BMRB Entry 25584

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25584
MolProbity Validation Chart

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Title:
NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the N-terminal activation domain of EKLF (TAD1)
Deposition date:
2015-04-27
Original release date:
2016-04-25
Authors:
Lecoq, Lauriane; Morse, Thomas; Raiola, Luca; Arseneault, Genevieve; Omichinski, James G.
Citation:

Citation: Morse, Thomas; Lecoq, Lauriane; Raiola, Luca; Arseneault, Genevieve; Omichinski, James. "Structural Characterization of the Complex between the N-terminal Transactivation Domain of EKLF and the p62/Tfb1 subunit of TFIIH"  .

Assembly members:

Assembly members:
RNA_polymerase_II_transcription_factor_B_subunit_1, polymer, 115 residues, 12903.807 Da.
N-terminal_transactivation_domain_of_Krueppel-like_factor_1, polymer, 19 residues, 2359.502 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: pGEX-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA_polymerase_II_transcription_factor_B_subunit_1: PSHSGAAIFEKVSGIIAINE DVSPAELTWRSTDGDKVHTV VLSTIDKLQATPASSEKMML RLIGKVDESKKRKDNEGNEV VPKPQRHMFSFNNRTVMDNI KMTLQQIISRYKDAD
N-terminal_transactivation_domain_of_Krueppel-like_factor_1: DTQDDFLKWWRSEEAQDMG

Data sets:
Data typeCount
13C chemical shifts578
15N chemical shifts144
1H chemical shifts938

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 115 residues - 12903.807 Da.

1   PROSERHISSERGLYALAALAILEPHEGLU
2   LYSVALSERGLYILEILEALAILEASNGLU
3   ASPVALSERPROALAGLULEUTHRTRPARG
4   SERTHRASPGLYASPLYSVALHISTHRVAL
5   VALLEUSERTHRILEASPLYSLEUGLNALA
6   THRPROALASERSERGLULYSMETMETLEU
7   ARGLEUILEGLYLYSVALASPGLUSERLYS
8   LYSARGLYSASPASNGLUGLYASNGLUVAL
9   VALPROLYSPROGLNARGHISMETPHESER
10   PHEASNASNARGTHRVALMETASPASNILE
11   LYSMETTHRLEUGLNGLNILEILESERARG
12   TYRLYSASPALAASP

Entity 2, entity_2 19 residues - 2359.502 Da.

1   ASPTHRGLNASPASPPHELEULYSTRPTRP
2   ARGSERGLUGLUALAGLNASPMETGLY

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 2 mM; H2O 90%; D2O 10%

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 2 mM; D2O 100%

sample_3: entity_2, [U-100% 13C; U-100% 15N], 0.8 mM; entity_1 2 mM; H2O 90%; D2O 10%

sample_4: entity_2, [U-100% 13C; U-100% 15N], 0.8 mM; entity_1 2 mM; D2O 100%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D intermolecular NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_4isotropicsample_conditions_1
3D intermolecular NOESYsample_4isotropicsample_conditions_1

Software:

No software information available

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
BMRB 6225
SP P32776 Q13351
REF NP_010597 K09204
NCBI 10661
AlphaFold E9P948 Q92899

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