BMRB Entry 19738

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19738
MolProbity Validation Chart

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Title:
Solution structures of second bromodomain of Brd4 with Di-acetylated Twist peptide
Deposition date:
2014-01-16
Original release date:
2014-03-17
Authors:
Zeng, Lei; Zhou, Ming-Ming
Citation:

Citation: Shi, Jian; Wang, Yifan; Zeng, Lei; Wu, Yadi; Deng, Jiong; Zhang, Qiang; Lin, Yiwei; Li, Junlin; Kang, Tiebang; Tao, Min; Rusinova, Elena; Zhang, Guangtao; Wang, Chi; Zhu, Haining; Yao, Jun; Zeng, Yi-Xin; Evers, B.; Zhou, Ming-Ming; Zhou, Binhua. "Disrupting the Interaction of BRD4 with Diacetylated Twist Suppresses Tumorigenesis in Basal-like Breast Cancer"  Cancer Cell 25, 210-225 (2014).
PubMed: 24525235

Assembly members:

Assembly members:
entity_1, polymer, 12 residues, 1300.477 Da.
entity_2, polymer, 128 residues, 14842.159 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SPAQGXRGXKSA
entity_2: KDVPDSQQHPAPEKSSKVSE QLKCCSGILKEMFAKKHAAY AWPFYKPVDVEALGLHDYCD IIKHPMDMSTIKSKLEAREY RDAQEFGADVRLMFSNCYKY NPPDHEVVAMARKLQDVFEM RFAKMPDE

Data sets:
Data typeCount
13C chemical shifts454
15N chemical shifts118
1H chemical shifts874

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 12 residues - 1300.477 Da.

1   SERPROALAGLNGLYALYARGGLYALYLYS
2   SERALA

Entity 2, entity_2 128 residues - 14842.159 Da.

1   LYSASPVALPROASPSERGLNGLNHISPRO
2   ALAPROGLULYSSERSERLYSVALSERGLU
3   GLNLEULYSCYSCYSSERGLYILELEULYS
4   GLUMETPHEALALYSLYSHISALAALATYR
5   ALATRPPROPHETYRLYSPROVALASPVAL
6   GLUALALEUGLYLEUHISASPTYRCYSASP
7   ILEILELYSHISPROMETASPMETSERTHR
8   ILELYSSERLYSLEUGLUALAARGGLUTYR
9   ARGASPALAGLNGLUPHEGLYALAASPVAL
10   ARGLEUMETPHESERASNCYSTYRLYSTYR
11   ASNPROPROASPHISGLUVALVALALAMET
12   ALAARGLYSLEUGLNASPVALPHEGLUMET
13   ARGPHEALALYSMETPROASPGLU

Samples:

sample_1: entity mM; DTT, [U-100% 2H], 5 mM; sodium phosphate 100 mM; D2O 100%

sample_2: entity mM; DTT, [U-100% 2H], 5 mM; sodium phosphate 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 13C-edited 13C/15N-filtered NOESY aromaticsample_1isotropicsample_conditions_1
3D 13C-edited 13C/15N-filtered NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

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

NMRPipe v7.1, 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 - geometry optimization, structure solution

TOPSPIN v1.3, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15057 18439
PDB
REF XP_004761195 XP_006524755 XP_006524756 XP_008763395
AlphaFold Q99804

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