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Biological Magnetic Resonance Data Bank


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BMRB Entry 17073

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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/BMR17073
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Title: Structure of CBP nuclear coactivator binding domain in complex with p53 TAD   PubMed: 20961098

Deposition date: 2010-07-22 Original release date: 2010-10-22

Authors: Lee, Chul Won; Martinez-Yamout, Maria; Dyson, Helen; Wright, Peter

Citation: Lee, Chul Won; Martinez-Yamout, Maria; Dyson, H. Jane; Wright, Peter. "Structure of the p53 Transactivation Domain in Complex with the Nuclear Receptor Coactivator Binding Domain of CREB Binding Protein."  Biochemistry 49, 9964-9971 (2010).

Assembly members:
CBP, polymer, 59 residues, 6568.623 Da.
TAD, polymer, 49 residues, 5574.146 Da.

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
CBP: PNRSISPSALQDLLRTLKSP SSPQQQQQVLNILKSNPQLM AAFIKQRTAKYVANQPGMQ
TAD: PLSQETFSDLWKLLPENNVL SPLPSQAMDDLMLSPDDIEQ WFTEDPGPD

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts115
1H chemical shifts787

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBP1
2TAD2

Entities:

Entity 1, CBP 59 residues - 6568.623 Da.

1   PROASNARGSERILESERPROSERALALEU
2   GLNASPLEULEUARGTHRLEULYSSERPRO
3   SERSERPROGLNGLNGLNGLNGLNVALLEU
4   ASNILELEULYSSERASNPROGLNLEUMET
5   ALAALAPHEILELYSGLNARGTHRALALYS
6   TYRVALALAASNGLNPROGLYMETGLN

Entity 2, TAD 49 residues - 5574.146 Da.

1   PROLEUSERGLNGLUTHRPHESERASPLEU
2   TRPLYSLEULEUPROGLUASNASNVALLEU
3   SERPROLEUPROSERGLNALAMETASPASP
4   LEUMETLEUSERPROASPASPILEGLUGLN
5   TRPPHETHRGLUASPPROGLYPROASP

Samples:

sample_1: CBP, [U-99% 15N], 0.5 mM; TAD, [U-99% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_2: CBP, [U-99% 13C; U-99% 15N], 0.5 mM; TAD, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 750 MHz
  • Bruker DRX 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 15398 16363 15944 17760 18709
PDB
DBJ BAE06125 BAI45616 BAC16799 BAG35463 BAG59884 BAG60244 BAI45431
GB AAB28651 AAC17736 AAC51331 AAC51340 AAC51770 AAA59987 AAA59988 AAA59989 AAA61211 AAA61212
PRF 1923401A
REF NP_001020603 NP_001073315 NP_001247644 NP_004371 NP_596872 NP_000537 NP_001119584 NP_001119585 NP_001119586 NP_001274298
SP P45481 Q6JHU9 Q92793 P04637 Q9TTA1
EMBL CAA26306 CAA38095 CAA42625 CAA42626 CAA42627

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts