BMRB Entry 30206

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30206
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structures of Brd2 second bromodomain in complex with stat3 peptide
Deposition date:
2016-12-07
Original release date:
2017-02-20
Authors:
Zeng, L.; Zhou, M.
Citation:

Citation: Cheung, K.; Zhang, F.; Jaganathan, A.; Sharma, R.; Zhang, Q.; Konuma, T.; Shen, T.; Lee, J.-Y., J.; Ren, C.; Chen, C.-H., C.; Lu, G.; Olson, M.; Zhang, W.; Kaplan, M.; Littman, D.; Walsh, M.; Xiong, H.; Zeng, L.; Zhou, M.. "Distinct Roles of Brd2 and Brd4 in Potentiating the Transcriptional Program for Th17 Cell Differentiation"  Mol. Cell 65, 1068-1080 (2017).
PubMed: 28262505

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 13157.136 Da.
entity_2, polymer, 12 residues, 1540.808 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: GKLSEQLKHCNGILKELLSK KHAAYAWPFYKPVDASALGL HDYHDIIKHPMDLSTVKRKM ENRDYRDAQEFAADVRLMFS NCYKYNPPDHDVVAMARKLQ DVFEFRYAKMPD
entity_2: HNLLRIXQFLQS

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts100
1H chemical shifts834

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_1 112 residues - 13157.136 Da.

1   GLYLYSLEUSERGLUGLNLEULYSHISCYS
2   ASNGLYILELEULYSGLULEULEUSERLYS
3   LYSHISALAALATYRALATRPPROPHETYR
4   LYSPROVALASPALASERALALEUGLYLEU
5   HISASPTYRHISASPILEILELYSHISPRO
6   METASPLEUSERTHRVALLYSARGLYSMET
7   GLUASNARGASPTYRARGASPALAGLNGLU
8   PHEALAALAASPVALARGLEUMETPHESER
9   ASNCYSTYRLYSTYRASNPROPROASPHIS
10   ASPVALVALALAMETALAARGLYSLEUGLN
11   ASPVALPHEGLUPHEARGTYRALALYSMET
12   PROASP

Entity 2, entity_2 12 residues - 1540.808 Da.

1   HISASNLEULEUARGILEALYGLNPHELEU
2   GLNSER

Samples:

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

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

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C filtered NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C filtered NOESY aromaticsample_1isotropicsample_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 v5.04, Johnson, One Moon Scientific - chemical shift assignment, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

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

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