BMRB Entry 34201
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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/BMR34201
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Title: Rtt109 peptide bound to Asf1 PubMed: 29300933
Deposition date: 2017-11-21 Original release date: 2017-12-21
Authors: Lercher, L.; Kirkpatrick, J.; Carlomagno, T.
Citation: Lercher, Lukas; Danilenko, Nataliya; Kirkpatrick, John; Carlomagno, Teresa. "Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation" Nucleic Acids Res. 46, 2279-2289 (2018).
Assembly members:
entity_1, polymer, 172 residues, 19327.652 Da.
entity_2, polymer, 15 residues, 1687.207 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GAMGSIVSLLGIKVLNNPAK
FTDPYEFEITFECLESLKHD
LEWKLTYVGSSRSLDHDQEL
DSILVGPVPVGVNKFVFSAD
PPSAELIPASELVSVTVILL
SCSYDGREFVRVGYYVNNEY
DEEELRENPPAKVQVDHIVR
NILAEKPRVTRFNIVWDNEN
EGDLYPPEQPGV
entity_2: LAITMLKPRKKAKAL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 750 |
| 15N chemical shifts | 176 |
| 1H chemical shifts | 1494 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 172 residues - 19327.652 Da.
| 1 | GLY | ALA | MET | GLY | SER | ILE | VAL | SER | LEU | LEU | ||||
| 2 | GLY | ILE | LYS | VAL | LEU | ASN | ASN | PRO | ALA | LYS | ||||
| 3 | PHE | THR | ASP | PRO | TYR | GLU | PHE | GLU | ILE | THR | ||||
| 4 | PHE | GLU | CYS | LEU | GLU | SER | LEU | LYS | HIS | ASP | ||||
| 5 | LEU | GLU | TRP | LYS | LEU | THR | TYR | VAL | GLY | SER | ||||
| 6 | SER | ARG | SER | LEU | ASP | HIS | ASP | GLN | GLU | LEU | ||||
| 7 | ASP | SER | ILE | LEU | VAL | GLY | PRO | VAL | PRO | VAL | ||||
| 8 | GLY | VAL | ASN | LYS | PHE | VAL | PHE | SER | ALA | ASP | ||||
| 9 | PRO | PRO | SER | ALA | GLU | LEU | ILE | PRO | ALA | SER | ||||
| 10 | GLU | LEU | VAL | SER | VAL | THR | VAL | ILE | LEU | LEU | ||||
| 11 | SER | CYS | SER | TYR | ASP | GLY | ARG | GLU | PHE | VAL | ||||
| 12 | ARG | VAL | GLY | TYR | TYR | VAL | ASN | ASN | GLU | TYR | ||||
| 13 | ASP | GLU | GLU | GLU | LEU | ARG | GLU | ASN | PRO | PRO | ||||
| 14 | ALA | LYS | VAL | GLN | VAL | ASP | HIS | ILE | VAL | ARG | ||||
| 15 | ASN | ILE | LEU | ALA | GLU | LYS | PRO | ARG | VAL | THR | ||||
| 16 | ARG | PHE | ASN | ILE | VAL | TRP | ASP | ASN | GLU | ASN | ||||
| 17 | GLU | GLY | ASP | LEU | TYR | PRO | PRO | GLU | GLN | PRO | ||||
| 18 | GLY | VAL |
Entity 2, entity_2 15 residues - 1687.207 Da.
| 1 | LEU | ALA | ILE | THR | MET | LEU | LYS | PRO | ARG | LYS | ||||
| 2 | LYS | ALA | LYS | ALA | LEU |
Samples:
sample_1: Histone chaperone Asf1, [U-99% 13C; U-99% 15N], 0.5 mM; histone acetyltransferase Rtt109 C-terminus 3 mM
sample_2: Histone chaperone Asf1, [U-99% 13C; U-99% 15N], 0.15 mM; histone acetyltransferase Rtt109 C-terminus 0.5 mM
sample_3: histone acetyltransferase Rtt109 C-terminus 0.15 mM; Histone chaperone ASF1, [U-99% 13C; U-99% 15N; U-99% 2D], 0.5 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| (HB)CB(CGCD)HD | 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 13C,15N filtered 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY-HSQC | sample_1 | anisotropic | sample_conditions_2 |
| 2D 1H-15N TROSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis v2.4.2, CCPN - chemical shift assignment, peak picking
CNS v1.21, Brunger, Adams, Clore, Delano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warren - structure calculation
ARIA v2.3, W. Rieping, M. Habeck, B. Bardiaux, A. Bernard, T.E. Malliavin, M. Nilges - structure calculation
PALES, M. Zweckstetter - data analysis
TALOS-N, Y. Shen, A. Bax - data analysis
NMR spectrometers:
- Bruker Avance III HD 850 MHz
- Bruker Avance III HD 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts