BMRB Entry 34200
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34200
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Title: NMR structure of the C-terminal domain of the human RPAP3 protein PubMed: 29844425
Deposition date: 2017-11-14 Original release date: 2018-04-13
Authors: Fabre, P.; Chagot, M.; Bragantini, B.; Manival, X.; Quinternet, M.
Citation: Maurizy, Chloe; Quinternet, Marc; Abel, Yoann; Verheggen, Celine; Santo, Paulo; Bourguet, Maxime; C F Paiva, Ana; Bragantini, Benoit; Chagot, Marie-Eve; Robert, Marie-Cecile; Abeza, Claire; Fabre, Philippe; Fort, Philippe; Vandermoere, Franck; M F Sousa, Pedro; Rain, Jean-Christophe; Charpentier, Bruno; Cianferani, Sarah; Bandeiras, Tiago; Pradet-Balade, Berengere; Manival, Xavier; Bertrand, Edouard. "The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones" Nat. Commun. 9, 2093-2093 (2018).
Assembly members:
entity_1, polymer, 135 residues, 15804.365 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):
entity_1: GPHMAQFATTVLPPIPANSF
QLESDFRQLKSSPDMLYQYL
KQIEPSLYPKLFQKNLDPDV
FNQIVKILHDFYIEKEKPLL
IFEILQRLSELKRFDMAVMF
MSETEKKIARALFNHIDKSG
LKDSSVEELKKRYGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 615 |
| 15N chemical shifts | 142 |
| 1H chemical shifts | 1041 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 135 residues - 15804.365 Da.
| 1 | GLY | PRO | HIS | MET | ALA | GLN | PHE | ALA | THR | THR | ||||
| 2 | VAL | LEU | PRO | PRO | ILE | PRO | ALA | ASN | SER | PHE | ||||
| 3 | GLN | LEU | GLU | SER | ASP | PHE | ARG | GLN | LEU | LYS | ||||
| 4 | SER | SER | PRO | ASP | MET | LEU | TYR | GLN | TYR | LEU | ||||
| 5 | LYS | GLN | ILE | GLU | PRO | SER | LEU | TYR | PRO | LYS | ||||
| 6 | LEU | PHE | GLN | LYS | ASN | LEU | ASP | PRO | ASP | VAL | ||||
| 7 | PHE | ASN | GLN | ILE | VAL | LYS | ILE | LEU | HIS | ASP | ||||
| 8 | PHE | TYR | ILE | GLU | LYS | GLU | LYS | PRO | LEU | LEU | ||||
| 9 | ILE | PHE | GLU | ILE | LEU | GLN | ARG | LEU | SER | GLU | ||||
| 10 | LEU | LYS | ARG | PHE | ASP | MET | ALA | VAL | MET | PHE | ||||
| 11 | MET | SER | GLU | THR | GLU | LYS | LYS | ILE | ALA | ARG | ||||
| 12 | ALA | LEU | PHE | ASN | HIS | ILE | ASP | LYS | SER | GLY | ||||
| 13 | LEU | LYS | ASP | SER | SER | VAL | GLU | GLU | LEU | LYS | ||||
| 14 | LYS | ARG | TYR | GLY | GLY |
Samples:
sample_1: RPAP3 C-terminal domain, [U-13C; U-15N], 1 mM; TCEP 0.5 mM; sodium chloride 150 mM; sodium phosphate 10 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | not available | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | not available | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | not available | sample_conditions_1 |
| 3D HNCA | sample_1 | not available | sample_conditions_1 |
| 3D HNCACB | sample_1 | not available | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | not available | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | not available | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | not available | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | not available | sample_conditions_1 |
| 3D (H)CCCONH | sample_1 | not available | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | not available | sample_conditions_1 |
| 3D HNHA | sample_1 | not available | sample_conditions_1 |
| 3D HNCO E.cosy | sample_1 | not available | sample_conditions_1 |
| 3D HNCACO | sample_1 | not available | sample_conditions_1 |
| 3D HNCO | sample_1 | not available | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | not available | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | not available | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | not available | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CARA, Keller and Wuthrich - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
TALOS, Cornilescu, Delaglio and Bax - structure calculation
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts