BMRB Entry 18244

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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/BMR18244
MolProbity Validation Chart

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Title:
Structure of the complex of the central activation doamin of Gcn4 bound to the mediator co-activator domain 1 of Gal11/med15
Deposition date:
2012-02-07
Original release date:
2012-03-28
Authors:
Brzovic, Peter; Heikaus, Clemens; Kisselev, Leonid; Vernon, Robert; Herbig, Eric; Pacheco, Derek; Warfield, Linda; Littlefield, Peter; Baker, David; Klevit, Rachel; Hahn, Steven
Citation:

Citation: Brzovic, Peter; Heikaus, Clemens; Kisselev, Leonid; Vernon, Robert; Herbig, Eric; Pacheco, Derek; Warfield, Linda; Baker, David; Klevit, Rachel; Hahn, Steven. "The Acidic Transcription Activator Gcn4 Binds the Mediator Subunit Gal11/Med15 Using a Simple Protein Interface Forming a Fuzzy Complex"  Mol. Cell 44, 942-953 (2011).
PubMed: 22195967

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9514.164 Da.
entity_2, polymer, 34 residues, 3958.110 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QRRQLTPQQQQLVNQMKVAP IPKQLLQRIPNIPPNINTWQ QVTALAQQKLLTPQDMEAAK QVYKIHQQLLFKARLQQQQA Q
entity_2: STDSTPMFEYENLEDNSKEW TSLFDNDIPVTTDD

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts102
1H chemical shifts761

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1central activation doamin of Gcn41
2domain 1 of Gal11/med152

Entities:

Entity 1, central activation doamin of Gcn4 81 residues - 9514.164 Da.

1   GLNARGARGGLNLEUTHRPROGLNGLNGLN
2   GLNLEUVALASNGLNMETLYSVALALAPRO
3   ILEPROLYSGLNLEULEUGLNARGILEPRO
4   ASNILEPROPROASNILEASNTHRTRPGLN
5   GLNVALTHRALALEUALAGLNGLNLYSLEU
6   LEUTHRPROGLNASPMETGLUALAALALYS
7   GLNVALTYRLYSILEHISGLNGLNLEULEU
8   PHELYSALAARGLEUGLNGLNGLNGLNALA
9   GLN

Entity 2, domain 1 of Gal11/med15 34 residues - 3958.110 Da.

1   SERTHRASPSERTHRPROMETPHEGLUTYR
2   GLUASNLEUGLUASPASNSERLYSGLUTRP
3   THRSERLEUPHEASPASNASPILEPROVAL
4   THRTHRASPASP

Samples:

sample_1: Gal11, [U-15N], 1-1.2 mM; Gcn4 2-2.4 mM; Sodum phosphate 20 mM; Sodum chloride 150 mM; PMSF 1 mM; DTT 5 mM; H20 90%; D2O 10%

sample_2: Gal11 2-2.4 mM; Gcn4, [U-15N], 1-1.2 mM; Sodum phosphate 20 mM; Sodum chloride 150 mM; PMSF 1 mM; DTT 5 mM; H20 90%; D2O 10%

sample_3: Gal11, [U-13C; U-15N], 1-1.2 mM; Gcn4 2-2.4 mM; Sodum phosphate 20 mM; Sodum chloride 150 mM; PMSF 1 mM; DTT 5 mM; H20 90%; D2O 10%

sample_4: Gal11, [U-13C; U-15N], 1-1.2 mM; Gcn4 2-2.4 mM; Sodum phosphate 20 mM; Sodum chloride 150 mM; PMSF 1 mM; DTT 5 mM; D2O 100%

sample_5: Gal11 2-2.4 mM; Gcn4, [U-13C; U-15N], 1-1.2 mM; Sodum phosphate 20 mM; Sodum chloride 150 mM; PMSF 1 mM; DTT 5 mM; H20 90%; D2O 10%

sample_conditions_1: ionic strength: 0.150 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_5isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCAsample_5isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCACBsample_5isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_5isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_5isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_5isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_5isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

HADDOCK v2.1, Alexandre Bonvin - structure solution

VNMR, Varian - collection

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz
  • Bruker DMX 500 MHz

Related Database Links:

PDB
DBJ GAA26277 GAA22815
EMBL CAA62537 CAA99056 CAY86238 CAE52206 CAE52207 CAE52208 CAE52209 CAE52210
GB AAA34622 AHY77262 AJP41494 AJT70913 AJT71404 AAA34640 AAA65521 AAB64486 AHY75543 EDN62959
REF NP_014591 NP_010907
SP P19659 P03069
TPG DAA10733 DAA07643
AlphaFold P19659 P03069

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