BMRB Entry 16266
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16266
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Citation: Xu, Yiren; Amero, Carlos; Pulukkunat, Dileep; Gopalan, Venkat; Foster, Mark. "Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions." J. Mol. Biol. 393, 1043-1055 (2009).
PubMed: 19733182
Assembly members:
Pfu_RPP29, polymer, 127 residues, 14953.2 Da.
Pfu_RPP21, polymer, 123 residues, 14751.8 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Pyrococcus furiosus Taxonomy ID: 2261 Superkingdom: Eukaryota Kingdom: not available Genus/species: Pyrococcus furiosus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET33b
Entity Sequences (FASTA):
Pfu_RPP29: MWRNSEERENRTSGRSQGSY
QEIIGRTWIFRGAHRGRVNK
KNIVWHELIGLKVRVVNSTH
PGYVGIEGYVIDETRNMLVI
AGENKVWKVPKDVCIFEFET
WDGTKIKISGEKLVGRPEMR
LKKRWRK
Pfu_RPP21: MAKYNEKKEKKRIAKERIDI
LFSLAERVFPYSPELAKRYV
ELALLVQQKAKVKIPRKWKR
RYCKKCHAFLVPGINARVRL
RQKRMPHIVVKCLECGHIMR
YPYIKEIKKRRIEKMEYGGL
VPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 490 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 744 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Subunit 1 | 1 |
| 2 | Subunit 2 | 2 |
| 3 | ZINC ION | 3 |
Entities:
Entity 1, Subunit 1 127 residues - 14953.2 Da.
Residues 1-18 are not present in the solution structure ensemble.
| 1 | MET | TRP | ARG | ASN | SER | GLU | GLU | ARG | GLU | ASN | ||||
| 2 | ARG | THR | SER | GLY | ARG | SER | GLN | GLY | SER | TYR | ||||
| 3 | GLN | GLU | ILE | ILE | GLY | ARG | THR | TRP | ILE | PHE | ||||
| 4 | ARG | GLY | ALA | HIS | ARG | GLY | ARG | VAL | ASN | LYS | ||||
| 5 | LYS | ASN | ILE | VAL | TRP | HIS | GLU | LEU | ILE | GLY | ||||
| 6 | LEU | LYS | VAL | ARG | VAL | VAL | ASN | SER | THR | HIS | ||||
| 7 | PRO | GLY | TYR | VAL | GLY | ILE | GLU | GLY | TYR | VAL | ||||
| 8 | ILE | ASP | GLU | THR | ARG | ASN | MET | LEU | VAL | ILE | ||||
| 9 | ALA | GLY | GLU | ASN | LYS | VAL | TRP | LYS | VAL | PRO | ||||
| 10 | LYS | ASP | VAL | CYS | ILE | PHE | GLU | PHE | GLU | THR | ||||
| 11 | TRP | ASP | GLY | THR | LYS | ILE | LYS | ILE | SER | GLY | ||||
| 12 | GLU | LYS | LEU | VAL | GLY | ARG | PRO | GLU | MET | ARG | ||||
| 13 | LEU | LYS | LYS | ARG | TRP | ARG | LYS |
Entity 2, Subunit 2 123 residues - 14751.8 Da.
Residues 1-8 and 106-123 are not present in the solution structure ensemble. Last six residues are leftover after cleavage of His-tag.
| 1 | MET | ALA | LYS | TYR | ASN | GLU | LYS | LYS | GLU | LYS | ||||
| 2 | LYS | ARG | ILE | ALA | LYS | GLU | ARG | ILE | ASP | ILE | ||||
| 3 | LEU | PHE | SER | LEU | ALA | GLU | ARG | VAL | PHE | PRO | ||||
| 4 | TYR | SER | PRO | GLU | LEU | ALA | LYS | ARG | TYR | VAL | ||||
| 5 | GLU | LEU | ALA | LEU | LEU | VAL | GLN | GLN | LYS | ALA | ||||
| 6 | LYS | VAL | LYS | ILE | PRO | ARG | LYS | TRP | LYS | ARG | ||||
| 7 | ARG | TYR | CYS | LYS | LYS | CYS | HIS | ALA | PHE | LEU | ||||
| 8 | VAL | PRO | GLY | ILE | ASN | ALA | ARG | VAL | ARG | LEU | ||||
| 9 | ARG | GLN | LYS | ARG | MET | PRO | HIS | ILE | VAL | VAL | ||||
| 10 | LYS | CYS | LEU | GLU | CYS | GLY | HIS | ILE | MET | ARG | ||||
| 11 | TYR | PRO | TYR | ILE | LYS | GLU | ILE | LYS | LYS | ARG | ||||
| 12 | ARG | ILE | GLU | LYS | MET | GLU | TYR | GLY | GLY | LEU | ||||
| 13 | VAL | PRO | ARG |
Entity 3, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Related Database Links:
| BMRB | 15935 15776 15935 |
| PDB | 2KI7 2K3R |
| GB | AAL81940 AAL81737 AFN05027 |
| REF | WP_048059096 NP_579342 WP_011012760 YP_006493319 |
| SP | Q8U007 Q8U0H6 |
| AlphaFold | Q8U007 Q8U0H6 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks