BMRB Entry 34728
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34728
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: Blatter, Markus; Meylan, Charlotte; Clery, Antoine; Giambruno, Roberto; Nikolaev, Yaroslav; Heidecker, Michel; Solanki, Jessica Arvindbhai; Diaz, Manuel; Gabellini, Davide; Allain, Frederic H-T. "RNA binding induces an allosteric switch in Cyp33 to repress MLL1-mediated transcription" Sci. Adv. 9, eadf5330-eadf5330 (2023).
PubMed: 37075125
Assembly members:
entity_1, polymer, 93 residues, 10349.721 Da.
entity_2, polymer, 64 residues, 7437.360 Da.
entity_3, polymer, 13 residues, 1407.620 Da.
entity_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 Vector: PTYB12
Entity Sequences (FASTA):
entity_1: AGHMATTKRVLYVGGLAEEV
DDKVLHAAFIPFGDITDIQI
PLDYETEKHRGFAFVEFELA
EDAAAAIDNMNESELFGRTI
RVNLAKPMRIKEG
entity_2: AKGNFCPLCDKCYDDDDYES
KMMQCGKCDRWVHSKCENLS
DEMYEILSNLPESVAYTCVN
CTER
entity_3: ARTXQTARKSTGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 459 |
| 15N chemical shifts | 155 |
| 1H chemical shifts | 1062 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
| 3 | unit_3 | 3 |
| 4 | unit_4 | 4 |
| 5 | unit_5 | 4 |
Entities:
Entity 1, unit_1 93 residues - 10349.721 Da.
| 1 | ALA | GLY | HIS | MET | ALA | THR | THR | LYS | ARG | VAL | ||||
| 2 | LEU | TYR | VAL | GLY | GLY | LEU | ALA | GLU | GLU | VAL | ||||
| 3 | ASP | ASP | LYS | VAL | LEU | HIS | ALA | ALA | PHE | ILE | ||||
| 4 | PRO | PHE | GLY | ASP | ILE | THR | ASP | ILE | GLN | ILE | ||||
| 5 | PRO | LEU | ASP | TYR | GLU | THR | GLU | LYS | HIS | ARG | ||||
| 6 | GLY | PHE | ALA | PHE | VAL | GLU | PHE | GLU | LEU | ALA | ||||
| 7 | GLU | ASP | ALA | ALA | ALA | ALA | ILE | ASP | ASN | MET | ||||
| 8 | ASN | GLU | SER | GLU | LEU | PHE | GLY | ARG | THR | ILE | ||||
| 9 | ARG | VAL | ASN | LEU | ALA | LYS | PRO | MET | ARG | ILE | ||||
| 10 | LYS | GLU | GLY |
Entity 2, unit_2 64 residues - 7437.360 Da.
| 1 | ALA | LYS | GLY | ASN | PHE | CYS | PRO | LEU | CYS | ASP | ||||
| 2 | LYS | CYS | TYR | ASP | ASP | ASP | ASP | TYR | GLU | SER | ||||
| 3 | LYS | MET | MET | GLN | CYS | GLY | LYS | CYS | ASP | ARG | ||||
| 4 | TRP | VAL | HIS | SER | LYS | CYS | GLU | ASN | LEU | SER | ||||
| 5 | ASP | GLU | MET | TYR | GLU | ILE | LEU | SER | ASN | LEU | ||||
| 6 | PRO | GLU | SER | VAL | ALA | TYR | THR | CYS | VAL | ASN | ||||
| 7 | CYS | THR | GLU | ARG |
Entity 3, unit_3 13 residues - 1407.620 Da.
| 1 | ALA | ARG | THR | M3L | GLN | THR | ALA | ARG | LYS | SER | ||||
| 2 | THR | GLY | GLY |
Entity 4, unit_4 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 15N], 1 mM; HISTONE-LYSINE N-METHYLTRANSFERASE 2A, [U-100% 15N], 1 mM; HISTONE H3 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM; zinc chloride 50 uM
sample_2: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 13C; U-100% 15N], 1 mM; HISTONE-LYSINE N-METHYLTRANSFERASE 2A, [U-100% 13C; U-100% 15N], 1 mM; HISTONE H3 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM; zinc chloride 10 uM
sample_3: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 13C; U-100% 15N], 1 mM; HISTONE-LYSINE N-METHYLTRANSFERASE 2A 1 mM; HISTONE H3 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM; zinc chloride 10 uM
sample_4: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E 1 mM; HISTONE-LYSINE N-METHYLTRANSFERASE 2A, [U-100% 13C; U-100% 15N], 1 mM; HISTONE H3 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM; zinc chloride 10 uM
sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 310.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D F3-FILTERED- F2-EDITED 13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D F2- FILTERED NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D F3-FILTERED- F2-EDITED 13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D F3-FILTERED- F2-EDITED 13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D F2- FILTERED NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D F2- FILTERED NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
Software:
Amber, CASE, DARDEN, CHEATHAM, III, SIMMERLING, WANG, DUKE, LUO, ... AND KOLLMAN - refinement
CYANA v3, Guntert, Mumenthaler and Wuthrich - structure calculation
Sparky, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE III 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks