BMRB Entry 30373

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30373
MolProbity Validation Chart

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Title:
Solution NMR structures of BRD4 ET domain with JMJD6 peptide
Deposition date:
2017-11-16
Original release date:
2017-12-06
Authors:
Konuma, T.; Yu, D.; Zhao, C.; Ju, Y.; Sharma, R.; Ren, C.; Zhang, Q.; Zhou, M.; Zeng, L.
Citation:

Citation: Liu, Jingyi; Duan, Zhibing; Guo, Weijie; Zeng, Lei; Wu, Yadi; Chen, Yule; Tai, Fang; Wang, Yifan; Lin, Yiwei; Zhang, Qiang; He, Yanling; Deng, Jiong; Stewart, Rachel; Wang, Chi; Lin, Pengnian Charles; Ghaffari, Saghi; Evers, B Mark; Liu, Suling; Zhou, Ming-Ming; Zhou, Binhua; Shi, Jian. "Targeting the BRD4/FOXO3a/CDK6 axis sensitizes AKT inhibition in luminal breast cancer"  Nat. Commun. 9, 5200-5200 (2018).
PubMed: 30518851

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 9745.136 Da.
entity_2, polymer, 13 residues, 1797.156 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEEEDKCKPMSYEEKRQLSL DINKLPGEKLGRVVHIIQSR EPSLKNSNPDEIEIDFETLK PSTLRELERYVTSCLRKKRK PQA
entity_2: KWTLERLKRKYRN

Data sets:
Data typeCount
13C chemical shifts343
15N chemical shifts81
1H chemical shifts662

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 83 residues - 9745.136 Da.

1   SERGLUGLUGLUASPLYSCYSLYSPROMET
2   SERTYRGLUGLULYSARGGLNLEUSERLEU
3   ASPILEASNLYSLEUPROGLYGLULYSLEU
4   GLYARGVALVALHISILEILEGLNSERARG
5   GLUPROSERLEULYSASNSERASNPROASP
6   GLUILEGLUILEASPPHEGLUTHRLEULYS
7   PROSERTHRLEUARGGLULEUGLUARGTYR
8   VALTHRSERCYSLEUARGLYSLYSARGLYS
9   PROGLNALA

Entity 2, entity_2 13 residues - 1797.156 Da.

1   LYSTRPTHRLEUGLUARGLEULYSARGLYS
2   TYRARGASN

Samples:

sample_2: entity_1 mM; entity_2 mM; DTT, [U-100% 2H], 2 mM; sodium chloride 100 mM; sodium phosphate 10 mM

sample_1: entity_1 mM; entity_2 mM; DTT, [U-100% 2H], 2 mM; sodium chloride 100 mM; sodium phosphate 10 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availablesample_conditions_1
3D HNCACBsample_1not availablesample_conditions_1
3D CBCA(CO)NHsample_1not availablesample_conditions_1
3D 1H-15N NOESYsample_1not availablesample_conditions_1
3D 1H-13C NOESY aliphaticsample_2not availablesample_conditions_1
3D 1H-13C NOESY aromaticsample_2not availablesample_conditions_1
3D filtered 1H-13C NOESY aliphaticsample_2not availablesample_conditions_1
3D filtered 1H-13C NOESY aromaticsample_2not availablesample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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