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BMRB Entry 16411

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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/BMR16411
MolProbity Validation Chart

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Title: Solution structure of Rtt103 CTD interacting domain   PubMed: 20818393

Deposition date: 2009-07-20 Original release date: 2010-09-17

Authors: Lunde, Bradley; Reichow, Steve; Kim, Minkyu; Leeper, Thomas; Becker, Roland; 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 CTD interacting domain, polymer, 142 residues, 15885.456 Da.

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 CTD interacting domain: MAFSSEQFTTKLNTLEDSQE SISSASKWLLLQYRDAPKVA EMWKEYMLRPSVNTRRKLLG LYLMNHVVQQAKGQKIIQFQ DSFGKVAAEVLGRINQEFPR DLKKKLSRVVNILKERNIFS KQVVNDIERSLAAALEHHHH HH

Data sets:
Data typeCount
13C chemical shifts570
15N chemical shifts150
1H chemical shifts1016

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Rtt103 CTD interacting domain1

Entities:

Entity 1, Rtt103 CTD interacting domain 142 residues - 15885.456 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_1: Rtt103, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; potassium chloride 100 mM; potassium phosphate 35 mM; H2O 95%; D2O 5%

sample_2: Rtt1030.5 – 1 mM; potassium chloride 100 mM; potassium phosphate 35 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1

Software:

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

NMR spectrometers:

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

Related Database Links:

BMRB 16412 17044
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:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts