BMRB Entry 16412
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16412
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Title: Solution structure of Rtt103 bound to CTD peptide PubMed: 20818393
Deposition date: 2009-07-21 Original release date: 2010-09-17
Authors: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Leeper, Thomas; Becker, Roland; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele
Citation: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Suh, Hyunsuk; Leeper, Thomas; Yang, Fan; Mutschler, Hannes; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele. "Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain." Nat. Struct. Mol. Biol. 17, 1195-1201 (2010).
Assembly members:
Rtt103 bound to CTD peptide, polymer, 142 residues, 15747.308 Da.
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET-28b
Entity Sequences (FASTA):
Rtt103 bound to CTD peptide: MAFSSEQFTTKLNTLEDSQE
SISSASKWLLLQYRDAPKVA
EMWKEYMLRPSVNTRRKLLG
LYLMNHVVQQAKGQKIIQFQ
DSFGKVAAEVLGRINQEFPR
DLKKKLSRVVNILKERNIFS
KQVVNDIERSLAAALEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 1001 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rtt103 bound to CTD peptide | 1 |
Entities:
Entity 1, Rtt103 bound to CTD peptide 142 residues - 15747.308 Da.
| 1 | MET | ALA | PHE | SER | SER | GLU | GLN | PHE | THR | THR | ||||
| 2 | LYS | LEU | ASN | THR | LEU | GLU | ASP | SER | GLN | GLU | ||||
| 3 | SER | ILE | SER | SER | ALA | SER | LYS | TRP | LEU | LEU | ||||
| 4 | LEU | GLN | TYR | ARG | ASP | ALA | PRO | LYS | VAL | ALA | ||||
| 5 | GLU | MET | TRP | LYS | GLU | TYR | MET | LEU | ARG | PRO | ||||
| 6 | SER | VAL | ASN | THR | ARG | ARG | LYS | LEU | LEU | GLY | ||||
| 7 | LEU | TYR | LEU | MET | ASN | HIS | VAL | VAL | GLN | GLN | ||||
| 8 | ALA | LYS | GLY | GLN | LYS | ILE | ILE | GLN | PHE | GLN | ||||
| 9 | ASP | SER | PHE | GLY | LYS | VAL | ALA | ALA | GLU | VAL | ||||
| 10 | LEU | GLY | ARG | ILE | ASN | GLN | GLU | PHE | PRO | ARG | ||||
| 11 | ASP | LEU | LYS | LYS | LYS | LEU | SER | ARG | VAL | VAL | ||||
| 12 | ASN | ILE | LEU | LYS | GLU | ARG | ASN | ILE | PHE | SER | ||||
| 13 | LYS | GLN | VAL | VAL | ASN | ASP | ILE | GLU | ARG | SER | ||||
| 14 | LEU | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 15 | HIS | HIS |
Samples:
sample_2: sodium chloride 120 mM; TRIS 10 mM; Rtt1030.5 – 1 mM; CTD1 – 1.5 mM; D2O 100%
sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
NMR spectrometers:
- Bruker DMX 500 MHz
- Bruker DMX 600 MHz
- Bruker DMX 750 MHz
- Varian INOVA 800 MHz
Related Database Links:
| BMRB | 16411 17044 |
| PDB | |
| DBJ | GAA22510 |
| EMBL | CAY78790 |
| GB | AAB64467 AAS56119 AHY75263 AJP37990 AJU58113 |
| REF | NP_010575 |
| SP | Q05543 |
| TPG | DAA12129 |
| AlphaFold | Q05543 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts