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BMRB Entry 17044

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17044
MolProbity Validation Chart

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Title: Solution structure of Rtt103 CTD-interacting domain bound to a Ser2 phosphorylated CTD peptide   PubMed: 20818393

Deposition date: 2010-07-06 Original release date: 2010-09-24

Authors: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Suh, Hyunsuk; Leeper, Thomas; Yang, Fan; Mutschler, Hannes; Buratowski, Stephen; Meinhart, Anton; Varani, Gabriele

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).

Assembly members:
Rtt103, polymer, 142 residues, Formula weight is not available
CTD, polymer, 14 residues, Formula weight is not available

Natural source:   Common Name: Baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Rtt103: MAFSSEQFTTKLNTLEDSQE SISSASKWLLLQYRDAPKVA EMWKEYMLRPSVNTRRKLLG LYLMNHVVQQAKGQKIIQFQ DSFGKVAAEVLGRINQEFPR DLKKKLSRVVNILKERNIFS KQVVNDIERSLAAALEHHHH HH
CTD: YSPTSPSYSPTSPS

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

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Rtt1031
2CTD2

Entities:

Entity 1, Rtt103 142 residues - Formula weight is not available

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

Entity 2, CTD 14 residues - Formula weight is not available

1   TYRSERPROTHRSERPROSERTYRSERPRO
2   THRSERPROSER

Samples:

sample_1: Rtt103, [U-98% 13C; U-98% 15N], 1 mM; TRIS, [U-99% 2H], 10 mM; sodium chloride 120 mM; CTD 1.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.120 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read, HADDOCK -Bonvin - structure solution

NMR spectrometers:

  • Bruker AMX 500 MHz

Related Database Links:

BMRB 16411 16412
PDB
DBJ GAA22510
EMBL CAY78790
GB AAB64467 AAS56119 AHY75263 AJP37990 AJU58113
REF NP_010575
SP Q05543
TPG DAA12129

Download simulated HSQC data in one of the following formats:
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