BMRB Entry 17557
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17557
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer PubMed: 22135285
Deposition date: 2011-03-30 Original release date: 2011-12-14
Authors: Lee, Ka-Ming; Yu, Conny Wing-Heng; Chiu, Teddy Yu-Hin; Sze, Kong-Hung; Shaw, Pang-Chui; Wong, Kam-Bo
Citation: Lee, Ka-Ming; Yu, Conny Wing-Heng; Chiu, Teddy Yu-Hin; Sze, Kong-Hung; Shaw, Pang-Chui; Wong, Kam-Bo. "Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex." Nucleic Acids Res. 40, 3172-3182 (2012).
Assembly members:
entity_1, polymer, 69 residues, 7088.202 Da.
entity_2, polymer, 70 residues, 7207.247 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: MASVSELACIYSALILHDDE
VTVTEDKINALIKAAGVNVE
PFWPGLFAKALANVNIGSLI
CNVGAGGPA
entity_2: AMRYVASYLLAALGGNSSPS
AKDIKKILDSVGIEADDDRL
NKVISELNGKNIEDVIAQGI
GKLASVPAGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 401 |
| 1H chemical shifts | 801 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 69 residues - 7088.202 Da.
| 1 | MET | ALA | SER | VAL | SER | GLU | LEU | ALA | CYS | ILE | ||||
| 2 | TYR | SER | ALA | LEU | ILE | LEU | HIS | ASP | ASP | GLU | ||||
| 3 | VAL | THR | VAL | THR | GLU | ASP | LYS | ILE | ASN | ALA | ||||
| 4 | LEU | ILE | LYS | ALA | ALA | GLY | VAL | ASN | VAL | GLU | ||||
| 5 | PRO | PHE | TRP | PRO | GLY | LEU | PHE | ALA | LYS | ALA | ||||
| 6 | LEU | ALA | ASN | VAL | ASN | ILE | GLY | SER | LEU | ILE | ||||
| 7 | CYS | ASN | VAL | GLY | ALA | GLY | GLY | PRO | ALA |
Entity 2, entity_2 70 residues - 7207.247 Da.
| 1 | ALA | MET | ARG | TYR | VAL | ALA | SER | TYR | LEU | LEU | |
| 2 | ALA | ALA | LEU | GLY | GLY | ASN | SER | SER | PRO | SER | |
| 3 | ALA | LYS | ASP | ILE | LYS | LYS | ILE | LEU | ASP | SER | |
| 4 | VAL | GLY | ILE | GLU | ALA | ASP | ASP | ASP | ARG | LEU | |
| 5 | ASN | LYS | VAL | ILE | SER | GLU | LEU | ASN | GLY | LYS | |
| 6 | ASN | ILE | GLU | ASP | VAL | ILE | ALA | GLN | GLY | ILE | |
| 7 | GLY | LYS | LEU | ALA | SER | VAL | PRO | ALA | GLY | GLY |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Brunger, Adams, Clore, Gros, Nilges and Read, Linge, O, . - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19086 15997 19086 |
| PDB | |
| DBJ | BAB25292 BAB27095 BAB79474 BAC40128 BAE41097 BAB22086 BAB25616 BAB27066 BAB28217 BAB79475 |
| EMBL | CAA33200 CAG29335 CAG47005 CAG47008 CAG47044 |
| GB | AAA36471 AAA70106 AAH03369 AAH07590 AAH58151 AAA36472 AAC48755 AAH05354 AAH05920 AAH07573 |
| PRF | 1718187B |
| REF | NP_000994 NP_001007605 NP_001020511 NP_001123436 NP_001180503 NP_000995 NP_001078905 NP_001180505 NP_001231795 NP_001270094 |
| SP | A1XQU7 P05386 P19944 P47955 Q56K14 P05387 P19943 P42899 P99027 Q6X9Z5 |
| TPG | DAA21200 DAA25760 DAA13527 |