BMRB Entry 11160
Click here to enlarge.
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/BMR11160
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 HMG box of human Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog
Deposition date: 2010-04-15 Original release date: 2011-05-05
Authors: Abe, H.; Tochio, N.; Miyamoto, K.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.
Citation: Abe, H.; Tochio, N.; Miyamoto, K.; Koshiba, S.; Harada, T.; Watanabe, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the HMG box of human Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog" . ., .-..
Assembly members:
HMG (high mobility group) box, UNP residues 1631-1713, polymer, 90 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: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
HMG (high mobility group) box, UNP residues 1631-1713: GSSGSSGNAQRSTLKWEKEE
ALGEMATVAPVLYTNINFPN
LKEEFPDWTTRVKQIAKLWR
KASSQERAPYVQKARDNRAA
LRINKVQMSN
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 380 |
15N chemical shifts | 89 |
1H chemical shifts | 603 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HMG (high mobility group) box, UNP residues 1631-1713 | 1 |
Entities:
Entity 1, HMG (high mobility group) box, UNP residues 1631-1713 90 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | ASN | ALA | GLN | |
2 | ARG | SER | THR | LEU | LYS | TRP | GLU | LYS | GLU | GLU | |
3 | ALA | LEU | GLY | GLU | MET | ALA | THR | VAL | ALA | PRO | |
4 | VAL | LEU | TYR | THR | ASN | ILE | ASN | PHE | PRO | ASN | |
5 | LEU | LYS | GLU | GLU | PHE | PRO | ASP | TRP | THR | THR | |
6 | ARG | VAL | LYS | GLN | ILE | ALA | LYS | LEU | TRP | ARG | |
7 | LYS | ALA | SER | SER | GLN | GLU | ARG | ALA | PRO | TYR | |
8 | VAL | GLN | LYS | ALA | ARG | ASP | ASN | ARG | ALA | ALA | |
9 | LEU | ARG | ILE | ASN | LYS | VAL | GLN | MET | SER | ASN |
Samples:
sample_1: HMG (high mobility group) box, UNP residues 1631-1713, [U-13C; U-15N], 1.11 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.9747, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
PDB | |
GB | KFP32916 |
REF | XP_010203152 XP_012426828 XP_012426830 XP_012426831 XP_012426832 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts