Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11429
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Citation: KURITA, J.; UEWAKI, J.; SHIMAHARA, H.; YOSHIDA, M.; TATE, S.. "STRUCUTRAL COMPARISON OF TWO HMG-BOXES IN THE NON-HISTONE PROTEIN HMG-2 WITH IN THE HMG-1" .
Assembly members:
HMG2A, polymer, 77 residues, Formula weight is not available
Natural source: Common Name: pig Taxonomy ID: 9823 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Sus scrofa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Entity Sequences (FASTA):
HMG2A: MGKGDPNKPRGKMSSYAFFV
QTSREEHKKKHPDSSVNFAE
FSKKCSERWKTMSAKEKSKF
EDMAKSDKARYDREMKN
Data type | Count |
13C chemical shifts | 220 |
15N chemical shifts | 77 |
1H chemical shifts | 483 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HMG2A | 1 |
Entity 1, HMG2A 77 residues - Formula weight is not available
1 | MET | GLY | LYS | GLY | ASP | PRO | ASN | LYS | PRO | ARG | ||||
2 | GLY | LYS | MET | SER | SER | TYR | ALA | PHE | PHE | VAL | ||||
3 | GLN | THR | SER | ARG | GLU | GLU | HIS | LYS | LYS | LYS | ||||
4 | HIS | PRO | ASP | SER | SER | VAL | ASN | PHE | ALA | GLU | ||||
5 | PHE | SER | LYS | LYS | CYS | SER | GLU | ARG | TRP | LYS | ||||
6 | THR | MET | SER | ALA | LYS | GLU | LYS | SER | LYS | PHE | ||||
7 | GLU | ASP | MET | ALA | LYS | SER | ASP | LYS | ALA | ARG | ||||
8 | TYR | ASP | ARG | GLU | MET | LYS | ASN |
sample_1: HMG2A, [U-13C; U-15N], 1 mM; H2O 95%; D2O 5%; sodium acetate 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 5.0; pressure: 1 atm; temperature: 293 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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