BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17393

Title: Solution NMR structures of CBP bromodomain with small molecule of HBS   PubMed: 21513889

Deposition date: 2011-01-04 Original release date: 2011-02-09

Authors: Borah, Jagat; Mujtaba, Shiraz; Karakikes, Ioannis; Zeng, Lei; Muller, Michaela; Patel, Jigneshkumar; Moshkina, Natasha; Morohashi, Keita; Zhang, Weijia; Gerona-navarro, Guillermo; Hajjar, Roger; Zhou, Ming-ming

Citation: Borah, Jagat; Mujtaba, Shiraz; Karakikes, Ioannis; Zeng, Lei; Muller, Michaela; Patel, Jigneshkumar; Moshkina, Natasha; Morohashi, Keita; Zhang, Weijia; Gerona-Navarro, Guillermo; Hajjar, Roger; Zhou, Ming-Ming. "A Small Molecule Binding to the Coactivator CREB-Binding Protein Blocks Apoptosis in Cardiomyocytes."  Chem. Biol. 18, 531-541 (2011).

Assembly members:
entity_1, polymer, 121 residues, 14418.670 Da.
L85, non-polymer, 278.284 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: PET15B

Entity Sequences (FASTA):
entity_1: GSHMRKKIFKPEELRQALMP TLEALYRQDPESLPFRQPVD PQLLGIPDYFDIVKNPMDLS TIKRKLDTGQYQEPWQYVDD VWLMFNNAWLYNRKTSRVYK FCSKLAEVFEQEIDPVMQSL G

Data sets:
Data typeCount
13C chemical shifts430
15N chemical shifts122
1H chemical shifts826

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBP bromodomain1
2S,3-HYDROXYBUTAN-2-ONE2

Entities:

Entity 1, CBP bromodomain 121 residues - 14418.670 Da.

1   GLYSERHISMETARGLYSLYSILEPHELYS
2   PROGLUGLULEUARGGLNALALEUMETPRO
3   THRLEUGLUALALEUTYRARGGLNASPPRO
4   GLUSERLEUPROPHEARGGLNPROVALASP
5   PROGLNLEULEUGLYILEPROASPTYRPHE
6   ASPILEVALLYSASNPROMETASPLEUSER
7   THRILELYSARGLYSLEUASPTHRGLYGLN
8   TYRGLNGLUPROTRPGLNTYRVALASPASP
9   VALTRPLEUMETPHEASNASNALATRPLEU
10   TYRASNARGLYSTHRSERARGVALTYRLYS
11   PHECYSSERLYSLEUALAGLUVALPHEGLU
12   GLNGLUILEASPPROVALMETGLNSERLEU
13   GLY

Entity 2, S,3-HYDROXYBUTAN-2-ONE - C12 H10 N2 O4 S - 278.284 Da.

1   L85

Samples:

sample_2: CBP bromodomain, [U-100% 13C; U-100% 15N], 0.5 mM; (E)-4-((4-hydroxyphenyl)diazenyl)benzenesulfonic acid 3 mM; sodium phosphate 100 mM; DTT, [U-100% 2H], 3 mM; D2O 100%

sample_1: CBP bromodomain, [U-100% 13C; U-100% 15N], 0.5 mM; (E)-4-((4-hydroxyphenyl)diazenyl)benzenesulfonic acid 3 mM; sodium phosphate 100 mM; DTT, [U-100% 2H], 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 13C-edited 13C/15N-FILTERED NOESYsample_2isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, processing

NMRView v5.04, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 17392
PDB
DBJ BAE06125 BAG65526 BAI45616
GB AAB28651 AAC51331 AAC51770 AAH72594 AAI72737
PRF 1923401A
REF NP_001020603 NP_001073315 NP_001157494 NP_001247644 NP_004371
SP P45481 Q6JHU9 Q92793
TPG DAA15549
AlphaFold Q92793

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