BMRB Entry 16412

Title:
Solution structure of Rtt103 bound to CTD peptide
Deposition date:
2009-07-21
Original release date:
2010-09-17
Authors:
Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Leeper, Thomas; Becker, Roland; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele
Citation:

Citation: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Suh, Hyunsuk; Leeper, Thomas; Yang, Fan; Mutschler, Hannes; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele. "Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain."  Nat. Struct. Mol. Biol. 17, 1195-1201 (2010).
PubMed: 20818393

Assembly members:

Assembly members:
Rtt103 bound to CTD peptide, polymer, 142 residues, 15747.308 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: PET-28b

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts137
1H chemical shifts1001

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rtt103 bound to CTD peptide1

Entities:

Entity 1, Rtt103 bound to CTD peptide 142 residues - 15747.308 Da.

1   METALAPHESERSERGLUGLNPHETHRTHR
2   LYSLEUASNTHRLEUGLUASPSERGLNGLU
3   SERILESERSERALASERLYSTRPLEULEU
4   LEUGLNTYRARGASPALAPROLYSVALALA
5   GLUMETTRPLYSGLUTYRMETLEUARGPRO
6   SERVALASNTHRARGARGLYSLEULEUGLY
7   LEUTYRLEUMETASNHISVALVALGLNGLN
8   ALALYSGLYGLNLYSILEILEGLNPHEGLN
9   ASPSERPHEGLYLYSVALALAALAGLUVAL
10   LEUGLYARGILEASNGLNGLUPHEPROARG
11   ASPLEULYSLYSLYSLEUSERARGVALVAL
12   ASNILELEULYSGLUARGASNILEPHESER
13   LYSGLNVALVALASNASPILEGLUARGSER
14   LEUALAALAALALEUGLUHISHISHISHIS
15   HISHIS

Samples:

sample_2: sodium chloride 120 mM; TRIS 10 mM; Rtt1030.5 – 1 mM; CTD1 – 1.5 mM; D2O 100%

sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz
  • Bruker DMX 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16411 17044
PDB
DBJ GAA22510
EMBL CAY78790
GB AAB64467 AAS56119 AHY75263 AJP37990 AJU58113
REF NP_010575
SP Q05543
TPG DAA12129
AlphaFold Q05543

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