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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11532
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Jing, Wang; Tochio, Naoya; Tate, Shin-ichi. "Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA" Biochem. Biophys. Res. Commun. ., .-..
PubMed: 24513216
Assembly members:
entity, polymer, 87 residues, 10118.729 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 Vector: pET28a
Entity Sequences (FASTA):
entity: GSHMGKGDPKKPRGKMSSYA
FFVQTCREEHKKKHPDASVN
FSEFSKKCSERWKTMSAKEK
GKFEDMAKADKARYEREMKT
YIPPKGE
Data type | Count |
13C chemical shifts | 398 |
15N chemical shifts | 87 |
1H chemical shifts | 572 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entity 1, entity 87 residues - 10118.729 Da.
1 | GLY | SER | HIS | MET | GLY | LYS | GLY | ASP | PRO | LYS | ||||
2 | LYS | PRO | ARG | GLY | LYS | MET | SER | SER | TYR | ALA | ||||
3 | PHE | PHE | VAL | GLN | THR | CYS | ARG | GLU | GLU | HIS | ||||
4 | LYS | LYS | LYS | HIS | PRO | ASP | ALA | SER | VAL | ASN | ||||
5 | PHE | SER | GLU | PHE | SER | LYS | LYS | CYS | SER | GLU | ||||
6 | ARG | TRP | LYS | THR | MET | SER | ALA | LYS | GLU | LYS | ||||
7 | GLY | LYS | PHE | GLU | ASP | MET | ALA | LYS | ALA | ASP | ||||
8 | LYS | ALA | ARG | TYR | GLU | ARG | GLU | MET | LYS | THR | ||||
9 | TYR | ILE | PRO | PRO | LYS | GLY | GLU |
sample_1: entity, [U-13C; U-15N], 0.5 0.6 mM; potassium phosphate 50 mM; potassium chloride 150 mM; D2O, [U-2H], 10%; H2O 90%
sample_2: entity, [U-13C; U-15N], 0.5 0.6 mM; C12E5/n-hexanol 6%; potassium chloride 150 mM; potassium phosphate 50 mM; D2O, [U-2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 200 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N IPAP-HSQC | sample_2 | anisotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MAGRO, Kobayashi N. - data analysis
NMRView, Johnson, One Moon Scientific - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY, Goddard - data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
BMRB | 11147 15148 15149 15502 18709 4079 |
PDB | |
DBJ | BAA09924 BAC29902 BAC34367 BAC34773 BAC38678 |
EMBL | CAA31110 CAA31284 CAA56631 CAA68441 CAA68526 |
GB | AAA20508 AAA31050 AAA40729 AAA57042 AAA64970 |
PIR | S29857 |
REF | NP_001002937 NP_001004034 NP_001075304 NP_001102843 NP_001162380 |
SP | A9RA84 B0CM99 B1MTB0 P07156 P09429 |
TPG | DAA21468 DAA23902 |
AlphaFold | P07156 B1MTB0 B0CM99 A9RA84 P09429 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks