BMRB Entry 15997
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15997
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Title: NMR STRUCTURE OF DIMERIZATION DOMAIN OF HUMAN RIBOSOMAL PROTEIN P2 PubMed: 20385603
Deposition date: 2008-10-22 Original release date: 2010-05-06
Authors: Lee, K.; Chan, S.; Sze, K.; Zhu, G.; Shaw, P.; Wong, K.
Citation: Lee, Ka-Ming; Yu, Conny Wing-Heng; Chan, Denise So-Bik; Chiu, Teddy Yu-Hin; Zhu, Guang; Sze, Kong-Hung; Shaw, Pang-Chui; Wong, Kam-Bo. "Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk." Nucleic Acids Res. 38, 5206-5216 (2010).
Assembly members:
HUMAN_RIBOSOME_PROTEIN_P2, polymer, 70 residues, Formula weight is not available
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):
HUMAN_RIBOSOME_PROTEIN_P2: AMRYVASYLLAALGGNSSPS
AKDIKKILDSVGIEADDDRL
NKVISELNGKNIEDVIAQGI
GKLASVPAGG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 210 |
15N chemical shifts | 67 |
1H chemical shifts | 577 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HUMAN RIBOSOME PROTEIN P2_1 | 1 |
2 | HUMAN RIBOSOME PROTEIN P2_2 | 1 |
Entities:
Entity 1, HUMAN RIBOSOME PROTEIN P2_1 70 residues - Formula weight is not available
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: HUMAN RIBOSOME PROTEIN P2, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; SODIUM SULFATE 200 mM
sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1.0 atm; temperature: 298.0 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
NOESY | sample_1 | isotropic | sample_conditions_1 |
COSY | sample_1 | isotropic | sample_conditions_1 |
TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN - refinement
NMRView, Johnson, One Moon Scientific - structure solution
NMR spectrometers:
- VARIAN UNITYINOVA 750 MHz
Related Database Links:
PDB | |
DBJ | BAB22086 BAB25616 BAB27066 BAB28217 BAB79475 |
EMBL | CAG47008 CAG47044 |
GB | AAA36472 AAC48755 AAH05354 AAH05920 AAH07573 |
REF | NP_000995 NP_001078905 NP_001180505 NP_001231795 NP_001270094 |
SP | P05387 P19943 P42899 P99027 Q6X9Z5 |
TPG | DAA13527 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts