dr | isotropic | sample_conditions_1 |
(H)CC(CO)NH-TOCSY | Dr | isotropic | sample_conditions_1 |
HCC(CO)NH-TOCSY | Dr | isotropic | sample_conditions_1 |
(HB)CB(CGCD)HD | Dr | isotropic | sample_conditions_1 |
(HB)CB(CGCDCE)HE | Dr | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | Dr | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | Dr | isotropic | sample_conditions_1 |
13C/15N isotope-filtered NOESY-HSQC | Dr | isotropic | sample_conditions_1 |
13C/15N isotope-filtered NOESY-HSQC | Rd | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | Rd | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | Rd | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | Rd | isotropic | sample_conditions_1 |
(H)CC(CO)NH-TOCSY | Rd | isotropic | sample_conditions_1 |
HCC(CO)NH-TOCSY | Rd | isotropic | sample_conditions_1 |
(HB)CB(CGCD)HD | Rd | isotropic | sample_conditions_1 |
(HB)CB(CGCD)HD-TOCSY | Rd | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | Rd | isotropic | sample_conditions_1 |
ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, semi automatic peak assignments, structure solution
BMRB | 17018 |
PDB | |
DBJ | BAA34295 BAD92730 BAF84876 BAG35867 BAG64733 BAF85327 |
EMBL | CAB09986 CAB09989 CAG33366 |
GB | AAB66585 AAB92671 AAC39853 AAC72843 AAI09074 AAC16001 AAC70910 AAD30061 AAD44175 AAH02173 |
REF | NP_001135441 NP_001135442 NP_001241646 NP_001341 XP_001170728 NP_001007755 NP_001068910 NP_062687 NP_733831 XP_001100583 |
SP | Q9UER7 |
TPG | DAA16909 |
AlphaFold | Q9UER7 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks