BMRB Entry 15693
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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/BMR15693
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Title: Solution structure of Human Pax8 Paired Box Domain PubMed: 18829450
Deposition date: 2008-03-26 Original release date: 2008-09-22
Authors: Codutti, Luca; Esposito, Gennaro; Corazza, Alessandra; Fogolari, Federico; Tell, Gianluca; Vascotto, Carlo; van Ingen, Hugo; Boelens, Rolf; Viglino, Paolo; Quadrifoglio, Franco
Citation: Codutti, Luca; van Ingen, Hugo; Vascotto, Carlo; Fogolari, Federico; Corazza, Alessandra; Tell, Gianluca; Quadrifoglio, Franco; Viglino, Paolo; Boelens, Rolf; Esposito, Gennaro. "The solution structure of DNA-free Pax-8 Paired Box domain accounts for redox regulation of transcriptional activity in Pax protein family" J. Biol. Chem. 283, 33321-33328 (2008).
Assembly members:
Pax8_Paired_Box_Domain, polymer, 159 residues, 17416.87 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):
Pax8_Paired_Box_Domain: MPHNSIRSGHGGLNQLGGAF
VNGRPLPEVVRQRIVDLAHQ
GVRPCDISRQLRVSHGCVSK
ILGRYYETGSIRPGVIGGSK
PKVATPKVVEKIGDYKRQNP
TMFAWEIRDRLLAEGVCDND
TVPSVSSINRIIRTKVQQPF
NLPMDSGAPGGGSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 558 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 903 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Pax8 PAIRED | 1 |
Entities:
Entity 1, Pax8 PAIRED 159 residues - 17416.87 Da.
| 1 | MET | PRO | HIS | ASN | SER | ILE | ARG | SER | GLY | HIS | ||||
| 2 | GLY | GLY | LEU | ASN | GLN | LEU | GLY | GLY | ALA | PHE | ||||
| 3 | VAL | ASN | GLY | ARG | PRO | LEU | PRO | GLU | VAL | VAL | ||||
| 4 | ARG | GLN | ARG | ILE | VAL | ASP | LEU | ALA | HIS | GLN | ||||
| 5 | GLY | VAL | ARG | PRO | CYS | ASP | ILE | SER | ARG | GLN | ||||
| 6 | LEU | ARG | VAL | SER | HIS | GLY | CYS | VAL | SER | LYS | ||||
| 7 | ILE | LEU | GLY | ARG | TYR | TYR | GLU | THR | GLY | SER | ||||
| 8 | ILE | ARG | PRO | GLY | VAL | ILE | GLY | GLY | SER | LYS | ||||
| 9 | PRO | LYS | VAL | ALA | THR | PRO | LYS | VAL | VAL | GLU | ||||
| 10 | LYS | ILE | GLY | ASP | TYR | LYS | ARG | GLN | ASN | PRO | ||||
| 11 | THR | MET | PHE | ALA | TRP | GLU | ILE | ARG | ASP | ARG | ||||
| 12 | LEU | LEU | ALA | GLU | GLY | VAL | CYS | ASP | ASN | ASP | ||||
| 13 | THR | VAL | PRO | SER | VAL | SER | SER | ILE | ASN | ARG | ||||
| 14 | ILE | ILE | ARG | THR | LYS | VAL | GLN | GLN | PRO | PHE | ||||
| 15 | ASN | LEU | PRO | MET | ASP | SER | GLY | ALA | PRO | GLY | ||||
| 16 | GLY | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Pax8 Paired Box Domain, [U-100% 13C; U-100% 15N], 0.9 ± 0.1 mM; DSS 40 ± 5 uM; sodium phosphate 50 ± 5 mM; sodium azide 0.1 ± 0.05 %; DTT, [U-100% 2H], 15 ± 2 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 298.00 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC CT | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS v(NMR-Pipe 3.5), Cornilescu, Delaglio and Bax - data analysis
ProcheckNMR v3.4, Laskowski and MacArthur - validation
TOPSPIN v1.3, Bruker Biospin - collection, processing
CARA v1.8.4, Rochus Keller - chemical shift assignment, data analysis, peak picking
DISCOVER v2.98, Accelrys Software Inc. - refinement
AQUA v3.2, Rullmann, Doreleijers and Kaptein - validation
WhatIF, Vriend - validation
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 2 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAF84880 BAI46656 |
| EMBL | CAA40725 CAA58571 CAA58572 CAA63930 CAA67904 |
| GB | AAA03539 AAB34216 AAB34217 AAB34218 AAH01060 |
| REF | NP_001003248 NP_001126820 NP_001128942 NP_003457 NP_035170 |
| SP | P47240 P51974 Q00288 Q06710 Q5R9M8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts