BMRB Entry 34041

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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/BMR34041
MolProbity Validation Chart

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Title:
Solution structure of Rtt103 CTD-interacting domain bound to a Thr4 phosphorylated CTD peptide
Deposition date:
2016-09-14
Original release date:
2017-05-08
Authors:
Jasnovidova, O.; Kubicek, K.; Krejcikova, M.; Stefl, R.
Citation:

Citation: Jasnovidova, O.; Krejcikova, M.; Kubicek, K.; Stefl, R.. "Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p"  Embo Rep. 18, 906-913 (2017).
PubMed: 28468956

Assembly members:

Assembly members:
entity_1, polymer, 142 residues, 16569.100 Da.
entity_2, polymer, 16 residues, 1721.669 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 559292   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAFSSEQFTTKLNTLEDSQE SISSASKWLLLQYRDAPKVA EMWKEYMLRPSVNTRRKLLG LYLMNHVVQQAKGQKIIQFQ DSFGKVAAEVLGRINQEFPR DLKKKLSRVVNILKERNIFS KQVVNDIERSLAAALEHHHH HH
entity_2: PSYSPXSPSYSPTSPS

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts144
1H chemical shifts998

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 142 residues - 16569.100 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

Entity 2, entity_2 16 residues - 1721.669 Da.

1   PROSERTYRSERPROTPOSERPROSERTYR
2   SERPROTHRSERPROSER

Samples:

sample_1: Rtt103 CID, [U-13C; U-15N], 1 ± 0.2 mM; pThr4-CTD 1.2 ± 0.2 mM; KH2PO4 35 mM; KCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 760 mmHg; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
4D HCCH TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
F1-13C/15N-filtered NOESY-[13C,1H]-HSQCsample_1isotropicsample_conditions_1

Software:

AMBER v16, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceIII 950 MHz
  • Bruker AvanceIII 700 MHz

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