BMRB Entry 30330

Title:
Solution structure of yeast Med15 ABD2 residues 277-368
Deposition date:
2017-08-08
Original release date:
2018-03-16
Authors:
Tuttle, L.; Pacheco, D.; Warfield, L.; Hahn, S.; Klevit, R.
Citation:

Citation: Tuttle, L.; Pachecko, D.; Warfield, L.; Luo, J.; Ranish, J.; Hahn, S.; Klevit, R.. "Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex."  Cell Rep. 22, 3251-3264 (2018).
PubMed: 29562181

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, 10525.714 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts87
1H chemical shifts464

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 92 residues - 10525.714 Da.

1   ASNASNPROLEUGLNGLNGLNSERSERGLN
2   ASNTHRVALPROASNVALLEUASNGLNILE
3   ASNGLNILEPHESERPROGLUGLUGLNARG
4   SERLEULEUGLNGLUALAILEGLUTHRCYS
5   LYSASNPHEGLULYSTHRGLNLEUGLYSER
6   THRMETTHRGLUPROVALLYSGLNSERPHE
7   ILEARGLYSTYRILEASNGLNLYSALALEU
8   ARGLYSILEGLNALALEUARGASPVALLYS
9   ASNASNASNASNALAASNASNASNGLYSER
10   ASNLEU

Samples:

sample_1: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_2: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-13C; U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_3: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-13C; U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_4: C12E6/Hexanol 10%; DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-15N], 2.6 mM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_4anisotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_1isotropicsample_conditions_1

Software:

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

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

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH v2.45, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 500 MHz
  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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