BMRB Entry 18709

Title:
HMGB1-facilitated p53 DNA binding occurs via HMG-box/p53 transactivation domain interaction and is regulated by the acidic tail
Deposition date:
2012-09-12
Original release date:
2012-10-29
Authors:
Rowell, John; Simpson, Kathryn; Stott, Katherine; Watson, Matthew; Thomas, Jean
Citation:

Citation: Rowell, John; Simpson, Kathryn; Stott, Katherine; Watson, Matthew; Thomas, Jean. "HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail."  Structure 20, 2014-2024 (2012).
PubMed: 23063560

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 9705.259 Da.
entity_2, polymer, 93 residues, 9979.1 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7-7 HMG1-A

Data sets:
Data typeCount
13C chemical shifts749
15N chemical shifts159
1H chemical shifts1172

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1abox1
2p532

Entities:

Entity 1, abox 83 residues - 9705.259 Da.

1   GLYLYSGLYASPPROLYSLYSPROARGGLY
2   LYSMETSERSERTYRALAPHEPHEVALGLN
3   THRCYSARGGLUGLUHISLYSLYSLYSHIS
4   PROASPALASERVALASNPHESERGLUPHE
5   SERLYSLYSCYSSERGLUARGTRPLYSTHR
6   METSERALALYSGLULYSGLYLYSPHEGLU
7   ASPMETALALYSALAASPLYSALAARGTYR
8   GLUARGGLUMETLYSTHRTYRILEPROPRO
9   LYSGLYGLU

Entity 2, p53 93 residues - 9979.1 Da.

1   METGLUGLUPROGLNSERASPPROSERVAL
2   GLUPROPROLEUSERGLNGLUTHRPHESER
3   ASPLEUTRPLYSLEULEUPROGLUASNASN
4   VALLEUSERPROLEUPROSERGLNALAMET
5   ASPASPLEUMETLEUSERPROASPASPILE
6   GLUGLNTRPPHETHRGLUASPPROGLYPRO
7   ASPGLUALAPROARGMETPROGLUALAALA
8   PROPROVALALAPROALAPROALAALAPRO
9   THRPROALAALAPROALAPROALAPROSER
10   TRPPROLEU

Samples:

sample_1: entity_10.1 – 1 mM; entity_20.1 – 1 mM; sodium phosphate 10 mM; EDTA 1 mM; DTT 1 mM; PMSF 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY, X-filterefsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

ARIA, CCPN - structure solution

Analysis, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 11147 11532 15148 15149 15502 4079 17073 17760
PDB
DBJ BAA09924 BAC29902 BAC34367 BAC34773 BAC38678 BAC16799 BAG35463 BAG64357 BAI45431 BAJ52715
EMBL CAA31110 CAA31284 CAA56631 CAA68441 CAA68526 CAA26306 CAA38095 CAA42625 CAA42626 CAA42627
GB AAA20508 AAA31050 AAA40729 AAA57042 AAA64970 AAA59987 AAA59988 AAA59989 AAA61211 AAA61212
PIR S29857
REF NP_001002937 NP_001004034 NP_001075304 NP_001102843 NP_001162380 NP_000537 NP_001119584 NP_001119585 NP_001119586 NP_001119590
SP A9RA84 B0CM99 B1MTB0 P07156 P09429 P04637 Q9TTA1
TPG DAA21468 DAA23902
AlphaFold A9RA84 B0CM99 B1MTB0 P07156 P09429 P04637 Q9TTA1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks